HEADER SIGNALING PROTEIN 06-DEC-22 8BWL TITLE CRYSTAL STRUCTURE OF HUMAN TWISTED GASTRULATION PROTEIN HOMOLOG 1 TITLE 2 (TWSG1) IN COMPLEX WITH HUMAN GROWTH DIFFERENTIATION FACTOR 5 (GDF5) TITLE 3 AND CALCIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: GROWTH/DIFFERENTIATION FACTOR 5; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: GDF-5,BONE MORPHOGENETIC PROTEIN 14,BMP-14,CARTILAGE-DERIVED COMPND 5 MORPHOGENETIC PROTEIN 1,CDMP-1,LIPOPOLYSACCHARIDE-ASSOCIATED PROTEIN COMPND 6 4,LAP-4,LPS-ASSOCIATED PROTEIN 4,RADOTERMIN; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: TWISTED GASTRULATION PROTEIN HOMOLOG 1; COMPND 10 CHAIN: C, D; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: GDF5, BMP14, CDMP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: TWSG1, TSG, PSEC0250; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 19 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3216; SOURCE 20 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PHR-CMV-TETO2-3C-MVENUS-HIS12 KEYWDS TWISTED GASTRULATION PROTEIN HOMOLOG 1 (TWSG1), GROWTH KEYWDS 2 DIFFERENTIATION FACTOR 5 (GDF5), TRANSFORMING GROWTH FACTOR BETA KEYWDS 3 (TGF-BETA) SIGNALLING PATHWAY, EXTRACELLULAR PROTEIN., SIGNALING KEYWDS 4 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.MALINAUSKAS,A.F.RUDOLF,G.MOORE,H.EGGINGTON,H.BELNOUE-DAVIS,K.EL AUTHOR 2 OMARI,R.E.WOOLLEY,S.C.GRIFFITHS,R.DUMAN,A.WAGNER,S.J.LEEDHAM, AUTHOR 3 C.BALDOCK,H.ASHE,C.SIEBOLD REVDAT 2 20-NOV-24 8BWL 1 REMARK REVDAT 1 19-JUN-24 8BWL 0 JRNL AUTH T.MALINAUSKAS,G.MOORE,A.F.RUDOLF,H.EGGINGTON, JRNL AUTH 2 H.L.BELNOUE-DAVIS,K.EL OMARI,S.C.GRIFFITHS,R.E.WOOLLEY, JRNL AUTH 3 R.DUMAN,A.WAGNER,S.J.LEEDHAM,C.BALDOCK,H.L.ASHE,C.SIEBOLD JRNL TITL MOLECULAR MECHANISM OF BMP SIGNAL CONTROL BY TWISTED JRNL TITL 2 GASTRULATION. JRNL REF NAT COMMUN V. 15 4976 2024 JRNL REFN ESSN 2041-1723 JRNL PMID 38862520 JRNL DOI 10.1038/S41467-024-49065-8 REMARK 2 REMARK 2 RESOLUTION. 1.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.25 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.2 REMARK 3 NUMBER OF REFLECTIONS : 30651 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.670 REMARK 3 FREE R VALUE TEST SET COUNT : 1431 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.2500 - 4.2200 1.00 3660 191 0.1795 0.1873 REMARK 3 2 4.2100 - 3.3500 1.00 3504 188 0.1620 0.2064 REMARK 3 3 3.3500 - 2.9200 1.00 3490 171 0.1816 0.2247 REMARK 3 4 2.9200 - 2.6600 1.00 3474 167 0.2160 0.2707 REMARK 3 5 2.6600 - 2.4700 1.00 3417 181 0.1840 0.1936 REMARK 3 6 2.4700 - 2.3200 1.00 3450 171 0.1897 0.2543 REMARK 3 7 2.3200 - 2.2000 1.00 3429 165 0.2291 0.2842 REMARK 3 8 2.2000 - 2.1100 0.90 3080 134 0.2449 0.2853 REMARK 3 9 2.1100 - 2.0300 0.43 1497 55 0.2565 0.2876 REMARK 3 10 2.0300 - 1.9600 0.06 219 8 0.2451 0.3920 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.675 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 50.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.55 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.016 2443 REMARK 3 ANGLE : 1.550 3309 REMARK 3 CHIRALITY : 0.070 370 REMARK 3 PLANARITY : 0.013 429 REMARK 3 DIHEDRAL : 12.882 915 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 397 THROUGH 501) REMARK 3 ORIGIN FOR THE GROUP (A): -14.4706 17.4401 -13.6119 REMARK 3 T TENSOR REMARK 3 T11: 0.4325 T22: 0.3172 REMARK 3 T33: 0.4128 T12: -0.0559 REMARK 3 T13: 0.0425 T23: -0.0197 REMARK 3 L TENSOR REMARK 3 L11: 3.9147 L22: 0.7747 REMARK 3 L33: 7.0611 L12: 0.3932 REMARK 3 L13: 4.6429 L23: 0.7867 REMARK 3 S TENSOR REMARK 3 S11: -0.2601 S12: -0.1418 S13: 0.1106 REMARK 3 S21: -0.1685 S22: 0.0169 S23: 0.0667 REMARK 3 S31: -0.1452 S32: -0.2049 S33: 0.2921 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 398 THROUGH 501) REMARK 3 ORIGIN FOR THE GROUP (A): -0.8093 10.8219 -6.1023 REMARK 3 T TENSOR REMARK 3 T11: 0.4382 T22: 0.3412 REMARK 3 T33: 0.3923 T12: 0.0116 REMARK 3 T13: 0.1352 T23: -0.0181 REMARK 3 L TENSOR REMARK 3 L11: 2.8081 L22: 3.4701 REMARK 3 L33: 7.1043 L12: -1.4175 REMARK 3 L13: 3.7798 L23: -3.7459 REMARK 3 S TENSOR REMARK 3 S11: 0.0035 S12: 0.4010 S13: 0.0771 REMARK 3 S21: -0.1755 S22: -0.1912 S23: -0.1546 REMARK 3 S31: 0.2285 S32: 0.3585 S33: 0.2088 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 25 THROUGH 77) REMARK 3 ORIGIN FOR THE GROUP (A): -6.0755 12.7919 -35.0310 REMARK 3 T TENSOR REMARK 3 T11: 1.0263 T22: 1.1830 REMARK 3 T33: 0.9049 T12: -0.0948 REMARK 3 T13: 0.1301 T23: -0.2523 REMARK 3 L TENSOR REMARK 3 L11: 2.3553 L22: 4.1529 REMARK 3 L33: 6.5714 L12: -1.8346 REMARK 3 L13: -2.3765 L23: 2.4397 REMARK 3 S TENSOR REMARK 3 S11: -0.0886 S12: 1.3985 S13: -0.9487 REMARK 3 S21: -1.3946 S22: 0.1586 S23: -1.0675 REMARK 3 S31: -0.2682 S32: 1.1383 S33: -0.0099 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 25 THROUGH 78) REMARK 3 ORIGIN FOR THE GROUP (A): -10.5940 13.2997 14.6395 REMARK 3 T TENSOR REMARK 3 T11: 0.7264 T22: 0.8403 REMARK 3 T33: 0.7970 T12: 0.0220 REMARK 3 T13: 0.2011 T23: 0.1795 REMARK 3 L TENSOR REMARK 3 L11: 8.8311 L22: 2.3949 REMARK 3 L33: 4.9231 L12: 1.1032 REMARK 3 L13: -1.6194 L23: 0.8858 REMARK 3 S TENSOR REMARK 3 S11: 0.0400 S12: -1.0327 S13: -0.2224 REMARK 3 S21: 1.0959 S22: 0.0945 S23: 1.2514 REMARK 3 S31: 0.3070 S32: -1.3044 S33: -0.1006 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8BWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-22. REMARK 100 THE DEPOSITION ID IS D_1292127227. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JAN-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5-8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30654 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.957 REMARK 200 RESOLUTION RANGE LOW (A) : 49.254 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.2 REMARK 200 DATA REDUNDANCY : 13.10 REMARK 200 R MERGE (I) : 0.06400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 22.5 REMARK 200 DATA REDUNDANCY IN SHELL : 13.70 REMARK 200 R MERGE FOR SHELL (I) : 1.93600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12.1% W/V PEG 1000, 12.1% W/V PEG REMARK 280 3350, 12.1% V/V MPD, 97 MM CACL2, 0.097 M BICINE/TRIZMA PH 8.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.52350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.81100 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.29400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.81100 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.52350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.29400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 381 REMARK 465 ALA A 382 REMARK 465 PRO A 383 REMARK 465 LEU A 384 REMARK 465 ALA A 385 REMARK 465 THR A 386 REMARK 465 ARG A 387 REMARK 465 GLN A 388 REMARK 465 GLY A 389 REMARK 465 LYS A 390 REMARK 465 ARG A 391 REMARK 465 PRO A 392 REMARK 465 SER A 393 REMARK 465 LYS A 394 REMARK 465 ASN A 395 REMARK 465 LEU A 396 REMARK 465 MET B 381 REMARK 465 ALA B 382 REMARK 465 PRO B 383 REMARK 465 LEU B 384 REMARK 465 ALA B 385 REMARK 465 THR B 386 REMARK 465 ARG B 387 REMARK 465 GLN B 388 REMARK 465 GLY B 389 REMARK 465 LYS B 390 REMARK 465 ARG B 391 REMARK 465 PRO B 392 REMARK 465 SER B 393 REMARK 465 LYS B 394 REMARK 465 ASN B 395 REMARK 465 LEU B 396 REMARK 465 LYS B 397 REMARK 465 GLU C 23 REMARK 465 THR C 24 REMARK 465 GLU C 50 REMARK 465 GLY C 51 REMARK 465 ASN C 52 REMARK 465 ASN C 78 REMARK 465 PRO C 79 REMARK 465 ARG C 80 REMARK 465 ASN C 81 REMARK 465 TYR C 82 REMARK 465 SER C 83 REMARK 465 GLY C 84 REMARK 465 THR C 85 REMARK 465 LEU C 86 REMARK 465 GLU C 87 REMARK 465 VAL C 88 REMARK 465 LEU C 89 REMARK 465 PHE C 90 REMARK 465 GLN C 91 REMARK 465 GLU D 23 REMARK 465 THR D 24 REMARK 465 GLY D 49 REMARK 465 GLU D 50 REMARK 465 GLY D 51 REMARK 465 ASN D 52 REMARK 465 PRO D 79 REMARK 465 ARG D 80 REMARK 465 ASN D 81 REMARK 465 TYR D 82 REMARK 465 SER D 83 REMARK 465 GLY D 84 REMARK 465 THR D 85 REMARK 465 LEU D 86 REMARK 465 GLU D 87 REMARK 465 VAL D 88 REMARK 465 LEU D 89 REMARK 465 PHE D 90 REMARK 465 GLN D 91 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HD1 HIS B 406 OE2 GLU B 425 1.52 REMARK 500 OD2 ASP B 411 O HOH B 701 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP B 480 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 CYS A 400 122.67 -27.64 REMARK 500 TRP A 417 -23.35 -141.07 REMARK 500 PHE A 427 165.23 76.67 REMARK 500 CYS B 400 119.81 -38.27 REMARK 500 PHE B 427 172.32 62.81 REMARK 500 GLU B 442 53.04 36.44 REMARK 500 ASP B 457 82.72 -153.03 REMARK 500 PRO C 48 46.63 -82.88 REMARK 500 SER C 54 -68.36 -104.33 REMARK 500 CYS D 55 4.65 -69.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 601 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY A 413 O REMARK 620 2 ASP A 416 OD1 76.1 REMARK 620 3 ASP A 416 OD2 125.1 49.1 REMARK 620 4 HOH A 702 O 171.9 104.4 55.4 REMARK 620 5 HOH A 758 O 82.5 97.8 99.0 89.4 REMARK 620 6 HOH A 765 O 107.0 160.6 123.2 69.9 64.2 REMARK 620 7 HOH C 201 O 140.3 97.6 63.4 47.8 137.0 91.8 REMARK 620 8 HOH C 203 O 80.7 125.5 131.2 105.0 127.1 73.6 71.4 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 601 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY B 413 O REMARK 620 2 ASP B 416 OD1 71.2 REMARK 620 3 ASP B 416 OD2 116.8 47.7 REMARK 620 4 HOH B 740 O 72.8 89.1 89.8 REMARK 620 5 HOH B 747 O 145.2 125.7 79.6 77.1 REMARK 620 6 HOH B 754 O 90.6 159.8 152.1 93.8 74.3 REMARK 620 7 HOH D 209 O 152.7 121.0 83.9 127.8 50.8 72.0 REMARK 620 8 HOH D 210 O 77.5 76.5 99.2 149.9 132.7 91.4 81.9 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 101 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA C 65 O REMARK 620 2 GLU C 69 OE2 95.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 101 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA D 65 O REMARK 620 2 GLU D 69 OE1 62.9 REMARK 620 3 GLU D 69 OE2 93.9 43.6 REMARK 620 4 HOH D 208 O 64.7 62.4 102.8 REMARK 620 5 HOH D 214 O 83.7 105.4 79.6 148.4 REMARK 620 N 1 2 3 4 DBREF 8BWL A 382 501 UNP P43026 GDF5_HUMAN 382 501 DBREF 8BWL B 382 501 UNP P43026 GDF5_HUMAN 382 501 DBREF 8BWL C 26 83 UNP Q9GZX9 TWSG1_HUMAN 26 83 DBREF 8BWL D 26 83 UNP Q9GZX9 TWSG1_HUMAN 26 83 SEQADV 8BWL MET A 381 UNP P43026 INITIATING METHIONINE SEQADV 8BWL MET B 381 UNP P43026 INITIATING METHIONINE SEQADV 8BWL GLU C 23 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL THR C 24 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLY C 25 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLY C 84 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL THR C 85 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL LEU C 86 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLU C 87 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL VAL C 88 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL LEU C 89 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL PHE C 90 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLN C 91 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLU D 23 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL THR D 24 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLY D 25 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLY D 84 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL THR D 85 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL LEU D 86 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLU D 87 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL VAL D 88 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL LEU D 89 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL PHE D 90 UNP Q9GZX9 EXPRESSION TAG SEQADV 8BWL GLN D 91 UNP Q9GZX9 EXPRESSION TAG SEQRES 1 A 121 MET ALA PRO LEU ALA THR ARG GLN GLY LYS ARG PRO SER SEQRES 2 A 121 LYS ASN LEU LYS ALA ARG CYS SER ARG LYS ALA LEU HIS SEQRES 3 A 121 VAL ASN PHE LYS ASP MET GLY TRP ASP ASP TRP ILE ILE SEQRES 4 A 121 ALA PRO LEU GLU TYR GLU ALA PHE HIS CYS GLU GLY LEU SEQRES 5 A 121 CYS GLU PHE PRO LEU ARG SER HIS LEU GLU PRO THR ASN SEQRES 6 A 121 HIS ALA VAL ILE GLN THR LEU MET ASN SER MET ASP PRO SEQRES 7 A 121 GLU SER THR PRO PRO THR CYS CYS VAL PRO THR ARG LEU SEQRES 8 A 121 SER PRO ILE SER ILE LEU PHE ILE ASP SER ALA ASN ASN SEQRES 9 A 121 VAL VAL TYR LYS GLN TYR GLU ASP MET VAL VAL GLU SER SEQRES 10 A 121 CYS GLY CYS ARG SEQRES 1 B 121 MET ALA PRO LEU ALA THR ARG GLN GLY LYS ARG PRO SER SEQRES 2 B 121 LYS ASN LEU LYS ALA ARG CYS SER ARG LYS ALA LEU HIS SEQRES 3 B 121 VAL ASN PHE LYS ASP MET GLY TRP ASP ASP TRP ILE ILE SEQRES 4 B 121 ALA PRO LEU GLU TYR GLU ALA PHE HIS CYS GLU GLY LEU SEQRES 5 B 121 CYS GLU PHE PRO LEU ARG SER HIS LEU GLU PRO THR ASN SEQRES 6 B 121 HIS ALA VAL ILE GLN THR LEU MET ASN SER MET ASP PRO SEQRES 7 B 121 GLU SER THR PRO PRO THR CYS CYS VAL PRO THR ARG LEU SEQRES 8 B 121 SER PRO ILE SER ILE LEU PHE ILE ASP SER ALA ASN ASN SEQRES 9 B 121 VAL VAL TYR LYS GLN TYR GLU ASP MET VAL VAL GLU SER SEQRES 10 B 121 CYS GLY CYS ARG SEQRES 1 C 69 GLU THR GLY CYS ASN LYS ALA LEU CYS ALA SER ASP VAL SEQRES 2 C 69 SER LYS CYS LEU ILE GLN GLU LEU CYS GLN CYS ARG PRO SEQRES 3 C 69 GLY GLU GLY ASN CYS SER CYS CYS LYS GLU CYS MET LEU SEQRES 4 C 69 CYS LEU GLY ALA LEU TRP ASP GLU CYS CYS ASP CYS VAL SEQRES 5 C 69 GLY MET CYS ASN PRO ARG ASN TYR SER GLY THR LEU GLU SEQRES 6 C 69 VAL LEU PHE GLN SEQRES 1 D 69 GLU THR GLY CYS ASN LYS ALA LEU CYS ALA SER ASP VAL SEQRES 2 D 69 SER LYS CYS LEU ILE GLN GLU LEU CYS GLN CYS ARG PRO SEQRES 3 D 69 GLY GLU GLY ASN CYS SER CYS CYS LYS GLU CYS MET LEU SEQRES 4 D 69 CYS LEU GLY ALA LEU TRP ASP GLU CYS CYS ASP CYS VAL SEQRES 5 D 69 GLY MET CYS ASN PRO ARG ASN TYR SER GLY THR LEU GLU SEQRES 6 D 69 VAL LEU PHE GLN HET CA A 601 1 HET CA B 601 1 HET CA C 101 1 HET CA D 101 1 HETNAM CA CALCIUM ION FORMUL 5 CA 4(CA 2+) FORMUL 9 HOH *150(H2 O) HELIX 1 AA1 ARG A 438 GLU A 442 5 5 HELIX 2 AA2 THR A 444 ASP A 457 1 14 HELIX 3 AA3 LYS B 410 GLY B 413 5 4 HELIX 4 AA4 ARG B 438 GLU B 442 5 5 HELIX 5 AA5 THR B 444 ASP B 457 1 14 HELIX 6 AA6 ASN C 27 GLN C 41 1 15 HELIX 7 AA7 CYS C 55 GLY C 64 1 10 HELIX 8 AA8 LEU C 66 CYS C 71 1 6 HELIX 9 AA9 ASP C 72 GLY C 75 5 4 HELIX 10 AB1 ASN D 27 GLN D 41 1 15 HELIX 11 AB2 CYS D 55 GLY D 64 1 10 HELIX 12 AB3 LEU D 66 CYS D 71 1 6 HELIX 13 AB4 ASP D 72 VAL D 74 5 3 SHEET 1 AA1 2 SER A 401 LYS A 403 0 SHEET 2 AA1 2 HIS A 428 GLU A 430 -1 O HIS A 428 N LYS A 403 SHEET 1 AA2 2 HIS A 406 ASN A 408 0 SHEET 2 AA2 2 GLU A 423 GLU A 425 -1 O TYR A 424 N VAL A 407 SHEET 1 AA3 3 ILE A 418 ALA A 420 0 SHEET 2 AA3 3 CYS A 466 ILE A 479 -1 O LEU A 477 N ALA A 420 SHEET 3 AA3 3 VAL A 485 CYS A 500 -1 O TYR A 490 N ILE A 474 SHEET 1 AA4 2 SER B 401 LYS B 403 0 SHEET 2 AA4 2 HIS B 428 GLU B 430 -1 O HIS B 428 N LYS B 403 SHEET 1 AA5 2 HIS B 406 ASN B 408 0 SHEET 2 AA5 2 GLU B 423 GLU B 425 -1 O TYR B 424 N VAL B 407 SHEET 1 AA6 3 ILE B 418 ALA B 420 0 SHEET 2 AA6 3 CYS B 466 ILE B 479 -1 O LEU B 477 N ALA B 420 SHEET 3 AA6 3 VAL B 485 CYS B 500 -1 O VAL B 486 N PHE B 478 SSBOND 1 CYS A 400 CYS A 466 1555 1555 2.09 SSBOND 2 CYS A 429 CYS A 498 1555 1555 2.06 SSBOND 3 CYS A 433 CYS A 500 1555 1555 2.05 SSBOND 4 CYS A 465 CYS B 465 1555 1555 2.04 SSBOND 5 CYS B 400 CYS B 466 1555 1555 2.10 SSBOND 6 CYS B 429 CYS B 498 1555 1555 2.04 SSBOND 7 CYS B 433 CYS B 500 1555 1555 2.06 SSBOND 8 CYS C 26 CYS C 73 1555 1555 2.05 SSBOND 9 CYS C 31 CYS C 70 1555 1555 2.03 SSBOND 10 CYS C 38 CYS C 62 1555 1555 2.05 SSBOND 11 CYS C 44 CYS C 59 1555 1555 2.04 SSBOND 12 CYS C 46 CYS C 55 1555 1555 2.04 SSBOND 13 CYS C 53 CYS C 56 1555 1555 2.03 SSBOND 14 CYS C 71 CYS C 77 1555 1555 2.05 SSBOND 15 CYS D 26 CYS D 73 1555 1555 2.05 SSBOND 16 CYS D 31 CYS D 70 1555 1555 2.04 SSBOND 17 CYS D 38 CYS D 62 1555 1555 2.08 SSBOND 18 CYS D 44 CYS D 59 1555 1555 2.06 SSBOND 19 CYS D 46 CYS D 55 1555 1555 2.05 SSBOND 20 CYS D 53 CYS D 56 1555 1555 2.04 SSBOND 21 CYS D 71 CYS D 77 1555 1555 2.06 LINK O GLY A 413 CA CA A 601 1555 1555 2.34 LINK OD1 ASP A 416 CA CA A 601 1555 1555 2.76 LINK OD2 ASP A 416 CA CA A 601 1555 1555 2.43 LINK CA CA A 601 O HOH A 702 1555 1555 2.74 LINK CA CA A 601 O HOH A 758 1555 1555 2.45 LINK CA CA A 601 O HOH A 765 1555 1555 2.29 LINK CA CA A 601 O HOH C 201 1555 1555 2.90 LINK CA CA A 601 O HOH C 203 1555 1555 2.39 LINK O GLY B 413 CA CA B 601 1555 1555 2.38 LINK OD1 ASP B 416 CA CA B 601 1555 1555 2.90 LINK OD2 ASP B 416 CA CA B 601 1555 1555 2.19 LINK CA CA B 601 O HOH B 740 1555 1555 2.56 LINK CA CA B 601 O HOH B 747 1555 1555 2.70 LINK CA CA B 601 O HOH B 754 1555 1555 2.30 LINK CA CA B 601 O HOH D 209 1555 1555 2.73 LINK CA CA B 601 O HOH D 210 1555 1555 2.43 LINK O ALA C 65 CA CA C 101 1555 1555 2.69 LINK OE2 GLU C 69 CA CA C 101 1555 1555 2.97 LINK O ALA D 65 CA CA D 101 1555 1555 2.84 LINK OE1 GLU D 69 CA CA D 101 1555 1555 3.14 LINK OE2 GLU D 69 CA CA D 101 1555 1555 2.47 LINK CA CA D 101 O HOH D 208 1555 1555 2.16 LINK CA CA D 101 O HOH D 214 1555 1555 2.53 CISPEP 1 ALA A 420 PRO A 421 0 -12.79 CISPEP 2 PHE A 435 PRO A 436 0 -0.65 CISPEP 3 ALA B 420 PRO B 421 0 -3.22 CISPEP 4 PHE B 435 PRO B 436 0 -2.21 CRYST1 57.047 88.588 97.622 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017529 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011288 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010244 0.00000 ATOM 1 N LYS A 397 -10.455 32.845 -1.678 1.00108.29 N ANISOU 1 N LYS A 397 15853 11054 14239 1680 -3772 -1948 N ATOM 2 CA LYS A 397 -10.179 31.575 -2.420 1.00 96.04 C ANISOU 2 CA LYS A 397 14041 9772 12677 1276 -3165 -1608 C ATOM 3 C LYS A 397 -10.785 30.365 -1.697 1.00 77.56 C ANISOU 3 C LYS A 397 11239 8010 10221 1474 -2631 -1744 C ATOM 4 O LYS A 397 -10.282 29.903 -0.692 1.00 80.37 O ANISOU 4 O LYS A 397 11410 8598 10530 1489 -2403 -1748 O ATOM 5 CB LYS A 397 -8.671 31.353 -2.608 1.00101.52 C ANISOU 5 CB LYS A 397 14794 10359 13420 761 -3010 -1213 C ATOM 6 CG LYS A 397 -8.343 30.451 -3.781 1.00 96.23 C ANISOU 6 CG LYS A 397 14003 9817 12745 349 -2615 -882 C ATOM 7 CD LYS A 397 -6.843 30.194 -3.882 1.00103.61 C ANISOU 7 CD LYS A 397 14915 10777 13675 -99 -2452 -553 C ATOM 8 CE LYS A 397 -6.519 29.321 -5.100 1.00121.31 C ANISOU 8 CE LYS A 397 17016 13201 15875 -451 -2094 -281 C ATOM 9 NZ LYS A 397 -7.278 28.011 -5.182 1.00 91.48 N ANISOU 9 NZ LYS A 397 12938 9749 12070 -271 -1628 -376 N ATOM 10 H LYS A 397 -9.773 33.025 -1.135 1.00129.97 H ATOM 11 HA LYS A 397 -10.585 31.649 -3.298 1.00115.27 H ATOM 12 HB2 LYS A 397 -8.243 32.210 -2.762 1.00121.85 H ATOM 13 HB3 LYS A 397 -8.311 30.942 -1.806 1.00121.85 H ATOM 14 HG2 LYS A 397 -8.792 29.599 -3.668 1.00115.51 H ATOM 15 HG3 LYS A 397 -8.636 30.874 -4.604 1.00115.51 H ATOM 16 HD2 LYS A 397 -6.375 31.038 -3.975 1.00124.36 H ATOM 17 HD3 LYS A 397 -6.539 29.733 -3.084 1.00124.36 H ATOM 18 HE2 LYS A 397 -6.726 29.825 -5.902 1.00145.59 H ATOM 19 HE3 LYS A 397 -5.573 29.105 -5.078 1.00145.59 H ATOM 20 HZ1 LYS A 397 -7.172 27.549 -4.429 1.00109.80 H ATOM 21 HZ2 LYS A 397 -8.146 28.169 -5.303 1.00109.80 H ATOM 22 HZ3 LYS A 397 -6.975 27.526 -5.864 1.00109.80 H ATOM 23 N ALA A 398 -11.833 29.804 -2.274 1.00 70.23 N ANISOU 23 N ALA A 398 10136 7312 9237 1563 -2438 -1808 N ATOM 24 CA ALA A 398 -12.577 28.732 -1.642 1.00 68.27 C ANISOU 24 CA ALA A 398 9473 7620 8845 1709 -2016 -1923 C ATOM 25 C ALA A 398 -11.767 27.430 -1.631 1.00 58.87 C ANISOU 25 C ALA A 398 8108 6594 7664 1326 -1513 -1592 C ATOM 26 O ALA A 398 -10.861 27.242 -2.432 1.00 58.31 O ANISOU 26 O ALA A 398 8182 6278 7696 976 -1438 -1302 O ATOM 27 CB ALA A 398 -13.891 28.551 -2.409 1.00 70.85 C ANISOU 27 CB ALA A 398 9694 8115 9112 1852 -2000 -2051 C ATOM 28 H ALA A 398 -12.139 30.029 -3.045 1.00 84.30 H ATOM 29 HA ALA A 398 -12.770 28.943 -0.715 1.00 81.94 H ATOM 30 HB1 ALA A 398 -14.405 27.843 -1.991 1.00 85.05 H ATOM 31 HB2 ALA A 398 -14.389 29.383 -2.382 1.00 85.05 H ATOM 32 HB3 ALA A 398 -13.690 28.316 -3.328 1.00 85.05 H ATOM 33 N ARG A 399 -12.125 26.518 -0.716 1.00 50.53 N ANISOU 33 N ARG A 399 6734 5992 6472 1400 -1199 -1649 N ATOM 34 CA ARG A 399 -11.704 25.130 -0.754 1.00 61.61 C ANISOU 34 CA ARG A 399 7976 7570 7863 1095 -770 -1380 C ATOM 35 C ARG A 399 -12.312 24.418 -1.950 1.00 48.85 C ANISOU 35 C ARG A 399 6332 5966 6264 924 -603 -1247 C ATOM 36 O ARG A 399 -13.385 24.773 -2.429 1.00 43.26 O ANISOU 36 O ARG A 399 5600 5323 5513 1084 -729 -1405 O ATOM 37 CB ARG A 399 -12.139 24.417 0.503 1.00 63.11 C ANISOU 37 CB ARG A 399 7868 8240 7872 1196 -564 -1467 C ATOM 38 CG ARG A 399 -11.408 24.930 1.683 1.00 74.71 C ANISOU 38 CG ARG A 399 9352 9714 9320 1329 -676 -1564 C ATOM 39 CD ARG A 399 -11.221 23.769 2.677 1.00 95.07 C ANISOU 39 CD ARG A 399 11698 12656 11767 1197 -365 -1440 C ATOM 40 NE ARG A 399 -12.486 23.199 3.145 1.00109.61 N ANISOU 40 NE ARG A 399 13234 15041 13371 1269 -232 -1543 N ATOM 41 CZ ARG A 399 -12.623 22.073 3.842 1.00101.38 C ANISOU 41 CZ ARG A 399 11989 14361 12171 1075 13 -1388 C ATOM 42 NH1 ARG A 399 -11.596 21.262 4.071 1.00 87.96 N ANISOU 42 NH1 ARG A 399 10383 12486 10552 826 160 -1128 N ATOM 43 NH2 ARG A 399 -13.826 21.748 4.318 1.00 98.02 N ANISOU 43 NH2 ARG A 399 11258 14510 11476 1120 84 -1493 N ATOM 44 H ARG A 399 -12.631 26.693 -0.042 1.00 60.66 H ATOM 45 HA ARG A 399 -10.737 25.096 -0.823 1.00 73.96 H ATOM 46 HB2 ARG A 399 -13.088 24.559 0.643 1.00 75.76 H ATOM 47 HB3 ARG A 399 -11.955 23.468 0.416 1.00 75.76 H ATOM 48 HG2 ARG A 399 -10.537 25.264 1.416 1.00 89.67 H ATOM 49 HG3 ARG A 399 -11.918 25.636 2.110 1.00 89.67 H ATOM 50 HD2 ARG A 399 -10.719 23.062 2.243 1.00114.10 H ATOM 51 HD3 ARG A 399 -10.737 24.094 3.451 1.00114.10 H ATOM 52 HE ARG A 399 -13.205 23.631 2.953 1.00131.56 H ATOM 53 HH11 ARG A 399 -10.817 21.459 3.767 1.00105.58 H ATOM 54 HH12 ARG A 399 -11.711 20.540 4.524 1.00105.58 H ATOM 55 HH21 ARG A 399 -14.499 22.264 4.174 1.00117.65 H ATOM 56 HH22 ARG A 399 -13.929 21.023 4.770 1.00117.65 H ATOM 57 N CYS A 400 -11.613 23.415 -2.413 1.00 43.29 N ANISOU 57 N CYS A 400 5630 5205 5614 629 -345 -985 N ATOM 58 CA CYS A 400 -12.090 22.526 -3.457 1.00 43.78 C ANISOU 58 CA CYS A 400 5659 5293 5684 458 -166 -854 C ATOM 59 C CYS A 400 -13.608 22.407 -3.504 1.00 51.05 C ANISOU 59 C CYS A 400 6413 6498 6486 602 -167 -1010 C ATOM 60 O CYS A 400 -14.212 22.027 -2.507 1.00 46.49 O ANISOU 60 O CYS A 400 5611 6300 5754 689 -82 -1102 O ATOM 61 CB CYS A 400 -11.489 21.182 -3.205 1.00 41.99 C ANISOU 61 CB CYS A 400 5352 5157 5443 258 107 -663 C ATOM 62 SG CYS A 400 -11.872 19.920 -4.457 1.00 46.64 S ANISOU 62 SG CYS A 400 5946 5724 6050 45 290 -499 S ATOM 63 H CYS A 400 -10.826 23.212 -2.132 1.00 51.97 H ATOM 64 HA CYS A 400 -11.826 22.881 -4.321 1.00 52.56 H ATOM 65 HB2 CYS A 400 -10.524 21.278 -3.175 1.00 50.41 H ATOM 66 HB3 CYS A 400 -11.817 20.855 -2.353 1.00 50.41 H ATOM 67 N SER A 401 -14.211 22.719 -4.640 1.00 42.25 N ANISOU 67 N SER A 401 5387 5252 5415 606 -266 -1033 N ATOM 68 CA SER A 401 -15.659 22.785 -4.713 1.00 41.75 C ANISOU 68 CA SER A 401 5154 5480 5230 781 -313 -1221 C ATOM 69 C SER A 401 -16.071 22.598 -6.162 1.00 47.42 C ANISOU 69 C SER A 401 5979 6021 6019 652 -310 -1127 C ATOM 70 O SER A 401 -15.271 22.792 -7.087 1.00 43.58 O ANISOU 70 O SER A 401 5718 5178 5663 490 -354 -972 O ATOM 71 CB SER A 401 -16.118 24.105 -4.093 1.00 50.28 C ANISOU 71 CB SER A 401 6237 6612 6255 1168 -640 -1548 C ATOM 72 OG SER A 401 -15.680 25.223 -4.855 1.00 59.84 O ANISOU 72 OG SER A 401 7772 7348 7616 1222 -965 -1568 O ATOM 73 H SER A 401 -13.805 22.896 -5.378 1.00 50.73 H ATOM 74 HA SER A 401 -16.097 22.065 -4.232 1.00 50.12 H ATOM 75 HB2 SER A 401 -17.088 24.113 -4.056 1.00 60.36 H ATOM 76 HB3 SER A 401 -15.752 24.174 -3.197 1.00 60.36 H ATOM 77 HG SER A 401 -16.060 25.922 -4.585 1.00 71.83 H ATOM 78 N ARG A 402 -17.310 22.137 -6.363 1.00 39.39 N ANISOU 78 N ARG A 402 4768 5312 4885 687 -241 -1204 N ATOM 79 CA ARG A 402 -17.852 22.031 -7.693 1.00 42.16 C ANISOU 79 CA ARG A 402 5204 5525 5289 605 -264 -1153 C ATOM 80 C ARG A 402 -18.425 23.395 -8.044 1.00 42.72 C ANISOU 80 C ARG A 402 5386 5469 5376 908 -616 -1400 C ATOM 81 O ARG A 402 -19.198 23.958 -7.272 1.00 41.92 O ANISOU 81 O ARG A 402 5120 5658 5150 1227 -767 -1685 O ATOM 82 CB ARG A 402 -18.967 20.977 -7.778 1.00 47.48 C ANISOU 82 CB ARG A 402 5632 6585 5825 493 -78 -1125 C ATOM 83 CG ARG A 402 -19.300 20.594 -9.222 1.00 42.59 C ANISOU 83 CG ARG A 402 5128 5774 5280 338 -54 -1012 C ATOM 84 CD ARG A 402 -20.474 19.656 -9.434 1.00 41.91 C ANISOU 84 CD ARG A 402 4828 6034 5062 210 72 -984 C ATOM 85 NE ARG A 402 -21.755 20.143 -8.956 1.00 42.56 N ANISOU 85 NE ARG A 402 4633 6579 4959 441 -28 -1237 N ATOM 86 CZ ARG A 402 -22.901 19.606 -9.321 1.00 48.73 C ANISOU 86 CZ ARG A 402 5214 7691 5608 354 23 -1249 C ATOM 87 NH1 ARG A 402 -22.948 18.660 -10.245 1.00 50.35 N ANISOU 87 NH1 ARG A 402 5523 7728 5880 60 134 -1028 N ATOM 88 NH2 ARG A 402 -24.025 20.012 -8.747 1.00 48.88 N ANISOU 88 NH2 ARG A 402 4909 8257 5404 576 -53 -1503 N ATOM 89 H ARG A 402 -17.845 21.884 -5.739 1.00 47.29 H ATOM 90 HA ARG A 402 -17.162 21.759 -8.319 1.00 50.61 H ATOM 91 HB2 ARG A 402 -18.683 20.175 -7.312 1.00 57.01 H ATOM 92 HB3 ARG A 402 -19.771 21.332 -7.368 1.00 57.01 H ATOM 93 HG2 ARG A 402 -19.500 21.408 -9.709 1.00 51.13 H ATOM 94 HG3 ARG A 402 -18.521 20.161 -9.605 1.00 51.13 H ATOM 95 HD2 ARG A 402 -20.565 19.490 -10.385 1.00 50.32 H ATOM 96 HD3 ARG A 402 -20.289 18.825 -8.969 1.00 50.32 H ATOM 97 HE ARG A 402 -21.766 20.810 -8.413 1.00 51.10 H ATOM 98 HH11 ARG A 402 -22.222 18.388 -10.618 1.00 60.45 H ATOM 99 HH12 ARG A 402 -23.703 18.319 -10.473 1.00 60.45 H ATOM 100 HH21 ARG A 402 -24.002 20.623 -8.142 1.00 58.67 H ATOM 101 HH22 ARG A 402 -24.776 19.666 -8.980 1.00 58.67 H ATOM 102 N LYS A 403 -18.209 23.831 -9.297 1.00 41.79 N ANISOU 102 N LYS A 403 5526 4973 5380 816 -760 -1305 N ATOM 103 CA LYS A 403 -18.553 25.187 -9.716 1.00 41.24 C ANISOU 103 CA LYS A 403 5671 4646 5353 1060 -1181 -1491 C ATOM 104 C LYS A 403 -19.163 25.140 -11.109 1.00 41.21 C ANISOU 104 C LYS A 403 5766 4512 5380 970 -1235 -1428 C ATOM 105 O LYS A 403 -19.051 24.158 -11.827 1.00 41.11 O ANISOU 105 O LYS A 403 5706 4533 5381 691 -957 -1216 O ATOM 106 CB LYS A 403 -17.314 26.087 -9.755 1.00 42.19 C ANISOU 106 CB LYS A 403 6115 4322 5593 965 -1424 -1375 C ATOM 107 CG LYS A 403 -16.629 26.322 -8.457 1.00 46.61 C ANISOU 107 CG LYS A 403 6633 4935 6140 1064 -1439 -1443 C ATOM 108 CD LYS A 403 -15.466 27.185 -8.572 1.00 52.16 C ANISOU 108 CD LYS A 403 7651 5220 6947 919 -1697 -1306 C ATOM 109 CE LYS A 403 -14.716 27.337 -7.192 1.00 52.52 C ANISOU 109 CE LYS A 403 7639 5335 6981 1009 -1688 -1369 C ATOM 110 NZ LYS A 403 -13.806 28.543 -7.387 1.00 60.70 N ANISOU 110 NZ LYS A 403 9050 5903 8111 904 -2111 -1281 N ATOM 111 H LYS A 403 -17.862 23.351 -9.921 1.00 50.17 H ATOM 112 HA LYS A 403 -19.202 25.549 -9.091 1.00 49.37 H ATOM 113 HB2 LYS A 403 -16.664 25.681 -10.351 1.00 50.65 H ATOM 114 HB3 LYS A 403 -17.581 26.955 -10.098 1.00 50.65 H ATOM 115 HG2 LYS A 403 -17.253 26.742 -7.844 1.00 55.95 H ATOM 116 HG3 LYS A 403 -16.334 25.470 -8.099 1.00 55.95 H ATOM 117 HD2 LYS A 403 -14.847 26.805 -9.214 1.00 62.61 H ATOM 118 HD3 LYS A 403 -15.748 28.066 -8.863 1.00 62.61 H ATOM 119 HE2 LYS A 403 -15.343 27.504 -6.471 1.00 63.05 H ATOM 120 HE3 LYS A 403 -14.187 26.548 -6.995 1.00 63.05 H ATOM 121 HZ1 LYS A 403 -13.324 28.683 -6.651 1.00 72.87 H ATOM 122 HZ2 LYS A 403 -13.254 28.401 -8.071 1.00 72.87 H ATOM 123 HZ3 LYS A 403 -14.294 29.268 -7.555 1.00 72.87 H ATOM 124 N ALA A 404 -19.787 26.246 -11.528 1.00 44.73 N ANISOU 124 N ALA A 404 6384 4773 5840 1226 -1641 -1627 N ATOM 125 CA ALA A 404 -20.488 26.208 -12.809 1.00 48.83 C ANISOU 125 CA ALA A 404 6980 5202 6372 1168 -1706 -1589 C ATOM 126 C ALA A 404 -19.523 26.059 -13.977 1.00 43.72 C ANISOU 126 C ALA A 404 6587 4204 5820 756 -1648 -1240 C ATOM 127 O ALA A 404 -18.444 26.650 -13.965 1.00 46.82 O ANISOU 127 O ALA A 404 7214 4301 6274 598 -1799 -1090 O ATOM 128 CB ALA A 404 -21.258 27.498 -12.979 1.00 53.15 C ANISOU 128 CB ALA A 404 7707 5569 6917 1550 -2227 -1883 C ATOM 129 H ALA A 404 -19.817 26.995 -11.107 1.00 53.71 H ATOM 130 HA ALA A 404 -21.088 25.446 -12.819 1.00 58.62 H ATOM 131 HB1 ALA A 404 -21.723 27.478 -13.830 1.00 63.80 H ATOM 132 HB2 ALA A 404 -21.897 27.583 -12.254 1.00 63.80 H ATOM 133 HB3 ALA A 404 -20.636 28.242 -12.960 1.00 63.80 H ATOM 134 N LEU A 405 -19.936 25.345 -15.016 1.00 44.38 N ANISOU 134 N LEU A 405 6620 4352 5889 582 -1465 -1122 N ATOM 135 CA LEU A 405 -19.171 25.314 -16.274 1.00 47.55 C ANISOU 135 CA LEU A 405 7242 4493 6332 234 -1456 -837 C ATOM 136 C LEU A 405 -20.187 25.010 -17.357 1.00 44.34 C ANISOU 136 C LEU A 405 6810 4139 5897 240 -1450 -864 C ATOM 137 O LEU A 405 -20.570 23.855 -17.523 1.00 47.77 O ANISOU 137 O LEU A 405 7027 4828 6296 161 -1126 -836 O ATOM 138 CB LEU A 405 -18.064 24.270 -16.290 1.00 47.92 C ANISOU 138 CB LEU A 405 7191 4642 6376 -70 -1075 -604 C ATOM 139 CG LEU A 405 -17.288 24.322 -17.614 1.00 51.03 C ANISOU 139 CG LEU A 405 7759 4880 6751 -400 -1085 -352 C ATOM 140 CD1 LEU A 405 -16.497 25.568 -17.663 1.00 53.08 C ANISOU 140 CD1 LEU A 405 8287 4862 7020 -524 -1428 -240 C ATOM 141 CD2 LEU A 405 -16.238 23.316 -17.804 1.00 50.20 C ANISOU 141 CD2 LEU A 405 7540 4926 6609 -635 -752 -183 C ATOM 142 H LEU A 405 -20.653 24.869 -15.025 1.00 53.28 H ATOM 143 HA LEU A 405 -18.752 26.179 -16.403 1.00 57.09 H ATOM 144 HB2 LEU A 405 -17.446 24.444 -15.562 1.00 57.53 H ATOM 145 HB3 LEU A 405 -18.452 23.386 -16.192 1.00 57.53 H ATOM 146 HG LEU A 405 -17.985 24.206 -18.279 1.00 61.27 H ATOM 147 HD11 LEU A 405 -15.886 25.524 -18.415 1.00 63.73 H ATOM 148 HD12 LEU A 405 -17.099 26.321 -17.769 1.00 63.73 H ATOM 149 HD13 LEU A 405 -15.998 25.657 -16.836 1.00 63.73 H ATOM 150 HD21 LEU A 405 -15.924 23.357 -18.721 1.00 60.27 H ATOM 151 HD22 LEU A 405 -15.507 23.505 -17.195 1.00 60.27 H ATOM 152 HD23 LEU A 405 -16.605 22.438 -17.618 1.00 60.27 H ATOM 153 N HIS A 406 -20.618 26.042 -18.087 1.00 50.46 N ANISOU 153 N HIS A 406 7834 4650 6689 323 -1848 -912 N ATOM 154 CA HIS A 406 -21.555 25.877 -19.195 1.00 52.06 C ANISOU 154 CA HIS A 406 8046 4870 6864 329 -1889 -934 C ATOM 155 C HIS A 406 -20.795 25.506 -20.457 1.00 45.25 C ANISOU 155 C HIS A 406 7318 3887 5986 -78 -1760 -621 C ATOM 156 O HIS A 406 -19.880 26.207 -20.870 1.00 53.85 O ANISOU 156 O HIS A 406 8659 4727 7073 -308 -1958 -422 O ATOM 157 CB HIS A 406 -22.339 27.195 -19.422 1.00 52.07 C ANISOU 157 CB HIS A 406 8288 4617 6881 627 -2436 -1140 C ATOM 158 CG HIS A 406 -23.417 27.106 -20.477 1.00 58.78 C ANISOU 158 CG HIS A 406 9137 5498 7700 694 -2520 -1206 C ATOM 159 ND1 HIS A 406 -24.630 26.490 -20.261 1.00 64.54 N ANISOU 159 ND1 HIS A 406 9539 6616 8365 936 -2356 -1442 N ATOM 160 CD2 HIS A 406 -23.443 27.536 -21.763 1.00 65.72 C ANISOU 160 CD2 HIS A 406 10292 6098 8582 515 -2750 -1048 C ATOM 161 CE1 HIS A 406 -25.363 26.550 -21.365 1.00 61.10 C ANISOU 161 CE1 HIS A 406 9181 6120 7914 934 -2481 -1447 C ATOM 162 NE2 HIS A 406 -24.662 27.175 -22.291 1.00 68.76 N ANISOU 162 NE2 HIS A 406 10523 6675 8928 688 -2719 -1211 N ATOM 163 H HIS A 406 -20.379 26.858 -17.956 1.00 60.58 H ATOM 164 HA HIS A 406 -22.185 25.169 -18.991 1.00 62.49 H ATOM 165 HB2 HIS A 406 -22.765 27.449 -18.588 1.00 62.51 H ATOM 166 HB3 HIS A 406 -21.714 27.884 -19.698 1.00 62.51 H ATOM 167 HD1 HIS A 406 -24.874 26.123 -19.523 1.00 77.47 H ATOM 168 HD2 HIS A 406 -22.763 27.990 -22.206 1.00 78.89 H ATOM 169 HE1 HIS A 406 -26.223 26.210 -21.468 1.00 73.34 H ATOM 170 N VAL A 407 -21.201 24.441 -21.109 1.00 46.32 N ANISOU 170 N VAL A 407 7287 4227 6087 -176 -1463 -580 N ATOM 171 CA VAL A 407 -20.593 24.063 -22.368 1.00 46.94 C ANISOU 171 CA VAL A 407 7458 4261 6116 -502 -1352 -341 C ATOM 172 C VAL A 407 -21.517 24.444 -23.510 1.00 47.08 C ANISOU 172 C VAL A 407 7606 4175 6108 -478 -1572 -364 C ATOM 173 O VAL A 407 -22.680 24.023 -23.544 1.00 51.36 O ANISOU 173 O VAL A 407 7996 4863 6654 -281 -1524 -540 O ATOM 174 CB VAL A 407 -20.277 22.566 -22.361 1.00 49.53 C ANISOU 174 CB VAL A 407 7553 4848 6419 -616 -914 -290 C ATOM 175 CG1 VAL A 407 -19.818 22.065 -23.658 1.00 51.72 C ANISOU 175 CG1 VAL A 407 7875 5160 6617 -861 -800 -128 C ATOM 176 CG2 VAL A 407 -19.188 22.252 -21.349 1.00 50.78 C ANISOU 176 CG2 VAL A 407 7628 5073 6594 -664 -739 -239 C ATOM 177 H VAL A 407 -21.831 23.918 -20.844 1.00 55.61 H ATOM 178 HA VAL A 407 -19.773 24.564 -22.503 1.00 56.35 H ATOM 179 HB VAL A 407 -21.110 22.125 -22.133 1.00 59.46 H ATOM 180 HG11 VAL A 407 -19.400 21.199 -23.532 1.00 62.09 H ATOM 181 HG12 VAL A 407 -20.580 21.981 -24.252 1.00 62.09 H ATOM 182 HG13 VAL A 407 -19.177 22.691 -24.029 1.00 62.09 H ATOM 183 HG21 VAL A 407 -19.046 21.293 -21.326 1.00 60.96 H ATOM 184 HG22 VAL A 407 -18.371 22.702 -21.615 1.00 60.96 H ATOM 185 HG23 VAL A 407 -19.469 22.566 -20.475 1.00 60.96 H ATOM 186 N ASN A 408 -20.990 25.183 -24.473 1.00 55.95 N ANISOU 186 N ASN A 408 8993 5085 7182 -717 -1810 -164 N ATOM 187 CA ASN A 408 -21.720 25.534 -25.696 1.00 58.15 C ANISOU 187 CA ASN A 408 9430 5248 7417 -757 -2031 -134 C ATOM 188 C ASN A 408 -20.998 24.875 -26.874 1.00 57.05 C ANISOU 188 C ASN A 408 9268 5257 7153 -1123 -1795 109 C ATOM 189 O ASN A 408 -19.837 25.198 -27.175 1.00 54.72 O ANISOU 189 O ASN A 408 9070 4960 6760 -1440 -1821 345 O ATOM 190 CB ASN A 408 -21.801 27.067 -25.778 1.00 60.72 C ANISOU 190 CB ASN A 408 10124 5184 7764 -720 -2608 -113 C ATOM 191 CG ASN A 408 -22.706 27.544 -26.895 1.00 64.61 C ANISOU 191 CG ASN A 408 10812 5511 8225 -689 -2922 -123 C ATOM 192 OD1 ASN A 408 -22.608 27.056 -27.986 1.00 58.71 O ANISOU 192 OD1 ASN A 408 10048 4873 7387 -943 -2763 44 O ATOM 193 ND2 ASN A 408 -23.565 28.511 -26.626 1.00 82.22 N ANISOU 193 ND2 ASN A 408 13234 7485 10521 -353 -3393 -341 N ATOM 194 H ASN A 408 -20.192 25.503 -24.446 1.00 67.17 H ATOM 195 HA ASN A 408 -22.624 25.184 -25.715 1.00 69.80 H ATOM 196 HB2 ASN A 408 -22.151 27.411 -24.941 1.00 72.89 H ATOM 197 HB3 ASN A 408 -20.913 27.423 -25.938 1.00 72.89 H ATOM 198 HD21 ASN A 408 -23.598 28.848 -25.835 1.00 98.69 H ATOM 199 HD22 ASN A 408 -24.092 28.802 -27.240 1.00 98.69 H ATOM 200 N PHE A 409 -21.645 23.913 -27.522 1.00 56.26 N ANISOU 200 N PHE A 409 9010 5339 7028 -1086 -1564 42 N ATOM 201 CA PHE A 409 -20.934 23.206 -28.583 1.00 60.21 C ANISOU 201 CA PHE A 409 9458 6030 7388 -1369 -1337 213 C ATOM 202 C PHE A 409 -20.649 24.104 -29.788 1.00 64.47 C ANISOU 202 C PHE A 409 10242 6467 7787 -1659 -1622 438 C ATOM 203 O PHE A 409 -19.627 23.932 -30.457 1.00 62.94 O ANISOU 203 O PHE A 409 10017 6479 7417 -1969 -1505 635 O ATOM 204 CB PHE A 409 -21.733 21.997 -29.003 1.00 57.48 C ANISOU 204 CB PHE A 409 8931 5856 7053 -1252 -1089 77 C ATOM 205 CG PHE A 409 -21.790 20.928 -27.967 1.00 60.68 C ANISOU 205 CG PHE A 409 9111 6400 7544 -1097 -805 -61 C ATOM 206 CD1 PHE A 409 -20.646 20.510 -27.341 1.00 56.51 C ANISOU 206 CD1 PHE A 409 8502 5968 7003 -1168 -615 -7 C ATOM 207 CD2 PHE A 409 -22.977 20.330 -27.628 1.00 61.42 C ANISOU 207 CD2 PHE A 409 9075 6555 7709 -912 -749 -229 C ATOM 208 CE1 PHE A 409 -20.688 19.543 -26.403 1.00 56.78 C ANISOU 208 CE1 PHE A 409 8372 6095 7108 -1050 -405 -109 C ATOM 209 CE2 PHE A 409 -22.989 19.302 -26.709 1.00 54.91 C ANISOU 209 CE2 PHE A 409 8067 5865 6930 -852 -521 -300 C ATOM 210 CZ PHE A 409 -21.845 18.933 -26.100 1.00 49.01 C ANISOU 210 CZ PHE A 409 7285 5151 6184 -916 -366 -237 C ATOM 211 H PHE A 409 -22.454 23.661 -27.376 1.00 67.54 H ATOM 212 HA PHE A 409 -20.078 22.912 -28.236 1.00 72.28 H ATOM 213 HB2 PHE A 409 -22.643 22.275 -29.193 1.00 69.00 H ATOM 214 HB3 PHE A 409 -21.329 21.617 -29.799 1.00 69.00 H ATOM 215 HD1 PHE A 409 -19.831 20.898 -27.565 1.00 67.84 H ATOM 216 HD2 PHE A 409 -23.771 20.618 -28.017 1.00 73.73 H ATOM 217 HE1 PHE A 409 -19.908 19.295 -25.962 1.00 68.16 H ATOM 218 HE2 PHE A 409 -23.785 18.864 -26.510 1.00 65.91 H ATOM 219 HZ PHE A 409 -21.857 18.252 -25.467 1.00 58.83 H ATOM 220 N LYS A 410 -21.550 25.023 -30.124 1.00 61.29 N ANISOU 220 N LYS A 410 10069 5792 7427 -1570 -2009 409 N ATOM 221 CA LYS A 410 -21.253 25.882 -31.270 1.00 63.15 C ANISOU 221 CA LYS A 410 10577 5906 7510 -1902 -2328 669 C ATOM 222 C LYS A 410 -20.034 26.736 -30.988 1.00 61.89 C ANISOU 222 C LYS A 410 10585 5663 7266 -2228 -2525 925 C ATOM 223 O LYS A 410 -19.168 26.905 -31.854 1.00 68.16 O ANISOU 223 O LYS A 410 11426 6633 7839 -2662 -2540 1216 O ATOM 224 CB LYS A 410 -22.448 26.753 -31.620 1.00 65.18 C ANISOU 224 CB LYS A 410 11095 5828 7840 -1713 -2782 574 C ATOM 225 CG LYS A 410 -22.183 27.718 -32.806 1.00 86.69 C ANISOU 225 CG LYS A 410 14169 8366 10402 -2096 -3198 881 C ATOM 226 CD LYS A 410 -23.470 28.331 -33.386 1.00 87.94 C ANISOU 226 CD LYS A 410 14566 8229 10619 -1877 -3617 761 C ATOM 227 CE LYS A 410 -23.140 29.406 -34.419 1.00 95.78 C ANISOU 227 CE LYS A 410 15976 8966 11452 -2294 -4121 1104 C ATOM 228 NZ LYS A 410 -24.361 29.793 -35.206 1.00121.45 N ANISOU 228 NZ LYS A 410 19432 11984 14729 -2102 -4477 998 N ATOM 229 H LYS A 410 -22.300 25.163 -29.728 1.00 73.57 H ATOM 230 HA LYS A 410 -21.072 25.323 -32.041 1.00 75.80 H ATOM 231 HB2 LYS A 410 -23.192 26.180 -31.863 1.00 78.24 H ATOM 232 HB3 LYS A 410 -22.681 27.289 -30.846 1.00 78.24 H ATOM 233 HG2 LYS A 410 -21.618 28.445 -32.500 1.00104.05 H ATOM 234 HG3 LYS A 410 -21.739 27.230 -33.516 1.00104.05 H ATOM 235 HD2 LYS A 410 -23.993 27.638 -33.818 1.00105.56 H ATOM 236 HD3 LYS A 410 -23.985 28.738 -32.672 1.00105.56 H ATOM 237 HE2 LYS A 410 -22.804 30.196 -33.967 1.00114.96 H ATOM 238 HE3 LYS A 410 -22.472 29.067 -35.036 1.00114.96 H ATOM 239 HZ1 LYS A 410 -24.158 30.436 -35.787 1.00145.76 H ATOM 240 HZ2 LYS A 410 -24.671 29.089 -35.653 1.00145.76 H ATOM 241 HZ3 LYS A 410 -24.996 30.090 -34.657 1.00145.76 H ATOM 242 N ASP A 411 -19.933 27.274 -29.749 1.00 72.02 N ANISOU 242 N ASP A 411 11938 6728 8698 -2039 -2682 823 N ATOM 243 CA ASP A 411 -18.756 28.046 -29.341 1.00 69.44 C ANISOU 243 CA ASP A 411 11766 6314 8306 -2348 -2874 1059 C ATOM 244 C ASP A 411 -17.489 27.217 -29.494 1.00 68.62 C ANISOU 244 C ASP A 411 11371 6671 8029 -2650 -2429 1219 C ATOM 245 O ASP A 411 -16.413 27.744 -29.772 1.00 73.94 O ANISOU 245 O ASP A 411 12124 7447 8523 -3085 -2549 1515 O ATOM 246 CB ASP A 411 -18.823 28.514 -27.862 1.00 74.64 C ANISOU 246 CB ASP A 411 12475 6730 9157 -2032 -3027 862 C ATOM 247 CG ASP A 411 -19.877 29.603 -27.593 1.00 80.04 C ANISOU 247 CG ASP A 411 13484 6951 9977 -1707 -3597 677 C ATOM 248 OD1 ASP A 411 -20.459 30.092 -28.584 1.00 87.35 O ANISOU 248 OD1 ASP A 411 14611 7740 10837 -1756 -3893 752 O ATOM 249 OD2 ASP A 411 -20.107 29.963 -26.391 1.00 87.38 O ANISOU 249 OD2 ASP A 411 14427 7726 11047 -1354 -3738 438 O ATOM 250 H ASP A 411 -20.533 27.203 -29.137 1.00 86.44 H ATOM 251 HA ASP A 411 -18.740 28.833 -29.909 1.00 83.36 H ATOM 252 HB2 ASP A 411 -19.039 27.751 -27.304 1.00 89.60 H ATOM 253 HB3 ASP A 411 -17.958 28.874 -27.610 1.00 89.60 H ATOM 254 N MET A 412 -17.583 25.920 -29.274 1.00 64.11 N ANISOU 254 N MET A 412 10463 6400 7497 -2422 -1948 1019 N ATOM 255 CA MET A 412 -16.396 25.106 -29.426 1.00 64.60 C ANISOU 255 CA MET A 412 10254 6903 7389 -2624 -1572 1107 C ATOM 256 C MET A 412 -16.186 24.600 -30.855 1.00 67.77 C ANISOU 256 C MET A 412 10546 7662 7541 -2861 -1427 1218 C ATOM 257 O MET A 412 -15.250 23.826 -31.074 1.00 66.67 O ANISOU 257 O MET A 412 10142 7963 7228 -2958 -1116 1226 O ATOM 258 CB MET A 412 -16.486 23.919 -28.486 1.00 56.24 C ANISOU 258 CB MET A 412 8924 5967 6476 -2271 -1188 841 C ATOM 259 CG MET A 412 -16.572 24.234 -27.012 1.00 72.85 C ANISOU 259 CG MET A 412 11055 7844 8780 -2039 -1252 718 C ATOM 260 SD MET A 412 -17.122 22.710 -26.185 1.00 74.43 S ANISOU 260 SD MET A 412 10970 8183 9126 -1657 -846 426 S ATOM 261 CE MET A 412 -15.827 21.518 -26.487 1.00 71.72 C ANISOU 261 CE MET A 412 10381 8245 8624 -1782 -476 462 C ATOM 262 H MET A 412 -18.300 25.503 -29.044 1.00 76.96 H ATOM 263 HA MET A 412 -15.623 25.639 -29.181 1.00 77.55 H ATOM 264 HB2 MET A 412 -17.280 23.412 -28.716 1.00 67.51 H ATOM 265 HB3 MET A 412 -15.695 23.372 -28.614 1.00 67.51 H ATOM 266 HG2 MET A 412 -15.703 24.495 -26.669 1.00 87.44 H ATOM 267 HG3 MET A 412 -17.217 24.941 -26.854 1.00 87.44 H ATOM 268 HE1 MET A 412 -16.067 20.677 -26.067 1.00 86.09 H ATOM 269 HE2 MET A 412 -15.730 21.394 -27.445 1.00 86.09 H ATOM 270 HE3 MET A 412 -14.998 21.851 -26.111 1.00 86.09 H ATOM 271 N GLY A 413 -17.042 24.984 -31.807 1.00 62.63 N ANISOU 271 N GLY A 413 10078 6859 6858 -2912 -1652 1269 N ATOM 272 CA GLY A 413 -16.937 24.553 -33.191 1.00 65.00 C ANISOU 272 CA GLY A 413 10285 7504 6908 -3125 -1539 1364 C ATOM 273 C GLY A 413 -17.462 23.160 -33.462 1.00 62.99 C ANISOU 273 C GLY A 413 9790 7444 6701 -2806 -1176 1088 C ATOM 274 O GLY A 413 -17.065 22.536 -34.446 1.00 73.00 O ANISOU 274 O GLY A 413 10892 9110 7734 -2926 -995 1105 O ATOM 275 H GLY A 413 -17.709 25.509 -31.667 1.00 75.18 H ATOM 276 HA2 GLY A 413 -17.434 25.171 -33.749 1.00 78.02 H ATOM 277 HA3 GLY A 413 -16.003 24.573 -33.453 1.00 78.02 H ATOM 278 N TRP A 414 -18.315 22.644 -32.592 1.00 63.54 N ANISOU 278 N TRP A 414 9827 7274 7041 -2417 -1088 836 N ATOM 279 CA TRP A 414 -18.862 21.310 -32.737 1.00 61.43 C ANISOU 279 CA TRP A 414 9376 7131 6835 -2152 -806 600 C ATOM 280 C TRP A 414 -20.298 21.313 -33.248 1.00 60.83 C ANISOU 280 C TRP A 414 9407 6843 6861 -2000 -942 500 C ATOM 281 O TRP A 414 -20.908 20.246 -33.336 1.00 60.13 O ANISOU 281 O TRP A 414 9196 6812 6838 -1805 -761 318 O ATOM 282 CB TRP A 414 -18.786 20.578 -31.403 1.00 55.55 C ANISOU 282 CB TRP A 414 8491 6338 6279 -1891 -604 420 C ATOM 283 CG TRP A 414 -17.424 20.164 -30.997 1.00 55.91 C ANISOU 283 CG TRP A 414 8374 6651 6219 -1963 -406 446 C ATOM 284 CD1 TRP A 414 -16.265 20.454 -31.627 1.00 58.12 C ANISOU 284 CD1 TRP A 414 8583 7258 6240 -2240 -385 608 C ATOM 285 CD2 TRP A 414 -17.072 19.379 -29.848 1.00 51.66 C ANISOU 285 CD2 TRP A 414 7702 6119 5807 -1760 -214 304 C ATOM 286 NE1 TRP A 414 -15.206 19.894 -30.953 1.00 56.78 N ANISOU 286 NE1 TRP A 414 8226 7317 6031 -2184 -185 544 N ATOM 287 CE2 TRP A 414 -15.681 19.227 -29.856 1.00 52.26 C ANISOU 287 CE2 TRP A 414 7637 6512 5708 -1883 -88 361 C ATOM 288 CE3 TRP A 414 -17.804 18.810 -28.804 1.00 54.61 C ANISOU 288 CE3 TRP A 414 8053 6298 6399 -1512 -152 149 C ATOM 289 CZ2 TRP A 414 -14.998 18.505 -28.868 1.00 56.60 C ANISOU 289 CZ2 TRP A 414 8052 7133 6322 -1723 83 246 C ATOM 290 CZ3 TRP A 414 -17.122 18.100 -27.825 1.00 56.17 C ANISOU 290 CZ3 TRP A 414 8133 6560 6649 -1402 13 72 C ATOM 291 CH2 TRP A 414 -15.739 17.966 -27.858 1.00 48.75 C ANISOU 291 CH2 TRP A 414 7086 5877 5562 -1488 118 113 C ATOM 292 H TRP A 414 -18.598 23.059 -31.894 1.00 76.27 H ATOM 293 HA TRP A 414 -18.325 20.824 -33.382 1.00 73.74 H ATOM 294 HB2 TRP A 414 -19.131 21.164 -30.710 1.00 66.69 H ATOM 295 HB3 TRP A 414 -19.329 19.777 -31.460 1.00 66.69 H ATOM 296 HD1 TRP A 414 -16.194 20.959 -32.405 1.00 69.76 H ATOM 297 HE1 TRP A 414 -14.380 19.953 -31.184 1.00 68.16 H ATOM 298 HE3 TRP A 414 -18.729 18.905 -28.765 1.00 65.56 H ATOM 299 HZ2 TRP A 414 -14.074 18.397 -28.899 1.00 67.95 H ATOM 300 HZ3 TRP A 414 -17.601 17.706 -27.132 1.00 67.43 H ATOM 301 HH2 TRP A 414 -15.311 17.498 -27.178 1.00 58.53 H ATOM 302 N ASP A 415 -20.829 22.470 -33.659 1.00 68.72 N ANISOU 302 N ASP A 415 10648 7605 7858 -2102 -1293 621 N ATOM 303 CA ASP A 415 -22.148 22.481 -34.295 1.00 61.78 C ANISOU 303 CA ASP A 415 9856 6578 7040 -1958 -1436 520 C ATOM 304 C ASP A 415 -22.179 21.836 -35.675 1.00 60.45 C ANISOU 304 C ASP A 415 9628 6658 6683 -2092 -1317 555 C ATOM 305 O ASP A 415 -23.279 21.569 -36.161 1.00 66.11 O ANISOU 305 O ASP A 415 10366 7293 7459 -1946 -1368 436 O ATOM 306 CB ASP A 415 -22.702 23.905 -34.424 1.00 73.00 C ANISOU 306 CB ASP A 415 11586 7651 8499 -1992 -1911 615 C ATOM 307 CG ASP A 415 -21.717 24.885 -35.069 1.00 78.24 C ANISOU 307 CG ASP A 415 12465 8306 8955 -2425 -2163 950 C ATOM 308 OD1 ASP A 415 -20.485 24.802 -34.784 1.00 81.90 O ANISOU 308 OD1 ASP A 415 12827 8989 9303 -2651 -2005 1091 O ATOM 309 OD2 ASP A 415 -22.199 25.775 -35.826 1.00 93.77 O ANISOU 309 OD2 ASP A 415 14712 10050 10865 -2552 -2557 1080 O ATOM 310 H ASP A 415 -20.454 23.240 -33.583 1.00 82.49 H ATOM 311 HA ASP A 415 -22.731 21.978 -33.705 1.00 74.16 H ATOM 312 HB2 ASP A 415 -23.501 23.882 -34.973 1.00 87.62 H ATOM 313 HB3 ASP A 415 -22.917 24.239 -33.539 1.00 87.62 H ATOM 314 N ASP A 416 -21.031 21.573 -36.325 1.00 64.10 N ANISOU 314 N ASP A 416 9992 7467 6898 -2349 -1166 692 N ATOM 315 CA ASP A 416 -21.067 20.888 -37.622 1.00 66.47 C ANISOU 315 CA ASP A 416 10202 8063 6991 -2422 -1047 672 C ATOM 316 C ASP A 416 -21.228 19.373 -37.505 1.00 67.41 C ANISOU 316 C ASP A 416 10109 8328 7176 -2143 -742 400 C ATOM 317 O ASP A 416 -21.334 18.692 -38.533 1.00 71.21 O ANISOU 317 O ASP A 416 10521 9029 7505 -2136 -661 325 O ATOM 318 CB ASP A 416 -19.824 21.196 -38.475 1.00 68.57 C ANISOU 318 CB ASP A 416 10399 8760 6894 -2801 -1026 899 C ATOM 319 CG ASP A 416 -18.515 20.955 -37.760 1.00 80.57 C ANISOU 319 CG ASP A 416 11723 10560 8330 -2858 -825 912 C ATOM 320 OD1 ASP A 416 -18.493 20.661 -36.552 1.00 76.77 O ANISOU 320 OD1 ASP A 416 11202 9883 8085 -2627 -727 777 O ATOM 321 OD2 ASP A 416 -17.468 21.121 -38.419 1.00 89.80 O ANISOU 321 OD2 ASP A 416 12762 12197 9159 -3164 -778 1073 O ATOM 322 H ASP A 416 -20.246 21.778 -36.041 1.00 76.95 H ATOM 323 HA ASP A 416 -21.833 21.244 -38.099 1.00 79.79 H ATOM 324 N TRP A 417 -21.282 18.812 -36.301 1.00 62.20 N ANISOU 324 N TRP A 417 9368 7537 6729 -1920 -611 252 N ATOM 325 CA TRP A 417 -21.475 17.356 -36.189 1.00 61.84 C ANISOU 325 CA TRP A 417 9187 7561 6747 -1694 -406 22 C ATOM 326 C TRP A 417 -22.393 16.953 -35.047 1.00 59.59 C ANISOU 326 C TRP A 417 8901 7004 6736 -1491 -397 -101 C ATOM 327 O TRP A 417 -22.960 15.851 -35.091 1.00 58.21 O ANISOU 327 O TRP A 417 8683 6806 6628 -1363 -328 -248 O ATOM 328 CB TRP A 417 -20.115 16.610 -36.042 1.00 61.66 C ANISOU 328 CB TRP A 417 8996 7851 6581 -1667 -204 -46 C ATOM 329 CG TRP A 417 -19.320 16.917 -34.822 1.00 63.70 C ANISOU 329 CG TRP A 417 9207 8077 6920 -1670 -146 5 C ATOM 330 CD1 TRP A 417 -18.548 18.023 -34.608 1.00 59.95 C ANISOU 330 CD1 TRP A 417 8753 7675 6352 -1895 -218 208 C ATOM 331 CD2 TRP A 417 -19.181 16.091 -33.649 1.00 51.76 C ANISOU 331 CD2 TRP A 417 7631 6452 5584 -1466 -29 -135 C ATOM 332 NE1 TRP A 417 -17.980 17.963 -33.358 1.00 59.18 N ANISOU 332 NE1 TRP A 417 8599 7511 6377 -1814 -138 184 N ATOM 333 CE2 TRP A 417 -18.343 16.785 -32.753 1.00 57.10 C ANISOU 333 CE2 TRP A 417 8278 7144 6274 -1548 -14 -25 C ATOM 334 CE3 TRP A 417 -19.685 14.846 -33.265 1.00 57.24 C ANISOU 334 CE3 TRP A 417 8316 7019 6416 -1257 27 -318 C ATOM 335 CZ2 TRP A 417 -18.015 16.278 -31.495 1.00 52.81 C ANISOU 335 CZ2 TRP A 417 7678 6508 5879 -1401 81 -106 C ATOM 336 CZ3 TRP A 417 -19.374 14.352 -32.002 1.00 60.24 C ANISOU 336 CZ3 TRP A 417 8660 7292 6937 -1146 95 -372 C ATOM 337 CH2 TRP A 417 -18.539 15.065 -31.136 1.00 57.85 C ANISOU 337 CH2 TRP A 417 8311 7026 6644 -1205 135 -274 C ATOM 338 H TRP A 417 -21.212 19.233 -35.554 1.00 74.67 H ATOM 339 HA TRP A 417 -21.869 17.036 -37.015 1.00 74.23 H ATOM 340 HB2 TRP A 417 -20.293 15.656 -36.032 1.00 74.01 H ATOM 341 HB3 TRP A 417 -19.562 16.836 -36.806 1.00 74.01 H ATOM 342 HD1 TRP A 417 -18.424 18.714 -35.218 1.00 71.97 H ATOM 343 HE1 TRP A 417 -17.477 18.568 -33.010 1.00 71.04 H ATOM 344 HE3 TRP A 417 -20.220 14.354 -33.845 1.00 68.72 H ATOM 345 HZ2 TRP A 417 -17.458 16.749 -30.918 1.00 63.40 H ATOM 346 HZ3 TRP A 417 -19.726 13.535 -31.730 1.00 72.31 H ATOM 347 HH2 TRP A 417 -18.337 14.710 -30.301 1.00 69.45 H ATOM 348 N ILE A 418 -22.546 17.776 -34.027 1.00 54.92 N ANISOU 348 N ILE A 418 8350 6238 6280 -1472 -485 -45 N ATOM 349 CA ILE A 418 -23.475 17.509 -32.948 1.00 51.86 C ANISOU 349 CA ILE A 418 7914 5697 6094 -1300 -485 -159 C ATOM 350 C ILE A 418 -24.798 18.163 -33.299 1.00 53.94 C ANISOU 350 C ILE A 418 8249 5837 6408 -1241 -694 -190 C ATOM 351 O ILE A 418 -24.869 19.374 -33.513 1.00 60.81 O ANISOU 351 O ILE A 418 9258 6591 7258 -1279 -918 -108 O ATOM 352 CB ILE A 418 -22.940 18.034 -31.611 1.00 56.53 C ANISOU 352 CB ILE A 418 8479 6223 6776 -1259 -475 -131 C ATOM 353 CG1 ILE A 418 -21.794 17.137 -31.151 1.00 54.33 C ANISOU 353 CG1 ILE A 418 8101 6074 6467 -1266 -261 -146 C ATOM 354 CG2 ILE A 418 -24.088 17.997 -30.587 1.00 55.66 C ANISOU 354 CG2 ILE A 418 8293 6037 6818 -1089 -518 -252 C ATOM 355 CD1 ILE A 418 -20.972 17.697 -30.000 1.00 56.39 C ANISOU 355 CD1 ILE A 418 8340 6307 6777 -1268 -241 -91 C ATOM 356 H ILE A 418 -22.113 18.513 -33.934 1.00 65.93 H ATOM 357 HA ILE A 418 -23.611 16.552 -32.866 1.00 62.26 H ATOM 358 HB ILE A 418 -22.613 18.942 -31.704 1.00 67.86 H ATOM 359 HG12 ILE A 418 -22.163 16.288 -30.860 1.00 65.22 H ATOM 360 HG13 ILE A 418 -21.192 16.997 -31.898 1.00 65.22 H ATOM 361 HG21 ILE A 418 -23.715 18.056 -29.693 1.00 66.81 H ATOM 362 HG22 ILE A 418 -24.679 18.749 -30.749 1.00 66.81 H ATOM 363 HG23 ILE A 418 -24.575 17.165 -30.689 1.00 66.81 H ATOM 364 HD11 ILE A 418 -20.177 17.153 -29.886 1.00 67.69 H ATOM 365 HD12 ILE A 418 -20.721 18.610 -30.207 1.00 67.69 H ATOM 366 HD13 ILE A 418 -21.507 17.676 -29.191 1.00 67.69 H ATOM 367 N ILE A 419 -25.852 17.357 -33.338 1.00 56.84 N ANISOU 367 N ILE A 419 8534 6228 6836 -1153 -658 -311 N ATOM 368 CA ILE A 419 -27.206 17.837 -33.603 1.00 59.89 C ANISOU 368 CA ILE A 419 8927 6569 7259 -1061 -842 -384 C ATOM 369 C ILE A 419 -27.893 18.305 -32.323 1.00 61.86 C ANISOU 369 C ILE A 419 9064 6828 7612 -890 -914 -489 C ATOM 370 O ILE A 419 -28.453 19.406 -32.254 1.00 58.81 O ANISOU 370 O ILE A 419 8739 6365 7242 -755 -1156 -546 O ATOM 371 CB ILE A 419 -27.996 16.701 -34.272 1.00 59.99 C ANISOU 371 CB ILE A 419 8874 6664 7255 -1082 -773 -458 C ATOM 372 CG1 ILE A 419 -27.378 16.337 -35.614 1.00 57.61 C ANISOU 372 CG1 ILE A 419 8676 6391 6821 -1198 -738 -402 C ATOM 373 CG2 ILE A 419 -29.421 17.077 -34.388 1.00 60.30 C ANISOU 373 CG2 ILE A 419 8859 6728 7324 -981 -937 -554 C ATOM 374 CD1 ILE A 419 -27.827 14.936 -36.112 1.00 67.78 C ANISOU 374 CD1 ILE A 419 9923 7730 8101 -1207 -660 -494 C ATOM 375 H ILE A 419 -25.811 16.507 -33.212 1.00 68.24 H ATOM 376 HA ILE A 419 -27.166 18.599 -34.202 1.00 71.89 H ATOM 377 HB ILE A 419 -27.948 15.907 -33.716 1.00 72.01 H ATOM 378 HG12 ILE A 419 -27.647 16.994 -36.276 1.00 69.15 H ATOM 379 HG13 ILE A 419 -26.412 16.332 -35.527 1.00 69.15 H ATOM 380 HG21 ILE A 419 -29.856 16.476 -35.013 1.00 72.38 H ATOM 381 HG22 ILE A 419 -29.839 17.006 -33.516 1.00 72.38 H ATOM 382 HG23 ILE A 419 -29.482 17.990 -34.710 1.00 72.38 H ATOM 383 HD11 ILE A 419 -27.365 14.732 -36.940 1.00 81.36 H ATOM 384 HD12 ILE A 419 -27.605 14.276 -35.438 1.00 81.36 H ATOM 385 HD13 ILE A 419 -28.785 14.947 -36.262 1.00 81.36 H ATOM 386 N ALA A 420 -27.886 17.476 -31.291 1.00 58.23 N ANISOU 386 N ALA A 420 8442 6481 7203 -877 -740 -532 N ATOM 387 CA ALA A 420 -28.499 17.878 -30.040 1.00 57.46 C ANISOU 387 CA ALA A 420 8187 6493 7151 -723 -787 -641 C ATOM 388 C ALA A 420 -27.854 17.103 -28.909 1.00 59.55 C ANISOU 388 C ALA A 420 8345 6832 7448 -786 -585 -603 C ATOM 389 O ALA A 420 -27.300 16.021 -29.150 1.00 51.51 O ANISOU 389 O ALA A 420 7359 5786 6426 -927 -437 -529 O ATOM 390 CB ALA A 420 -29.998 17.590 -30.082 1.00 59.52 C ANISOU 390 CB ALA A 420 8265 6966 7382 -654 -849 -771 C ATOM 391 H ALA A 420 -27.537 16.690 -31.292 1.00 69.90 H ATOM 392 HA ALA A 420 -28.352 18.823 -29.876 1.00 68.97 H ATOM 393 HB1 ALA A 420 -30.395 17.861 -29.239 1.00 71.44 H ATOM 394 HB2 ALA A 420 -30.396 18.092 -30.810 1.00 71.44 H ATOM 395 HB3 ALA A 420 -30.134 16.640 -30.222 1.00 71.44 H ATOM 396 N PRO A 421 -27.840 17.656 -27.670 1.00 51.09 N ANISOU 396 N PRO A 421 7168 5841 6401 -660 -606 -666 N ATOM 397 CA PRO A 421 -28.147 19.044 -27.293 1.00 55.35 C ANISOU 397 CA PRO A 421 7729 6352 6949 -431 -834 -785 C ATOM 398 C PRO A 421 -27.066 19.981 -27.841 1.00 56.25 C ANISOU 398 C PRO A 421 8120 6166 7088 -473 -968 -669 C ATOM 399 O PRO A 421 -25.982 19.527 -28.228 1.00 63.39 O ANISOU 399 O PRO A 421 9114 6990 7979 -667 -820 -513 O ATOM 400 CB PRO A 421 -28.164 18.983 -25.759 1.00 54.69 C ANISOU 400 CB PRO A 421 7443 6474 6864 -333 -754 -867 C ATOM 401 CG PRO A 421 -27.141 17.892 -25.429 1.00 54.36 C ANISOU 401 CG PRO A 421 7416 6390 6849 -554 -501 -703 C ATOM 402 CD PRO A 421 -27.335 16.871 -26.523 1.00 53.71 C ANISOU 402 CD PRO A 421 7388 6270 6750 -733 -424 -623 C ATOM 403 HA PRO A 421 -29.025 19.324 -27.595 1.00 66.44 H ATOM 404 HB2 PRO A 421 -27.899 19.838 -25.387 1.00 65.65 H ATOM 405 HB3 PRO A 421 -29.050 18.743 -25.443 1.00 65.65 H ATOM 406 HG2 PRO A 421 -26.243 18.258 -25.446 1.00 65.26 H ATOM 407 HG3 PRO A 421 -27.328 17.511 -24.557 1.00 65.26 H ATOM 408 HD2 PRO A 421 -26.493 16.445 -26.746 1.00 64.48 H ATOM 409 HD3 PRO A 421 -27.985 16.202 -26.255 1.00 64.48 H ATOM 410 N LEU A 422 -27.310 21.288 -27.888 1.00 55.89 N ANISOU 410 N LEU A 422 8214 5968 7052 -306 -1283 -742 N ATOM 411 CA LEU A 422 -26.296 22.250 -28.324 1.00 58.58 C ANISOU 411 CA LEU A 422 8843 6020 7393 -418 -1475 -586 C ATOM 412 C LEU A 422 -25.569 22.862 -27.152 1.00 59.14 C ANISOU 412 C LEU A 422 8944 6013 7513 -342 -1538 -598 C ATOM 413 O LEU A 422 -24.498 23.460 -27.335 1.00 59.99 O ANISOU 413 O LEU A 422 9257 5926 7608 -519 -1639 -421 O ATOM 414 CB LEU A 422 -26.943 23.318 -29.215 1.00 69.86 C ANISOU 414 CB LEU A 422 10501 7239 8803 -333 -1873 -616 C ATOM 415 CG LEU A 422 -27.290 22.682 -30.586 1.00 73.11 C ANISOU 415 CG LEU A 422 10927 7705 9146 -504 -1780 -528 C ATOM 416 CD1 LEU A 422 -28.038 23.710 -31.389 1.00 86.79 C ANISOU 416 CD1 LEU A 422 12880 9235 10860 -398 -2194 -570 C ATOM 417 CD2 LEU A 422 -26.080 22.094 -31.394 1.00 77.61 C ANISOU 417 CD2 LEU A 422 11560 8298 9629 -851 -1554 -280 C ATOM 418 H LEU A 422 -28.061 21.647 -27.671 1.00 67.09 H ATOM 419 HA LEU A 422 -25.626 21.817 -28.876 1.00 70.32 H ATOM 420 HB2 LEU A 422 -27.758 23.645 -28.802 1.00 83.86 H ATOM 421 HB3 LEU A 422 -26.325 24.052 -29.353 1.00 83.86 H ATOM 422 HG LEU A 422 -27.832 21.896 -30.416 1.00 87.76 H ATOM 423 HD11 LEU A 422 -28.279 23.326 -32.246 1.00104.17 H ATOM 424 HD12 LEU A 422 -28.838 23.968 -30.905 1.00104.17 H ATOM 425 HD13 LEU A 422 -27.467 24.483 -31.522 1.00104.17 H ATOM 426 HD21 LEU A 422 -26.354 21.952 -32.313 1.00 93.15 H ATOM 427 HD22 LEU A 422 -25.343 22.724 -31.362 1.00 93.15 H ATOM 428 HD23 LEU A 422 -25.813 21.252 -30.994 1.00 93.15 H ATOM 429 N GLU A 423 -26.065 22.631 -25.940 1.00 52.98 N ANISOU 429 N GLU A 423 7938 5432 6761 -126 -1455 -784 N ATOM 430 CA GLU A 423 -25.389 23.093 -24.749 1.00 55.89 C ANISOU 430 CA GLU A 423 8306 5763 7168 -39 -1485 -815 C ATOM 431 C GLU A 423 -25.735 22.189 -23.577 1.00 54.04 C ANISOU 431 C GLU A 423 7746 5871 6918 45 -1208 -928 C ATOM 432 O GLU A 423 -26.720 21.441 -23.603 1.00 51.53 O ANISOU 432 O GLU A 423 7205 5828 6548 74 -1084 -1016 O ATOM 433 CB GLU A 423 -25.737 24.568 -24.464 1.00 57.70 C ANISOU 433 CB GLU A 423 8725 5776 7423 242 -1951 -980 C ATOM 434 CG GLU A 423 -27.134 24.990 -24.758 1.00 71.27 C ANISOU 434 CG GLU A 423 10395 7574 9111 548 -2210 -1232 C ATOM 435 CD GLU A 423 -27.261 26.533 -24.954 1.00 87.08 C ANISOU 435 CD GLU A 423 12747 9193 11146 778 -2796 -1341 C ATOM 436 OE1 GLU A 423 -26.367 27.279 -24.459 1.00 76.49 O ANISOU 436 OE1 GLU A 423 11631 7581 9852 746 -2998 -1268 O ATOM 437 OE2 GLU A 423 -28.256 26.984 -25.600 1.00 84.27 O ANISOU 437 OE2 GLU A 423 12461 8792 10768 988 -3089 -1500 O ATOM 438 H GLU A 423 -26.796 22.205 -25.787 1.00 63.60 H ATOM 439 HA GLU A 423 -24.429 23.028 -24.867 1.00 67.10 H ATOM 440 HB2 GLU A 423 -25.582 24.737 -23.521 1.00 69.27 H ATOM 441 HB3 GLU A 423 -25.152 25.124 -25.001 1.00 69.27 H ATOM 442 HG2 GLU A 423 -27.431 24.558 -25.574 1.00 85.55 H ATOM 443 HG3 GLU A 423 -27.706 24.732 -24.019 1.00 85.55 H ATOM 444 N TYR A 424 -24.890 22.230 -22.552 1.00 49.27 N ANISOU 444 N TYR A 424 7116 5264 6341 39 -1121 -898 N ATOM 445 CA TYR A 424 -25.177 21.467 -21.342 1.00 53.37 C ANISOU 445 CA TYR A 424 7343 6113 6821 96 -899 -984 C ATOM 446 C TYR A 424 -24.292 21.990 -20.224 1.00 49.07 C ANISOU 446 C TYR A 424 6833 5502 6310 172 -930 -996 C ATOM 447 O TYR A 424 -23.367 22.791 -20.437 1.00 46.42 O ANISOU 447 O TYR A 424 6746 4859 6032 125 -1092 -903 O ATOM 448 CB TYR A 424 -25.042 19.926 -21.586 1.00 50.14 C ANISOU 448 CB TYR A 424 6821 5834 6394 -177 -570 -824 C ATOM 449 CG TYR A 424 -23.642 19.356 -21.444 1.00 48.53 C ANISOU 449 CG TYR A 424 6715 5486 6237 -373 -386 -640 C ATOM 450 CD1 TYR A 424 -22.719 19.459 -22.500 1.00 45.54 C ANISOU 450 CD1 TYR A 424 6540 4884 5878 -522 -390 -498 C ATOM 451 CD2 TYR A 424 -23.226 18.737 -20.252 1.00 52.53 C ANISOU 451 CD2 TYR A 424 7092 6129 6740 -403 -222 -618 C ATOM 452 CE1 TYR A 424 -21.412 19.008 -22.374 1.00 50.81 C ANISOU 452 CE1 TYR A 424 7253 5500 6553 -657 -240 -373 C ATOM 453 CE2 TYR A 424 -21.897 18.266 -20.120 1.00 43.01 C ANISOU 453 CE2 TYR A 424 5976 4792 5572 -535 -87 -482 C ATOM 454 CZ TYR A 424 -21.022 18.401 -21.179 1.00 50.54 C ANISOU 454 CZ TYR A 424 7102 5564 6539 -642 -94 -379 C ATOM 455 OH TYR A 424 -19.757 17.905 -20.983 1.00 47.00 O ANISOU 455 OH TYR A 424 6681 5082 6094 -732 38 -289 O ATOM 456 H TYR A 424 -24.159 22.683 -22.533 1.00 59.15 H ATOM 457 HA TYR A 424 -26.093 21.616 -21.062 1.00 64.07 H ATOM 458 HB2 TYR A 424 -25.606 19.466 -20.944 1.00 60.19 H ATOM 459 HB3 TYR A 424 -25.341 19.733 -22.488 1.00 60.19 H ATOM 460 HD1 TYR A 424 -22.991 19.839 -23.304 1.00 54.67 H ATOM 461 HD2 TYR A 424 -23.825 18.637 -19.548 1.00 63.06 H ATOM 462 HE1 TYR A 424 -20.807 19.108 -23.073 1.00 61.00 H ATOM 463 HE2 TYR A 424 -21.616 17.870 -19.327 1.00 51.63 H ATOM 464 HH TYR A 424 -19.719 17.498 -20.249 1.00 56.42 H ATOM 465 N GLU A 425 -24.620 21.575 -19.009 1.00 51.01 N ANISOU 465 N GLU A 425 6818 6067 6495 268 -798 -1104 N ATOM 466 CA GLU A 425 -23.908 22.008 -17.809 1.00 50.47 C ANISOU 466 CA GLU A 425 6739 5998 6440 370 -818 -1148 C ATOM 467 C GLU A 425 -22.963 20.918 -17.363 1.00 51.65 C ANISOU 467 C GLU A 425 6841 6174 6608 109 -506 -942 C ATOM 468 O GLU A 425 -23.395 19.865 -16.879 1.00 42.87 O ANISOU 468 O GLU A 425 5514 5349 5424 6 -302 -914 O ATOM 469 CB GLU A 425 -24.912 22.356 -16.715 1.00 49.33 C ANISOU 469 CB GLU A 425 6316 6253 6174 686 -910 -1437 C ATOM 470 CG GLU A 425 -25.822 23.472 -17.185 1.00 53.49 C ANISOU 470 CG GLU A 425 6908 6735 6679 1021 -1280 -1697 C ATOM 471 CD GLU A 425 -25.115 24.842 -17.206 1.00 65.90 C ANISOU 471 CD GLU A 425 8833 7849 8356 1196 -1666 -1754 C ATOM 472 OE1 GLU A 425 -23.950 24.983 -16.707 1.00 58.47 O ANISOU 472 OE1 GLU A 425 8032 6698 7486 1068 -1626 -1611 O ATOM 473 OE2 GLU A 425 -25.781 25.776 -17.719 1.00 64.89 O ANISOU 473 OE2 GLU A 425 8848 7577 8230 1462 -2047 -1946 O ATOM 474 H GLU A 425 -25.266 21.030 -18.848 1.00 61.23 H ATOM 475 HA GLU A 425 -23.370 22.790 -18.011 1.00 60.59 H ATOM 476 HB2 GLU A 425 -25.454 21.578 -16.509 1.00 59.22 H ATOM 477 HB3 GLU A 425 -24.441 22.651 -15.921 1.00 59.22 H ATOM 478 HG2 GLU A 425 -26.125 23.276 -18.085 1.00 64.21 H ATOM 479 HG3 GLU A 425 -26.582 23.535 -16.586 1.00 64.21 H ATOM 480 N ALA A 426 -21.662 21.198 -17.453 1.00 48.28 N ANISOU 480 N ALA A 426 6615 5469 6262 -3 -508 -800 N ATOM 481 CA ALA A 426 -20.642 20.192 -17.220 1.00 46.47 C ANISOU 481 CA ALA A 426 6371 5232 6052 -216 -253 -625 C ATOM 482 C ALA A 426 -20.054 20.301 -15.833 1.00 46.21 C ANISOU 482 C ALA A 426 6259 5280 6018 -146 -207 -655 C ATOM 483 O ALA A 426 -19.587 19.305 -15.290 1.00 43.92 O ANISOU 483 O ALA A 426 5888 5082 5718 -266 -5 -562 O ATOM 484 CB ALA A 426 -19.497 20.360 -18.220 1.00 41.74 C ANISOU 484 CB ALA A 426 5981 4384 5494 -395 -260 -458 C ATOM 485 H ALA A 426 -21.348 21.974 -17.650 1.00 57.97 H ATOM 486 HA ALA A 426 -21.031 19.312 -17.344 1.00 55.78 H ATOM 487 HB1 ALA A 426 -18.825 19.682 -18.047 1.00 50.11 H ATOM 488 HB2 ALA A 426 -19.845 20.259 -19.120 1.00 50.11 H ATOM 489 HB3 ALA A 426 -19.110 21.243 -18.112 1.00 50.11 H ATOM 490 N PHE A 427 -19.973 21.513 -15.321 1.00 45.32 N ANISOU 490 N PHE A 427 6213 5085 5920 46 -433 -777 N ATOM 491 CA PHE A 427 -19.403 21.800 -14.012 1.00 45.21 C ANISOU 491 CA PHE A 427 6143 5130 5903 145 -435 -831 C ATOM 492 C PHE A 427 -17.882 21.730 -14.140 1.00 42.33 C ANISOU 492 C PHE A 427 5932 4544 5606 -58 -361 -633 C ATOM 493 O PHE A 427 -17.334 21.206 -15.111 1.00 39.73 O ANISOU 493 O PHE A 427 5680 4123 5293 -265 -251 -474 O ATOM 494 CB PHE A 427 -19.970 20.866 -12.902 1.00 43.71 C ANISOU 494 CB PHE A 427 5665 5333 5611 167 -228 -885 C ATOM 495 CG PHE A 427 -21.446 21.096 -12.655 1.00 40.30 C ANISOU 495 CG PHE A 427 5012 5249 5052 375 -320 -1108 C ATOM 496 CD1 PHE A 427 -21.920 22.141 -11.885 1.00 40.14 C ANISOU 496 CD1 PHE A 427 4905 5383 4962 715 -543 -1381 C ATOM 497 CD2 PHE A 427 -22.361 20.306 -13.301 1.00 43.32 C ANISOU 497 CD2 PHE A 427 5275 5812 5372 251 -219 -1068 C ATOM 498 CE1 PHE A 427 -23.304 22.362 -11.789 1.00 47.43 C ANISOU 498 CE1 PHE A 427 5586 6700 5734 948 -644 -1630 C ATOM 499 CE2 PHE A 427 -23.707 20.521 -13.185 1.00 51.22 C ANISOU 499 CE2 PHE A 427 6041 7189 6232 426 -304 -1273 C ATOM 500 CZ PHE A 427 -24.184 21.524 -12.431 1.00 45.07 C ANISOU 500 CZ PHE A 427 5134 6628 5361 782 -504 -1563 C ATOM 501 H PHE A 427 -20.251 22.220 -15.725 1.00 54.40 H ATOM 502 HA PHE A 427 -19.653 22.688 -13.713 1.00 54.27 H ATOM 503 HB2 PHE A 427 -19.850 19.943 -13.173 1.00 52.48 H ATOM 504 HB3 PHE A 427 -19.496 21.034 -12.073 1.00 52.48 H ATOM 505 HD1 PHE A 427 -21.325 22.696 -11.433 1.00 48.04 H ATOM 506 HD2 PHE A 427 -22.059 19.605 -13.832 1.00 52.01 H ATOM 507 HE1 PHE A 427 -23.625 23.078 -11.290 1.00 56.94 H ATOM 508 HE2 PHE A 427 -24.300 19.965 -13.636 1.00 61.49 H ATOM 509 HZ PHE A 427 -25.102 21.651 -12.343 1.00 54.10 H ATOM 510 N HIS A 428 -17.201 22.254 -13.138 1.00 41.83 N ANISOU 510 N HIS A 428 5887 4448 5561 16 -426 -665 N ATOM 511 CA HIS A 428 -15.797 21.920 -12.992 1.00 39.68 C ANISOU 511 CA HIS A 428 5664 4092 5319 -171 -293 -494 C ATOM 512 C HIS A 428 -15.412 21.965 -11.523 1.00 45.90 C ANISOU 512 C HIS A 428 6354 4986 6098 -57 -260 -564 C ATOM 513 O HIS A 428 -16.141 22.499 -10.693 1.00 39.97 O ANISOU 513 O HIS A 428 5526 4352 5311 174 -388 -752 O ATOM 514 CB HIS A 428 -14.924 22.886 -13.782 1.00 41.87 C ANISOU 514 CB HIS A 428 6169 4114 5625 -321 -495 -370 C ATOM 515 CG HIS A 428 -14.877 24.291 -13.259 1.00 42.08 C ANISOU 515 CG HIS A 428 6363 3941 5683 -193 -852 -458 C ATOM 516 ND1 HIS A 428 -13.703 24.857 -12.791 1.00 44.83 N ANISOU 516 ND1 HIS A 428 6816 4168 6048 -310 -953 -358 N ATOM 517 CD2 HIS A 428 -15.810 25.277 -13.222 1.00 43.36 C ANISOU 517 CD2 HIS A 428 6640 3976 5858 41 -1187 -641 C ATOM 518 CE1 HIS A 428 -13.921 26.135 -12.480 1.00 41.50 C ANISOU 518 CE1 HIS A 428 6598 3510 5659 -171 -1357 -462 C ATOM 519 NE2 HIS A 428 -15.194 26.400 -12.714 1.00 44.83 N ANISOU 519 NE2 HIS A 428 7031 3922 6079 74 -1513 -654 N ATOM 520 H HIS A 428 -17.519 22.791 -12.546 1.00 50.23 H ATOM 521 HA HIS A 428 -15.660 21.016 -13.315 1.00 47.63 H ATOM 522 HB2 HIS A 428 -14.015 22.547 -13.779 1.00 50.27 H ATOM 523 HB3 HIS A 428 -15.260 22.928 -14.690 1.00 50.27 H ATOM 524 HD2 HIS A 428 -16.698 25.207 -13.490 1.00 52.05 H ATOM 525 HE1 HIS A 428 -13.289 26.734 -12.154 1.00 49.82 H ATOM 526 HE2 HIS A 428 -15.579 27.156 -12.572 1.00 53.81 H ATOM 527 N CYS A 429 -14.190 21.556 -11.248 1.00 40.45 N ANISOU 527 N CYS A 429 5674 4267 5429 -197 -127 -432 N ATOM 528 CA CYS A 429 -13.664 21.426 -9.888 1.00 41.85 C ANISOU 528 CA CYS A 429 5762 4544 5597 -126 -64 -465 C ATOM 529 C CYS A 429 -12.494 22.353 -9.690 1.00 42.69 C ANISOU 529 C CYS A 429 6005 4472 5744 -180 -216 -408 C ATOM 530 O CYS A 429 -11.520 22.328 -10.459 1.00 43.76 O ANISOU 530 O CYS A 429 6217 4525 5885 -389 -188 -251 O ATOM 531 CB CYS A 429 -13.214 19.997 -9.659 1.00 39.78 C ANISOU 531 CB CYS A 429 5396 4402 5316 -242 199 -359 C ATOM 532 SG CYS A 429 -14.534 18.833 -9.663 1.00 45.56 S ANISOU 532 SG CYS A 429 5990 5339 5981 -257 326 -377 S ATOM 533 H CYS A 429 -13.617 21.337 -11.851 1.00 48.57 H ATOM 534 HA CYS A 429 -14.349 21.673 -9.247 1.00 50.25 H ATOM 535 HB2 CYS A 429 -12.596 19.748 -10.364 1.00 47.76 H ATOM 536 HB3 CYS A 429 -12.773 19.943 -8.797 1.00 47.76 H ATOM 537 N GLU A 430 -12.557 23.151 -8.642 1.00 39.92 N ANISOU 537 N GLU A 430 5666 4106 5396 -4 -386 -540 N ATOM 538 CA GLU A 430 -11.511 24.102 -8.428 1.00 41.52 C ANISOU 538 CA GLU A 430 6029 4110 5638 -77 -588 -480 C ATOM 539 C GLU A 430 -11.520 24.477 -6.966 1.00 47.01 C ANISOU 539 C GLU A 430 6664 4877 6321 148 -670 -644 C ATOM 540 O GLU A 430 -12.594 24.607 -6.368 1.00 41.79 O ANISOU 540 O GLU A 430 5900 4371 5608 414 -729 -861 O ATOM 541 CB GLU A 430 -11.795 25.303 -9.317 1.00 46.51 C ANISOU 541 CB GLU A 430 6907 4466 6298 -108 -948 -477 C ATOM 542 CG GLU A 430 -10.864 26.413 -9.066 1.00 49.75 C ANISOU 542 CG GLU A 430 7531 4635 6738 -215 -1255 -404 C ATOM 543 CD GLU A 430 -11.098 27.573 -10.044 1.00 59.67 C ANISOU 543 CD GLU A 430 9095 5564 8011 -320 -1680 -344 C ATOM 544 OE1 GLU A 430 -12.186 28.184 -9.922 1.00 66.39 O ANISOU 544 OE1 GLU A 430 10044 6294 8887 -18 -1955 -571 O ATOM 545 OE2 GLU A 430 -10.223 27.856 -10.926 1.00 63.18 O ANISOU 545 OE2 GLU A 430 9672 5913 8422 -702 -1756 -76 O ATOM 546 H GLU A 430 -13.186 23.153 -8.056 1.00 47.93 H ATOM 547 HA GLU A 430 -10.629 23.749 -8.625 1.00 49.85 H ATOM 548 HB2 GLU A 430 -11.706 25.038 -10.246 1.00 55.83 H ATOM 549 HB3 GLU A 430 -12.696 25.619 -9.147 1.00 55.83 H ATOM 550 HG2 GLU A 430 -10.994 26.743 -8.163 1.00 59.73 H ATOM 551 HG3 GLU A 430 -9.953 26.100 -9.177 1.00 59.73 H ATOM 552 N GLY A 431 -10.329 24.730 -6.407 1.00 41.89 N ANISOU 552 N GLY A 431 6065 4157 5696 47 -697 -557 N ATOM 553 CA GLY A 431 -10.242 25.356 -5.118 1.00 47.13 C ANISOU 553 CA GLY A 431 6729 4825 6351 258 -857 -718 C ATOM 554 C GLY A 431 -9.107 24.772 -4.274 1.00 46.54 C ANISOU 554 C GLY A 431 6551 4861 6270 156 -655 -616 C ATOM 555 O GLY A 431 -8.504 23.764 -4.649 1.00 49.59 O ANISOU 555 O GLY A 431 6844 5347 6652 -29 -384 -454 O ATOM 556 H GLY A 431 -9.570 24.544 -6.766 1.00 50.30 H ATOM 557 HA2 GLY A 431 -10.084 26.306 -5.231 1.00 56.57 H ATOM 558 HA3 GLY A 431 -11.077 25.229 -4.641 1.00 56.57 H ATOM 559 N LEU A 432 -8.879 25.395 -3.123 1.00 42.42 N ANISOU 559 N LEU A 432 6046 4330 5741 323 -814 -746 N ATOM 560 CA ALEU A 432 -7.775 25.025 -2.243 0.50 52.62 C ANISOU 560 CA ALEU A 432 7263 5701 7028 247 -680 -666 C ATOM 561 CA BLEU A 432 -7.777 25.022 -2.240 0.50 51.12 C ANISOU 561 CA BLEU A 432 7073 5513 6839 247 -680 -666 C ATOM 562 C LEU A 432 -7.901 23.610 -1.731 1.00 43.52 C ANISOU 562 C LEU A 432 5883 4837 5816 252 -323 -630 C ATOM 563 O LEU A 432 -8.994 23.141 -1.355 1.00 40.40 O ANISOU 563 O LEU A 432 5348 4661 5341 396 -232 -741 O ATOM 564 CB ALEU A 432 -7.728 26.007 -1.069 0.50 52.17 C ANISOU 564 CB ALEU A 432 7272 5588 6962 474 -954 -856 C ATOM 565 CB BLEU A 432 -7.729 25.987 -1.053 0.50 52.13 C ANISOU 565 CB BLEU A 432 7262 5588 6955 475 -948 -857 C ATOM 566 CG ALEU A 432 -6.447 26.091 -0.252 0.50 59.06 C ANISOU 566 CG ALEU A 432 8152 6437 7850 377 -950 -774 C ATOM 567 CG BLEU A 432 -7.302 27.392 -1.452 0.50 59.35 C ANISOU 567 CG BLEU A 432 8479 6129 7942 412 -1388 -847 C ATOM 568 CD1ALEU A 432 -5.236 26.453 -1.090 0.50 59.34 C ANISOU 568 CD1ALEU A 432 8332 6274 7942 30 -1037 -531 C ATOM 569 CD1BLEU A 432 -7.525 28.408 -0.334 0.50 71.13 C ANISOU 569 CD1BLEU A 432 10073 7531 9423 730 -1742 -1114 C ATOM 570 CD2ALEU A 432 -6.606 27.126 0.851 0.50 58.11 C ANISOU 570 CD2ALEU A 432 8119 6246 7714 652 -1271 -1010 C ATOM 571 CD2BLEU A 432 -5.823 27.375 -1.856 0.50 65.10 C ANISOU 571 CD2BLEU A 432 9272 6761 8704 27 -1347 -563 C ATOM 572 H LEU A 432 -9.352 26.047 -2.822 1.00 50.93 H ATOM 573 HA LEU A 432 -6.944 25.069 -2.741 1.00 61.37 H ATOM 574 HB2ALEU A 432 -7.891 26.895 -1.423 0.50 62.62 H ATOM 575 HB2BLEU A 432 -8.613 26.042 -0.656 0.50 62.58 H ATOM 576 HB3ALEU A 432 -8.435 25.761 -0.452 0.50 62.62 H ATOM 577 HB3BLEU A 432 -7.093 25.652 -0.401 0.50 62.58 H ATOM 578 HG ALEU A 432 -6.289 25.212 0.124 0.50 70.89 H ATOM 579 HG BLEU A 432 -7.849 27.677 -2.201 0.50 71.24 H ATOM 580 HD11ALEU A 432 -4.483 26.619 -0.501 0.50 71.24 H ATOM 581 HD11BLEU A 432 -7.278 29.290 -0.655 0.50 85.38 H ATOM 582 HD12ALEU A 432 -5.033 25.716 -1.687 0.50 71.24 H ATOM 583 HD12BLEU A 432 -8.461 28.398 -0.080 0.50 85.38 H ATOM 584 HD13ALEU A 432 -5.434 27.251 -1.604 0.50 71.24 H ATOM 585 HD13BLEU A 432 -6.973 28.166 0.427 0.50 85.38 H ATOM 586 HD21ALEU A 432 -5.738 27.299 1.249 0.50 69.75 H ATOM 587 HD21BLEU A 432 -5.471 28.278 -1.805 0.50 78.15 H ATOM 588 HD22ALEU A 432 -6.964 27.943 0.469 0.50 69.75 H ATOM 589 HD22BLEU A 432 -5.337 26.795 -1.250 0.50 78.15 H ATOM 590 HD23ALEU A 432 -7.214 26.780 1.523 0.50 69.75 H ATOM 591 HD23BLEU A 432 -5.748 27.042 -2.764 0.50 78.15 H ATOM 592 N CYS A 433 -6.765 22.923 -1.697 1.00 38.17 N ANISOU 592 N CYS A 433 5168 4181 5155 83 -154 -472 N ATOM 593 CA CYS A 433 -6.594 21.567 -1.188 1.00 43.89 C ANISOU 593 CA CYS A 433 5749 5091 5836 65 106 -411 C ATOM 594 C CYS A 433 -5.560 21.679 -0.072 1.00 51.35 C ANISOU 594 C CYS A 433 6669 6067 6777 90 93 -407 C ATOM 595 O CYS A 433 -4.359 21.647 -0.324 1.00 47.28 O ANISOU 595 O CYS A 433 6173 5497 6292 -37 109 -307 O ATOM 596 CB CYS A 433 -6.129 20.707 -2.258 1.00 46.47 C ANISOU 596 CB CYS A 433 6078 5391 6186 -94 251 -277 C ATOM 597 SG CYS A 433 -7.489 20.154 -3.298 1.00 46.77 S ANISOU 597 SG CYS A 433 6114 5446 6211 -107 317 -283 S ATOM 598 H CYS A 433 -6.022 23.247 -1.986 1.00 45.83 H ATOM 599 HA CYS A 433 -7.422 21.208 -0.831 1.00 52.69 H ATOM 600 HB2 CYS A 433 -5.500 21.196 -2.812 1.00 55.78 H ATOM 601 HB3 CYS A 433 -5.698 19.926 -1.878 1.00 55.78 H ATOM 602 N GLU A 434 -5.993 21.873 1.148 1.00 45.18 N ANISOU 602 N GLU A 434 5820 5415 5931 254 52 -527 N ATOM 603 CA GLU A 434 -4.998 22.005 2.215 1.00 49.09 C ANISOU 603 CA GLU A 434 6298 5933 6420 280 28 -526 C ATOM 604 C GLU A 434 -5.523 21.324 3.462 1.00 46.83 C ANISOU 604 C GLU A 434 5870 5911 6013 386 135 -577 C ATOM 605 O GLU A 434 -6.682 20.900 3.509 1.00 47.29 O ANISOU 605 O GLU A 434 5831 6163 5974 421 201 -616 O ATOM 606 CB GLU A 434 -4.673 23.466 2.468 1.00 54.90 C ANISOU 606 CB GLU A 434 7157 6504 7197 354 -257 -631 C ATOM 607 CG GLU A 434 -5.872 24.237 2.923 1.00 73.62 C ANISOU 607 CG GLU A 434 9528 8935 9507 611 -441 -865 C ATOM 608 CD GLU A 434 -5.517 25.691 3.330 1.00 89.78 C ANISOU 608 CD GLU A 434 11753 10761 11597 736 -816 -1007 C ATOM 609 OE1 GLU A 434 -4.316 26.138 3.261 1.00 89.17 O ANISOU 609 OE1 GLU A 434 11804 10481 11596 555 -931 -879 O ATOM 610 OE2 GLU A 434 -6.483 26.381 3.738 1.00104.56 O ANISOU 610 OE2 GLU A 434 13632 12688 13408 1026 -1024 -1264 O ATOM 611 H GLU A 434 -6.818 21.931 1.385 1.00 54.24 H ATOM 612 HA GLU A 434 -4.176 21.555 1.966 1.00 58.93 H ATOM 613 HB2 GLU A 434 -3.994 23.526 3.158 1.00 65.90 H ATOM 614 HB3 GLU A 434 -4.348 23.866 1.647 1.00 65.90 H ATOM 615 HG2 GLU A 434 -6.518 24.275 2.200 1.00 88.36 H ATOM 616 HG3 GLU A 434 -6.261 23.794 3.693 1.00 88.36 H ATOM 617 N PHE A 435 -4.628 21.113 4.431 1.00 44.47 N ANISOU 617 N PHE A 435 5544 5656 5697 390 158 -546 N ATOM 618 CA PHE A 435 -5.035 20.459 5.659 1.00 47.32 C ANISOU 618 CA PHE A 435 5776 6289 5914 442 242 -557 C ATOM 619 C PHE A 435 -6.030 21.369 6.349 1.00 48.44 C ANISOU 619 C PHE A 435 5822 6650 5932 655 118 -781 C ATOM 620 O PHE A 435 -5.744 22.566 6.500 1.00 48.41 O ANISOU 620 O PHE A 435 5900 6512 5981 807 -90 -936 O ATOM 621 CB PHE A 435 -3.895 20.196 6.635 1.00 43.86 C ANISOU 621 CB PHE A 435 5337 5854 5473 434 254 -503 C ATOM 622 CG PHE A 435 -4.437 19.609 7.881 1.00 45.63 C ANISOU 622 CG PHE A 435 5435 6388 5516 458 312 -500 C ATOM 623 CD1 PHE A 435 -4.777 18.256 7.925 1.00 46.97 C ANISOU 623 CD1 PHE A 435 5586 6653 5606 288 427 -322 C ATOM 624 CD2 PHE A 435 -4.800 20.424 8.955 1.00 52.10 C ANISOU 624 CD2 PHE A 435 6150 7439 6207 638 219 -682 C ATOM 625 CE1 PHE A 435 -5.383 17.706 9.063 1.00 55.47 C ANISOU 625 CE1 PHE A 435 6539 8071 6465 227 458 -271 C ATOM 626 CE2 PHE A 435 -5.372 19.877 10.105 1.00 52.18 C ANISOU 626 CE2 PHE A 435 5996 7843 5987 628 284 -671 C ATOM 627 CZ PHE A 435 -5.689 18.528 10.151 1.00 56.41 C ANISOU 627 CZ PHE A 435 6506 8498 6428 390 409 -443 C ATOM 628 H PHE A 435 -3.799 21.337 4.396 1.00 53.39 H ATOM 629 HA PHE A 435 -5.405 19.594 5.424 1.00 56.81 H ATOM 630 HB2 PHE A 435 -3.264 19.572 6.242 1.00 52.65 H ATOM 631 HB3 PHE A 435 -3.447 21.029 6.849 1.00 52.65 H ATOM 632 HD1 PHE A 435 -4.599 17.713 7.191 1.00 56.39 H ATOM 633 HD2 PHE A 435 -4.659 21.342 8.903 1.00 62.55 H ATOM 634 HE1 PHE A 435 -5.581 16.797 9.094 1.00 66.58 H ATOM 635 HE2 PHE A 435 -5.541 20.419 10.842 1.00 62.64 H ATOM 636 HZ PHE A 435 -6.103 18.172 10.903 1.00 67.71 H ATOM 637 N PRO A 436 -7.251 20.868 6.756 1.00 49.97 N ANISOU 637 N PRO A 436 5838 7212 5936 676 203 -821 N ATOM 638 CA PRO A 436 -7.784 19.482 6.600 1.00 48.74 C ANISOU 638 CA PRO A 436 5611 7219 5689 446 382 -617 C ATOM 639 C PRO A 436 -8.552 19.220 5.326 1.00 53.51 C ANISOU 639 C PRO A 436 6247 7738 6347 359 419 -575 C ATOM 640 O PRO A 436 -9.260 20.108 4.827 1.00 56.01 O ANISOU 640 O PRO A 436 6538 8074 6668 515 323 -753 O ATOM 641 CB PRO A 436 -8.757 19.324 7.785 1.00 59.89 C ANISOU 641 CB PRO A 436 6773 9173 6809 481 412 -691 C ATOM 642 CG PRO A 436 -9.306 20.677 7.929 1.00 57.80 C ANISOU 642 CG PRO A 436 6423 9043 6495 804 256 -1014 C ATOM 643 CD PRO A 436 -8.142 21.657 7.622 1.00 55.40 C ANISOU 643 CD PRO A 436 6357 8257 6436 932 90 -1086 C ATOM 644 HA PRO A 436 -7.018 18.889 6.662 1.00 58.51 H ATOM 645 HB2 PRO A 436 -9.450 18.679 7.572 1.00 71.89 H ATOM 646 HB3 PRO A 436 -8.280 19.046 8.583 1.00 71.89 H ATOM 647 HG2 PRO A 436 -10.033 20.802 7.298 1.00 69.38 H ATOM 648 HG3 PRO A 436 -9.628 20.802 8.835 1.00 69.38 H ATOM 649 HD2 PRO A 436 -8.467 22.443 7.156 1.00 66.51 H ATOM 650 HD3 PRO A 436 -7.688 21.918 8.438 1.00 66.51 H ATOM 651 N LEU A 437 -8.392 18.034 4.744 1.00 50.99 N ANISOU 651 N LEU A 437 6010 7286 6077 136 519 -359 N ATOM 652 CA LEU A 437 -9.237 17.691 3.623 1.00 51.15 C ANISOU 652 CA LEU A 437 6046 7271 6119 43 552 -319 C ATOM 653 C LEU A 437 -10.618 17.385 4.162 1.00 59.77 C ANISOU 653 C LEU A 437 6922 8820 6967 -23 587 -331 C ATOM 654 O LEU A 437 -10.786 17.138 5.354 1.00 52.16 O ANISOU 654 O LEU A 437 5816 8194 5810 -67 605 -306 O ATOM 655 CB LEU A 437 -8.720 16.478 2.863 1.00 55.49 C ANISOU 655 CB LEU A 437 6756 7556 6771 -146 601 -119 C ATOM 656 CG LEU A 437 -7.352 16.693 2.240 1.00 49.27 C ANISOU 656 CG LEU A 437 6113 6438 6169 -84 583 -123 C ATOM 657 CD1 LEU A 437 -6.944 15.474 1.435 1.00 52.72 C ANISOU 657 CD1 LEU A 437 6682 6675 6675 -193 601 2 C ATOM 658 CD2 LEU A 437 -7.320 17.885 1.287 1.00 56.90 C ANISOU 658 CD2 LEU A 437 7110 7273 7236 10 531 -242 C ATOM 659 H LEU A 437 -7.819 17.436 4.977 1.00 61.21 H ATOM 660 HA LEU A 437 -9.260 18.426 2.991 1.00 61.41 H ATOM 661 HB2 LEU A 437 -8.653 15.730 3.477 1.00 66.61 H ATOM 662 HB3 LEU A 437 -9.342 16.267 2.150 1.00 66.61 H ATOM 663 HG LEU A 437 -6.738 16.857 2.973 1.00 59.15 H ATOM 664 HD11 LEU A 437 -6.141 15.682 0.932 1.00 63.29 H ATOM 665 HD12 LEU A 437 -6.772 14.738 2.042 1.00 63.29 H ATOM 666 HD13 LEU A 437 -7.663 15.241 0.828 1.00 63.29 H ATOM 667 HD21 LEU A 437 -6.463 17.904 0.833 1.00 68.30 H ATOM 668 HD22 LEU A 437 -8.035 17.789 0.638 1.00 68.30 H ATOM 669 HD23 LEU A 437 -7.443 18.700 1.797 1.00 68.30 H ATOM 670 N ARG A 438 -11.601 17.396 3.288 1.00 57.41 N ANISOU 670 N ARG A 438 6577 8585 6650 -50 594 -363 N ATOM 671 CA ARG A 438 -12.945 17.057 3.748 1.00 62.87 C ANISOU 671 CA ARG A 438 7015 9801 7071 -152 632 -365 C ATOM 672 C ARG A 438 -12.967 15.562 3.941 1.00 59.00 C ANISOU 672 C ARG A 438 6584 9334 6500 -528 680 -50 C ATOM 673 O ARG A 438 -13.058 14.800 2.982 1.00 59.76 O ANISOU 673 O ARG A 438 6837 9168 6702 -700 676 97 O ATOM 674 CB ARG A 438 -13.997 17.510 2.752 1.00 66.75 C ANISOU 674 CB ARG A 438 7433 10367 7561 -64 606 -500 C ATOM 675 CG ARG A 438 -14.231 19.014 2.818 1.00 68.13 C ANISOU 675 CG ARG A 438 7536 10608 7743 329 473 -842 C ATOM 676 CD ARG A 438 -15.027 19.553 1.596 1.00 80.11 C ANISOU 676 CD ARG A 438 9080 12023 9334 448 392 -975 C ATOM 677 NE ARG A 438 -14.378 19.245 0.327 1.00 82.19 N ANISOU 677 NE ARG A 438 9623 11754 9852 299 413 -803 N ATOM 678 CZ ARG A 438 -14.966 19.276 -0.866 1.00 79.90 C ANISOU 678 CZ ARG A 438 9390 11337 9631 276 391 -808 C ATOM 679 NH1 ARG A 438 -16.225 19.680 -1.009 1.00 64.49 N ANISOU 679 NH1 ARG A 438 7251 9713 7539 415 329 -991 N ATOM 680 NH2 ARG A 438 -14.285 18.870 -1.934 1.00 65.42 N ANISOU 680 NH2 ARG A 438 7781 9087 7987 124 427 -643 N ATOM 681 H ARG A 438 -11.526 17.587 2.453 1.00 68.92 H ATOM 682 HA ARG A 438 -13.143 17.505 4.585 1.00 75.46 H ATOM 683 HB2 ARG A 438 -13.704 17.287 1.855 1.00 80.12 H ATOM 684 HB3 ARG A 438 -14.835 17.063 2.948 1.00 80.12 H ATOM 685 HG2 ARG A 438 -14.736 19.221 3.620 1.00 81.78 H ATOM 686 HG3 ARG A 438 -13.373 19.467 2.840 1.00 81.78 H ATOM 687 HD2 ARG A 438 -15.909 19.149 1.589 1.00 96.15 H ATOM 688 HD3 ARG A 438 -15.105 20.517 1.669 1.00 96.15 H ATOM 689 HE ARG A 438 -13.547 19.026 0.352 1.00 98.65 H ATOM 690 HH11 ARG A 438 -16.677 19.929 -0.321 1.00 77.41 H ATOM 691 HH12 ARG A 438 -16.586 19.693 -1.789 1.00 77.41 H ATOM 692 HH21 ARG A 438 -13.476 18.592 -1.848 1.00 78.52 H ATOM 693 HH22 ARG A 438 -14.655 18.885 -2.711 1.00 78.52 H ATOM 694 N SER A 439 -12.901 15.134 5.197 1.00 62.66 N ANISOU 694 N SER A 439 6939 10107 6760 -661 687 55 N ATOM 695 CA SER A 439 -12.558 13.745 5.476 1.00 72.96 C ANISOU 695 CA SER A 439 8412 11275 8034 -1012 647 378 C ATOM 696 C SER A 439 -13.704 12.794 5.164 1.00 75.43 C ANISOU 696 C SER A 439 8669 11825 8167 -1382 622 592 C ATOM 697 O SER A 439 -13.460 11.626 4.834 1.00 68.57 O ANISOU 697 O SER A 439 8056 10631 7367 -1654 516 847 O ATOM 698 CB SER A 439 -12.153 13.574 6.938 1.00 72.07 C ANISOU 698 CB SER A 439 8219 11427 7737 -1086 632 459 C ATOM 699 OG SER A 439 -13.183 13.959 7.832 1.00 72.54 O ANISOU 699 OG SER A 439 7913 12201 7445 -1124 682 382 O ATOM 700 H SER A 439 -13.046 15.618 5.893 1.00 75.21 H ATOM 701 HA SER A 439 -11.803 13.513 4.913 1.00 87.58 H ATOM 702 HB2 SER A 439 -11.942 12.640 7.094 1.00 86.51 H ATOM 703 HB3 SER A 439 -11.373 14.124 7.110 1.00 86.51 H ATOM 704 HG SER A 439 -12.929 13.854 8.626 1.00 87.07 H ATOM 705 N HIS A 440 -14.955 13.262 5.308 1.00 69.53 N ANISOU 705 N HIS A 440 7587 11663 7170 -1394 683 482 N ATOM 706 CA HIS A 440 -16.141 12.478 4.956 1.00 79.12 C ANISOU 706 CA HIS A 440 8693 13186 8183 -1766 662 674 C ATOM 707 C HIS A 440 -16.200 12.173 3.456 1.00 76.54 C ANISOU 707 C HIS A 440 8608 12352 8120 -1766 627 694 C ATOM 708 O HIS A 440 -16.968 11.301 3.032 1.00 73.17 O ANISOU 708 O HIS A 440 8205 12003 7593 -2117 564 906 O ATOM 709 CB HIS A 440 -17.438 13.203 5.447 1.00 77.04 C ANISOU 709 CB HIS A 440 7941 13769 7560 -1698 745 475 C ATOM 710 CG HIS A 440 -17.694 14.523 4.776 1.00 82.34 C ANISOU 710 CG HIS A 440 8505 14415 8366 -1201 778 70 C ATOM 711 ND1 HIS A 440 -17.083 15.693 5.177 1.00 77.56 N ANISOU 711 ND1 HIS A 440 7882 13728 7858 -750 765 -238 N ATOM 712 CD2 HIS A 440 -18.452 14.846 3.701 1.00 82.71 C ANISOU 712 CD2 HIS A 440 8507 14443 8478 -1096 776 -63 C ATOM 713 CE1 HIS A 440 -17.467 16.682 4.387 1.00 76.44 C ANISOU 713 CE1 HIS A 440 7712 13500 7833 -400 721 -535 C ATOM 714 NE2 HIS A 440 -18.273 16.189 3.464 1.00 82.84 N ANISOU 714 NE2 HIS A 440 8505 14337 8633 -592 739 -436 N ATOM 715 H HIS A 440 -15.142 14.044 5.612 1.00 83.46 H ATOM 716 HA HIS A 440 -16.118 11.627 5.422 1.00 94.97 H ATOM 717 HB2 HIS A 440 -18.201 12.630 5.269 1.00 92.47 H ATOM 718 HB3 HIS A 440 -17.361 13.367 6.399 1.00 92.47 H ATOM 719 HD2 HIS A 440 -18.994 14.268 3.214 1.00 99.28 H ATOM 720 HE1 HIS A 440 -17.213 17.573 4.468 1.00 91.76 H ATOM 721 HE2 HIS A 440 -18.628 16.635 2.820 1.00 99.43 H ATOM 722 N LEU A 441 -15.392 12.828 2.638 1.00 65.31 N ANISOU 722 N LEU A 441 7373 10430 7014 -1419 647 501 N ATOM 723 CA LEU A 441 -15.366 12.535 1.210 1.00 66.42 C ANISOU 723 CA LEU A 441 7732 10124 7380 -1413 616 515 C ATOM 724 C LEU A 441 -14.385 11.402 0.849 1.00 66.16 C ANISOU 724 C LEU A 441 8066 9542 7530 -1550 502 712 C ATOM 725 O LEU A 441 -14.154 11.143 -0.342 1.00 58.42 O ANISOU 725 O LEU A 441 7281 8175 6742 -1491 466 689 O ATOM 726 CB LEU A 441 -15.027 13.839 0.456 1.00 65.06 C ANISOU 726 CB LEU A 441 7560 9751 7409 -1009 668 221 C ATOM 727 CG LEU A 441 -15.990 15.024 0.673 1.00 77.29 C ANISOU 727 CG LEU A 441 8805 11754 8806 -780 695 -41 C ATOM 728 CD1 LEU A 441 -15.809 16.094 -0.375 1.00 70.12 C ANISOU 728 CD1 LEU A 441 7998 10533 8111 -477 657 -259 C ATOM 729 CD2 LEU A 441 -17.444 14.629 0.642 1.00 73.19 C ANISOU 729 CD2 LEU A 441 8032 11748 8030 -987 711 4 C ATOM 730 H LEU A 441 -14.848 13.448 2.884 1.00 78.40 H ATOM 731 HA LEU A 441 -16.238 12.235 0.908 1.00 79.73 H ATOM 732 HB2 LEU A 441 -14.146 14.130 0.740 1.00 78.10 H ATOM 733 HB3 LEU A 441 -15.021 13.645 -0.495 1.00 78.10 H ATOM 734 HG LEU A 441 -15.770 15.362 1.555 1.00 92.77 H ATOM 735 HD11 LEU A 441 -16.417 16.826 -0.187 1.00 84.16 H ATOM 736 HD12 LEU A 441 -14.893 16.411 -0.348 1.00 84.16 H ATOM 737 HD13 LEU A 441 -16.004 15.718 -1.248 1.00 84.16 H ATOM 738 HD21 LEU A 441 -17.989 15.417 0.793 1.00 87.86 H ATOM 739 HD22 LEU A 441 -17.649 14.247 -0.226 1.00 87.86 H ATOM 740 HD23 LEU A 441 -17.609 13.974 1.338 1.00 87.86 H ATOM 741 N GLU A 442 -13.733 10.785 1.831 1.00 62.79 N ANISOU 741 N GLU A 442 7740 9069 7048 -1676 423 868 N ATOM 742 CA GLU A 442 -12.825 9.678 1.523 1.00 64.83 C ANISOU 742 CA GLU A 442 8360 8807 7464 -1748 249 1012 C ATOM 743 C GLU A 442 -11.724 10.004 0.509 1.00 50.96 C ANISOU 743 C GLU A 442 6768 6604 5990 -1404 275 815 C ATOM 744 O GLU A 442 -11.743 9.497 -0.613 1.00 59.31 O ANISOU 744 O GLU A 442 7994 7377 7165 -1396 202 806 O ATOM 745 CB GLU A 442 -13.713 8.526 1.046 1.00 61.99 C ANISOU 745 CB GLU A 442 8142 8391 7020 -2122 78 1246 C ATOM 746 CG GLU A 442 -14.523 7.877 2.237 1.00 81.31 C ANISOU 746 CG GLU A 442 10485 11270 9140 -2591 -24 1546 C ATOM 747 CD GLU A 442 -15.610 6.871 1.785 1.00 86.94 C ANISOU 747 CD GLU A 442 11289 12029 9716 -3051 -205 1809 C ATOM 748 OE1 GLU A 442 -15.955 6.808 0.589 1.00 93.71 O ANISOU 748 OE1 GLU A 442 12224 12672 10710 -2982 -211 1727 O ATOM 749 OE2 GLU A 442 -16.124 6.115 2.623 1.00 93.85 O ANISOU 749 OE2 GLU A 442 12167 13163 10329 -3521 -366 2124 O ATOM 750 H GLU A 442 -13.797 10.982 2.665 1.00 75.37 H ATOM 751 HA GLU A 442 -12.312 9.448 2.314 1.00 77.81 H ATOM 752 HB2 GLU A 442 -14.347 8.861 0.393 1.00 74.41 H ATOM 753 HB3 GLU A 442 -13.157 7.839 0.647 1.00 74.41 H ATOM 754 HG2 GLU A 442 -13.904 7.403 2.813 1.00 97.60 H ATOM 755 HG3 GLU A 442 -14.964 8.583 2.734 1.00 97.60 H ATOM 756 N PRO A 443 -10.850 10.944 0.816 1.00 52.69 N ANISOU 756 N PRO A 443 6904 6823 6293 -1130 381 645 N ATOM 757 CA PRO A 443 -9.630 11.151 0.009 1.00 49.10 C ANISOU 757 CA PRO A 443 6580 6027 6048 -870 388 501 C ATOM 758 C PRO A 443 -8.759 9.907 0.040 1.00 47.59 C ANISOU 758 C PRO A 443 6651 5514 5918 -879 201 585 C ATOM 759 O PRO A 443 -8.865 9.097 0.962 1.00 47.64 O ANISOU 759 O PRO A 443 6758 5521 5823 -1068 57 761 O ATOM 760 CB PRO A 443 -8.921 12.296 0.728 1.00 49.74 C ANISOU 760 CB PRO A 443 6517 6236 6145 -676 488 370 C ATOM 761 CG PRO A 443 -9.400 12.156 2.092 1.00 54.24 C ANISOU 761 CG PRO A 443 6982 7096 6532 -820 475 476 C ATOM 762 CD PRO A 443 -10.803 11.638 2.099 1.00 53.85 C ANISOU 762 CD PRO A 443 6856 7296 6309 -1089 453 611 C ATOM 763 HA PRO A 443 -9.848 11.406 -0.901 1.00 58.94 H ATOM 764 HB2 PRO A 443 -7.958 12.187 0.675 1.00 59.71 H ATOM 765 HB3 PRO A 443 -9.179 13.149 0.346 1.00 59.71 H ATOM 766 HG2 PRO A 443 -8.820 11.535 2.560 1.00 65.12 H ATOM 767 HG3 PRO A 443 -9.370 13.025 2.520 1.00 65.12 H ATOM 768 HD2 PRO A 443 -10.951 11.027 2.838 1.00 64.65 H ATOM 769 HD3 PRO A 443 -11.447 12.363 2.133 1.00 64.65 H ATOM 770 N THR A 444 -7.902 9.742 -0.969 1.00 44.57 N ANISOU 770 N THR A 444 6378 4881 5676 -671 170 451 N ATOM 771 CA THR A 444 -7.002 8.577 -0.999 1.00 42.74 C ANISOU 771 CA THR A 444 6392 4352 5497 -578 -56 450 C ATOM 772 C THR A 444 -5.974 8.704 0.128 1.00 37.73 C ANISOU 772 C THR A 444 5737 3746 4852 -470 -74 438 C ATOM 773 O THR A 444 -5.708 9.796 0.591 1.00 37.91 O ANISOU 773 O THR A 444 5554 3983 4866 -406 109 377 O ATOM 774 CB THR A 444 -6.235 8.524 -2.321 1.00 46.75 C ANISOU 774 CB THR A 444 6933 4721 6107 -315 -58 242 C ATOM 775 OG1 THR A 444 -5.576 9.788 -2.508 1.00 44.96 O ANISOU 775 OG1 THR A 444 6477 4698 5908 -170 162 109 O ATOM 776 CG2 THR A 444 -7.149 8.309 -3.504 1.00 49.23 C ANISOU 776 CG2 THR A 444 7294 4976 6436 -395 -65 239 C ATOM 777 H THR A 444 -7.820 10.277 -1.637 1.00 53.51 H ATOM 778 HA THR A 444 -7.525 7.767 -0.899 1.00 51.32 H ATOM 779 HB THR A 444 -5.608 7.785 -2.288 1.00 56.12 H ATOM 780 HG1 THR A 444 -5.246 9.829 -3.279 1.00 53.98 H ATOM 781 HG21 THR A 444 -6.648 8.394 -4.330 1.00 59.10 H ATOM 782 HG22 THR A 444 -7.542 7.423 -3.463 1.00 59.10 H ATOM 783 HG23 THR A 444 -7.860 8.969 -3.498 1.00 59.10 H ATOM 784 N ASN A 445 -5.418 7.588 0.597 1.00 39.71 N ANISOU 784 N ASN A 445 6226 3759 5102 -449 -336 496 N ATOM 785 CA ASN A 445 -4.319 7.713 1.538 1.00 42.10 C ANISOU 785 CA ASN A 445 6507 4082 5407 -299 -360 451 C ATOM 786 C ASN A 445 -3.214 8.611 0.988 1.00 47.17 C ANISOU 786 C ASN A 445 6952 4843 6128 -1 -182 210 C ATOM 787 O ASN A 445 -2.638 9.409 1.732 1.00 39.88 O ANISOU 787 O ASN A 445 5871 4090 5192 50 -59 181 O ATOM 788 CB ASN A 445 -3.838 6.309 1.904 1.00 46.46 C ANISOU 788 CB ASN A 445 7392 4298 5962 -267 -736 512 C ATOM 789 CG ASN A 445 -4.879 5.596 2.759 1.00 49.87 C ANISOU 789 CG ASN A 445 7998 4686 6266 -678 -921 832 C ATOM 790 OD1 ASN A 445 -5.650 6.278 3.402 1.00 46.03 O ANISOU 790 OD1 ASN A 445 7298 4529 5663 -915 -717 965 O ATOM 791 ND2 ASN A 445 -4.786 4.303 2.910 1.00 47.66 N ANISOU 791 ND2 ASN A 445 8085 4043 5980 -753 -1328 948 N ATOM 792 H ASN A 445 -5.650 6.785 0.394 1.00 47.53 H ATOM 793 HA ASN A 445 -4.612 8.141 2.359 1.00 50.55 H ATOM 794 HB2 ASN A 445 -3.696 5.794 1.095 1.00 55.78 H ATOM 795 HB3 ASN A 445 -3.012 6.370 2.408 1.00 55.78 H ATOM 796 HD21 ASN A 445 -4.147 3.870 2.531 1.00 57.07 H ATOM 797 HD22 ASN A 445 -5.364 3.883 3.389 1.00 57.07 H ATOM 798 N HIS A 446 -2.905 8.493 -0.299 1.00 43.41 N ANISOU 798 N HIS A 446 6474 4313 5706 169 -180 45 N ATOM 799 CA HIS A 446 -1.797 9.289 -0.840 1.00 39.56 C ANISOU 799 CA HIS A 446 5775 4020 5238 388 -32 -152 C ATOM 800 C HIS A 446 -2.104 10.756 -0.682 1.00 37.94 C ANISOU 800 C HIS A 446 5348 4040 5026 252 215 -106 C ATOM 801 O HIS A 446 -1.243 11.578 -0.354 1.00 37.51 O ANISOU 801 O HIS A 446 5139 4145 4967 315 304 -164 O ATOM 802 CB HIS A 446 -1.571 8.934 -2.319 1.00 42.78 C ANISOU 802 CB HIS A 446 6182 4422 5652 553 -62 -325 C ATOM 803 CG HIS A 446 -0.345 9.586 -2.877 1.00 45.01 C ANISOU 803 CG HIS A 446 6220 4991 5890 740 58 -512 C ATOM 804 ND1 HIS A 446 -0.339 10.880 -3.354 1.00 40.72 N ANISOU 804 ND1 HIS A 446 5457 4690 5324 607 283 -488 N ATOM 805 CD2 HIS A 446 0.920 9.127 -3.004 1.00 43.86 C ANISOU 805 CD2 HIS A 446 6007 4967 5691 1028 -44 -718 C ATOM 806 CE1 HIS A 446 0.886 11.207 -3.706 1.00 42.15 C ANISOU 806 CE1 HIS A 446 5437 5150 5426 740 327 -627 C ATOM 807 NE2 HIS A 446 1.677 10.161 -3.509 1.00 45.46 N ANISOU 807 NE2 HIS A 446 5912 5545 5817 1016 153 -789 N ATOM 808 H HIS A 446 -3.302 7.981 -0.864 1.00 52.11 H ATOM 809 HA HIS A 446 -0.976 9.085 -0.364 1.00 47.50 H ATOM 810 HB2 HIS A 446 -1.468 7.973 -2.404 1.00 51.36 H ATOM 811 HB3 HIS A 446 -2.335 9.233 -2.838 1.00 51.36 H ATOM 812 HD1 HIS A 446 -1.028 11.393 -3.412 1.00 48.88 H ATOM 813 HD2 HIS A 446 1.223 8.274 -2.791 1.00 52.65 H ATOM 814 HE1 HIS A 446 1.153 12.033 -4.038 1.00 50.60 H ATOM 815 N ALA A 447 -3.338 11.125 -0.951 1.00 37.44 N ANISOU 815 N ALA A 447 5277 3989 4959 72 294 -14 N ATOM 816 CA ALA A 447 -3.635 12.532 -0.879 1.00 37.42 C ANISOU 816 CA ALA A 447 5104 4159 4954 2 454 -16 C ATOM 817 C ALA A 447 -3.602 13.013 0.571 1.00 36.22 C ANISOU 817 C ALA A 447 4894 4106 4762 -32 467 38 C ATOM 818 O ALA A 447 -3.297 14.178 0.833 1.00 38.64 O ANISOU 818 O ALA A 447 5083 4522 5077 -6 533 -13 O ATOM 819 CB ALA A 447 -4.997 12.786 -1.499 1.00 39.49 C ANISOU 819 CB ALA A 447 5364 4433 5209 -130 503 30 C ATOM 820 H ALA A 447 -3.988 10.605 -1.167 1.00 44.95 H ATOM 821 HA ALA A 447 -2.978 13.040 -1.380 1.00 44.93 H ATOM 822 HB1 ALA A 447 -5.225 13.722 -1.387 1.00 47.42 H ATOM 823 HB2 ALA A 447 -4.960 12.565 -2.442 1.00 47.42 H ATOM 824 HB3 ALA A 447 -5.655 12.230 -1.054 1.00 47.42 H ATOM 825 N VAL A 448 -3.987 12.159 1.513 1.00 42.83 N ANISOU 825 N VAL A 448 5824 4910 5538 -116 376 152 N ATOM 826 CA VAL A 448 -3.864 12.553 2.919 1.00 35.11 C ANISOU 826 CA VAL A 448 4775 4074 4491 -139 386 195 C ATOM 827 C VAL A 448 -2.402 12.809 3.262 1.00 40.99 C ANISOU 827 C VAL A 448 5490 4796 5286 29 372 105 C ATOM 828 O VAL A 448 -2.059 13.788 3.938 1.00 41.44 O ANISOU 828 O VAL A 448 5432 4981 5333 66 427 60 O ATOM 829 CB VAL A 448 -4.477 11.492 3.839 1.00 37.35 C ANISOU 829 CB VAL A 448 5169 4362 4660 -318 266 375 C ATOM 830 CG1 VAL A 448 -4.175 11.859 5.320 1.00 45.87 C ANISOU 830 CG1 VAL A 448 6162 5624 5643 -325 274 410 C ATOM 831 CG2 VAL A 448 -6.026 11.345 3.629 1.00 38.79 C ANISOU 831 CG2 VAL A 448 5314 4688 4738 -544 291 484 C ATOM 832 H VAL A 448 -4.310 11.374 1.375 1.00 51.42 H ATOM 833 HA VAL A 448 -4.358 13.377 3.051 1.00 42.16 H ATOM 834 HB VAL A 448 -4.078 10.635 3.620 1.00 44.84 H ATOM 835 HG11 VAL A 448 -4.763 11.347 5.898 1.00 55.07 H ATOM 836 HG12 VAL A 448 -3.250 11.644 5.517 1.00 55.07 H ATOM 837 HG13 VAL A 448 -4.329 12.808 5.448 1.00 55.07 H ATOM 838 HG21 VAL A 448 -6.373 10.708 4.274 1.00 46.58 H ATOM 839 HG22 VAL A 448 -6.445 12.210 3.760 1.00 46.58 H ATOM 840 HG23 VAL A 448 -6.194 11.029 2.728 1.00 46.58 H ATOM 841 N ILE A 449 -1.535 11.899 2.873 1.00 38.07 N ANISOU 841 N ILE A 449 5225 4281 4957 147 265 63 N ATOM 842 CA ILE A 449 -0.111 12.038 3.206 1.00 38.31 C ANISOU 842 CA ILE A 449 5195 4356 5008 320 240 -39 C ATOM 843 C ILE A 449 0.465 13.236 2.525 1.00 39.26 C ANISOU 843 C ILE A 449 5130 4635 5153 349 371 -139 C ATOM 844 O ILE A 449 1.165 14.055 3.140 1.00 42.92 O ANISOU 844 O ILE A 449 5485 5214 5610 361 402 -163 O ATOM 845 CB ILE A 449 0.565 10.725 2.779 1.00 37.16 C ANISOU 845 CB ILE A 449 5197 4047 4877 496 55 -115 C ATOM 846 CG1 ILE A 449 0.175 9.699 3.817 1.00 41.89 C ANISOU 846 CG1 ILE A 449 6018 4461 5439 414 -145 34 C ATOM 847 CG2 ILE A 449 2.034 10.816 2.783 1.00 42.52 C ANISOU 847 CG2 ILE A 449 5758 4848 5551 720 32 -277 C ATOM 848 CD1 ILE A 449 0.498 8.252 3.473 1.00 48.42 C ANISOU 848 CD1 ILE A 449 7107 5008 6285 560 -444 -12 C ATOM 849 H ILE A 449 -1.730 11.195 2.419 1.00 45.70 H ATOM 850 HA ILE A 449 0.023 12.181 4.156 1.00 46.00 H ATOM 851 HB ILE A 449 0.283 10.507 1.877 1.00 44.62 H ATOM 852 HG12 ILE A 449 0.642 9.909 4.641 1.00 50.30 H ATOM 853 HG13 ILE A 449 -0.783 9.755 3.955 1.00 50.30 H ATOM 854 HG21 ILE A 449 2.406 9.920 2.778 1.00 51.05 H ATOM 855 HG22 ILE A 449 2.323 11.298 1.992 1.00 51.05 H ATOM 856 HG23 ILE A 449 2.320 11.288 3.581 1.00 51.05 H ATOM 857 HD11 ILE A 449 0.201 7.681 4.199 1.00 58.13 H ATOM 858 HD12 ILE A 449 0.037 8.012 2.654 1.00 58.13 H ATOM 859 HD13 ILE A 449 1.456 8.162 3.352 1.00 58.13 H ATOM 860 N GLN A 450 0.126 13.415 1.244 1.00 40.61 N ANISOU 860 N GLN A 450 5274 4815 5341 318 427 -176 N ATOM 861 CA GLN A 450 0.682 14.572 0.533 1.00 37.26 C ANISOU 861 CA GLN A 450 4693 4552 4911 273 512 -225 C ATOM 862 C GLN A 450 0.197 15.863 1.142 1.00 36.63 C ANISOU 862 C GLN A 450 4586 4484 4848 152 537 -169 C ATOM 863 O GLN A 450 0.969 16.825 1.264 1.00 38.64 O ANISOU 863 O GLN A 450 4754 4834 5095 107 525 -180 O ATOM 864 CB GLN A 450 0.339 14.528 -0.963 1.00 40.32 C ANISOU 864 CB GLN A 450 5068 4963 5291 237 554 -256 C ATOM 865 CG GLN A 450 1.110 15.558 -1.785 1.00 40.35 C ANISOU 865 CG GLN A 450 4909 5181 5240 140 604 -273 C ATOM 866 CD GLN A 450 0.877 15.491 -3.290 1.00 40.21 C ANISOU 866 CD GLN A 450 4855 5247 5175 92 644 -299 C ATOM 867 OE1 GLN A 450 0.553 14.445 -3.866 1.00 44.34 O ANISOU 867 OE1 GLN A 450 5442 5710 5695 216 628 -371 O ATOM 868 NE2 GLN A 450 1.170 16.594 -3.951 1.00 43.10 N ANISOU 868 NE2 GLN A 450 5124 5767 5484 -100 663 -239 N ATOM 869 H GLN A 450 -0.397 12.909 0.786 1.00 48.76 H ATOM 870 HA GLN A 450 1.648 14.532 0.608 1.00 44.73 H ATOM 871 HB2 GLN A 450 0.555 13.648 -1.309 1.00 48.41 H ATOM 872 HB3 GLN A 450 -0.608 14.705 -1.074 1.00 48.41 H ATOM 873 HG2 GLN A 450 0.847 16.444 -1.490 1.00 48.44 H ATOM 874 HG3 GLN A 450 2.058 15.426 -1.632 1.00 48.44 H ATOM 875 HE21 GLN A 450 1.469 17.281 -3.529 1.00 51.74 H ATOM 876 HE22 GLN A 450 1.063 16.626 -4.804 1.00 51.74 H ATOM 877 N THR A 451 -1.072 15.928 1.528 1.00 36.50 N ANISOU 877 N THR A 451 4636 4398 4836 102 541 -123 N ATOM 878 CA THR A 451 -1.585 17.124 2.191 1.00 38.45 C ANISOU 878 CA THR A 451 4853 4680 5077 73 518 -137 C ATOM 879 C THR A 451 -0.876 17.386 3.522 1.00 42.08 C ANISOU 879 C THR A 451 5276 5199 5512 132 476 -152 C ATOM 880 O THR A 451 -0.599 18.543 3.866 1.00 40.05 O ANISOU 880 O THR A 451 4995 4955 5267 132 410 -198 O ATOM 881 CB THR A 451 -3.077 16.891 2.399 1.00 40.43 C ANISOU 881 CB THR A 451 5125 4954 5282 47 534 -118 C ATOM 882 OG1 THR A 451 -3.720 16.719 1.125 1.00 41.19 O ANISOU 882 OG1 THR A 451 5257 4987 5408 -9 563 -109 O ATOM 883 CG2 THR A 451 -3.697 17.979 3.116 1.00 41.77 C ANISOU 883 CG2 THR A 451 5243 5215 5412 95 484 -195 C ATOM 884 H THR A 451 -1.653 15.302 1.421 1.00 43.83 H ATOM 885 HA THR A 451 -1.437 17.914 1.649 1.00 46.17 H ATOM 886 HB THR A 451 -3.195 16.091 2.934 1.00 48.54 H ATOM 887 HG1 THR A 451 -3.607 17.404 0.652 1.00 49.46 H ATOM 888 HG21 THR A 451 -4.636 18.040 2.880 1.00 50.15 H ATOM 889 HG22 THR A 451 -3.621 17.832 4.072 1.00 50.15 H ATOM 890 HG23 THR A 451 -3.261 18.816 2.891 1.00 50.15 H ATOM 891 N LEU A 452 -0.585 16.326 4.283 1.00 39.02 N ANISOU 891 N LEU A 452 4914 4822 5089 177 474 -112 N ATOM 892 CA LEU A 452 0.176 16.483 5.522 1.00 43.94 C ANISOU 892 CA LEU A 452 5505 5506 5683 236 433 -122 C ATOM 893 C LEU A 452 1.579 17.001 5.222 1.00 39.74 C ANISOU 893 C LEU A 452 4904 5004 5192 263 412 -172 C ATOM 894 O LEU A 452 2.052 17.923 5.887 1.00 42.09 O ANISOU 894 O LEU A 452 5158 5346 5488 260 362 -200 O ATOM 895 CB LEU A 452 0.212 15.154 6.296 1.00 39.76 C ANISOU 895 CB LEU A 452 5055 4952 5100 253 390 -43 C ATOM 896 CG LEU A 452 1.229 15.083 7.444 1.00 43.81 C ANISOU 896 CG LEU A 452 5550 5508 5587 332 332 -51 C ATOM 897 CD1 LEU A 452 0.924 16.188 8.441 1.00 42.50 C ANISOU 897 CD1 LEU A 452 5302 5479 5369 327 342 -88 C ATOM 898 CD2 LEU A 452 1.235 13.788 8.267 1.00 42.58 C ANISOU 898 CD2 LEU A 452 5519 5292 5367 323 230 54 C ATOM 899 H LEU A 452 -0.815 15.516 4.106 1.00 46.85 H ATOM 900 HA LEU A 452 -0.263 17.129 6.097 1.00 52.75 H ATOM 901 HB2 LEU A 452 -0.667 15.000 6.678 1.00 47.73 H ATOM 902 HB3 LEU A 452 0.431 14.444 5.672 1.00 47.73 H ATOM 903 HG LEU A 452 2.092 15.153 7.008 1.00 52.59 H ATOM 904 HD11 LEU A 452 1.444 16.038 9.246 1.00 51.03 H ATOM 905 HD12 LEU A 452 1.163 17.042 8.047 1.00 51.03 H ATOM 906 HD13 LEU A 452 -0.023 16.173 8.650 1.00 51.03 H ATOM 907 HD21 LEU A 452 2.119 13.656 8.642 1.00 51.12 H ATOM 908 HD22 LEU A 452 0.581 13.863 8.980 1.00 51.12 H ATOM 909 HD23 LEU A 452 1.007 13.044 7.687 1.00 51.12 H ATOM 910 N MET A 453 2.237 16.459 4.206 1.00 37.81 N ANISOU 910 N MET A 453 4630 4777 4960 282 434 -192 N ATOM 911 CA MET A 453 3.579 16.959 3.880 1.00 40.56 C ANISOU 911 CA MET A 453 4845 5278 5288 270 422 -234 C ATOM 912 C MET A 453 3.530 18.389 3.412 1.00 38.60 C ANISOU 912 C MET A 453 4566 5053 5049 90 393 -198 C ATOM 913 O MET A 453 4.414 19.191 3.718 1.00 37.32 O ANISOU 913 O MET A 453 4333 4983 4864 5 328 -185 O ATOM 914 CB MET A 453 4.198 16.056 2.834 1.00 42.19 C ANISOU 914 CB MET A 453 4983 5594 5454 359 446 -304 C ATOM 915 CG MET A 453 4.604 14.746 3.471 1.00 43.10 C ANISOU 915 CG MET A 453 5162 5654 5561 573 371 -366 C ATOM 916 SD MET A 453 5.047 13.627 2.113 1.00 51.39 S ANISOU 916 SD MET A 453 6172 6796 6559 762 337 -518 S ATOM 917 CE MET A 453 6.742 14.153 1.843 1.00 45.86 C ANISOU 917 CE MET A 453 5155 6539 5731 814 363 -642 C ATOM 918 H MET A 453 1.946 15.825 3.703 1.00 45.40 H ATOM 919 HA MET A 453 4.138 16.928 4.672 1.00 48.69 H ATOM 920 HB2 MET A 453 3.553 15.877 2.132 1.00 50.65 H ATOM 921 HB3 MET A 453 4.986 16.480 2.460 1.00 50.65 H ATOM 922 HG2 MET A 453 5.371 14.873 4.051 1.00 51.75 H ATOM 923 HG3 MET A 453 3.865 14.370 3.975 1.00 51.75 H ATOM 924 HE1 MET A 453 7.134 13.607 1.143 1.00 55.06 H ATOM 925 HE2 MET A 453 6.745 15.085 1.577 1.00 55.06 H ATOM 926 HE3 MET A 453 7.242 14.042 2.667 1.00 55.06 H ATOM 927 N ASN A 454 2.475 18.751 2.695 1.00 41.87 N ANISOU 927 N ASN A 454 5056 5360 5491 15 400 -172 N ATOM 928 CA ASN A 454 2.375 20.143 2.240 1.00 39.02 C ANISOU 928 CA ASN A 454 4730 4953 5143 -158 294 -131 C ATOM 929 C ASN A 454 2.085 21.076 3.400 1.00 43.57 C ANISOU 929 C ASN A 454 5388 5417 5751 -118 157 -167 C ATOM 930 O ASN A 454 2.594 22.194 3.418 1.00 42.26 O ANISOU 930 O ASN A 454 5259 5208 5589 -249 -7 -137 O ATOM 931 CB ASN A 454 1.312 20.249 1.177 1.00 36.95 C ANISOU 931 CB ASN A 454 4542 4596 4902 -213 308 -114 C ATOM 932 CG ASN A 454 0.926 21.676 0.893 1.00 43.58 C ANISOU 932 CG ASN A 454 5493 5297 5768 -348 124 -84 C ATOM 933 OD1 ASN A 454 -0.064 22.171 1.422 1.00 40.40 O ANISOU 933 OD1 ASN A 454 5191 4754 5405 -240 29 -157 O ATOM 934 ND2 ASN A 454 1.672 22.319 0.007 1.00 43.91 N ANISOU 934 ND2 ASN A 454 5516 5403 5764 -585 42 18 N ATOM 935 H ASN A 454 1.826 18.236 2.463 1.00 50.26 H ATOM 936 HA ASN A 454 3.215 20.421 1.843 1.00 46.85 H ATOM 937 HB2 ASN A 454 1.645 19.858 0.354 1.00 44.37 H ATOM 938 HB3 ASN A 454 0.519 19.776 1.472 1.00 44.37 H ATOM 939 HD21 ASN A 454 2.334 21.919 -0.369 1.00 52.71 H ATOM 940 HD22 ASN A 454 1.494 23.137 -0.191 1.00 52.71 H ATOM 941 N SER A 455 1.369 20.608 4.418 1.00 43.97 N ANISOU 941 N SER A 455 5458 5450 5797 48 195 -228 N ATOM 942 CA SER A 455 1.211 21.408 5.626 1.00 46.02 C ANISOU 942 CA SER A 455 5753 5684 6047 136 68 -305 C ATOM 943 C SER A 455 2.516 21.476 6.422 1.00 46.38 C ANISOU 943 C SER A 455 5744 5797 6082 127 31 -291 C ATOM 944 O SER A 455 2.885 22.548 6.955 1.00 46.82 O ANISOU 944 O SER A 455 5848 5792 6149 106 -147 -328 O ATOM 945 CB SER A 455 0.042 20.788 6.394 1.00 45.08 C ANISOU 945 CB SER A 455 5616 5647 5867 278 144 -361 C ATOM 946 OG SER A 455 -0.110 21.365 7.660 1.00 49.71 O ANISOU 946 OG SER A 455 6187 6304 6396 404 46 -464 O ATOM 947 H SER A 455 0.972 19.845 4.435 1.00 52.78 H ATOM 948 HA SER A 455 0.997 22.335 5.437 1.00 55.24 H ATOM 949 HB2 SER A 455 -0.773 20.927 5.887 1.00 54.12 H ATOM 950 HB3 SER A 455 0.208 19.838 6.501 1.00 54.12 H ATOM 951 HG SER A 455 -0.724 20.976 8.081 1.00 59.68 H ATOM 952 N MET A 456 3.267 20.385 6.464 1.00 39.50 N ANISOU 952 N MET A 456 4786 5035 5187 150 154 -250 N ATOM 953 CA MET A 456 4.568 20.472 7.098 1.00 41.33 C ANISOU 953 CA MET A 456 4940 5363 5399 145 113 -248 C ATOM 954 C MET A 456 5.419 21.506 6.423 1.00 44.25 C ANISOU 954 C MET A 456 5274 5773 5768 -63 3 -197 C ATOM 955 O MET A 456 6.141 22.259 7.080 1.00 41.77 O ANISOU 955 O MET A 456 4954 5471 5446 -126 -129 -193 O ATOM 956 CB MET A 456 5.310 19.126 7.100 1.00 44.51 C ANISOU 956 CB MET A 456 5258 5885 5770 246 214 -249 C ATOM 957 CG MET A 456 4.716 17.967 7.973 1.00 55.02 C ANISOU 957 CG MET A 456 6665 7159 7081 394 251 -247 C ATOM 958 SD MET A 456 4.579 18.353 9.739 1.00 57.70 S ANISOU 958 SD MET A 456 7030 7519 7373 460 182 -263 S ATOM 959 CE MET A 456 6.228 18.971 9.900 1.00 49.88 C ANISOU 959 CE MET A 456 5931 6625 6397 439 110 -296 C ATOM 960 H MET A 456 3.054 19.615 6.146 1.00 47.42 H ATOM 961 HA MET A 456 4.409 20.709 8.025 1.00 49.62 H ATOM 962 HB2 MET A 456 5.338 18.802 6.186 1.00 53.44 H ATOM 963 HB3 MET A 456 6.211 19.285 7.423 1.00 53.44 H ATOM 964 HG2 MET A 456 3.826 17.761 7.648 1.00 66.05 H ATOM 965 HG3 MET A 456 5.290 17.190 7.887 1.00 66.05 H ATOM 966 HE1 MET A 456 6.305 19.799 9.401 1.00 59.88 H ATOM 967 HE2 MET A 456 6.414 19.132 10.839 1.00 59.88 H ATOM 968 HE3 MET A 456 6.847 18.313 9.548 1.00 59.88 H ATOM 969 N ASP A 457 5.503 21.487 5.087 1.00 39.14 N ANISOU 969 N ASP A 457 4582 5191 5099 -209 46 -137 N ATOM 970 CA ASP A 457 6.384 22.436 4.447 1.00 40.34 C ANISOU 970 CA ASP A 457 4678 5452 5198 -489 -74 -39 C ATOM 971 C ASP A 457 5.910 22.710 3.067 1.00 45.34 C ANISOU 971 C ASP A 457 5343 6075 5810 -667 -77 39 C ATOM 972 O ASP A 457 6.227 21.998 2.102 1.00 44.17 O ANISOU 972 O ASP A 457 5046 6156 5583 -694 67 48 O ATOM 973 CB ASP A 457 7.840 21.943 4.429 1.00 44.16 C ANISOU 973 CB ASP A 457 4920 6285 5572 -529 -3 -34 C ATOM 974 CG ASP A 457 8.773 23.033 3.926 1.00 52.70 C ANISOU 974 CG ASP A 457 5920 7549 6554 -901 -154 107 C ATOM 975 OD1 ASP A 457 8.247 24.095 3.544 1.00 53.96 O ANISOU 975 OD1 ASP A 457 6262 7491 6749 -1123 -339 212 O ATOM 976 OD2 ASP A 457 10.008 22.888 3.908 1.00 49.91 O ANISOU 976 OD2 ASP A 457 5331 7560 6072 -996 -128 123 O ATOM 977 H ASP A 457 5.075 20.954 4.564 1.00 47.00 H ATOM 978 HA ASP A 457 6.342 23.268 4.943 1.00 48.43 H ATOM 979 HB2 ASP A 457 8.110 21.697 5.327 1.00 53.01 H ATOM 980 HB3 ASP A 457 7.915 21.177 3.838 1.00 53.01 H ATOM 981 N PRO A 458 5.164 23.792 2.896 1.00 46.10 N ANISOU 981 N PRO A 458 5640 5913 5964 -781 -275 81 N ATOM 982 CA PRO A 458 4.586 24.036 1.591 1.00 44.75 C ANISOU 982 CA PRO A 458 5530 5697 5778 -939 -295 158 C ATOM 983 C PRO A 458 5.619 24.490 0.623 1.00 53.14 C ANISOU 983 C PRO A 458 6476 7012 6703 -1313 -356 329 C ATOM 984 O PRO A 458 5.374 24.466 -0.590 1.00 54.46 O ANISOU 984 O PRO A 458 6623 7264 6806 -1470 -321 409 O ATOM 985 CB PRO A 458 3.518 25.088 1.871 1.00 41.74 C ANISOU 985 CB PRO A 458 5416 4949 5494 -897 -551 118 C ATOM 986 CG PRO A 458 3.872 25.660 3.178 1.00 49.42 C ANISOU 986 CG PRO A 458 6454 5821 6500 -809 -718 50 C ATOM 987 CD PRO A 458 4.559 24.602 3.960 1.00 50.27 C ANISOU 987 CD PRO A 458 6358 6167 6576 -656 -477 -2 C ATOM 988 HA PRO A 458 4.125 23.260 1.236 1.00 53.73 H ATOM 989 HB2 PRO A 458 3.537 25.768 1.179 1.00 50.11 H ATOM 990 HB3 PRO A 458 2.644 24.670 1.902 1.00 50.11 H ATOM 991 HG2 PRO A 458 4.463 26.419 3.046 1.00 59.32 H ATOM 992 HG3 PRO A 458 3.064 25.945 3.632 1.00 59.32 H ATOM 993 HD2 PRO A 458 5.237 24.980 4.542 1.00 60.35 H ATOM 994 HD3 PRO A 458 3.926 24.083 4.480 1.00 60.35 H ATOM 995 N GLU A 459 6.802 24.828 1.113 1.00 50.11 N ANISOU 995 N GLU A 459 5979 6819 6242 -1473 -431 393 N ATOM 996 CA GLU A 459 7.870 25.148 0.194 1.00 61.72 C ANISOU 996 CA GLU A 459 7257 8676 7515 -1870 -463 568 C ATOM 997 C GLU A 459 8.570 23.906 -0.315 1.00 62.35 C ANISOU 997 C GLU A 459 6987 9254 7447 -1735 -165 473 C ATOM 998 O GLU A 459 9.377 24.005 -1.218 1.00 65.67 O ANISOU 998 O GLU A 459 7172 10127 7651 -2022 -140 579 O ATOM 999 CB GLU A 459 8.861 26.090 0.876 1.00 62.34 C ANISOU 999 CB GLU A 459 7345 8800 7542 -2151 -702 691 C ATOM 1000 CG GLU A 459 8.205 27.330 1.494 1.00 74.25 C ANISOU 1000 CG GLU A 459 9241 9767 9202 -2213 -1076 731 C ATOM 1001 CD GLU A 459 7.708 28.373 0.450 1.00 97.30 C ANISOU 1001 CD GLU A 459 12412 12457 12099 -2581 -1381 928 C ATOM 1002 OE1 GLU A 459 7.783 28.144 -0.802 1.00 80.63 O ANISOU 1002 OE1 GLU A 459 10168 10619 9847 -2819 -1270 1059 O ATOM 1003 OE2 GLU A 459 7.247 29.446 0.923 1.00117.37 O ANISOU 1003 OE2 GLU A 459 15304 14535 14756 -2614 -1772 938 O ATOM 1004 H GLU A 459 7.000 24.877 1.948 1.00 60.16 H ATOM 1005 HA GLU A 459 7.517 25.618 -0.577 1.00 74.08 H ATOM 1006 HB2 GLU A 459 9.312 25.608 1.586 1.00 74.84 H ATOM 1007 HB3 GLU A 459 9.507 26.393 0.218 1.00 74.84 H ATOM 1008 HG2 GLU A 459 7.438 27.048 2.017 1.00 89.12 H ATOM 1009 HG3 GLU A 459 8.853 27.771 2.066 1.00 89.12 H ATOM 1010 N SER A 460 8.285 22.739 0.255 1.00 52.14 N ANISOU 1010 N SER A 460 5658 7910 6245 -1305 25 270 N ATOM 1011 CA SER A 460 8.987 21.550 -0.178 1.00 47.62 C ANISOU 1011 CA SER A 460 4796 7761 5538 -1111 225 133 C ATOM 1012 C SER A 460 8.091 20.575 -0.875 1.00 48.52 C ANISOU 1012 C SER A 460 4965 7771 5701 -866 362 20 C ATOM 1013 O SER A 460 8.513 19.945 -1.825 1.00 50.86 O ANISOU 1013 O SER A 460 5048 8435 5841 -820 463 -58 O ATOM 1014 CB SER A 460 9.635 20.860 1.007 1.00 59.82 C ANISOU 1014 CB SER A 460 6259 9354 7116 -819 264 -12 C ATOM 1015 OG SER A 460 10.693 21.688 1.435 1.00 65.60 O ANISOU 1015 OG SER A 460 6861 10315 7749 -1077 151 87 O ATOM 1016 H SER A 460 7.703 22.621 0.877 1.00 62.60 H ATOM 1017 HA SER A 460 9.695 21.808 -0.789 1.00 57.17 H ATOM 1018 HB2 SER A 460 8.988 20.753 1.722 1.00 71.81 H ATOM 1019 HB3 SER A 460 9.980 19.994 0.739 1.00 71.81 H ATOM 1020 HG SER A 460 10.985 21.421 2.175 1.00 78.75 H ATOM 1021 N THR A 461 6.844 20.470 -0.441 1.00 48.14 N ANISOU 1021 N THR A 461 5185 7264 5841 -714 349 1 N ATOM 1022 CA THR A 461 5.939 19.532 -1.033 1.00 44.95 C ANISOU 1022 CA THR A 461 4853 6739 5487 -514 454 -86 C ATOM 1023 C THR A 461 4.723 20.275 -1.573 1.00 45.46 C ANISOU 1023 C THR A 461 5121 6519 5634 -670 393 15 C ATOM 1024 O THR A 461 4.013 20.919 -0.784 1.00 44.98 O ANISOU 1024 O THR A 461 5245 6152 5692 -664 289 42 O ATOM 1025 CB THR A 461 5.469 18.504 -0.010 1.00 44.62 C ANISOU 1025 CB THR A 461 4928 6462 5563 -192 488 -198 C ATOM 1026 OG1 THR A 461 6.574 17.726 0.452 1.00 45.87 O ANISOU 1026 OG1 THR A 461 4932 6846 5652 -3 502 -314 O ATOM 1027 CG2 THR A 461 4.530 17.567 -0.683 1.00 45.71 C ANISOU 1027 CG2 THR A 461 5161 6466 5740 -52 551 -255 C ATOM 1028 H THR A 461 6.509 20.937 0.198 1.00 57.79 H ATOM 1029 HA THR A 461 6.395 19.081 -1.759 1.00 53.97 H ATOM 1030 HB THR A 461 5.048 18.956 0.738 1.00 53.57 H ATOM 1031 HG1 THR A 461 6.301 17.099 0.940 1.00 55.07 H ATOM 1032 HG21 THR A 461 4.359 16.801 -0.113 1.00 54.88 H ATOM 1033 HG22 THR A 461 3.690 18.015 -0.869 1.00 54.88 H ATOM 1034 HG23 THR A 461 4.913 17.257 -1.519 1.00 54.88 H ATOM 1035 N PRO A 462 4.366 20.119 -2.856 1.00 43.35 N ANISOU 1035 N PRO A 462 4825 6345 5303 -752 445 36 N ATOM 1036 CA PRO A 462 3.179 20.811 -3.386 1.00 46.33 C ANISOU 1036 CA PRO A 462 5404 6441 5759 -877 364 120 C ATOM 1037 C PRO A 462 1.889 20.203 -2.921 1.00 43.74 C ANISOU 1037 C PRO A 462 5235 5810 5575 -631 411 30 C ATOM 1038 O PRO A 462 1.857 19.048 -2.419 1.00 41.96 O ANISOU 1038 O PRO A 462 4982 5585 5376 -397 511 -71 O ATOM 1039 CB PRO A 462 3.332 20.683 -4.918 1.00 53.61 C ANISOU 1039 CB PRO A 462 6206 7628 6533 -1037 423 165 C ATOM 1040 CG PRO A 462 4.126 19.487 -5.124 1.00 51.19 C ANISOU 1040 CG PRO A 462 5673 7661 6116 -828 571 15 C ATOM 1041 CD PRO A 462 5.136 19.476 -3.942 1.00 49.69 C ANISOU 1041 CD PRO A 462 5384 7577 5920 -754 548 -24 C ATOM 1042 HA PRO A 462 3.203 21.743 -3.119 1.00 55.62 H ATOM 1043 HB2 PRO A 462 2.458 20.593 -5.330 1.00 64.35 H ATOM 1044 HB3 PRO A 462 3.786 21.464 -5.270 1.00 64.35 H ATOM 1045 HG2 PRO A 462 3.556 18.702 -5.102 1.00 61.45 H ATOM 1046 HG3 PRO A 462 4.588 19.537 -5.975 1.00 61.45 H ATOM 1047 HD2 PRO A 462 5.383 18.569 -3.703 1.00 59.66 H ATOM 1048 HD3 PRO A 462 5.929 19.991 -4.157 1.00 59.66 H ATOM 1049 N PRO A 463 0.788 20.966 -2.980 1.00 41.80 N ANISOU 1049 N PRO A 463 5165 5306 5410 -680 303 64 N ATOM 1050 CA PRO A 463 -0.514 20.451 -2.585 1.00 38.70 C ANISOU 1050 CA PRO A 463 4872 4726 5107 -483 348 -17 C ATOM 1051 C PRO A 463 -1.118 19.487 -3.584 1.00 40.76 C ANISOU 1051 C PRO A 463 5120 5012 5354 -437 469 -38 C ATOM 1052 O PRO A 463 -0.732 19.408 -4.752 1.00 40.59 O ANISOU 1052 O PRO A 463 5036 5127 5258 -546 503 -6 O ATOM 1053 CB PRO A 463 -1.387 21.694 -2.460 1.00 41.36 C ANISOU 1053 CB PRO A 463 5365 4850 5499 -525 156 -14 C ATOM 1054 CG PRO A 463 -0.832 22.660 -3.448 1.00 48.49 C ANISOU 1054 CG PRO A 463 6314 5758 6353 -799 8 111 C ATOM 1055 CD PRO A 463 0.697 22.375 -3.465 1.00 43.06 C ANISOU 1055 CD PRO A 463 5447 5354 5562 -933 87 179 C ATOM 1056 HA PRO A 463 -0.427 20.009 -1.726 1.00 46.47 H ATOM 1057 HB2 PRO A 463 -2.308 21.473 -2.671 1.00 49.65 H ATOM 1058 HB3 PRO A 463 -1.329 22.048 -1.559 1.00 49.65 H ATOM 1059 HG2 PRO A 463 -1.225 22.503 -4.321 1.00 58.22 H ATOM 1060 HG3 PRO A 463 -1.013 23.569 -3.160 1.00 58.22 H ATOM 1061 HD2 PRO A 463 1.053 22.455 -4.364 1.00 51.70 H ATOM 1062 HD3 PRO A 463 1.167 22.977 -2.868 1.00 51.70 H ATOM 1063 N THR A 464 -2.093 18.733 -3.079 1.00 39.98 N ANISOU 1063 N THR A 464 5076 4810 5305 -290 521 -90 N ATOM 1064 CA THR A 464 -2.941 17.941 -3.937 1.00 44.95 C ANISOU 1064 CA THR A 464 5740 5401 5937 -266 585 -101 C ATOM 1065 C THR A 464 -3.783 18.873 -4.778 1.00 39.88 C ANISOU 1065 C THR A 464 5163 4679 5310 -369 516 -75 C ATOM 1066 O THR A 464 -3.778 20.099 -4.584 1.00 42.07 O ANISOU 1066 O THR A 464 5493 4889 5602 -437 380 -57 O ATOM 1067 CB THR A 464 -3.825 17.029 -3.097 1.00 44.23 C ANISOU 1067 CB THR A 464 5694 5244 5868 -167 614 -117 C ATOM 1068 OG1 THR A 464 -4.517 17.813 -2.106 1.00 44.50 O ANISOU 1068 OG1 THR A 464 5731 5269 5907 -145 561 -134 O ATOM 1069 CG2 THR A 464 -2.928 16.052 -2.384 1.00 40.90 C ANISOU 1069 CG2 THR A 464 5257 4854 5431 -75 627 -128 C ATOM 1070 H THR A 464 -2.277 18.668 -2.241 1.00 48.00 H ATOM 1071 HA THR A 464 -2.410 17.379 -4.522 1.00 53.96 H ATOM 1072 HB THR A 464 -4.473 16.566 -3.650 1.00 53.10 H ATOM 1073 HG1 THR A 464 -3.963 18.175 -1.588 1.00 53.42 H ATOM 1074 HG21 THR A 464 -3.454 15.489 -1.794 1.00 49.11 H ATOM 1075 HG22 THR A 464 -2.470 15.491 -3.030 1.00 49.11 H ATOM 1076 HG23 THR A 464 -2.268 16.530 -1.858 1.00 49.11 H ATOM 1077 N CYS A 465 -4.568 18.290 -5.686 1.00 43.92 N ANISOU 1077 N CYS A 465 5704 5164 5821 -370 566 -82 N ATOM 1078 CA CYS A 465 -5.311 19.097 -6.643 1.00 43.51 C ANISOU 1078 CA CYS A 465 5718 5040 5774 -464 491 -58 C ATOM 1079 C CYS A 465 -6.799 18.757 -6.666 1.00 42.63 C ANISOU 1079 C CYS A 465 5648 4858 5693 -389 501 -104 C ATOM 1080 O CYS A 465 -7.198 17.597 -6.531 1.00 39.35 O ANISOU 1080 O CYS A 465 5215 4466 5272 -341 590 -112 O ATOM 1081 CB CYS A 465 -4.652 18.961 -8.030 1.00 49.02 C ANISOU 1081 CB CYS A 465 6373 5857 6395 -591 529 -10 C ATOM 1082 SG CYS A 465 -5.091 20.415 -8.938 1.00 57.39 S ANISOU 1082 SG CYS A 465 7548 6817 7443 -789 349 80 S ATOM 1083 H CYS A 465 -4.681 17.441 -5.763 1.00 52.73 H ATOM 1084 HA CYS A 465 -5.301 20.028 -6.373 1.00 52.23 H ATOM 1085 HB2 CYS A 465 -3.687 18.910 -7.943 1.00 58.85 H ATOM 1086 HB3 CYS A 465 -4.987 18.175 -8.489 1.00 58.85 H ATOM 1087 N CYS A 466 -7.629 19.803 -6.793 1.00 40.15 N ANISOU 1087 N CYS A 466 5396 4461 5398 -382 367 -136 N ATOM 1088 CA CYS A 466 -9.104 19.630 -6.763 1.00 38.81 C ANISOU 1088 CA CYS A 466 5214 4306 5224 -295 362 -209 C ATOM 1089 C CYS A 466 -9.561 19.070 -8.117 1.00 39.56 C ANISOU 1089 C CYS A 466 5339 4377 5315 -377 419 -168 C ATOM 1090 O CYS A 466 -9.397 19.733 -9.128 1.00 40.91 O ANISOU 1090 O CYS A 466 5582 4474 5487 -464 337 -132 O ATOM 1091 CB CYS A 466 -9.725 21.000 -6.466 1.00 38.72 C ANISOU 1091 CB CYS A 466 5262 4226 5225 -190 147 -313 C ATOM 1092 SG CYS A 466 -11.511 20.859 -6.292 1.00 41.54 S ANISOU 1092 SG CYS A 466 5523 4735 5525 -34 135 -456 S ATOM 1093 H CYS A 466 -7.372 20.617 -6.896 1.00 48.20 H ATOM 1094 HA CYS A 466 -9.388 19.000 -6.081 1.00 46.59 H ATOM 1095 HB2 CYS A 466 -9.359 21.349 -5.639 1.00 46.49 H ATOM 1096 HB3 CYS A 466 -9.532 21.608 -7.197 1.00 46.49 H ATOM 1097 N VAL A 467 -10.055 17.830 -8.168 1.00 36.07 N ANISOU 1097 N VAL A 467 4859 3990 4856 -379 532 -156 N ATOM 1098 CA VAL A 467 -10.486 17.299 -9.467 1.00 37.18 C ANISOU 1098 CA VAL A 467 5040 4094 4992 -442 562 -135 C ATOM 1099 C VAL A 467 -11.823 16.570 -9.326 1.00 42.21 C ANISOU 1099 C VAL A 467 5647 4784 5605 -448 582 -144 C ATOM 1100 O VAL A 467 -12.309 16.319 -8.207 1.00 40.92 O ANISOU 1100 O VAL A 467 5410 4737 5401 -434 592 -147 O ATOM 1101 CB VAL A 467 -9.475 16.324 -10.059 1.00 35.80 C ANISOU 1101 CB VAL A 467 4880 3920 4801 -463 634 -110 C ATOM 1102 CG1 VAL A 467 -8.158 16.980 -10.431 1.00 42.48 C ANISOU 1102 CG1 VAL A 467 5696 4833 5613 -504 629 -92 C ATOM 1103 CG2 VAL A 467 -9.283 15.233 -9.044 1.00 39.66 C ANISOU 1103 CG2 VAL A 467 5369 4406 5293 -414 660 -103 C ATOM 1104 H VAL A 467 -10.148 17.301 -7.496 1.00 43.31 H ATOM 1105 HA VAL A 467 -10.590 18.066 -10.051 1.00 44.64 H ATOM 1106 HB VAL A 467 -9.810 15.966 -10.896 1.00 42.98 H ATOM 1107 HG11 VAL A 467 -7.584 16.320 -10.851 1.00 51.00 H ATOM 1108 HG12 VAL A 467 -8.331 17.708 -11.048 1.00 51.00 H ATOM 1109 HG13 VAL A 467 -7.736 17.321 -9.626 1.00 51.00 H ATOM 1110 HG21 VAL A 467 -8.505 14.707 -9.289 1.00 47.61 H ATOM 1111 HG22 VAL A 467 -9.148 15.634 -8.171 1.00 47.61 H ATOM 1112 HG23 VAL A 467 -10.072 14.670 -9.032 1.00 47.61 H ATOM 1113 N PRO A 468 -12.423 16.183 -10.441 1.00 40.86 N ANISOU 1113 N PRO A 468 5517 4574 5432 -500 584 -137 N ATOM 1114 CA PRO A 468 -13.654 15.402 -10.406 1.00 38.05 C ANISOU 1114 CA PRO A 468 5130 4287 5038 -561 589 -120 C ATOM 1115 C PRO A 468 -13.364 14.031 -9.872 1.00 42.20 C ANISOU 1115 C PRO A 468 5704 4781 5548 -635 602 -40 C ATOM 1116 O PRO A 468 -12.439 13.367 -10.325 1.00 41.73 O ANISOU 1116 O PRO A 468 5744 4590 5523 -606 594 -38 O ATOM 1117 CB PRO A 468 -14.070 15.334 -11.880 1.00 42.63 C ANISOU 1117 CB PRO A 468 5776 4788 5633 -596 571 -130 C ATOM 1118 CG PRO A 468 -13.458 16.563 -12.493 1.00 39.70 C ANISOU 1118 CG PRO A 468 5440 4360 5285 -556 528 -158 C ATOM 1119 CD PRO A 468 -12.108 16.652 -11.804 1.00 44.98 C ANISOU 1119 CD PRO A 468 6102 5026 5963 -534 560 -136 C ATOM 1120 HA PRO A 468 -14.343 15.842 -9.885 1.00 45.68 H ATOM 1121 HB2 PRO A 468 -13.719 14.527 -12.288 1.00 51.18 H ATOM 1122 HB3 PRO A 468 -15.037 15.350 -11.954 1.00 51.18 H ATOM 1123 HG2 PRO A 468 -13.359 16.450 -13.451 1.00 47.67 H ATOM 1124 HG3 PRO A 468 -14.003 17.343 -12.305 1.00 47.67 H ATOM 1125 HD2 PRO A 468 -11.459 16.072 -12.232 1.00 54.00 H ATOM 1126 HD3 PRO A 468 -11.781 17.565 -11.792 1.00 54.00 H ATOM 1127 N THR A 469 -14.174 13.596 -8.917 1.00 38.79 N ANISOU 1127 N THR A 469 5199 4497 5041 -731 589 20 N ATOM 1128 CA THR A 469 -14.036 12.261 -8.378 1.00 40.37 C ANISOU 1128 CA THR A 469 5494 4634 5212 -865 531 141 C ATOM 1129 C THR A 469 -15.203 11.388 -8.707 1.00 43.62 C ANISOU 1129 C THR A 469 5934 5084 5556 -1073 458 241 C ATOM 1130 O THR A 469 -15.157 10.194 -8.454 1.00 50.00 O ANISOU 1130 O THR A 469 6888 5766 6342 -1228 334 367 O ATOM 1131 CB THR A 469 -13.905 12.305 -6.852 1.00 46.92 C ANISOU 1131 CB THR A 469 6232 5633 5963 -905 541 199 C ATOM 1132 OG1 THR A 469 -14.993 13.056 -6.325 1.00 49.73 O ANISOU 1132 OG1 THR A 469 6371 6322 6201 -924 584 159 O ATOM 1133 CG2 THR A 469 -12.622 12.963 -6.498 1.00 42.43 C ANISOU 1133 CG2 THR A 469 5671 4985 5467 -724 583 120 C ATOM 1134 H THR A 469 -14.809 14.059 -8.568 1.00 46.57 H ATOM 1135 HA THR A 469 -13.227 11.868 -8.741 1.00 48.47 H ATOM 1136 HB THR A 469 -13.915 11.413 -6.471 1.00 56.33 H ATOM 1137 HG1 THR A 469 -14.897 13.159 -5.496 1.00 59.70 H ATOM 1138 HG21 THR A 469 -12.525 13.006 -5.534 1.00 50.94 H ATOM 1139 HG22 THR A 469 -11.878 12.461 -6.867 1.00 50.94 H ATOM 1140 HG23 THR A 469 -12.601 13.864 -6.857 1.00 50.94 H ATOM 1141 N ARG A 470 -16.259 11.954 -9.258 1.00 44.93 N ANISOU 1141 N ARG A 470 5979 5412 5682 -1090 492 191 N ATOM 1142 CA AARG A 470 -17.396 11.166 -9.743 0.50 48.10 C ANISOU 1142 CA AARG A 470 6393 5870 6015 -1306 420 284 C ATOM 1143 CA BARG A 470 -17.404 11.170 -9.729 0.50 48.24 C ANISOU 1143 CA BARG A 470 6408 5892 6030 -1307 420 284 C ATOM 1144 C ARG A 470 -17.966 11.964 -10.901 1.00 46.95 C ANISOU 1144 C ARG A 470 6189 5742 5906 -1189 461 156 C ATOM 1145 O ARG A 470 -18.082 13.200 -10.795 1.00 44.00 O ANISOU 1145 O ARG A 470 5680 5506 5530 -1016 516 27 O ATOM 1146 CB AARG A 470 -18.481 10.948 -8.693 0.50 50.32 C ANISOU 1146 CB AARG A 470 6474 6545 6100 -1540 409 398 C ATOM 1147 CB BARG A 470 -18.472 11.011 -8.643 0.50 50.15 C ANISOU 1147 CB BARG A 470 6441 6539 6076 -1530 416 391 C ATOM 1148 CG AARG A 470 -19.753 10.206 -9.203 0.50 49.07 C ANISOU 1148 CG AARG A 470 6288 6523 5835 -1823 325 515 C ATOM 1149 CG BARG A 470 -19.106 9.624 -8.442 0.50 57.10 C ANISOU 1149 CG BARG A 470 7414 7437 6846 -1912 266 628 C ATOM 1150 CD AARG A 470 -20.727 9.869 -8.029 0.50 50.53 C ANISOU 1150 CD AARG A 470 6233 7208 5755 -2140 306 674 C ATOM 1151 CD BARG A 470 -20.066 9.593 -7.206 0.50 56.27 C ANISOU 1151 CD BARG A 470 7026 7880 6472 -2179 283 755 C ATOM 1152 NE AARG A 470 -22.106 10.236 -8.337 0.50 52.54 N ANISOU 1152 NE AARG A 470 6211 7901 5850 -2219 342 622 N ATOM 1153 NE BARG A 470 -19.534 10.297 -6.036 0.50 61.99 N ANISOU 1153 NE BARG A 470 7597 8817 7140 -2024 382 683 N ATOM 1154 CZ AARG A 470 -22.766 11.218 -7.746 0.50 52.66 C ANISOU 1154 CZ AARG A 470 5870 8440 5698 -2072 443 458 C ATOM 1155 CZ BARG A 470 -18.418 9.962 -5.395 0.50 66.82 C ANISOU 1155 CZ BARG A 470 8382 9181 7827 -1992 344 748 C ATOM 1156 NH1AARG A 470 -22.239 11.900 -6.740 0.50 58.43 N ANISOU 1156 NH1AARG A 470 6483 9328 6390 -1877 513 355 N ATOM 1157 NH1BARG A 470 -17.662 8.953 -5.799 0.50 72.58 N ANISOU 1157 NH1BARG A 470 9446 9439 8693 -2058 193 856 N ATOM 1158 NH2AARG A 470 -24.002 11.508 -8.154 0.50 62.02 N ANISOU 1158 NH2AARG A 470 6804 10023 6738 -2100 451 374 N ATOM 1159 NH2BARG A 470 -18.034 10.676 -4.341 0.50 66.79 N ANISOU 1159 NH2BARG A 470 8214 9407 7757 -1850 436 670 N ATOM 1160 H ARG A 470 -16.351 12.802 -9.367 1.00 53.95 H ATOM 1161 HA ARG A 470 -17.100 10.283 -10.012 1.00 57.91 H ATOM 1162 HB2AARG A 470 -18.106 10.420 -7.970 0.50 60.41 H ATOM 1163 HB2BARG A 470 -18.069 11.257 -7.796 0.50 60.21 H ATOM 1164 HB3AARG A 470 -18.763 11.814 -8.359 0.50 60.41 H ATOM 1165 HB3BARG A 470 -19.198 11.619 -8.854 0.50 60.21 H ATOM 1166 HG2AARG A 470 -20.223 10.772 -9.836 0.50 58.91 H ATOM 1167 HG2BARG A 470 -19.619 9.390 -9.231 0.50 68.55 H ATOM 1168 HG3AARG A 470 -19.491 9.376 -9.631 0.50 58.91 H ATOM 1169 HG3BARG A 470 -18.404 8.971 -8.297 0.50 68.55 H ATOM 1170 HD2AARG A 470 -20.699 8.914 -7.856 0.50 60.65 H ATOM 1171 HD2BARG A 470 -20.905 10.015 -7.449 0.50 67.54 H ATOM 1172 HD3AARG A 470 -20.453 10.357 -7.237 0.50 60.65 H ATOM 1173 HD3BARG A 470 -20.220 8.670 -6.952 0.50 67.54 H ATOM 1174 HE AARG A 470 -22.516 9.784 -8.943 0.50 63.07 H ATOM 1175 HE BARG A 470 -19.974 10.975 -5.743 0.50 74.41 H ATOM 1176 HH11AARG A 470 -21.450 11.707 -6.458 0.50 70.14 H ATOM 1177 HH11BARG A 470 -17.889 8.497 -6.491 0.50 87.12 H ATOM 1178 HH12AARG A 470 -22.685 12.535 -6.370 0.50 70.14 H ATOM 1179 HH12BARG A 470 -16.945 8.754 -5.369 0.50 87.12 H ATOM 1180 HH21AARG A 470 -24.359 11.059 -8.795 0.50 74.45 H ATOM 1181 HH21BARG A 470 -18.506 11.346 -4.081 0.50 80.18 H ATOM 1182 HH22AARG A 470 -24.441 12.144 -7.778 0.50 74.45 H ATOM 1183 HH22BARG A 470 -17.314 10.467 -3.920 0.50 80.18 H ATOM 1184 N LEU A 471 -18.302 11.294 -11.980 1.00 44.29 N ANISOU 1184 N LEU A 471 5979 5246 5604 -1270 396 183 N ATOM 1185 CA LEU A 471 -18.893 11.957 -13.146 1.00 44.80 C ANISOU 1185 CA LEU A 471 6007 5320 5694 -1184 417 80 C ATOM 1186 C LEU A 471 -20.061 11.156 -13.669 1.00 49.80 C ANISOU 1186 C LEU A 471 6643 6018 6262 -1395 337 157 C ATOM 1187 O LEU A 471 -20.246 9.990 -13.340 1.00 48.14 O ANISOU 1187 O LEU A 471 6530 5755 6007 -1624 232 305 O ATOM 1188 CB LEU A 471 -17.885 12.143 -14.270 1.00 45.26 C ANISOU 1188 CB LEU A 471 6222 5115 5861 -1029 428 1 C ATOM 1189 CG LEU A 471 -16.723 13.057 -13.944 1.00 48.82 C ANISOU 1189 CG LEU A 471 6658 5535 6358 -865 492 -60 C ATOM 1190 CD1 LEU A 471 -15.576 12.031 -13.583 1.00 47.77 C ANISOU 1190 CD1 LEU A 471 6649 5249 6252 -854 468 -24 C ATOM 1191 CD2 LEU A 471 -16.199 13.835 -15.024 1.00 49.07 C ANISOU 1191 CD2 LEU A 471 6731 5491 6423 -771 506 -125 C ATOM 1192 H LEU A 471 -18.202 10.445 -12.072 1.00 53.17 H ATOM 1193 HA LEU A 471 -19.215 12.828 -12.865 1.00 53.78 H ATOM 1194 HB2 LEU A 471 -17.518 11.275 -14.498 1.00 54.34 H ATOM 1195 HB3 LEU A 471 -18.347 12.519 -15.036 1.00 54.34 H ATOM 1196 HG LEU A 471 -17.008 13.700 -13.276 1.00 58.61 H ATOM 1197 HD11 LEU A 471 -14.793 12.523 -13.290 1.00 57.35 H ATOM 1198 HD12 LEU A 471 -15.886 11.449 -12.871 1.00 57.35 H ATOM 1199 HD13 LEU A 471 -15.362 11.506 -14.370 1.00 57.35 H ATOM 1200 HD21 LEU A 471 -15.742 14.610 -14.662 1.00 58.91 H ATOM 1201 HD22 LEU A 471 -15.578 13.292 -15.532 1.00 58.91 H ATOM 1202 HD23 LEU A 471 -16.932 14.120 -15.593 1.00 58.91 H ATOM 1203 N SER A 472 -20.914 11.796 -14.482 1.00 44.09 N ANISOU 1203 N SER A 472 5825 5404 5522 -1340 350 68 N ATOM 1204 CA SER A 472 -22.108 11.181 -14.961 1.00 43.99 C ANISOU 1204 CA SER A 472 5770 5513 5431 -1541 281 131 C ATOM 1205 C SER A 472 -22.231 11.475 -16.466 1.00 47.08 C ANISOU 1205 C SER A 472 6262 5721 5903 -1426 263 34 C ATOM 1206 O SER A 472 -21.553 12.374 -16.969 1.00 44.97 O ANISOU 1206 O SER A 472 6041 5331 5714 -1211 310 -73 O ATOM 1207 CB SER A 472 -23.360 11.654 -14.203 1.00 51.66 C ANISOU 1207 CB SER A 472 6421 6984 6224 -1615 306 111 C ATOM 1208 OG SER A 472 -23.492 13.036 -14.358 1.00 54.27 O ANISOU 1208 OG SER A 472 6624 7423 6572 -1317 347 -94 O ATOM 1209 H SER A 472 -20.799 12.601 -14.761 1.00 52.93 H ATOM 1210 HA SER A 472 -22.060 10.221 -14.829 1.00 52.81 H ATOM 1211 HB2 SER A 472 -24.143 11.212 -14.567 1.00 62.02 H ATOM 1212 HB3 SER A 472 -23.267 11.442 -13.261 1.00 62.02 H ATOM 1213 HG SER A 472 -24.171 13.307 -13.944 1.00 65.14 H ATOM 1214 N PRO A 473 -23.031 10.700 -17.184 1.00 48.47 N ANISOU 1214 N PRO A 473 6490 5876 6049 -1599 176 91 N ATOM 1215 CA PRO A 473 -23.109 10.853 -18.651 1.00 50.70 C ANISOU 1215 CA PRO A 473 6886 5982 6397 -1500 151 5 C ATOM 1216 C PRO A 473 -24.190 11.807 -19.134 1.00 51.37 C ANISOU 1216 C PRO A 473 6793 6294 6430 -1427 163 -93 C ATOM 1217 O PRO A 473 -25.109 12.170 -18.403 1.00 52.65 O ANISOU 1217 O PRO A 473 6715 6807 6482 -1464 171 -112 O ATOM 1218 CB PRO A 473 -23.460 9.432 -19.121 1.00 50.70 C ANISOU 1218 CB PRO A 473 7058 5817 6387 -1726 1 111 C ATOM 1219 CG PRO A 473 -24.313 8.892 -18.025 1.00 53.12 C ANISOU 1219 CG PRO A 473 7229 6386 6567 -2025 -54 271 C ATOM 1220 CD PRO A 473 -23.805 9.558 -16.704 1.00 52.85 C ANISOU 1220 CD PRO A 473 7037 6546 6499 -1934 66 265 C ATOM 1221 HA PRO A 473 -22.248 11.150 -18.983 1.00 60.87 H ATOM 1222 HB2 PRO A 473 -23.946 9.467 -19.959 1.00 60.86 H ATOM 1223 HB3 PRO A 473 -22.651 8.906 -19.227 1.00 60.86 H ATOM 1224 HG2 PRO A 473 -25.241 9.124 -18.190 1.00 63.77 H ATOM 1225 HG3 PRO A 473 -24.216 7.928 -17.982 1.00 63.77 H ATOM 1226 HD2 PRO A 473 -24.549 9.850 -16.155 1.00 63.45 H ATOM 1227 HD3 PRO A 473 -23.243 8.946 -16.202 1.00 63.45 H ATOM 1228 N ILE A 474 -24.048 12.225 -20.399 1.00 51.13 N ANISOU 1228 N ILE A 474 6873 6094 6461 -1304 146 -173 N ATOM 1229 CA ILE A 474 -25.182 12.740 -21.154 1.00 54.62 C ANISOU 1229 CA ILE A 474 7219 6676 6859 -1277 95 -247 C ATOM 1230 C ILE A 474 -25.259 12.002 -22.494 1.00 56.67 C ANISOU 1230 C ILE A 474 7654 6729 7148 -1354 36 -227 C ATOM 1231 O ILE A 474 -24.270 11.447 -22.978 1.00 52.31 O ANISOU 1231 O ILE A 474 7291 5934 6648 -1333 38 -214 O ATOM 1232 CB ILE A 474 -25.088 14.258 -21.367 1.00 54.16 C ANISOU 1232 CB ILE A 474 7128 6627 6825 -1032 75 -375 C ATOM 1233 CG1 ILE A 474 -23.950 14.589 -22.300 1.00 52.03 C ANISOU 1233 CG1 ILE A 474 7071 6069 6629 -965 81 -362 C ATOM 1234 CG2 ILE A 474 -24.879 15.027 -20.062 1.00 53.70 C ANISOU 1234 CG2 ILE A 474 6932 6726 6744 -903 94 -433 C ATOM 1235 CD1 ILE A 474 -24.129 15.954 -22.842 1.00 56.31 C ANISOU 1235 CD1 ILE A 474 7643 6575 7176 -817 -27 -440 C ATOM 1236 H ILE A 474 -23.306 12.218 -20.833 1.00 61.38 H ATOM 1237 HA ILE A 474 -26.000 12.558 -20.665 1.00 65.57 H ATOM 1238 HB ILE A 474 -25.937 14.528 -21.751 1.00 65.02 H ATOM 1239 HG12 ILE A 474 -23.110 14.551 -21.818 1.00 62.46 H ATOM 1240 HG13 ILE A 474 -23.938 13.958 -23.037 1.00 62.46 H ATOM 1241 HG21 ILE A 474 -24.924 15.978 -20.245 1.00 64.46 H ATOM 1242 HG22 ILE A 474 -25.575 14.778 -19.434 1.00 64.46 H ATOM 1243 HG23 ILE A 474 -24.009 14.801 -19.698 1.00 64.46 H ATOM 1244 HD11 ILE A 474 -23.445 16.121 -23.508 1.00 67.59 H ATOM 1245 HD12 ILE A 474 -25.008 16.020 -23.246 1.00 67.59 H ATOM 1246 HD13 ILE A 474 -24.049 16.594 -22.117 1.00 67.59 H ATOM 1247 N SER A 475 -26.461 11.965 -23.058 1.00 51.79 N ANISOU 1247 N SER A 475 6950 6254 6475 -1424 -29 -250 N ATOM 1248 CA SER A 475 -26.676 11.458 -24.402 1.00 50.18 C ANISOU 1248 CA SER A 475 6895 5882 6288 -1467 -99 -259 C ATOM 1249 C SER A 475 -26.616 12.551 -25.438 1.00 55.93 C ANISOU 1249 C SER A 475 7661 6554 7034 -1281 -106 -358 C ATOM 1250 O SER A 475 -27.031 13.688 -25.202 1.00 53.79 O ANISOU 1250 O SER A 475 7272 6418 6747 -1146 -127 -432 O ATOM 1251 CB SER A 475 -28.010 10.733 -24.418 1.00 55.53 C ANISOU 1251 CB SER A 475 7464 6751 6884 -1696 -187 -201 C ATOM 1252 OG SER A 475 -27.859 9.775 -23.394 1.00 58.30 O ANISOU 1252 OG SER A 475 7825 7121 7205 -1915 -214 -62 O ATOM 1253 H SER A 475 -27.181 12.234 -22.672 1.00 62.17 H ATOM 1254 HA SER A 475 -25.971 10.841 -24.653 1.00 60.24 H ATOM 1255 HB2 SER A 475 -28.738 11.342 -24.219 1.00 66.66 H ATOM 1256 HB3 SER A 475 -28.161 10.304 -25.275 1.00 66.66 H ATOM 1257 HG SER A 475 -28.549 9.299 -23.342 1.00 69.98 H ATOM 1258 N ILE A 476 -25.984 12.222 -26.560 1.00 49.95 N ANISOU 1258 N ILE A 476 7087 5596 6296 -1260 -118 -367 N ATOM 1259 CA ILE A 476 -25.753 13.164 -27.635 1.00 45.85 C ANISOU 1259 CA ILE A 476 6635 5025 5761 -1150 -139 -414 C ATOM 1260 C ILE A 476 -26.211 12.529 -28.949 1.00 54.45 C ANISOU 1260 C ILE A 476 7818 6056 6814 -1204 -205 -440 C ATOM 1261 O ILE A 476 -26.019 11.336 -29.155 1.00 50.38 O ANISOU 1261 O ILE A 476 7395 5449 6300 -1270 -227 -441 O ATOM 1262 CB ILE A 476 -24.270 13.575 -27.681 1.00 53.59 C ANISOU 1262 CB ILE A 476 7702 5920 6739 -1082 -68 -394 C ATOM 1263 CG1 ILE A 476 -23.974 14.270 -26.359 1.00 55.35 C ANISOU 1263 CG1 ILE A 476 7835 6190 7003 -1029 -32 -375 C ATOM 1264 CG2 ILE A 476 -24.032 14.418 -28.911 1.00 55.42 C ANISOU 1264 CG2 ILE A 476 8016 6136 6907 -1062 -118 -391 C ATOM 1265 CD1 ILE A 476 -22.536 14.664 -26.214 1.00 52.99 C ANISOU 1265 CD1 ILE A 476 7595 5840 6698 -997 32 -338 C ATOM 1266 H ILE A 476 -25.673 11.436 -26.721 1.00 59.96 H ATOM 1267 HA ILE A 476 -26.286 13.964 -27.506 1.00 55.05 H ATOM 1268 HB ILE A 476 -23.661 12.825 -27.764 1.00 64.33 H ATOM 1269 HG12 ILE A 476 -24.512 15.075 -26.299 1.00 66.44 H ATOM 1270 HG13 ILE A 476 -24.194 13.668 -25.631 1.00 66.44 H ATOM 1271 HG21 ILE A 476 -23.153 14.824 -28.850 1.00 66.53 H ATOM 1272 HG22 ILE A 476 -24.081 13.851 -29.696 1.00 66.53 H ATOM 1273 HG23 ILE A 476 -24.712 15.108 -28.958 1.00 66.53 H ATOM 1274 HD11 ILE A 476 -22.375 14.937 -25.297 1.00 63.61 H ATOM 1275 HD12 ILE A 476 -21.976 13.904 -26.436 1.00 63.61 H ATOM 1276 HD13 ILE A 476 -22.348 15.401 -26.816 1.00 63.61 H ATOM 1277 N LEU A 477 -26.909 13.308 -29.777 1.00 52.55 N ANISOU 1277 N LEU A 477 7568 5856 6542 -1166 -279 -473 N ATOM 1278 CA LEU A 477 -27.269 12.901 -31.133 1.00 52.80 C ANISOU 1278 CA LEU A 477 7693 5843 6525 -1200 -343 -502 C ATOM 1279 C LEU A 477 -26.304 13.606 -32.074 1.00 55.88 C ANISOU 1279 C LEU A 477 8191 6195 6846 -1149 -331 -489 C ATOM 1280 O LEU A 477 -26.170 14.819 -32.004 1.00 52.43 O ANISOU 1280 O LEU A 477 7760 5761 6402 -1113 -377 -450 O ATOM 1281 CB LEU A 477 -28.695 13.300 -31.465 1.00 53.20 C ANISOU 1281 CB LEU A 477 7653 5997 6562 -1205 -449 -540 C ATOM 1282 CG LEU A 477 -29.181 12.916 -32.864 1.00 59.61 C ANISOU 1282 CG LEU A 477 8558 6768 7324 -1244 -528 -571 C ATOM 1283 CD1 LEU A 477 -29.423 11.411 -32.958 1.00 54.60 C ANISOU 1283 CD1 LEU A 477 7970 6081 6696 -1376 -551 -570 C ATOM 1284 CD2 LEU A 477 -30.440 13.676 -33.188 1.00 58.58 C ANISOU 1284 CD2 LEU A 477 8334 6750 7174 -1196 -648 -622 C ATOM 1285 H LEU A 477 -27.192 14.093 -29.570 1.00 63.08 H ATOM 1286 HA LEU A 477 -27.198 11.938 -31.229 1.00 63.38 H ATOM 1287 HB2 LEU A 477 -29.286 12.872 -30.826 1.00 63.86 H ATOM 1288 HB3 LEU A 477 -28.766 14.264 -31.389 1.00 63.86 H ATOM 1289 HG LEU A 477 -28.502 13.145 -33.516 1.00 71.55 H ATOM 1290 HD11 LEU A 477 -29.688 11.189 -33.864 1.00 65.55 H ATOM 1291 HD12 LEU A 477 -28.604 10.944 -32.729 1.00 65.55 H ATOM 1292 HD13 LEU A 477 -30.128 11.165 -32.338 1.00 65.55 H ATOM 1293 HD21 LEU A 477 -30.764 13.393 -34.058 1.00 70.32 H ATOM 1294 HD22 LEU A 477 -31.106 13.488 -32.509 1.00 70.32 H ATOM 1295 HD23 LEU A 477 -30.241 14.625 -33.202 1.00 70.32 H ATOM 1296 N PHE A 478 -25.600 12.854 -32.914 1.00 51.15 N ANISOU 1296 N PHE A 478 7677 5585 6173 -1152 -300 -523 N ATOM 1297 CA PHE A 478 -24.527 13.466 -33.683 1.00 56.59 C ANISOU 1297 CA PHE A 478 8406 6362 6734 -1147 -264 -495 C ATOM 1298 C PHE A 478 -24.323 12.675 -34.965 1.00 54.45 C ANISOU 1298 C PHE A 478 8188 6166 6333 -1125 -278 -586 C ATOM 1299 O PHE A 478 -24.866 11.587 -35.131 1.00 56.78 O ANISOU 1299 O PHE A 478 8527 6377 6670 -1092 -333 -679 O ATOM 1300 CB PHE A 478 -23.229 13.486 -32.886 1.00 54.06 C ANISOU 1300 CB PHE A 478 8046 6090 6404 -1118 -155 -473 C ATOM 1301 CG PHE A 478 -22.647 12.101 -32.600 1.00 55.83 C ANISOU 1301 CG PHE A 478 8280 6294 6637 -1026 -111 -587 C ATOM 1302 CD1 PHE A 478 -23.081 11.364 -31.541 1.00 53.40 C ANISOU 1302 CD1 PHE A 478 7983 5843 6465 -1025 -134 -592 C ATOM 1303 CD2 PHE A 478 -21.655 11.557 -33.408 1.00 65.69 C ANISOU 1303 CD2 PHE A 478 9531 7696 7731 -935 -84 -697 C ATOM 1304 CE1 PHE A 478 -22.531 10.097 -31.291 1.00 54.36 C ANISOU 1304 CE1 PHE A 478 8178 5878 6597 -942 -174 -688 C ATOM 1305 CE2 PHE A 478 -21.092 10.329 -33.160 1.00 61.86 C ANISOU 1305 CE2 PHE A 478 9087 7166 7251 -785 -114 -847 C ATOM 1306 CZ PHE A 478 -21.525 9.591 -32.110 1.00 58.26 C ANISOU 1306 CZ PHE A 478 8703 6473 6961 -790 -181 -835 C ATOM 1307 H PHE A 478 -25.723 12.014 -33.051 1.00 61.41 H ATOM 1308 HA PHE A 478 -24.782 14.374 -33.910 1.00 67.93 H ATOM 1309 HB2 PHE A 478 -22.565 13.986 -33.387 1.00 64.89 H ATOM 1310 HB3 PHE A 478 -23.395 13.917 -32.033 1.00 64.89 H ATOM 1311 HD1 PHE A 478 -23.744 11.700 -30.981 1.00 64.11 H ATOM 1312 HD2 PHE A 478 -21.362 12.043 -34.145 1.00 78.85 H ATOM 1313 HE1 PHE A 478 -22.840 9.592 -30.574 1.00 65.25 H ATOM 1314 HE2 PHE A 478 -20.416 10.005 -33.711 1.00 74.26 H ATOM 1315 HZ PHE A 478 -21.155 8.755 -31.939 1.00 69.94 H ATOM 1316 N ILE A 479 -23.503 13.221 -35.852 1.00 59.96 N ANISOU 1316 N ILE A 479 8882 7051 6852 -1160 -251 -554 N ATOM 1317 CA ILE A 479 -23.137 12.570 -37.107 1.00 59.45 C ANISOU 1317 CA ILE A 479 8823 7166 6600 -1113 -253 -669 C ATOM 1318 C ILE A 479 -21.707 12.099 -36.953 1.00 64.47 C ANISOU 1318 C ILE A 479 9371 8022 7104 -1011 -150 -763 C ATOM 1319 O ILE A 479 -20.823 12.904 -36.626 1.00 65.13 O ANISOU 1319 O ILE A 479 9373 8268 7105 -1101 -73 -650 O ATOM 1320 CB ILE A 479 -23.284 13.532 -38.287 1.00 60.24 C ANISOU 1320 CB ILE A 479 8941 7422 6526 -1254 -309 -560 C ATOM 1321 CG1 ILE A 479 -24.694 14.078 -38.304 1.00 63.56 C ANISOU 1321 CG1 ILE A 479 9446 7615 7091 -1305 -442 -492 C ATOM 1322 CG2 ILE A 479 -23.044 12.843 -39.607 1.00 68.99 C ANISOU 1322 CG2 ILE A 479 10030 8767 7415 -1196 -313 -697 C ATOM 1323 CD1 ILE A 479 -24.816 15.202 -39.250 1.00 70.76 C ANISOU 1323 CD1 ILE A 479 10423 8601 7860 -1455 -554 -350 C ATOM 1324 H ILE A 479 -23.134 13.991 -35.749 1.00 71.98 H ATOM 1325 HA ILE A 479 -23.704 11.800 -37.272 1.00 71.37 H ATOM 1326 HB ILE A 479 -22.626 14.236 -38.171 1.00 72.31 H ATOM 1327 HG12 ILE A 479 -25.307 13.378 -38.578 1.00 76.30 H ATOM 1328 HG13 ILE A 479 -24.927 14.395 -37.418 1.00 76.30 H ATOM 1329 HG21 ILE A 479 -23.094 13.499 -40.319 1.00 82.81 H ATOM 1330 HG22 ILE A 479 -22.165 12.434 -39.594 1.00 82.81 H ATOM 1331 HG23 ILE A 479 -23.723 12.162 -39.736 1.00 82.81 H ATOM 1332 HD11 ILE A 479 -25.704 15.584 -39.172 1.00 84.93 H ATOM 1333 HD12 ILE A 479 -24.148 15.871 -39.034 1.00 84.93 H ATOM 1334 HD13 ILE A 479 -24.676 14.873 -40.151 1.00 84.93 H ATOM 1335 N ASP A 480 -21.481 10.792 -37.116 1.00 62.98 N ANISOU 1335 N ASP A 480 9206 7825 6897 -815 -186 -980 N ATOM 1336 CA ASP A 480 -20.153 10.253 -36.858 1.00 72.53 C ANISOU 1336 CA ASP A 480 10326 9243 7990 -642 -126 -1128 C ATOM 1337 C ASP A 480 -19.276 10.428 -38.098 1.00 76.24 C ANISOU 1337 C ASP A 480 10644 10207 8115 -605 -72 -1226 C ATOM 1338 O ASP A 480 -19.678 11.021 -39.114 1.00 67.08 O ANISOU 1338 O ASP A 480 9472 9201 6814 -754 -81 -1136 O ATOM 1339 CB ASP A 480 -20.227 8.791 -36.379 1.00 69.60 C ANISOU 1339 CB ASP A 480 10083 8613 7749 -416 -262 -1337 C ATOM 1340 CG ASP A 480 -20.591 7.782 -37.482 1.00 77.13 C ANISOU 1340 CG ASP A 480 11141 9552 8613 -247 -431 -1567 C ATOM 1341 OD1 ASP A 480 -20.890 8.173 -38.644 1.00 74.70 O ANISOU 1341 OD1 ASP A 480 10787 9451 8144 -303 -414 -1569 O ATOM 1342 OD2 ASP A 480 -20.565 6.563 -37.152 1.00 75.00 O ANISOU 1342 OD2 ASP A 480 11027 9036 8434 -57 -619 -1747 O ATOM 1343 H ASP A 480 -22.068 10.216 -37.368 1.00 75.59 H ATOM 1344 HA ASP A 480 -19.743 10.753 -36.135 1.00 87.06 H ATOM 1345 HB2 ASP A 480 -19.362 8.537 -36.022 1.00 83.55 H ATOM 1346 HB3 ASP A 480 -20.904 8.726 -35.687 1.00 83.55 H ATOM 1347 N SER A 481 -18.054 9.909 -38.011 1.00 86.37 N ANISOU 1347 N SER A 481 11792 11792 9232 -403 -27 -1416 N ATOM 1348 CA SER A 481 -17.104 10.107 -39.095 1.00 82.10 C ANISOU 1348 CA SER A 481 11024 11873 8297 -376 46 -1519 C ATOM 1349 C SER A 481 -17.623 9.567 -40.425 1.00 80.16 C ANISOU 1349 C SER A 481 10811 11757 7891 -264 -52 -1698 C ATOM 1350 O SER A 481 -17.233 10.076 -41.479 1.00 82.41 O ANISOU 1350 O SER A 481 10920 12552 7839 -381 12 -1671 O ATOM 1351 CB SER A 481 -15.763 9.468 -38.728 1.00 94.90 C ANISOU 1351 CB SER A 481 12466 13833 9760 -94 84 -1773 C ATOM 1352 OG SER A 481 -15.938 8.120 -38.339 1.00100.93 O ANISOU 1352 OG SER A 481 13400 14251 10698 269 -93 -2063 O ATOM 1353 H SER A 481 -17.757 9.448 -37.348 1.00103.67 H ATOM 1354 HA SER A 481 -16.960 11.059 -39.214 1.00 98.54 H ATOM 1355 HB2 SER A 481 -15.176 9.500 -39.500 1.00113.91 H ATOM 1356 HB3 SER A 481 -15.369 9.961 -37.991 1.00113.91 H ATOM 1357 HG SER A 481 -15.198 7.724 -38.331 1.00121.14 H ATOM 1358 N ALA A 482 -18.531 8.577 -40.418 1.00 74.98 N ANISOU 1358 N ALA A 482 10378 10660 7450 -83 -225 -1854 N ATOM 1359 CA ALA A 482 -18.983 7.914 -41.649 1.00 75.48 C ANISOU 1359 CA ALA A 482 10494 10817 7369 73 -356 -2072 C ATOM 1360 C ALA A 482 -20.341 8.407 -42.137 1.00 68.78 C ANISOU 1360 C ALA A 482 9790 9694 6649 -182 -400 -1859 C ATOM 1361 O ALA A 482 -20.977 7.756 -42.966 1.00 74.69 O ANISOU 1361 O ALA A 482 10644 10364 7369 -69 -543 -2019 O ATOM 1362 CB ALA A 482 -19.043 6.401 -41.437 1.00 73.43 C ANISOU 1362 CB ALA A 482 10420 10248 7232 452 -599 -2414 C ATOM 1363 H ALA A 482 -18.901 8.271 -39.705 1.00 90.00 H ATOM 1364 HA ALA A 482 -18.333 8.106 -42.342 1.00 90.61 H ATOM 1365 HB1 ALA A 482 -19.340 5.979 -42.258 1.00 88.14 H ATOM 1366 HB2 ALA A 482 -18.159 6.079 -41.200 1.00 88.14 H ATOM 1367 HB3 ALA A 482 -19.668 6.207 -40.721 1.00 88.14 H ATOM 1368 N ASN A 483 -20.830 9.499 -41.580 1.00 65.88 N ANISOU 1368 N ASN A 483 9445 9150 6437 -490 -315 -1529 N ATOM 1369 CA ASN A 483 -22.128 10.078 -41.902 1.00 66.92 C ANISOU 1369 CA ASN A 483 9701 9026 6701 -703 -376 -1338 C ATOM 1370 C ASN A 483 -23.316 9.234 -41.455 1.00 68.43 C ANISOU 1370 C ASN A 483 10079 8738 7181 -643 -524 -1396 C ATOM 1371 O ASN A 483 -24.427 9.423 -41.947 1.00 71.54 O ANISOU 1371 O ASN A 483 10554 8989 7640 -753 -605 -1324 O ATOM 1372 CB ASN A 483 -22.215 10.405 -43.391 1.00 82.34 C ANISOU 1372 CB ASN A 483 11600 11321 8366 -773 -394 -1349 C ATOM 1373 CG ASN A 483 -21.762 11.835 -43.666 1.00 99.52 C ANISOU 1373 CG ASN A 483 13675 13789 10351 -1081 -309 -1062 C ATOM 1374 OD1 ASN A 483 -22.591 12.723 -43.917 1.00107.04 O ANISOU 1374 OD1 ASN A 483 14734 14567 11369 -1300 -385 -842 O ATOM 1375 ND2 ASN A 483 -20.442 12.081 -43.545 1.00 93.80 N ANISOU 1375 ND2 ASN A 483 12756 13492 9390 -1111 -188 -1054 N ATOM 1376 H ASN A 483 -20.409 9.949 -40.980 1.00 79.08 H ATOM 1377 HA ASN A 483 -22.213 10.907 -41.405 1.00 80.33 H ATOM 1378 HB2 ASN A 483 -21.642 9.801 -43.887 1.00 98.83 H ATOM 1379 HB3 ASN A 483 -23.134 10.312 -43.688 1.00 98.83 H ATOM 1380 HD21 ASN A 483 -19.905 11.448 -43.322 1.00112.58 H ATOM 1381 HD22 ASN A 483 -20.137 12.872 -43.690 1.00112.58 H ATOM 1382 N ASN A 484 -23.126 8.377 -40.465 1.00 67.01 N ANISOU 1382 N ASN A 484 9970 8321 7171 -514 -577 -1490 N ATOM 1383 CA ASN A 484 -24.233 7.759 -39.768 1.00 62.06 C ANISOU 1383 CA ASN A 484 9499 7272 6808 -582 -714 -1443 C ATOM 1384 C ASN A 484 -24.773 8.747 -38.754 1.00 60.88 C ANISOU 1384 C ASN A 484 9289 7015 6826 -796 -611 -1187 C ATOM 1385 O ASN A 484 -24.039 9.572 -38.222 1.00 57.80 O ANISOU 1385 O ASN A 484 8794 6757 6409 -830 -471 -1086 O ATOM 1386 CB ASN A 484 -23.738 6.503 -39.067 1.00 61.04 C ANISOU 1386 CB ASN A 484 9492 6934 6765 -400 -855 -1610 C ATOM 1387 CG ASN A 484 -23.054 5.545 -40.025 1.00 64.28 C ANISOU 1387 CG ASN A 484 9962 7473 6988 -89 -1005 -1939 C ATOM 1388 OD1 ASN A 484 -23.568 5.281 -41.099 1.00 63.12 O ANISOU 1388 OD1 ASN A 484 9871 7364 6749 -51 -1110 -2044 O ATOM 1389 ND2 ASN A 484 -21.899 5.036 -39.640 1.00 74.05 N ANISOU 1389 ND2 ASN A 484 11178 8802 8157 163 -1032 -2128 N ATOM 1390 H ASN A 484 -22.353 8.136 -40.175 1.00 80.44 H ATOM 1391 HA ASN A 484 -24.946 7.508 -40.375 1.00 74.49 H ATOM 1392 HB2 ASN A 484 -23.100 6.752 -38.380 1.00 73.27 H ATOM 1393 HB3 ASN A 484 -24.493 6.043 -38.667 1.00 73.27 H ATOM 1394 HD21 ASN A 484 -21.568 5.252 -38.876 1.00 88.89 H ATOM 1395 HD22 ASN A 484 -21.477 4.489 -40.152 1.00 88.89 H ATOM 1396 N VAL A 485 -26.064 8.679 -38.495 1.00 51.98 N ANISOU 1396 N VAL A 485 8213 5686 5851 -934 -698 -1097 N ATOM 1397 CA VAL A 485 -26.632 9.439 -37.388 1.00 53.74 C ANISOU 1397 CA VAL A 485 8354 5846 6220 -1074 -633 -920 C ATOM 1398 C VAL A 485 -26.681 8.530 -36.179 1.00 50.85 C ANISOU 1398 C VAL A 485 8031 5299 5992 -1106 -686 -909 C ATOM 1399 O VAL A 485 -27.122 7.384 -36.288 1.00 59.11 O ANISOU 1399 O VAL A 485 9206 6177 7076 -1135 -857 -970 O ATOM 1400 CB VAL A 485 -28.024 9.963 -37.740 1.00 58.87 C ANISOU 1400 CB VAL A 485 8973 6487 6909 -1192 -701 -848 C ATOM 1401 CG1 VAL A 485 -28.519 10.867 -36.615 1.00 54.67 C ANISOU 1401 CG1 VAL A 485 8318 5973 6481 -1258 -650 -728 C ATOM 1402 CG2 VAL A 485 -27.928 10.713 -39.015 1.00 59.06 C ANISOU 1402 CG2 VAL A 485 9006 6649 6783 -1171 -701 -853 C ATOM 1403 H VAL A 485 -26.629 8.206 -38.938 1.00 62.40 H ATOM 1404 HA VAL A 485 -26.068 10.202 -37.187 1.00 64.52 H ATOM 1405 HB VAL A 485 -28.657 9.236 -37.845 1.00 70.67 H ATOM 1406 HG11 VAL A 485 -29.348 11.289 -36.891 1.00 65.63 H ATOM 1407 HG12 VAL A 485 -28.669 10.331 -35.821 1.00 65.63 H ATOM 1408 HG13 VAL A 485 -27.848 11.544 -36.436 1.00 65.63 H ATOM 1409 HG21 VAL A 485 -28.792 11.106 -39.215 1.00 70.89 H ATOM 1410 HG22 VAL A 485 -27.261 11.410 -38.921 1.00 70.89 H ATOM 1411 HG23 VAL A 485 -27.671 10.101 -39.722 1.00 70.89 H ATOM 1412 N VAL A 486 -26.210 9.028 -35.040 1.00 51.09 N ANISOU 1412 N VAL A 486 7976 5351 6085 -1121 -573 -820 N ATOM 1413 CA VAL A 486 -25.953 8.227 -33.854 1.00 54.63 C ANISOU 1413 CA VAL A 486 8468 5659 6630 -1148 -611 -797 C ATOM 1414 C VAL A 486 -26.503 8.939 -32.626 1.00 53.89 C ANISOU 1414 C VAL A 486 8227 5628 6621 -1277 -527 -648 C ATOM 1415 O VAL A 486 -26.190 10.102 -32.390 1.00 54.98 O ANISOU 1415 O VAL A 486 8258 5886 6748 -1229 -403 -608 O ATOM 1416 CB VAL A 486 -24.448 7.954 -33.659 1.00 57.49 C ANISOU 1416 CB VAL A 486 8864 6038 6944 -963 -559 -897 C ATOM 1417 CG1 VAL A 486 -24.272 7.031 -32.427 1.00 53.41 C ANISOU 1417 CG1 VAL A 486 8437 5320 6535 -1000 -656 -865 C ATOM 1418 CG2 VAL A 486 -23.861 7.307 -34.941 1.00 55.50 C ANISOU 1418 CG2 VAL A 486 8703 5835 6551 -770 -647 -1108 C ATOM 1419 H VAL A 486 -26.025 9.860 -34.928 1.00 61.33 H ATOM 1420 HA VAL A 486 -26.423 7.385 -33.954 1.00 65.58 H ATOM 1421 HB VAL A 486 -23.963 8.779 -33.501 1.00 69.02 H ATOM 1422 HG11 VAL A 486 -23.345 6.752 -32.372 1.00 64.11 H ATOM 1423 HG12 VAL A 486 -24.518 7.521 -31.627 1.00 64.11 H ATOM 1424 HG13 VAL A 486 -24.845 6.255 -32.529 1.00 64.11 H ATOM 1425 HG21 VAL A 486 -22.922 7.109 -34.793 1.00 66.63 H ATOM 1426 HG22 VAL A 486 -24.345 6.489 -35.132 1.00 66.63 H ATOM 1427 HG23 VAL A 486 -23.956 7.928 -35.680 1.00 66.63 H ATOM 1428 N TYR A 487 -27.260 8.209 -31.810 1.00 54.22 N ANISOU 1428 N TYR A 487 8272 5606 6725 -1448 -622 -569 N ATOM 1429 CA TYR A 487 -27.643 8.665 -30.475 1.00 56.87 C ANISOU 1429 CA TYR A 487 8441 6071 7098 -1556 -547 -454 C ATOM 1430 C TYR A 487 -26.925 7.830 -29.426 1.00 55.62 C ANISOU 1430 C TYR A 487 8370 5782 6982 -1605 -583 -401 C ATOM 1431 O TYR A 487 -27.251 6.656 -29.257 1.00 54.71 O ANISOU 1431 O TYR A 487 8395 5514 6878 -1770 -770 -347 O ATOM 1432 CB TYR A 487 -29.139 8.509 -30.265 1.00 51.68 C ANISOU 1432 CB TYR A 487 7653 5567 6414 -1773 -628 -377 C ATOM 1433 CG TYR A 487 -29.635 9.056 -28.948 1.00 58.44 C ANISOU 1433 CG TYR A 487 8268 6686 7250 -1857 -547 -300 C ATOM 1434 CD1 TYR A 487 -29.491 10.409 -28.634 1.00 58.97 C ANISOU 1434 CD1 TYR A 487 8183 6906 7317 -1664 -426 -362 C ATOM 1435 CD2 TYR A 487 -30.267 8.223 -28.020 1.00 65.59 C ANISOU 1435 CD2 TYR A 487 9102 7710 8110 -2142 -628 -164 C ATOM 1436 CE1 TYR A 487 -29.965 10.922 -27.406 1.00 64.18 C ANISOU 1436 CE1 TYR A 487 8603 7850 7934 -1683 -374 -344 C ATOM 1437 CE2 TYR A 487 -30.752 8.726 -26.812 1.00 72.17 C ANISOU 1437 CE2 TYR A 487 9661 8892 8870 -2215 -545 -112 C ATOM 1438 CZ TYR A 487 -30.622 10.073 -26.532 1.00 65.34 C ANISOU 1438 CZ TYR A 487 8625 8196 8006 -1951 -414 -230 C ATOM 1439 OH TYR A 487 -31.095 10.536 -25.342 1.00 76.97 O ANISOU 1439 OH TYR A 487 9819 10042 9386 -1973 -356 -227 O ATOM 1440 H TYR A 487 -27.569 7.431 -32.010 1.00 65.09 H ATOM 1441 HA TYR A 487 -27.376 9.594 -30.391 1.00 68.27 H ATOM 1442 HB2 TYR A 487 -29.603 8.980 -30.974 1.00 62.03 H ATOM 1443 HB3 TYR A 487 -29.359 7.565 -30.294 1.00 62.03 H ATOM 1444 HD1 TYR A 487 -29.079 10.980 -29.241 1.00 70.79 H ATOM 1445 HD2 TYR A 487 -30.367 7.319 -28.211 1.00 78.74 H ATOM 1446 HE1 TYR A 487 -29.837 11.817 -27.188 1.00 77.04 H ATOM 1447 HE2 TYR A 487 -31.159 8.158 -26.198 1.00 86.63 H ATOM 1448 HH TYR A 487 -31.500 9.922 -24.937 1.00 92.39 H ATOM 1449 N LYS A 488 -26.008 8.440 -28.687 1.00 51.92 N ANISOU 1449 N LYS A 488 7837 5357 6534 -1488 -444 -399 N ATOM 1450 CA LYS A 488 -25.066 7.701 -27.851 1.00 55.09 C ANISOU 1450 CA LYS A 488 8347 5614 6972 -1467 -481 -382 C ATOM 1451 C LYS A 488 -24.961 8.339 -26.475 1.00 56.24 C ANISOU 1451 C LYS A 488 8328 5905 7136 -1514 -355 -285 C ATOM 1452 O LYS A 488 -24.919 9.555 -26.368 1.00 48.58 O ANISOU 1452 O LYS A 488 7204 5096 6158 -1418 -214 -304 O ATOM 1453 CB LYS A 488 -23.661 7.717 -28.481 1.00 59.10 C ANISOU 1453 CB LYS A 488 8944 6057 7455 -1208 -436 -531 C ATOM 1454 CG LYS A 488 -22.557 7.217 -27.565 1.00 59.35 C ANISOU 1454 CG LYS A 488 9044 5989 7517 -1118 -453 -547 C ATOM 1455 CD LYS A 488 -21.148 7.209 -28.234 1.00 65.28 C ANISOU 1455 CD LYS A 488 9821 6788 8194 -839 -411 -733 C ATOM 1456 CE LYS A 488 -20.028 6.864 -27.209 1.00 72.25 C ANISOU 1456 CE LYS A 488 10731 7618 9105 -725 -415 -759 C ATOM 1457 NZ LYS A 488 -18.654 6.983 -27.755 1.00 96.69 N ANISOU 1457 NZ LYS A 488 13766 10883 12087 -458 -348 -946 N ATOM 1458 H LYS A 488 -25.909 9.293 -28.651 1.00 62.33 H ATOM 1459 HA LYS A 488 -25.387 6.791 -27.752 1.00 66.13 H ATOM 1460 HB2 LYS A 488 -23.669 7.150 -29.268 1.00 70.94 H ATOM 1461 HB3 LYS A 488 -23.445 8.629 -28.730 1.00 70.94 H ATOM 1462 HG2 LYS A 488 -22.512 7.793 -26.786 1.00 71.24 H ATOM 1463 HG3 LYS A 488 -22.762 6.308 -27.295 1.00 71.24 H ATOM 1464 HD2 LYS A 488 -21.131 6.542 -28.938 1.00 78.36 H ATOM 1465 HD3 LYS A 488 -20.963 8.087 -28.603 1.00 78.36 H ATOM 1466 HE2 LYS A 488 -20.098 7.470 -26.455 1.00 86.73 H ATOM 1467 HE3 LYS A 488 -20.148 5.949 -26.911 1.00 86.73 H ATOM 1468 HZ1 LYS A 488 -18.556 6.439 -28.452 1.00116.05 H ATOM 1469 HZ2 LYS A 488 -18.502 7.819 -28.018 1.00116.05 H ATOM 1470 HZ3 LYS A 488 -18.059 6.763 -27.131 1.00116.05 H ATOM 1471 N GLN A 489 -24.821 7.517 -25.452 1.00 50.06 N ANISOU 1471 N GLN A 489 7608 5040 6371 -1646 -440 -190 N ATOM 1472 CA GLN A 489 -24.550 8.026 -24.123 1.00 50.85 C ANISOU 1472 CA GLN A 489 7563 5283 6474 -1669 -324 -113 C ATOM 1473 C GLN A 489 -23.053 8.212 -23.987 1.00 50.45 C ANISOU 1473 C GLN A 489 7588 5115 6465 -1438 -248 -198 C ATOM 1474 O GLN A 489 -22.295 7.256 -24.151 1.00 53.66 O ANISOU 1474 O GLN A 489 8192 5304 6893 -1366 -375 -251 O ATOM 1475 CB GLN A 489 -25.079 7.023 -23.116 1.00 51.65 C ANISOU 1475 CB GLN A 489 7703 5381 6542 -1966 -472 59 C ATOM 1476 CG GLN A 489 -24.795 7.511 -21.748 1.00 55.55 C ANISOU 1476 CG GLN A 489 8036 6060 7013 -1987 -351 130 C ATOM 1477 CD GLN A 489 -25.465 6.682 -20.733 1.00 60.70 C ANISOU 1477 CD GLN A 489 8666 6821 7576 -2344 -483 336 C ATOM 1478 OE1 GLN A 489 -26.650 6.854 -20.469 1.00 66.75 O ANISOU 1478 OE1 GLN A 489 9206 7934 8222 -2564 -469 419 O ATOM 1479 NE2 GLN A 489 -24.709 5.787 -20.121 1.00 60.15 N ANISOU 1479 NE2 GLN A 489 8816 6499 7540 -2416 -629 424 N ATOM 1480 H GLN A 489 -24.879 6.661 -25.501 1.00 60.09 H ATOM 1481 HA GLN A 489 -24.977 8.882 -23.966 1.00 61.04 H ATOM 1482 HB2 GLN A 489 -26.038 6.924 -23.223 1.00 62.01 H ATOM 1483 HB3 GLN A 489 -24.642 6.166 -23.243 1.00 62.01 H ATOM 1484 HG2 GLN A 489 -23.839 7.478 -21.587 1.00 66.69 H ATOM 1485 HG3 GLN A 489 -25.115 8.423 -21.659 1.00 66.69 H ATOM 1486 HE21 GLN A 489 -23.877 5.716 -20.325 1.00 72.21 H ATOM 1487 HE22 GLN A 489 -25.050 5.276 -19.519 1.00 72.21 H ATOM 1488 N TYR A 490 -22.611 9.444 -23.804 1.00 48.97 N ANISOU 1488 N TYR A 490 7255 5074 6278 -1305 -77 -234 N ATOM 1489 CA TYR A 490 -21.205 9.725 -23.597 1.00 51.96 C ANISOU 1489 CA TYR A 490 7659 5413 6671 -1134 5 -291 C ATOM 1490 C TYR A 490 -20.948 9.689 -22.108 1.00 53.49 C ANISOU 1490 C TYR A 490 7795 5638 6892 -1186 36 -207 C ATOM 1491 O TYR A 490 -21.582 10.447 -21.366 1.00 48.82 O ANISOU 1491 O TYR A 490 7041 5222 6288 -1247 102 -153 O ATOM 1492 CB TYR A 490 -20.828 11.101 -24.128 1.00 52.46 C ANISOU 1492 CB TYR A 490 7625 5600 6706 -1030 123 -330 C ATOM 1493 CG TYR A 490 -20.604 11.133 -25.613 1.00 53.20 C ANISOU 1493 CG TYR A 490 7780 5698 6734 -967 106 -409 C ATOM 1494 CD1 TYR A 490 -21.680 11.113 -26.491 1.00 54.21 C ANISOU 1494 CD1 TYR A 490 7927 5823 6846 -1030 40 -416 C ATOM 1495 CD2 TYR A 490 -19.331 11.139 -26.148 1.00 56.69 C ANISOU 1495 CD2 TYR A 490 8235 6204 7100 -851 152 -483 C ATOM 1496 CE1 TYR A 490 -21.502 11.143 -27.854 1.00 54.79 C ANISOU 1496 CE1 TYR A 490 8052 5926 6839 -982 22 -485 C ATOM 1497 CE2 TYR A 490 -19.140 11.146 -27.531 1.00 60.93 C ANISOU 1497 CE2 TYR A 490 8791 6835 7524 -808 140 -560 C ATOM 1498 CZ TYR A 490 -20.241 11.158 -28.368 1.00 60.90 C ANISOU 1498 CZ TYR A 490 8828 6794 7517 -877 74 -555 C ATOM 1499 OH TYR A 490 -20.104 11.188 -29.724 1.00 61.59 O ANISOU 1499 OH TYR A 490 8930 6992 7478 -846 59 -624 O ATOM 1500 H TYR A 490 -23.114 10.142 -23.795 1.00 58.79 H ATOM 1501 HA TYR A 490 -20.672 9.061 -24.061 1.00 62.38 H ATOM 1502 HB2 TYR A 490 -21.544 11.722 -23.923 1.00 62.97 H ATOM 1503 HB3 TYR A 490 -20.007 11.387 -23.698 1.00 62.97 H ATOM 1504 HD1 TYR A 490 -22.544 11.078 -26.147 1.00 65.07 H ATOM 1505 HD2 TYR A 490 -18.593 11.139 -25.581 1.00 68.05 H ATOM 1506 HE1 TYR A 490 -22.239 11.154 -28.421 1.00 65.77 H ATOM 1507 HE2 TYR A 490 -18.280 11.142 -27.886 1.00 73.14 H ATOM 1508 HH TYR A 490 -19.290 11.182 -29.931 1.00 73.93 H ATOM 1509 N GLU A 491 -19.982 8.892 -21.680 1.00 53.75 N ANISOU 1509 N GLU A 491 7950 5527 6946 -1125 -23 -223 N ATOM 1510 CA GLU A 491 -19.659 8.793 -20.253 1.00 50.64 C ANISOU 1510 CA GLU A 491 7520 5151 6569 -1181 -8 -133 C ATOM 1511 C GLU A 491 -18.803 9.962 -19.774 1.00 47.83 C ANISOU 1511 C GLU A 491 7026 4925 6221 -1042 162 -168 C ATOM 1512 O GLU A 491 -18.185 10.703 -20.547 1.00 43.63 O ANISOU 1512 O GLU A 491 6462 4441 5674 -915 240 -248 O ATOM 1513 CB GLU A 491 -18.945 7.458 -19.966 1.00 50.76 C ANISOU 1513 CB GLU A 491 7760 4918 6608 -1154 -197 -142 C ATOM 1514 CG GLU A 491 -19.727 6.187 -20.346 1.00 57.82 C ANISOU 1514 CG GLU A 491 8869 5599 7500 -1324 -461 -87 C ATOM 1515 CD GLU A 491 -20.998 5.996 -19.538 1.00 62.09 C ANISOU 1515 CD GLU A 491 9340 6258 7993 -1687 -514 135 C ATOM 1516 OE1 GLU A 491 -21.058 6.475 -18.376 1.00 73.73 O ANISOU 1516 OE1 GLU A 491 10649 7934 9431 -1782 -400 239 O ATOM 1517 OE2 GLU A 491 -21.934 5.370 -20.078 1.00 75.61 O ANISOU 1517 OE2 GLU A 491 11142 7907 9679 -1883 -674 200 O ATOM 1518 H GLU A 491 -19.497 8.396 -22.189 1.00 64.52 H ATOM 1519 HA GLU A 491 -20.484 8.826 -19.745 1.00 60.79 H ATOM 1520 HB2 GLU A 491 -18.113 7.444 -20.465 1.00 60.94 H ATOM 1521 HB3 GLU A 491 -18.762 7.409 -19.014 1.00 60.94 H ATOM 1522 HG2 GLU A 491 -19.976 6.240 -21.282 1.00 69.40 H ATOM 1523 HG3 GLU A 491 -19.161 5.414 -20.196 1.00 69.40 H ATOM 1524 N ASP A 492 -18.835 10.199 -18.457 1.00 45.59 N ANISOU 1524 N ASP A 492 6652 4730 5939 -1103 202 -88 N ATOM 1525 CA ASP A 492 -17.927 11.166 -17.837 1.00 45.19 C ANISOU 1525 CA ASP A 492 6508 4758 5904 -978 318 -117 C ATOM 1526 C ASP A 492 -18.030 12.549 -18.469 1.00 43.47 C ANISOU 1526 C ASP A 492 6202 4634 5679 -904 384 -169 C ATOM 1527 O ASP A 492 -17.033 13.212 -18.735 1.00 43.07 O ANISOU 1527 O ASP A 492 6154 4584 5627 -820 430 -199 O ATOM 1528 CB ASP A 492 -16.481 10.692 -17.908 1.00 50.55 C ANISOU 1528 CB ASP A 492 7281 5327 6596 -841 311 -179 C ATOM 1529 CG ASP A 492 -16.247 9.300 -17.228 1.00 52.35 C ANISOU 1529 CG ASP A 492 7664 5386 6842 -875 163 -142 C ATOM 1530 OD1 ASP A 492 -16.895 8.986 -16.201 1.00 57.54 O ANISOU 1530 OD1 ASP A 492 8312 6061 7490 -1050 116 -11 O ATOM 1531 OD2 ASP A 492 -15.413 8.506 -17.750 1.00 64.71 O ANISOU 1531 OD2 ASP A 492 9364 6815 8407 -725 60 -252 O ATOM 1532 H ASP A 492 -19.371 9.813 -17.906 1.00 54.73 H ATOM 1533 HA ASP A 492 -18.197 11.242 -16.909 1.00 54.25 H ATOM 1534 HB2 ASP A 492 -16.222 10.614 -18.840 1.00 60.68 H ATOM 1535 HB3 ASP A 492 -15.916 11.340 -17.460 1.00 60.68 H ATOM 1536 N MET A 493 -19.250 13.018 -18.612 1.00 46.87 N ANISOU 1536 N MET A 493 6553 5164 6090 -953 359 -170 N ATOM 1537 CA MET A 493 -19.455 14.324 -19.201 1.00 46.10 C ANISOU 1537 CA MET A 493 6424 5100 5991 -873 342 -223 C ATOM 1538 C MET A 493 -19.728 15.418 -18.186 1.00 43.29 C ANISOU 1538 C MET A 493 5957 4858 5634 -785 317 -263 C ATOM 1539 O MET A 493 -19.481 16.588 -18.498 1.00 41.38 O ANISOU 1539 O MET A 493 5759 4558 5407 -702 243 -299 O ATOM 1540 CB MET A 493 -20.641 14.232 -20.173 1.00 47.58 C ANISOU 1540 CB MET A 493 6610 5316 6153 -918 280 -248 C ATOM 1541 CG MET A 493 -20.314 13.448 -21.470 1.00 46.37 C ANISOU 1541 CG MET A 493 6588 5038 5990 -956 272 -248 C ATOM 1542 SD MET A 493 -19.061 14.159 -22.529 1.00 49.35 S ANISOU 1542 SD MET A 493 7041 5381 6329 -899 297 -262 S ATOM 1543 CE MET A 493 -19.940 15.560 -23.266 1.00 51.83 C ANISOU 1543 CE MET A 493 7363 5704 6628 -904 189 -259 C ATOM 1544 H MET A 493 -19.967 12.605 -18.378 1.00 56.26 H ATOM 1545 HA MET A 493 -18.660 14.581 -19.694 1.00 55.34 H ATOM 1546 HB2 MET A 493 -21.376 13.781 -19.729 1.00 57.12 H ATOM 1547 HB3 MET A 493 -20.908 15.130 -20.427 1.00 57.12 H ATOM 1548 HG2 MET A 493 -20.007 12.563 -21.219 1.00 55.66 H ATOM 1549 HG3 MET A 493 -21.127 13.380 -21.995 1.00 55.66 H ATOM 1550 HE1 MET A 493 -19.406 15.921 -23.992 1.00 62.23 H ATOM 1551 HE2 MET A 493 -20.795 15.253 -23.605 1.00 62.23 H ATOM 1552 HE3 MET A 493 -20.077 16.239 -22.587 1.00 62.23 H ATOM 1553 N VAL A 494 -20.275 15.070 -17.017 1.00 40.20 N ANISOU 1553 N VAL A 494 5432 4639 5202 -810 339 -260 N ATOM 1554 CA VAL A 494 -20.781 15.991 -16.015 1.00 42.53 C ANISOU 1554 CA VAL A 494 5571 5137 5453 -685 299 -353 C ATOM 1555 C VAL A 494 -20.138 15.697 -14.662 1.00 46.00 C ANISOU 1555 C VAL A 494 5950 5654 5874 -703 368 -309 C ATOM 1556 O VAL A 494 -20.215 14.570 -14.164 1.00 45.30 O ANISOU 1556 O VAL A 494 5836 5634 5742 -868 419 -203 O ATOM 1557 CB VAL A 494 -22.318 15.850 -15.933 1.00 42.30 C ANISOU 1557 CB VAL A 494 5349 5411 5314 -708 262 -416 C ATOM 1558 CG1 VAL A 494 -22.896 16.697 -14.822 1.00 45.51 C ANISOU 1558 CG1 VAL A 494 5534 6136 5620 -530 213 -568 C ATOM 1559 CG2 VAL A 494 -22.958 16.186 -17.293 1.00 47.04 C ANISOU 1559 CG2 VAL A 494 6017 5920 5937 -672 178 -469 C ATOM 1560 H VAL A 494 -20.366 14.250 -16.773 1.00 48.26 H ATOM 1561 HA VAL A 494 -20.532 16.901 -16.240 1.00 51.07 H ATOM 1562 HB VAL A 494 -22.532 14.929 -15.719 1.00 50.79 H ATOM 1563 HG11 VAL A 494 -23.850 16.798 -14.967 1.00 54.63 H ATOM 1564 HG12 VAL A 494 -22.735 16.257 -13.973 1.00 54.63 H ATOM 1565 HG13 VAL A 494 -22.467 17.566 -14.831 1.00 54.63 H ATOM 1566 HG21 VAL A 494 -23.915 16.039 -17.237 1.00 56.47 H ATOM 1567 HG22 VAL A 494 -22.778 17.116 -17.506 1.00 56.47 H ATOM 1568 HG23 VAL A 494 -22.574 15.611 -17.973 1.00 56.47 H ATOM 1569 N VAL A 495 -19.540 16.710 -14.040 1.00 41.27 N ANISOU 1569 N VAL A 495 5348 5031 5301 -548 332 -381 N ATOM 1570 CA VAL A 495 -18.957 16.469 -12.731 1.00 41.47 C ANISOU 1570 CA VAL A 495 5307 5147 5301 -554 394 -348 C ATOM 1571 C VAL A 495 -20.043 16.315 -11.718 1.00 41.72 C ANISOU 1571 C VAL A 495 5099 5570 5184 -562 402 -398 C ATOM 1572 O VAL A 495 -20.974 17.128 -11.662 1.00 47.13 O ANISOU 1572 O VAL A 495 5637 6476 5792 -399 317 -564 O ATOM 1573 CB VAL A 495 -18.020 17.618 -12.338 1.00 43.40 C ANISOU 1573 CB VAL A 495 5620 5264 5607 -397 329 -413 C ATOM 1574 CG1 VAL A 495 -17.565 17.375 -10.961 1.00 46.42 C ANISOU 1574 CG1 VAL A 495 5912 5775 5949 -390 390 -396 C ATOM 1575 CG2 VAL A 495 -16.924 17.623 -13.337 1.00 44.18 C ANISOU 1575 CG2 VAL A 495 5902 5093 5791 -469 340 -325 C ATOM 1576 H VAL A 495 -19.463 17.511 -14.344 1.00 49.54 H ATOM 1577 HA VAL A 495 -18.446 15.646 -12.769 1.00 49.78 H ATOM 1578 HB VAL A 495 -18.434 18.496 -12.342 1.00 52.11 H ATOM 1579 HG11 VAL A 495 -16.880 18.023 -10.736 1.00 55.72 H ATOM 1580 HG12 VAL A 495 -18.320 17.468 -10.358 1.00 55.72 H ATOM 1581 HG13 VAL A 495 -17.203 16.477 -10.902 1.00 55.72 H ATOM 1582 HG21 VAL A 495 -16.204 18.187 -13.015 1.00 53.04 H ATOM 1583 HG22 VAL A 495 -16.604 16.715 -13.459 1.00 53.04 H ATOM 1584 HG23 VAL A 495 -17.264 17.968 -14.178 1.00 53.04 H ATOM 1585 N GLU A 496 -19.934 15.290 -10.867 1.00 44.67 N ANISOU 1585 N GLU A 496 5416 6070 5486 -746 476 -265 N ATOM 1586 CA GLU A 496 -20.881 15.113 -9.792 1.00 45.47 C ANISOU 1586 CA GLU A 496 5249 6642 5386 -818 492 -277 C ATOM 1587 C GLU A 496 -20.298 15.341 -8.421 1.00 48.79 C ANISOU 1587 C GLU A 496 5582 7212 5745 -758 524 -290 C ATOM 1588 O GLU A 496 -21.040 15.689 -7.520 1.00 49.78 O ANISOU 1588 O GLU A 496 5436 7799 5678 -700 522 -392 O ATOM 1589 CB GLU A 496 -21.498 13.703 -9.776 1.00 45.17 C ANISOU 1589 CB GLU A 496 5186 6737 5240 -1179 503 -64 C ATOM 1590 CG GLU A 496 -22.398 13.307 -10.954 1.00 47.41 C ANISOU 1590 CG GLU A 496 5492 6998 5523 -1297 459 -40 C ATOM 1591 CD GLU A 496 -23.686 14.085 -11.039 1.00 59.00 C ANISOU 1591 CD GLU A 496 6672 8903 6843 -1173 439 -219 C ATOM 1592 OE1 GLU A 496 -24.191 14.420 -9.962 1.00 55.86 O ANISOU 1592 OE1 GLU A 496 5986 8991 6248 -1133 459 -299 O ATOM 1593 OE2 GLU A 496 -24.207 14.297 -12.159 1.00 55.88 O ANISOU 1593 OE2 GLU A 496 6322 8407 6504 -1114 393 -288 O ATOM 1594 H GLU A 496 -19.316 14.692 -10.900 1.00 53.63 H ATOM 1595 HA GLU A 496 -21.596 15.748 -9.956 1.00 54.59 H ATOM 1596 HB2 GLU A 496 -20.771 13.061 -9.752 1.00 54.23 H ATOM 1597 HB3 GLU A 496 -22.037 13.624 -8.974 1.00 54.23 H ATOM 1598 HG2 GLU A 496 -21.911 13.455 -11.780 1.00 56.91 H ATOM 1599 HG3 GLU A 496 -22.627 12.369 -10.868 1.00 56.91 H ATOM 1600 N SER A 497 -18.984 15.147 -8.238 1.00 42.99 N ANISOU 1600 N SER A 497 5047 6143 5145 -757 549 -206 N ATOM 1601 CA SER A 497 -18.353 15.489 -6.978 1.00 48.27 C ANISOU 1601 CA SER A 497 5649 6921 5771 -671 569 -235 C ATOM 1602 C SER A 497 -16.907 15.819 -7.298 1.00 44.43 C ANISOU 1602 C SER A 497 5389 6015 5476 -565 566 -229 C ATOM 1603 O SER A 497 -16.375 15.427 -8.345 1.00 40.16 O ANISOU 1603 O SER A 497 5029 5174 5055 -618 570 -164 O ATOM 1604 CB SER A 497 -18.537 14.345 -5.965 1.00 56.86 C ANISOU 1604 CB SER A 497 6652 8250 6702 -948 606 -45 C ATOM 1605 OG SER A 497 -17.847 13.222 -6.440 1.00 65.38 O ANISOU 1605 OG SER A 497 7986 8960 7897 -1132 583 142 O ATOM 1606 H SER A 497 -18.450 14.822 -8.829 1.00 51.62 H ATOM 1607 HA SER A 497 -18.731 16.274 -6.552 1.00 57.95 H ATOM 1608 HB2 SER A 497 -18.176 14.610 -5.105 1.00 68.25 H ATOM 1609 HB3 SER A 497 -19.480 14.135 -5.878 1.00 68.25 H ATOM 1610 HG SER A 497 -18.056 12.544 -5.990 1.00 78.48 H ATOM 1611 N CYS A 498 -16.308 16.637 -6.434 1.00 41.69 N ANISOU 1611 N CYS A 498 5006 5700 5133 -401 544 -322 N ATOM 1612 CA CYS A 498 -14.953 17.137 -6.560 1.00 43.90 C ANISOU 1612 CA CYS A 498 5450 5676 5555 -318 524 -321 C ATOM 1613 C CYS A 498 -14.165 16.619 -5.367 1.00 45.14 C ANISOU 1613 C CYS A 498 5588 5882 5681 -364 578 -243 C ATOM 1614 O CYS A 498 -14.727 16.430 -4.308 1.00 44.02 O ANISOU 1614 O CYS A 498 5287 6041 5396 -387 595 -249 O ATOM 1615 CB CYS A 498 -14.973 18.654 -6.503 1.00 42.01 C ANISOU 1615 CB CYS A 498 5214 5405 5343 -94 383 -500 C ATOM 1616 SG CYS A 498 -15.743 19.309 -8.059 1.00 48.92 S ANISOU 1616 SG CYS A 498 6182 6131 6272 -48 262 -570 S ATOM 1617 H CYS A 498 -16.695 16.931 -5.725 1.00 50.05 H ATOM 1618 HA CYS A 498 -14.537 16.846 -7.386 1.00 52.71 H ATOM 1619 HB2 CYS A 498 -15.498 18.949 -5.743 1.00 50.44 H ATOM 1620 HB3 CYS A 498 -14.067 18.993 -6.432 1.00 50.44 H ATOM 1621 N GLY A 499 -12.859 16.497 -5.495 1.00 40.18 N ANISOU 1621 N GLY A 499 5095 5014 5159 -365 593 -187 N ATOM 1622 CA GLY A 499 -12.145 16.100 -4.301 1.00 45.21 C ANISOU 1622 CA GLY A 499 5712 5703 5763 -378 620 -134 C ATOM 1623 C GLY A 499 -10.678 16.351 -4.574 1.00 46.11 C ANISOU 1623 C GLY A 499 5937 5595 5989 -324 618 -129 C ATOM 1624 O GLY A 499 -10.268 16.511 -5.724 1.00 40.98 O ANISOU 1624 O GLY A 499 5366 4797 5407 -332 613 -130 O ATOM 1625 H GLY A 499 -12.397 16.629 -6.208 1.00 48.24 H ATOM 1626 HA2 GLY A 499 -12.433 16.624 -3.537 1.00 54.28 H ATOM 1627 HA3 GLY A 499 -12.289 15.160 -4.111 1.00 54.28 H ATOM 1628 N CYS A 500 -9.922 16.447 -3.502 1.00 36.76 N ANISOU 1628 N CYS A 500 4727 4447 4792 -278 618 -126 N ATOM 1629 CA CYS A 500 -8.480 16.707 -3.583 1.00 45.91 C ANISOU 1629 CA CYS A 500 5944 5474 6024 -239 614 -124 C ATOM 1630 C CYS A 500 -7.745 15.399 -3.823 1.00 43.93 C ANISOU 1630 C CYS A 500 5766 5137 5790 -274 645 -55 C ATOM 1631 O CYS A 500 -7.954 14.445 -3.070 1.00 43.74 O ANISOU 1631 O CYS A 500 5767 5130 5722 -317 629 12 O ATOM 1632 CB CYS A 500 -8.076 17.367 -2.268 1.00 44.36 C ANISOU 1632 CB CYS A 500 5689 5365 5801 -158 578 -169 C ATOM 1633 SG CYS A 500 -8.737 19.032 -2.126 1.00 47.11 S ANISOU 1633 SG CYS A 500 6009 5748 6142 -30 440 -320 S ATOM 1634 H CYS A 500 -10.214 16.365 -2.697 1.00 44.13 H ATOM 1635 HA CYS A 500 -8.250 17.291 -4.323 1.00 55.11 H ATOM 1636 HB2 CYS A 500 -8.418 16.840 -1.528 1.00 53.26 H ATOM 1637 HB3 CYS A 500 -7.109 17.418 -2.220 1.00 53.26 H ATOM 1638 N ARG A 501 -6.934 15.295 -4.891 1.00 41.05 N ANISOU 1638 N ARG A 501 5436 4699 5463 -256 655 -77 N ATOM 1639 CA ARG A 501 -6.231 14.017 -5.154 1.00 38.39 C ANISOU 1639 CA ARG A 501 5166 4295 5124 -203 634 -83 C ATOM 1640 C ARG A 501 -4.760 14.227 -5.404 1.00 44.84 C ANISOU 1640 C ARG A 501 5918 5191 5930 -115 648 -149 C ATOM 1641 O ARG A 501 -3.933 13.305 -5.301 1.00 47.96 O ANISOU 1641 O ARG A 501 6336 5578 6307 6 601 -206 O ATOM 1642 CB ARG A 501 -6.829 13.312 -6.373 1.00 40.43 C ANISOU 1642 CB ARG A 501 5500 4477 5384 -225 614 -96 C ATOM 1643 CG ARG A 501 -8.290 13.005 -6.123 1.00 38.98 C ANISOU 1643 CG ARG A 501 5359 4266 5188 -349 590 -15 C ATOM 1644 CD ARG A 501 -8.281 11.769 -5.236 1.00 49.43 C ANISOU 1644 CD ARG A 501 6793 5501 6486 -391 484 67 C ATOM 1645 NE ARG A 501 -9.570 11.123 -5.069 1.00 50.33 N ANISOU 1645 NE ARG A 501 6961 5616 6546 -581 421 187 N ATOM 1646 CZ ARG A 501 -10.450 11.431 -4.121 1.00 57.66 C ANISOU 1646 CZ ARG A 501 7778 6749 7382 -721 455 273 C ATOM 1647 NH1 ARG A 501 -10.257 12.459 -3.312 1.00 50.61 N ANISOU 1647 NH1 ARG A 501 6733 6036 6462 -644 541 219 N ATOM 1648 NH2 ARG A 501 -11.535 10.664 -3.963 1.00 55.63 N ANISOU 1648 NH2 ARG A 501 7553 6552 7032 -950 377 412 N ATOM 1649 OXT ARG A 501 -4.412 15.325 -5.830 1.00 43.21 O ANISOU 1649 OXT ARG A 501 5633 5076 5710 -174 678 -150 O TER 1650 ARG A 501 ANISOU 1651 N ALA B 398 8338 14436 9570 -235 1592 3816 N ANISOU 1652 CA ALA B 398 8694 14220 9988 -730 1274 3866 C ANISOU 1653 C ALA B 398 8778 13398 9620 -662 1363 3358 C ANISOU 1654 O ALA B 398 6972 10789 7831 -914 1074 3140 O ANISOU 1655 CB ALA B 398 7359 13328 8777 -894 1114 4205 C ANISOU 1661 N ARG B 399 7119 11689 7506 -246 1659 3039 N ANISOU 1662 CA ARG B 399 7097 10754 7051 -107 1658 2463 C ANISOU 1663 C ARG B 399 6714 9847 6605 23 1686 2090 C ANISOU 1664 O ARG B 399 6215 9706 6276 141 1791 2205 O ANISOU 1665 CB ARG B 399 7484 11259 6926 269 1898 2320 C ANISOU 1666 CG ARG B 399 9914 13749 9313 68 1780 2489 C ANISOU 1667 CD ARG B 399 11810 15168 10606 321 1856 2126 C ANISOU 1668 NE ARG B 399 14352 18325 12771 717 2127 2284 N ANISOU 1669 CZ ARG B 399 16009 19812 13898 902 2170 2163 C ANISOU 1670 NH1 ARG B 399 14313 17383 12044 694 1952 1901 N ANISOU 1671 NH2 ARG B 399 17400 21704 14959 1305 2370 2271 N ANISOU 1685 N CYS B 400 6546 8872 6223 -18 1575 1680 N ANISOU 1686 CA CYS B 400 6328 8122 5899 86 1586 1322 C ANISOU 1687 C CYS B 400 7063 9108 6443 449 1821 1262 C ANISOU 1688 O CYS B 400 6853 9021 5838 762 1984 1200 O ANISOU 1689 CB CYS B 400 6922 8067 6188 96 1515 967 C ANISOU 1690 SG CYS B 400 7213 7772 6377 167 1496 602 S ANISOU 1695 N SER B 401 6994 9121 6618 437 1824 1305 N ANISOU 1696 CA SER B 401 6208 8576 5679 803 2029 1266 C ANISOU 1697 C SER B 401 6348 8429 6021 710 1949 1155 C ANISOU 1698 O SER B 401 6336 8117 6261 385 1750 1150 O ANISOU 1699 CB SER B 401 6718 10074 6377 974 2210 1708 C ANISOU 1700 OG SER B 401 7363 11176 7605 606 2062 2119 O ANISOU 1706 N ARG B 402 6757 8834 6226 1039 2089 1029 N ANISOU 1707 CA ARG B 402 7026 8863 6656 981 2027 935 C ANISOU 1708 C ARG B 402 6205 8790 6301 929 2060 1350 C ANISOU 1709 O ARG B 402 5819 9098 5923 1225 2256 1589 O ANISOU 1710 CB ARG B 402 7216 8647 6385 1350 2114 626 C ANISOU 1711 CG ARG B 402 6658 7784 5971 1258 2030 517 C ANISOU 1712 CD ARG B 402 7264 7893 6106 1578 2048 228 C ANISOU 1713 NE ARG B 402 8208 9299 6885 2036 2236 346 N ANISOU 1714 CZ ARG B 402 7791 8598 6125 2388 2257 184 C ANISOU 1715 NH1 ARG B 402 8276 8379 6478 2261 2084 -61 N ANISOU 1716 NH2 ARG B 402 7540 8835 5706 2863 2435 313 N ANISOU 1730 N LYS B 403 5943 8382 6386 588 1861 1441 N ANISOU 1731 CA LYS B 403 5194 8250 6104 440 1797 1868 C ANISOU 1732 C LYS B 403 5487 8232 6449 448 1740 1730 C ANISOU 1733 O LYS B 403 4836 6857 5534 453 1693 1344 O ANISOU 1734 CB LYS B 403 6239 9299 7448 -25 1505 2155 C ANISOU 1735 CG LYS B 403 6526 9960 7721 -60 1545 2352 C ANISOU 1736 CD LYS B 403 7475 10985 8977 -518 1216 2728 C ANISOU 1737 CE LYS B 403 7348 11282 8844 -552 1262 2954 C ANISOU 1738 NZ LYS B 403 9946 13798 11693 -1051 851 3324 N ANISOU 1752 N ALA B 404 4920 8274 6258 424 1728 2097 N ANISOU 1753 CA ALA B 404 5566 8659 6974 414 1654 2006 C ANISOU 1754 C ALA B 404 4631 6993 6039 20 1342 1876 C ANISOU 1755 O ALA B 404 5285 7552 6808 -308 1104 2056 O ANISOU 1756 CB ALA B 404 5388 9388 7262 438 1676 2507 C ANISOU 1762 N LEU B 405 5617 7442 6852 79 1322 1581 N ANISOU 1763 CA LEU B 405 5124 6296 6286 -191 1060 1456 C ANISOU 1764 C LEU B 405 5169 6190 6296 -62 1104 1328 C ANISOU 1765 O LEU B 405 5506 6181 6353 140 1243 996 O ANISOU 1766 CB LEU B 405 5361 5872 6174 -216 1032 1098 C ANISOU 1767 CG LEU B 405 5458 5363 6139 -414 768 1012 C ANISOU 1768 CD1 LEU B 405 6208 6144 7033 -705 461 1338 C ANISOU 1769 CD2 LEU B 405 6716 6066 7055 -349 787 667 C ANISOU 1781 N HIS B 406 5197 6504 6620 -198 959 1632 N ANISOU 1782 CA HIS B 406 5943 7045 7349 -151 924 1549 C ANISOU 1783 C HIS B 406 5388 5681 6511 -349 699 1314 C ANISOU 1784 O HIS B 406 5897 5916 6994 -617 415 1439 O ANISOU 1785 CB HIS B 406 4938 6743 6810 -244 827 2036 C ANISOU 1786 CG HIS B 406 6415 8177 8333 -143 825 2010 C ANISOU 1787 ND1 HIS B 406 6966 8839 8763 253 1089 1820 N ANISOU 1788 CD2 HIS B 406 7343 8832 9329 -381 556 2112 C ANISOU 1789 CE1 HIS B 406 7771 9476 9602 244 999 1811 C ANISOU 1790 NE2 HIS B 406 7570 9078 9532 -139 690 1994 N ANISOU 1798 N VAL B 407 5454 5358 6329 -200 799 1005 N ANISOU 1799 CA VAL B 407 5828 5084 6403 -294 659 788 C ANISOU 1800 C VAL B 407 6298 5514 6944 -323 564 869 C ANISOU 1801 O VAL B 407 5848 5222 6538 -140 724 805 O ANISOU 1802 CB VAL B 407 6382 5344 6668 -133 841 450 C ANISOU 1803 CG1 VAL B 407 6950 5409 6947 -177 744 280 C ANISOU 1804 CG2 VAL B 407 6118 5130 6336 -95 939 366 C ANISOU 1814 N ASN B 408 5791 4697 6371 -538 272 985 N ANISOU 1815 CA ASN B 408 6397 5196 7004 -598 135 1067 C ANISOU 1816 C ASN B 408 6566 4658 6687 -597 36 795 C ANISOU 1817 O ASN B 408 6888 4543 6707 -676 -153 741 O ANISOU 1818 CB ASN B 408 6383 5404 7280 -863 -177 1481 C ANISOU 1819 CG ASN B 408 7904 6714 8780 -970 -388 1575 C ANISOU 1820 OD1 ASN B 408 7535 5664 7972 -1002 -542 1368 O ANISOU 1821 ND2 ASN B 408 7384 6816 8710 -971 -364 1879 N ANISOU 1828 N PHE B 409 6415 4402 6417 -472 170 626 N ANISOU 1829 CA PHE B 409 6633 4117 6181 -411 163 384 C ANISOU 1830 C PHE B 409 8277 5253 7501 -523 -153 430 C ANISOU 1831 O PHE B 409 7921 4438 6677 -440 -226 268 O ANISOU 1832 CB PHE B 409 6463 3996 5978 -294 352 253 C ANISOU 1833 CG PHE B 409 6724 4503 6342 -179 587 150 C ANISOU 1834 CD1 PHE B 409 6988 4770 6514 -144 668 58 C ANISOU 1835 CD2 PHE B 409 6963 4893 6708 -96 693 138 C ANISOU 1836 CE1 PHE B 409 6895 4856 6483 -61 847 -29 C ANISOU 1837 CE2 PHE B 409 6883 4904 6619 9 845 33 C ANISOU 1838 CZ PHE B 409 6415 4457 6082 6 915 -42 C ANISOU 1848 N LYS B 410 7356 4398 6790 -693 -373 670 N ANISOU 1849 CA LYS B 410 8458 4904 7518 -833 -758 731 C ANISOU 1850 C LYS B 410 8463 4501 7270 -946 -1058 788 C ANISOU 1851 O LYS B 410 9166 4444 7355 -923 -1344 672 O ANISOU 1852 CB LYS B 410 8439 5117 7852 -1026 -952 1032 C ANISOU 1853 CG LYS B 410 9902 5931 8950 -1248 -1453 1167 C ANISOU 1854 CD LYS B 410 11199 7506 10633 -1456 -1657 1499 C ANISOU 1855 CE LYS B 410 12241 7836 11299 -1745 -2254 1689 C ANISOU 1856 NZ LYS B 410 13535 9558 13125 -2035 -2519 2148 N ANISOU 1870 N ASP B 411 7451 3936 6668 -1050 -1026 972 N ANISOU 1871 CA ASP B 411 8240 4331 7242 -1196 -1350 1065 C ANISOU 1872 C ASP B 411 8574 4105 6977 -939 -1280 708 C ANISOU 1873 O ASP B 411 9184 4077 7153 -986 -1630 702 O ANISOU 1874 CB ASP B 411 7889 4708 7484 -1329 -1253 1344 C ANISOU 1875 CG ASP B 411 8470 5917 8657 -1582 -1394 1809 C ANISOU 1876 OD1 ASP B 411 8977 6182 9090 -1695 -1626 1904 O ANISOU 1877 OD2 ASP B 411 9096 7299 9808 -1663 -1292 2111 O ANISOU 1882 N MET B 412 8275 4065 6669 -673 -861 452 N ANISOU 1883 CA MET B 412 8832 4298 6754 -398 -739 170 C ANISOU 1884 C MET B 412 9443 4491 6809 -165 -720 -36 C ANISOU 1885 O MET B 412 8769 3748 5802 122 -536 -236 O ANISOU 1886 CB MET B 412 7910 3987 6174 -266 -307 70 C ANISOU 1887 CG MET B 412 11236 7723 9917 -384 -247 203 C ANISOU 1888 SD MET B 412 10754 7899 9826 -272 202 121 S ANISOU 1889 CE MET B 412 9092 6192 7901 -50 414 -109 C ANISOU 1899 N GLY B 413 9743 4683 7086 -263 -836 37 N ANISOU 1900 CA GLY B 413 9752 4288 6513 -40 -839 -132 C ANISOU 1901 C GLY B 413 9770 4860 6769 75 -436 -196 C ANISOU 1902 O GLY B 413 10003 4936 6562 294 -355 -311 O ANISOU 1906 N TRP B 414 8567 4289 6214 -59 -204 -104 N ANISOU 1907 CA TRP B 414 8269 4429 6108 18 113 -149 C ANISOU 1908 C TRP B 414 8433 4699 6490 -114 87 -50 C ANISOU 1909 O TRP B 414 7536 4108 5776 -100 284 -54 O ANISOU 1910 CB TRP B 414 8014 4646 6273 3 341 -149 C ANISOU 1911 CG TRP B 414 7872 4518 5920 177 453 -255 C ANISOU 1912 CD1 TRP B 414 7997 4283 5509 393 376 -354 C ANISOU 1913 CD2 TRP B 414 7301 4332 5626 191 653 -269 C ANISOU 1914 NE1 TRP B 414 8043 4558 5546 552 547 -411 N ANISOU 1915 CE2 TRP B 414 7174 4143 5195 395 704 -351 C ANISOU 1916 CE3 TRP B 414 6827 4212 5574 80 777 -223 C ANISOU 1917 CZ2 TRP B 414 7724 5032 5931 440 872 -360 C ANISOU 1918 CZ3 TRP B 414 7520 5150 6375 123 921 -256 C ANISOU 1919 CH2 TRP B 414 7788 5408 6415 274 966 -308 C ANISOU 1930 N ASP B 415 8749 4716 6748 -249 -199 58 N ANISOU 1931 CA ASP B 415 9125 5221 7363 -362 -234 174 C ANISOU 1932 C ASP B 415 8796 4696 6655 -270 -197 94 C ANISOU 1933 O ASP B 415 9958 6020 8021 -333 -157 161 O ANISOU 1934 CB ASP B 415 9187 5098 7530 -568 -580 380 C ANISOU 1935 CG ASP B 415 10291 5505 8044 -588 -926 346 C ANISOU 1936 OD1 ASP B 415 11131 6130 8561 -441 -889 196 O ANISOU 1937 OD2 ASP B 415 12798 7623 10358 -732 -1262 465 O ANISOU 1942 N ASP B 416 9443 5001 6724 -93 -217 -34 N ANISOU 1943 CA ASP B 416 9853 5324 6751 28 -154 -71 C ANISOU 1944 C ASP B 416 9777 5794 6929 69 166 -52 C ANISOU 1945 O ASP B 416 10478 6558 7429 113 226 -11 O ANISOU 1946 CB ASP B 416 10615 5583 6726 298 -257 -205 C ANISOU 1947 CG ASP B 416 10668 5675 6647 502 -145 -316 C ANISOU 1948 OD1 ASP B 416 11039 6494 7543 411 29 -286 O ANISOU 1949 OD2 ASP B 416 13331 7850 8618 782 -261 -443 O ANISOU 1952 N TRP B 417 8786 5185 6352 33 339 -52 N ANISOU 1953 CA TRP B 417 8108 4941 5867 20 554 8 C ANISOU 1954 C TRP B 417 8626 5675 6878 -130 596 45 C ANISOU 1955 O TRP B 417 8280 5515 6658 -212 651 125 O ANISOU 1956 CB TRP B 417 8450 5540 6012 215 740 -16 C ANISOU 1957 CG TRP B 417 8566 5738 6307 250 794 -91 C ANISOU 1958 CD1 TRP B 417 8186 5040 5727 350 686 -196 C ANISOU 1959 CD2 TRP B 417 7535 5086 5644 170 930 -48 C ANISOU 1960 NE1 TRP B 417 8319 5384 6114 344 777 -221 N ANISOU 1961 CE2 TRP B 417 7732 5223 5867 243 933 -140 C ANISOU 1962 CE3 TRP B 417 8398 6267 6767 28 1002 74 C ANISOU 1963 CZ2 TRP B 417 7520 5281 5946 188 1031 -129 C ANISOU 1964 CZ3 TRP B 417 7876 5959 6490 -29 1064 86 C ANISOU 1965 CH2 TRP B 417 8518 6563 7159 63 1096 -22 C ANISOU 1976 N ILE B 418 7942 4948 6435 -163 538 14 N ANISOU 1977 CA ILE B 418 7625 4795 6470 -214 579 34 C ANISOU 1978 C ILE B 418 7820 4897 6811 -260 449 107 C ANISOU 1979 O ILE B 418 7944 4940 6965 -288 322 165 O ANISOU 1980 CB ILE B 418 7622 4926 6645 -170 638 -10 C ANISOU 1981 CG1 ILE B 418 7659 5084 6571 -118 766 -71 C ANISOU 1982 CG2 ILE B 418 7389 4807 6666 -149 660 8 C ANISOU 1983 CD1 ILE B 418 7480 5024 6552 -88 816 -109 C ANISOU 1995 N ILE B 419 7967 5030 7029 -277 440 132 N ANISOU 1996 CA ILE B 419 8628 5621 7823 -269 323 205 C ANISOU 1997 C ILE B 419 8290 5468 7753 -131 362 216 C ANISOU 1998 O ILE B 419 8360 5691 8032 -93 299 331 O ANISOU 1999 CB ILE B 419 7770 4585 6844 -328 256 233 C ANISOU 2000 CG1 ILE B 419 8398 5156 7211 -438 240 281 C ANISOU 2001 CG2 ILE B 419 8601 5316 7796 -272 131 296 C ANISOU 2002 CD1 ILE B 419 8496 5179 7219 -553 177 370 C ANISOU 2014 N ALA B 420 7465 4675 6911 -46 461 125 N ANISOU 2015 CA ALA B 420 7700 5073 7293 161 517 122 C ANISOU 2016 C ALA B 420 8096 5469 7594 217 618 9 C ANISOU 2017 O ALA B 420 8352 5517 7665 99 592 -53 O ANISOU 2018 CB ALA B 420 8242 5404 7758 312 423 119 C ANISOU 2024 N PRO B 421 7656 5298 7278 388 722 15 N ANISOU 2025 CA PRO B 421 6633 4700 6544 519 764 177 C ANISOU 2026 C PRO B 421 6880 5093 6953 273 714 291 C ANISOU 2027 O PRO B 421 7059 5043 6962 109 691 201 O ANISOU 2028 CB PRO B 421 7022 5296 6905 768 900 136 C ANISOU 2029 CG PRO B 421 6512 4570 6226 591 924 -6 C ANISOU 2030 CD PRO B 421 7271 4912 6788 411 808 -86 C ANISOU 2038 N LEU B 422 6903 5492 7276 261 668 517 N ANISOU 2039 CA LEU B 422 7399 6025 7875 15 524 663 C ANISOU 2040 C LEU B 422 6366 5211 6925 -18 582 705 C ANISOU 2041 O LEU B 422 6202 4931 6745 -225 416 794 O ANISOU 2042 CB LEU B 422 6865 5823 7674 -57 371 975 C ANISOU 2043 CG LEU B 422 9137 7941 9930 -37 276 1000 C ANISOU 2044 CD1 LEU B 422 9349 8628 10562 -104 125 1377 C ANISOU 2045 CD2 LEU B 422 9009 7194 9410 -218 149 821 C ANISOU 2057 N GLU B 423 5930 5062 6547 193 772 667 N ANISOU 2058 CA GLU B 423 5901 5345 6644 173 832 762 C ANISOU 2059 C GLU B 423 6523 6049 7122 457 1048 600 C ANISOU 2060 O GLU B 423 6170 5594 6635 685 1108 499 O ANISOU 2061 CB GLU B 423 6495 6541 7662 96 746 1160 C ANISOU 2062 CG GLU B 423 7072 7663 8458 395 894 1314 C ANISOU 2063 CD GLU B 423 9142 10486 11042 288 792 1809 C ANISOU 2064 OE1 GLU B 423 9510 10857 11568 -75 555 2031 O ANISOU 2065 OE2 GLU B 423 10464 12411 12601 577 924 2009 O ANISOU 2072 N TYR B 424 5878 5495 6439 446 1124 566 N ANISOU 2073 CA TYR B 424 6282 5976 6663 726 1296 442 C ANISOU 2074 C TYR B 424 6339 6380 6842 673 1356 563 C ANISOU 2075 O TYR B 424 6014 6125 6699 404 1235 709 O ANISOU 2076 CB TYR B 424 5912 4999 5896 758 1284 130 C ANISOU 2077 CG TYR B 424 6227 5085 6114 549 1257 18 C ANISOU 2078 CD1 TYR B 424 6348 5032 6270 313 1158 20 C ANISOU 2079 CD2 TYR B 424 6716 5544 6438 630 1328 -79 C ANISOU 2080 CE1 TYR B 424 6549 5095 6372 198 1154 -65 C ANISOU 2081 CE2 TYR B 424 5486 4175 5157 459 1306 -151 C ANISOU 2082 CZ TYR B 424 6064 4647 5801 263 1232 -139 C ANISOU 2083 OH TYR B 424 6842 5335 6509 166 1226 -200 O ANISOU 2093 N GLU B 425 5764 6002 6123 957 1514 523 N ANISOU 2094 CA GLU B 425 5273 5870 5702 956 1596 638 C ANISOU 2095 C GLU B 425 5996 6072 6099 886 1581 354 C ANISOU 2096 O GLU B 425 6223 5965 5964 1095 1622 135 O ANISOU 2097 CB GLU B 425 5760 6902 6160 1359 1788 770 C ANISOU 2098 CG GLU B 425 6900 8698 7706 1426 1805 1121 C ANISOU 2099 CD GLU B 425 9062 11384 10385 1028 1670 1531 C ANISOU 2100 OE1 GLU B 425 7178 9580 8542 838 1640 1605 O ANISOU 2101 OE2 GLU B 425 10555 13156 12218 896 1552 1794 O ANISOU 2108 N ALA B 426 5761 5722 5966 593 1481 371 N ANISOU 2109 CA ALA B 426 6107 5676 6077 516 1463 155 C ANISOU 2110 C ALA B 426 5968 5765 5902 566 1538 202 C ANISOU 2111 O ALA B 426 5847 5362 5536 588 1546 24 O ANISOU 2112 CB ALA B 426 5992 5305 6020 257 1325 136 C ANISOU 2118 N PHE B 427 5576 5897 5768 544 1564 477 N ANISOU 2119 CA PHE B 427 5790 6411 6008 532 1611 599 C ANISOU 2120 C PHE B 427 5882 6154 6072 278 1473 515 C ANISOU 2121 O PHE B 427 5253 5098 5380 158 1366 365 O ANISOU 2122 CB PHE B 427 6366 7020 6242 863 1780 465 C ANISOU 2123 CG PHE B 427 5880 6852 5676 1230 1924 531 C ANISOU 2124 CD1 PHE B 427 6417 6952 5956 1402 1904 309 C ANISOU 2125 CD2 PHE B 427 5873 7624 5855 1419 2071 849 C ANISOU 2126 CE1 PHE B 427 6826 7606 6250 1788 2018 360 C ANISOU 2127 CE2 PHE B 427 6738 8858 6644 1831 2224 930 C ANISOU 2128 CZ PHE B 427 6897 8480 6495 2033 2193 660 C ANISOU 2138 N HIS B 428 5533 6040 5777 211 1467 653 N ANISOU 2139 CA HIS B 428 5809 5995 5991 30 1338 576 C ANISOU 2140 C HIS B 428 6177 6660 6325 70 1409 679 C ANISOU 2141 O HIS B 428 5291 6275 5485 222 1548 853 O ANISOU 2142 CB HIS B 428 5205 5230 5538 -223 1090 730 C ANISOU 2143 CG HIS B 428 5444 5903 6040 -394 971 1114 C ANISOU 2144 ND1 HIS B 428 5777 6141 6384 -589 777 1253 N ANISOU 2145 CD2 HIS B 428 5224 6265 6115 -421 989 1448 C ANISOU 2146 CE1 HIS B 428 5924 6794 6825 -770 663 1678 C ANISOU 2147 NE2 HIS B 428 5828 7164 6931 -672 797 1821 N ANISOU 2155 N CYS B 429 6048 6251 6102 -38 1319 585 N ANISOU 2156 CA CYS B 429 6204 6562 6163 -14 1366 626 C ANISOU 2157 C CYS B 429 5595 5990 5718 -255 1169 844 C ANISOU 2158 O CYS B 429 5830 5792 5922 -374 986 757 O ANISOU 2159 CB CYS B 429 6055 6010 5750 55 1386 338 C ANISOU 2160 SG CYS B 429 6756 6516 6143 296 1511 108 S ANISOU 2165 N GLU B 430 5896 6785 6140 -298 1194 1133 N ANISOU 2166 CA GLU B 430 6224 7180 6638 -573 954 1423 C ANISOU 2167 C GLU B 430 6337 7821 6775 -560 1050 1658 C ANISOU 2168 O GLU B 430 6288 8330 6724 -348 1291 1766 O ANISOU 2169 CB GLU B 430 6728 7888 7428 -775 771 1745 C ANISOU 2170 CG GLU B 430 8518 9502 9328 -1127 381 2046 C ANISOU 2171 CD GLU B 430 10052 11112 11104 -1367 121 2366 C ANISOU 2172 OE1 GLU B 430 9190 11049 10577 -1382 243 2723 O ANISOU 2173 OE2 GLU B 430 9595 9915 10464 -1504 -206 2259 O ANISOU 2180 N GLY B 431 5905 7202 6327 -755 852 1744 N ANISOU 2181 CA GLY B 431 6285 8121 6776 -820 881 2062 C ANISOU 2182 C GLY B 431 5966 7440 6248 -858 799 1915 C ANISOU 2183 O GLY B 431 6324 7183 6426 -802 742 1567 O ANISOU 2187 N LEU B 432 5787 7699 6111 -950 790 2212 N ANISOU 2188 CA LEU B 432 6077 7644 6233 -1029 660 2124 C ANISOU 2189 C LEU B 432 5959 7330 5779 -748 887 1747 C ANISOU 2190 O LEU B 432 6157 7817 5804 -488 1152 1667 O ANISOU 2191 CB LEU B 432 7549 9652 7836 -1233 566 2584 C ANISOU 2192 CG LEU B 432 8060 10314 8677 -1623 214 3061 C ANISOU 2193 CD1 LEU B 432 8803 11782 9564 -1803 187 3570 C ANISOU 2194 CD2 LEU B 432 9112 10433 9630 -1822 -203 2906 C ANISOU 2206 N CYS B 433 6381 7238 6079 -796 744 1542 N ANISOU 2207 CA CYS B 433 6620 7246 6034 -628 853 1255 C ANISOU 2208 C CYS B 433 6664 7294 6034 -767 708 1403 C ANISOU 2209 O CYS B 433 8206 8446 7625 -875 495 1347 O ANISOU 2210 CB CYS B 433 6531 6650 5924 -570 804 939 C ANISOU 2211 SG CYS B 433 6579 6674 5972 -407 977 756 S ANISOU 2216 N GLU B 434 7240 8331 6502 -741 816 1617 N ANISOU 2217 CA GLU B 434 8065 9180 7272 -886 674 1780 C ANISOU 2218 C GLU B 434 7926 9171 6739 -685 850 1691 C ANISOU 2219 O GLU B 434 7536 8928 6092 -419 1077 1574 O ANISOU 2220 CB GLU B 434 8319 9914 7773 -1131 546 2261 C ANISOU 2221 CG GLU B 434 11344 12628 11082 -1408 214 2410 C ANISOU 2222 CD GLU B 434 11844 13639 11839 -1724 21 2980 C ANISOU 2223 OE1 GLU B 434 10888 13441 10892 -1689 220 3280 O ANISOU 2224 OE2 GLU B 434 13734 15142 13879 -1994 -356 3137 O ANISOU 2231 N PHE B 435 7639 8782 6344 -794 718 1754 N ANISOU 2232 CA PHE B 435 8374 9556 6620 -605 842 1667 C ANISOU 2233 C PHE B 435 8773 10659 6874 -437 1072 1948 C ANISOU 2234 O PHE B 435 8928 11351 7355 -626 1036 2354 O ANISOU 2235 CB PHE B 435 8802 9770 6964 -766 642 1710 C ANISOU 2236 CG PHE B 435 9666 10684 7292 -585 740 1673 C ANISOU 2237 CD1 PHE B 435 9788 10288 7016 -443 707 1346 C ANISOU 2238 CD2 PHE B 435 9823 11410 7301 -548 845 1994 C ANISOU 2239 CE1 PHE B 435 10712 11123 7324 -256 744 1292 C ANISOU 2240 CE2 PHE B 435 9830 11409 6707 -320 935 1937 C ANISOU 2241 CZ PHE B 435 10249 11178 6655 -163 872 1562 C ANISOU 2251 N PRO B 436 9158 11068 6752 -65 1292 1772 N ANISOU 2252 CA PRO B 436 9806 11031 6938 146 1279 1332 C ANISOU 2253 C PRO B 436 10235 11272 7490 255 1350 1126 C ANISOU 2254 O PRO B 436 10447 11956 7867 383 1527 1274 O ANISOU 2255 CB PRO B 436 11324 12655 7737 521 1434 1310 C ANISOU 2256 CG PRO B 436 11261 13530 7852 658 1684 1703 C ANISOU 2257 CD PRO B 436 10518 13164 7863 192 1536 2058 C ANISOU 2265 N LEU B 437 10239 10654 7489 173 1199 834 N ANISOU 2266 CA LEU B 437 9483 9683 6741 300 1260 635 C ANISOU 2267 C LEU B 437 12160 12164 8720 694 1366 466 C ANISOU 2268 O LEU B 437 12248 11826 8255 787 1251 329 O ANISOU 2269 CB LEU B 437 8896 8579 6333 104 1066 433 C ANISOU 2270 CG LEU B 437 8677 8435 6680 -178 948 539 C ANISOU 2271 CD1 LEU B 437 8369 7741 6468 -248 830 350 C ANISOU 2272 CD2 LEU B 437 8811 8947 7215 -240 1022 728 C ANISOU 2284 N ARG B 438 13090 13376 9618 954 1563 487 N ANISOU 2285 CA ARG B 438 15153 15197 10931 1424 1658 307 C ANISOU 2286 C ARG B 438 15570 14688 10970 1419 1422 -45 C ANISOU 2287 O ARG B 438 14131 13097 9956 1198 1345 -109 O ANISOU 2288 CB ARG B 438 15838 16499 11753 1719 1930 457 C ANISOU 2289 CG ARG B 438 15541 17228 11909 1663 2125 908 C ANISOU 2290 CD ARG B 438 16022 17925 11970 1785 2166 1042 C ANISOU 2291 NE ARG B 438 17912 19197 12882 2242 2157 724 N ANISOU 2292 CZ ARG B 438 17276 18169 11707 2265 2029 631 C ANISOU 2293 NH1 ARG B 438 16090 17242 10887 1885 1941 850 N ANISOU 2294 NH2 ARG B 438 17787 17925 11240 2675 1943 306 N ANISOU 2308 N SER B 439 15890 14367 10454 1651 1272 -249 N ANISOU 2309 CA SER B 439 16142 13672 10279 1606 961 -530 C ANISOU 2310 C SER B 439 17541 14855 11570 1831 1005 -674 C ANISOU 2311 O SER B 439 16654 13244 10489 1696 720 -847 O ANISOU 2312 CB SER B 439 16974 13761 10098 1843 735 -706 C ANISOU 2313 OG SER B 439 16860 13744 10088 1577 632 -583 O ANISOU 2319 N HIS B 440 21654 19608 15841 2139 1330 -565 N ANISOU 2320 CA HIS B 440 21014 18927 15355 2255 1390 -640 C ANISOU 2321 C HIS B 440 19053 17246 14324 1768 1370 -530 C ANISOU 2322 O HIS B 440 18355 16370 13761 1764 1344 -614 O ANISOU 2323 CB HIS B 440 20757 19370 14992 2762 1744 -505 C ANISOU 2324 CG HIS B 440 22382 22102 17483 2558 2006 -124 C ANISOU 2325 ND1 HIS B 440 22181 22688 17296 2744 2227 158 N ANISOU 2326 CD2 HIS B 440 22861 22983 18816 2162 2024 45 C ANISOU 2327 CE1 HIS B 440 22338 23670 18277 2436 2350 511 C ANISOU 2328 NE2 HIS B 440 21980 23033 18411 2088 2212 426 N ANISOU 2336 N LEU B 441 20803 19380 16654 1392 1367 -351 N ANISOU 2337 CA LEU B 441 16862 15518 13408 988 1291 -297 C ANISOU 2338 C LEU B 441 16737 14769 13193 738 998 -438 C ANISOU 2339 O LEU B 441 13919 12079 10920 444 946 -372 O ANISOU 2340 CB LEU B 441 14996 14215 12106 733 1354 -55 C ANISOU 2341 CG LEU B 441 15684 15631 12987 857 1578 210 C ANISOU 2342 CD1 LEU B 441 12584 12918 10347 551 1530 466 C ANISOU 2343 CD2 LEU B 441 13613 13854 11189 961 1716 269 C ANISOU 2355 N GLU B 442 14868 12241 10612 859 783 -598 N ANISOU 2356 CA GLU B 442 13871 10638 9459 594 431 -662 C ANISOU 2357 C GLU B 442 12791 9914 9059 200 377 -492 C ANISOU 2358 O GLU B 442 11207 8285 7814 -42 245 -443 O ANISOU 2359 CB GLU B 442 15405 11746 10870 607 302 -771 C ANISOU 2360 CG GLU B 442 16234 12237 11015 1082 375 -949 C ANISOU 2361 CD GLU B 442 16489 12208 11292 1105 306 -1029 C ANISOU 2362 OE1 GLU B 442 14689 10948 10186 958 495 -923 O ANISOU 2363 OE2 GLU B 442 17932 12817 12010 1267 25 -1197 O ANISOU 2370 N PRO B 443 11226 8728 7686 154 472 -378 N ANISOU 2371 CA PRO B 443 9895 7778 7005 -121 464 -224 C ANISOU 2372 C PRO B 443 8755 6378 5900 -380 169 -170 C ANISOU 2373 O PRO B 443 9029 6145 5659 -410 -81 -222 O ANISOU 2374 CB PRO B 443 9360 7598 6526 -79 587 -115 C ANISOU 2375 CG PRO B 443 10057 7971 6502 136 546 -206 C ANISOU 2376 CD PRO B 443 11848 9416 7877 373 562 -372 C ANISOU 2384 N THR B 444 7739 5706 5472 -554 177 -46 N ANISOU 2385 CA THR B 444 6995 4929 4880 -799 -78 96 C ANISOU 2386 C THR B 444 7181 5207 5056 -858 -152 182 C ANISOU 2387 O THR B 444 6742 4996 4688 -743 26 173 O ANISOU 2388 CB THR B 444 7558 5971 6072 -883 -2 238 C ANISOU 2389 OG1 THR B 444 6268 5040 5080 -743 228 233 O ANISOU 2390 CG2 THR B 444 6749 5102 5307 -871 38 195 C ANISOU 2398 N ASN B 445 7024 4942 4902 -1078 -437 321 N ANISOU 2399 CA ASN B 445 7014 5096 4988 -1152 -512 438 C ANISOU 2400 C ASN B 445 6592 5242 5135 -1069 -295 525 C ANISOU 2401 O ASN B 445 6476 5197 4986 -1011 -239 530 O ANISOU 2402 CB ASN B 445 7339 5305 5338 -1434 -878 636 C ANISOU 2403 CG ASN B 445 8784 5965 6002 -1502 -1192 529 C ANISOU 2404 OD1 ASN B 445 9218 6053 5874 -1280 -1095 322 O ANISOU 2405 ND2 ASN B 445 8600 5504 5751 -1786 -1580 691 N ANISOU 2412 N HIS B 446 6699 5707 5704 -1048 -201 601 N ANISOU 2413 CA HIS B 446 6792 6187 6191 -897 -34 645 C ANISOU 2414 C HIS B 446 5802 5072 5038 -755 134 503 C ANISOU 2415 O HIS B 446 6036 5368 5333 -711 134 545 O ANISOU 2416 CB HIS B 446 5450 5195 5227 -829 56 723 C ANISOU 2417 CG HIS B 446 5605 5654 5664 -609 173 761 C ANISOU 2418 ND1 HIS B 446 5274 5154 5235 -442 301 613 N ANISOU 2419 CD2 HIS B 446 5176 5622 5542 -505 140 938 C ANISOU 2420 CE1 HIS B 446 5636 5666 5751 -243 308 662 C ANISOU 2421 NE2 HIS B 446 5336 5732 5692 -240 235 847 N ANISOU 2429 N ALA B 447 6304 5386 5302 -704 242 368 N ANISOU 2430 CA ALA B 447 5952 5047 4866 -600 387 320 C ANISOU 2431 C ALA B 447 5794 4836 4439 -628 343 367 C ANISOU 2432 O ALA B 447 6075 5253 4800 -617 385 448 O ANISOU 2433 CB ALA B 447 6342 5344 5086 -510 522 204 C ANISOU 2439 N VAL B 448 6628 5438 4895 -666 236 331 N ANISOU 2440 CA VAL B 448 6770 5551 4737 -665 200 386 C ANISOU 2441 C VAL B 448 6790 5740 5072 -779 93 533 C ANISOU 2442 O VAL B 448 7169 6264 5477 -784 124 635 O ANISOU 2443 CB VAL B 448 7156 5530 4552 -660 45 302 C ANISOU 2444 CG1 VAL B 448 8073 6428 5112 -637 9 366 C ANISOU 2445 CG2 VAL B 448 7511 5604 4483 -479 119 133 C ANISOU 2455 N ILE B 449 6538 5511 5088 -866 -46 581 N ANISOU 2456 CA ILE B 449 6305 5432 5120 -910 -151 718 C ANISOU 2457 C ILE B 449 6308 5553 5369 -810 -66 743 C ANISOU 2458 O ILE B 449 6586 5820 5635 -842 -141 840 O ANISOU 2459 CB ILE B 449 6293 5552 5387 -976 -294 813 C ANISOU 2460 CG1 ILE B 449 6868 5891 5637 -1150 -500 845 C ANISOU 2461 CG2 ILE B 449 6552 6016 5952 -918 -362 940 C ANISOU 2462 CD1 ILE B 449 7426 6570 6425 -1295 -682 986 C ANISOU 2474 N GLN B 450 6481 5777 5728 -703 43 671 N ANISOU 2475 CA GLN B 450 5638 4899 5018 -605 51 683 C ANISOU 2476 C GLN B 450 6223 5440 5447 -693 63 750 C ANISOU 2477 O GLN B 450 6732 5856 5992 -726 -68 859 O ANISOU 2478 CB GLN B 450 5925 5206 5430 -473 169 581 C ANISOU 2479 CG GLN B 450 5411 4525 4963 -333 104 576 C ANISOU 2480 CD GLN B 450 5993 5096 5603 -169 205 473 C ANISOU 2481 OE1 GLN B 450 5468 4789 5192 -117 317 440 O ANISOU 2482 NE2 GLN B 450 5975 4795 5485 -95 122 451 N ANISOU 2491 N THR B 451 6355 5654 5380 -723 195 720 N ANISOU 2492 CA THR B 451 6953 6398 5874 -779 243 856 C ANISOU 2493 C THR B 451 6976 6468 5791 -889 120 1020 C ANISOU 2494 O THR B 451 7161 6748 6051 -998 31 1224 O ANISOU 2495 CB THR B 451 6516 6080 5196 -683 440 781 C ANISOU 2496 OG1 THR B 451 7131 6657 5947 -604 536 663 O ANISOU 2497 CG2 THR B 451 7214 7108 5803 -704 516 995 C ANISOU 2505 N LEU B 452 6695 6097 5343 -895 65 965 N ANISOU 2506 CA LEU B 452 7638 7068 6177 -1004 -67 1124 C ANISOU 2507 C LEU B 452 7305 6623 6115 -1072 -271 1232 C ANISOU 2508 O LEU B 452 8362 7721 7165 -1194 -391 1434 O ANISOU 2509 CB LEU B 452 6809 6091 5097 -1011 -140 1044 C ANISOU 2510 CG LEU B 452 8436 7690 6642 -1128 -320 1188 C ANISOU 2511 CD1 LEU B 452 7829 7303 5837 -1155 -239 1354 C ANISOU 2512 CD2 LEU B 452 8413 7472 6310 -1151 -418 1113 C ANISOU 2524 N MET B 453 7290 6464 6307 -970 -330 1119 N ANISOU 2525 CA MET B 453 7208 6187 6370 -932 -537 1188 C ANISOU 2526 C MET B 453 7497 6329 6662 -985 -623 1282 C ANISOU 2527 O MET B 453 7455 6059 6591 -1062 -873 1429 O ANISOU 2528 CB MET B 453 7076 6018 6419 -716 -535 1063 C ANISOU 2529 CG MET B 453 6787 5917 6201 -726 -541 1074 C ANISOU 2530 SD MET B 453 7402 6766 7111 -499 -496 1041 S ANISOU 2531 CE MET B 453 6852 6034 6604 -230 -670 1085 C ANISOU 2541 N ASN B 454 7094 6000 6288 -956 -469 1215 N ANISOU 2542 CA ASN B 454 6866 5631 6077 -1054 -603 1350 C ANISOU 2543 C ASN B 454 7671 6670 6851 -1306 -681 1652 C ANISOU 2544 O ASN B 454 7845 6661 7043 -1477 -952 1875 O ANISOU 2545 CB ASN B 454 6982 5859 6250 -988 -407 1245 C ANISOU 2546 CG ASN B 454 7713 6596 7027 -1162 -529 1462 C ANISOU 2547 OD1 ASN B 454 7053 6368 6419 -1268 -378 1622 O ANISOU 2548 ND2 ASN B 454 7598 6001 6864 -1162 -810 1475 N ANISOU 2555 N SER B 455 8422 7822 7515 -1325 -466 1686 N ANISOU 2556 CA SER B 455 8558 8330 7599 -1512 -481 2007 C ANISOU 2557 C SER B 455 8455 8032 7463 -1669 -771 2182 C ANISOU 2558 O SER B 455 9015 8740 8071 -1903 -950 2527 O ANISOU 2559 CB SER B 455 8142 8298 6956 -1386 -180 1946 C ANISOU 2560 OG SER B 455 10793 11373 9521 -1511 -174 2274 O ANISOU 2566 N MET B 456 8950 8218 7905 -1556 -845 1983 N ANISOU 2567 CA MET B 456 8757 7820 7670 -1671 -1123 2131 C ANISOU 2568 C MET B 456 9673 8220 8639 -1703 -1483 2194 C ANISOU 2569 O MET B 456 9162 7538 8076 -1890 -1782 2437 O ANISOU 2570 CB MET B 456 8292 7266 7148 -1532 -1091 1938 C ANISOU 2571 CG MET B 456 9640 8928 8304 -1514 -847 1876 C ANISOU 2572 SD MET B 456 11036 10209 9592 -1467 -915 1758 S ANISOU 2573 CE MET B 456 11768 11123 9990 -1639 -961 1997 C ANISOU 2583 N ASP B 457 9140 7368 8141 -1508 -1496 1984 N ANISOU 2584 CA ASP B 457 9299 6882 8194 -1456 -1875 1998 C ANISOU 2585 C ASP B 457 9961 7354 8848 -1314 -1816 1838 C ANISOU 2586 O ASP B 457 9550 6781 8405 -986 -1710 1562 O ANISOU 2587 CB ASP B 457 10992 8241 9807 -1182 -2003 1835 C ANISOU 2588 CG ASP B 457 12122 8595 10688 -1058 -2437 1839 C ANISOU 2589 OD1 ASP B 457 12422 8527 10859 -1235 -2693 1972 O ANISOU 2590 OD2 ASP B 457 12471 8689 10942 -774 -2548 1727 O ANISOU 2595 N PRO B 458 9837 7322 8772 -1556 -1873 2039 N ANISOU 2596 CA PRO B 458 9747 7075 8675 -1449 -1816 1900 C ANISOU 2597 C PRO B 458 10639 7130 9275 -1237 -2164 1751 C ANISOU 2598 O PRO B 458 11204 7491 9760 -1070 -2113 1578 O ANISOU 2599 CB PRO B 458 9615 7255 8684 -1814 -1894 2260 C ANISOU 2600 CG PRO B 458 9785 7899 8952 -2074 -1897 2583 C ANISOU 2601 CD PRO B 458 9753 7546 8771 -1950 -2018 2458 C ANISOU 2609 N GLU B 459 11567 7520 9980 -1218 -2542 1818 N ANISOU 2610 CA GLU B 459 14208 9228 12195 -927 -2924 1654 C ANISOU 2611 C GLU B 459 12476 7542 10401 -386 -2643 1296 C ANISOU 2612 O GLU B 459 13111 7674 10719 -21 -2726 1079 O ANISOU 2613 CB GLU B 459 15939 10291 13645 -1059 -3471 1855 C ANISOU 2614 CG GLU B 459 16335 10798 14176 -1662 -3781 2332 C ANISOU 2615 CD GLU B 459 18669 12687 16365 -1935 -4185 2504 C ANISOU 2616 OE1 GLU B 459 18043 12044 15734 -1844 -4036 2393 O ANISOU 2617 OE2 GLU B 459 20218 14101 17878 -2239 -4611 2677 O ANISOU 2624 N SER B 460 10387 6105 8608 -336 -2310 1263 N ANISOU 2625 CA SER B 460 11754 7682 10016 117 -2064 1032 C ANISOU 2626 C SER B 460 10342 6891 8878 176 -1614 901 C ANISOU 2627 O SER B 460 11540 8133 10031 566 -1473 730 O ANISOU 2628 CB SER B 460 11567 7818 10000 119 -2033 1113 C ANISOU 2629 OG SER B 460 13560 10372 12270 -282 -1834 1257 O ANISOU 2635 N THR B 461 9547 6573 8329 -170 -1395 990 N ANISOU 2636 CA THR B 461 8483 5997 7470 -131 -1022 869 C ANISOU 2637 C THR B 461 8018 5523 7004 -327 -970 898 C ANISOU 2638 O THR B 461 8279 5923 7318 -643 -1019 1093 O ANISOU 2639 CB THR B 461 8105 6160 7310 -293 -814 925 C ANISOU 2640 OG1 THR B 461 7940 6020 7181 -129 -901 940 O ANISOU 2641 CG2 THR B 461 7226 5666 6584 -242 -514 809 C ANISOU 2649 N PRO B 462 7960 5393 6907 -150 -856 744 N ANISOU 2650 CA PRO B 462 6948 4430 5934 -343 -799 790 C ANISOU 2651 C PRO B 462 6551 4623 5765 -474 -465 793 C ANISOU 2652 O PRO B 462 6622 4997 5930 -412 -287 724 O ANISOU 2653 CB PRO B 462 7709 4856 6516 -57 -807 600 C ANISOU 2654 CG PRO B 462 8250 5679 7133 269 -594 452 C ANISOU 2655 CD PRO B 462 7658 5071 6549 250 -743 553 C ANISOU 2663 N PRO B 463 7073 5312 6353 -657 -407 899 N ANISOU 2664 CA PRO B 463 6401 5139 5796 -721 -112 902 C ANISOU 2665 C PRO B 463 6642 5430 6067 -541 100 678 C ANISOU 2666 O PRO B 463 5889 4422 5276 -380 48 558 O ANISOU 2667 CB PRO B 463 7735 6662 7205 -920 -149 1136 C ANISOU 2668 CG PRO B 463 7552 6009 6960 -942 -425 1160 C ANISOU 2669 CD PRO B 463 7359 5345 6592 -841 -668 1090 C ANISOU 2677 N THR B 464 5952 5039 5387 -546 318 628 N ANISOU 2678 CA THR B 464 6244 5374 5699 -432 484 461 C ANISOU 2679 C THR B 464 6667 5814 6159 -448 533 486 C ANISOU 2680 O THR B 464 6507 5680 6034 -567 427 661 O ANISOU 2681 CB THR B 464 6694 5980 6039 -442 610 410 C ANISOU 2682 OG1 THR B 464 6942 6407 6183 -501 657 536 O ANISOU 2683 CG2 THR B 464 6185 5449 5500 -468 520 417 C ANISOU 2691 N CYS B 465 6094 5254 5599 -360 665 354 N ANISOU 2692 CA CYS B 465 6582 5728 6138 -370 679 383 C ANISOU 2693 C CYS B 465 6250 5595 5785 -322 872 329 C ANISOU 2694 O CYS B 465 6108 5426 5553 -254 959 194 O ANISOU 2695 CB CYS B 465 6825 5695 6366 -262 613 271 C ANISOU 2696 SG CYS B 465 8283 6969 7826 -337 476 367 S ANISOU 2701 N CYS B 466 5757 5278 5367 -359 901 457 N ANISOU 2702 CA CYS B 466 5738 5467 5300 -252 1083 425 C ANISOU 2703 C CYS B 466 5856 5384 5435 -187 1117 263 C ANISOU 2704 O CYS B 466 6126 5554 5818 -240 1030 304 O ANISOU 2705 CB CYS B 466 6083 6215 5790 -307 1100 699 C ANISOU 2706 SG CYS B 466 6608 7113 6242 -82 1341 716 S ANISOU 2711 N VAL B 467 5404 4829 4832 -88 1204 99 N ANISOU 2712 CA VAL B 467 5339 4591 4796 -61 1213 -19 C ANISOU 2713 C VAL B 467 5589 4782 4856 47 1293 -114 C ANISOU 2714 O VAL B 467 5772 4961 4802 137 1323 -135 O ANISOU 2715 CB VAL B 467 6530 5642 6015 -89 1150 -92 C ANISOU 2716 CG1 VAL B 467 6077 5141 5653 -98 1055 -39 C ANISOU 2717 CG2 VAL B 467 5921 5001 5283 -118 1118 -120 C ANISOU 2727 N PRO B 468 6048 5112 5334 62 1298 -188 N ANISOU 2728 CA PRO B 468 5754 4626 4793 163 1308 -290 C ANISOU 2729 C PRO B 468 6506 5114 5331 101 1186 -357 C ANISOU 2730 O PRO B 468 6246 4852 5221 -42 1109 -325 O ANISOU 2731 CB PRO B 468 6452 5248 5609 137 1304 -317 C ANISOU 2732 CG PRO B 468 5963 4959 5386 86 1328 -218 C ANISOU 2733 CD PRO B 468 5902 4940 5369 14 1275 -179 C ANISOU 2741 N THR B 469 6527 4891 4958 231 1146 -436 N ANISOU 2742 CA THR B 469 7218 5192 5359 143 944 -488 C ANISOU 2743 C THR B 469 8286 5775 6082 189 788 -585 C ANISOU 2744 O THR B 469 8324 5460 5946 17 540 -570 O ANISOU 2745 CB THR B 469 7983 5856 5774 253 921 -518 C ANISOU 2746 OG1 THR B 469 7520 5428 5031 562 1063 -575 O ANISOU 2747 CG2 THR B 469 7427 5720 5552 156 1012 -397 C ANISOU 2755 N ARG B 470 8029 5476 5706 406 889 -655 N ANISOU 2756 CA AARG B 470 7957 4917 5339 446 722 -740 C ANISOU 2757 CA BARG B 470 7965 4923 5344 446 721 -740 C ANISOU 2758 C ARG B 470 8264 5502 5951 512 886 -715 C ANISOU 2759 O ARG B 470 7571 5228 5441 676 1108 -675 O ANISOU 2760 CB AARG B 470 9337 5725 5992 771 606 -904 C ANISOU 2761 CB BARG B 470 9342 5727 5990 772 604 -905 C ANISOU 2762 CG AARG B 470 10681 6543 6860 699 332 -955 C ANISOU 2763 CG BARG B 470 10684 6611 6851 743 375 -959 C ANISOU 2764 CD AARG B 470 12306 7431 7596 1090 168 -1156 C ANISOU 2765 CD BARG B 470 12197 7457 7483 1181 258 -1162 C ANISOU 2766 NE AARG B 470 12698 7271 7467 1021 -121 -1204 N ANISOU 2767 NE BARG B 470 12090 7051 7197 1366 216 -1245 N ANISOU 2768 CZ AARG B 470 13261 8073 7920 1141 11 -1204 C ANISOU 2769 CZ BARG B 470 12124 7128 6914 1856 399 -1346 C ANISOU 2770 NH1AARG B 470 12417 8016 7449 1326 412 -1137 N ANISOU 2771 NH1BARG B 470 13231 8528 7751 2246 622 -1371 N ANISOU 2772 NH2AARG B 470 14570 8814 8736 1040 -302 -1241 N ANISOU 2773 NH2BARG B 470 12378 7187 7131 1974 362 -1390 N ANISOU 2798 N LEU B 471 7701 4712 5434 367 750 -702 N ANISOU 2799 CA LEU B 471 7752 4967 5741 407 870 -678 C ANISOU 2800 C LEU B 471 8784 5456 6433 449 665 -748 C ANISOU 2801 O LEU B 471 9099 5256 6414 327 382 -764 O ANISOU 2802 CB LEU B 471 7342 4946 5819 161 937 -551 C ANISOU 2803 CG LEU B 471 7607 5636 6362 142 1090 -491 C ANISOU 2804 CD1 LEU B 471 8131 6239 7015 -60 1005 -411 C ANISOU 2805 CD2 LEU B 471 7348 5694 6416 148 1224 -432 C ANISOU 2817 N SER B 472 7701 4452 5414 612 767 -768 N ANISOU 2818 CA SER B 472 7799 4034 5191 693 579 -835 C ANISOU 2819 C SER B 472 7970 4468 5768 532 641 -735 C ANISOU 2820 O SER B 472 7642 4682 5893 429 838 -642 O ANISOU 2821 CB SER B 472 9266 5273 6198 1169 629 -975 C ANISOU 2822 OG SER B 472 9400 6101 6721 1330 941 -890 O ANISOU 2828 N PRO B 473 8079 4145 5684 478 433 -742 N ANISOU 2829 CA PRO B 473 8490 4779 6441 293 464 -630 C ANISOU 2830 C PRO B 473 8376 4730 6361 531 573 -670 C ANISOU 2831 O PRO B 473 8963 5092 6624 870 573 -781 O ANISOU 2832 CB PRO B 473 8502 4263 6211 55 119 -563 C ANISOU 2833 CG PRO B 473 9794 4832 6874 262 -125 -718 C ANISOU 2834 CD PRO B 473 9001 4259 6004 527 88 -833 C ANISOU 2842 N ILE B 474 7603 4224 5917 383 637 -571 N ANISOU 2843 CA ILE B 474 8144 4706 6460 536 642 -576 C ANISOU 2844 C ILE B 474 8097 4513 6480 280 496 -482 C ANISOU 2845 O ILE B 474 7989 4576 6535 4 480 -372 O ANISOU 2846 CB ILE B 474 7627 4747 6298 655 879 -513 C ANISOU 2847 CG1 ILE B 474 7142 4587 6146 389 952 -414 C ANISOU 2848 CG2 ILE B 474 8202 5621 6889 862 1034 -524 C ANISOU 2849 CD1 ILE B 474 8210 6012 7496 430 1052 -317 C ANISOU 2861 N SER B 475 8539 4693 6796 402 401 -499 N ANISOU 2862 CA SER B 475 8683 4700 6986 163 253 -389 C ANISOU 2863 C SER B 475 8822 5263 7456 148 426 -319 C ANISOU 2864 O SER B 475 8261 4920 7019 365 559 -347 O ANISOU 2865 CB SER B 475 9748 5101 7654 264 -32 -440 C ANISOU 2866 OG SER B 475 10303 5152 7835 201 -277 -480 O ANISOU 2872 N ILE B 476 8366 4966 7136 -107 416 -195 N ANISOU 2873 CA ILE B 476 7520 4417 6493 -127 537 -139 C ANISOU 2874 C ILE B 476 8496 5264 7413 -295 406 -23 C ANISOU 2875 O ILE B 476 7697 4385 6532 -492 281 88 O ANISOU 2876 CB ILE B 476 7707 4974 6820 -186 700 -119 C ANISOU 2877 CG1 ILE B 476 7585 4985 6770 -44 809 -205 C ANISOU 2878 CG2 ILE B 476 7602 5011 6779 -194 754 -80 C ANISOU 2879 CD1 ILE B 476 8074 5748 7355 -79 927 -194 C ANISOU 2891 N LEU B 477 7726 4508 6702 -242 414 -8 N ANISOU 2892 CA LEU B 477 7940 4624 6857 -385 303 106 C ANISOU 2893 C LEU B 477 8038 5018 7009 -419 435 148 C ANISOU 2894 O LEU B 477 7578 4622 6629 -314 491 96 O ANISOU 2895 CB LEU B 477 8211 4626 7098 -266 181 86 C ANISOU 2896 CG LEU B 477 9270 5570 8088 -432 52 215 C ANISOU 2897 CD1 LEU B 477 9118 5209 7782 -648 -130 331 C ANISOU 2898 CD2 LEU B 477 8965 5062 7800 -278 -48 196 C ANISOU 2910 N PHE B 478 7873 5035 6768 -551 464 267 N ANISOU 2911 CA PHE B 478 7971 5346 6777 -489 590 273 C ANISOU 2912 C PHE B 478 8072 5618 6733 -581 588 449 C ANISOU 2913 O PHE B 478 7762 5314 6457 -757 476 609 O ANISOU 2914 CB PHE B 478 7683 5295 6512 -406 735 220 C ANISOU 2915 CG PHE B 478 7860 5764 6744 -517 768 366 C ANISOU 2916 CD1 PHE B 478 7885 5668 6878 -635 659 382 C ANISOU 2917 CD2 PHE B 478 7916 6226 6715 -483 888 513 C ANISOU 2918 CE1 PHE B 478 7734 5780 6801 -799 623 571 C ANISOU 2919 CE2 PHE B 478 7642 6367 6581 -611 908 731 C ANISOU 2920 CZ PHE B 478 7818 6397 6915 -808 752 773 C ANISOU 2930 N ILE B 479 7855 5521 6305 -446 692 434 N ANISOU 2931 CA ILE B 479 8382 6293 6614 -435 745 600 C ANISOU 2932 C ILE B 479 8022 6380 6184 -283 938 659 C ANISOU 2933 O ILE B 479 8770 7039 6818 -85 1011 489 O ANISOU 2934 CB ILE B 479 8586 6214 6491 -314 694 526 C ANISOU 2935 CG1 ILE B 479 9660 6910 7702 -452 500 492 C ANISOU 2936 CG2 ILE B 479 8917 6844 6544 -266 768 717 C ANISOU 2937 CD1 ILE B 479 10477 7390 8246 -377 388 425 C ANISOU 2949 N ASP B 480 8484 7352 6726 -379 1000 935 N ANISOU 2950 CA ASP B 480 8151 7587 6392 -218 1196 1056 C ANISOU 2951 C ASP B 480 8348 8060 6167 101 1362 1119 C ANISOU 2952 O ASP B 480 8842 8259 6364 149 1299 1071 O ANISOU 2953 CB ASP B 480 8544 8468 7152 -512 1146 1388 C ANISOU 2954 CG ASP B 480 8650 8981 7280 -699 1097 1761 C ANISOU 2955 OD1 ASP B 480 8470 8776 6813 -576 1142 1774 O ANISOU 2956 OD2 ASP B 480 8722 9434 7664 -997 989 2087 O ANISOU 2961 N SER B 481 9001 9294 6749 361 1574 1238 N ANISOU 2962 CA SER B 481 9648 10170 6861 803 1754 1258 C ANISOU 2963 C SER B 481 9919 10858 7035 740 1789 1566 C ANISOU 2964 O SER B 481 10855 11776 7400 1111 1890 1528 O ANISOU 2965 CB SER B 481 11352 12550 8543 1142 1996 1381 C ANISOU 2966 OG SER B 481 12168 14037 9974 824 2015 1707 O ANISOU 2972 N ALA B 482 9516 10812 7117 293 1684 1890 N ANISOU 2973 CA ALA B 482 8804 10520 6370 154 1676 2243 C ANISOU 2974 C ALA B 482 8928 9873 6385 -75 1430 2075 C ANISOU 2975 O ALA B 482 8618 9785 6077 -265 1361 2356 O ANISOU 2976 CB ALA B 482 8364 10868 6494 -258 1617 2764 C ANISOU 2982 N ASN B 483 9151 9256 6562 -82 1286 1668 N ANISOU 2983 CA ASN B 483 9981 9399 7354 -278 1050 1520 C ANISOU 2984 C ASN B 483 9452 8789 7257 -724 821 1701 C ANISOU 2985 O ASN B 483 8989 7905 6761 -882 629 1682 O ANISOU 2986 CB ASN B 483 10832 10191 7716 -109 1068 1564 C ANISOU 2987 CG ASN B 483 12718 11390 9116 187 1020 1193 C ANISOU 2988 OD1 ASN B 483 14044 12121 10382 61 807 1057 O ANISOU 2989 ND2 ASN B 483 13984 12705 10032 575 1177 1047 N ANISOU 2996 N ASN B 484 9204 8839 7368 -914 797 1856 N ANISOU 2997 CA ASN B 484 9066 8340 7511 -1278 508 1919 C ANISOU 2998 C ASN B 484 8497 7081 6965 -1185 428 1517 C ANISOU 2999 O ASN B 484 8582 7142 7017 -953 586 1281 O ANISOU 3000 CB ASN B 484 8086 7835 6836 -1517 454 2230 C ANISOU 3001 CG ASN B 484 8306 8991 7114 -1557 597 2695 C ANISOU 3002 OD1 ASN B 484 7981 8878 6682 -1643 566 2940 O ANISOU 3003 ND2 ASN B 484 8151 9476 7146 -1487 760 2858 N ANISOU 3010 N VAL B 485 7948 6001 6468 -1352 175 1466 N ANISOU 3011 CA VAL B 485 8402 5952 6982 -1243 113 1158 C ANISOU 3012 C VAL B 485 7528 4997 6239 -1394 -22 1212 C ANISOU 3013 O VAL B 485 8271 5681 6997 -1672 -261 1465 O ANISOU 3014 CB VAL B 485 8673 5692 7189 -1237 -75 1054 C ANISOU 3015 CG1 VAL B 485 9392 6080 7983 -1040 -71 775 C ANISOU 3016 CG2 VAL B 485 9072 6187 7431 -1157 8 1070 C ANISOU 3026 N VAL B 486 7666 5084 6438 -1233 87 996 N ANISOU 3027 CA VAL B 486 7845 5162 6680 -1345 -35 1022 C ANISOU 3028 C VAL B 486 8487 5355 7267 -1130 -47 710 C ANISOU 3029 O VAL B 486 8309 5279 7138 -901 159 520 O ANISOU 3030 CB VAL B 486 8116 6049 7094 -1351 163 1148 C ANISOU 3031 CG1 VAL B 486 7749 5589 6791 -1542 -24 1251 C ANISOU 3032 CG2 VAL B 486 8232 6784 7246 -1433 270 1463 C ANISOU 3042 N TYR B 487 8489 4866 7131 -1204 -313 692 N ANISOU 3043 CA TYR B 487 9028 4994 7531 -979 -351 442 C ANISOU 3044 C TYR B 487 8754 4715 7224 -1129 -453 514 C ANISOU 3045 O TYR B 487 8638 4332 6988 -1409 -774 716 O ANISOU 3046 CB TYR B 487 9146 4394 7348 -886 -646 356 C ANISOU 3047 CG TYR B 487 10115 5014 8111 -527 -627 90 C ANISOU 3048 CD1 TYR B 487 9812 5072 7993 -231 -321 -59 C ANISOU 3049 CD2 TYR B 487 11031 5244 8611 -476 -937 16 C ANISOU 3050 CE1 TYR B 487 10856 5934 8863 130 -274 -246 C ANISOU 3051 CE2 TYR B 487 11331 5248 8638 -69 -896 -228 C ANISOU 3052 CZ TYR B 487 10609 5029 8159 243 -538 -343 C ANISOU 3053 OH TYR B 487 12525 6802 9833 667 -463 -528 O ANISOU 3063 N LYS B 488 8001 4214 6567 -967 -230 371 N ANISOU 3064 CA LYS B 488 9439 5830 8058 -1107 -254 460 C ANISOU 3065 C LYS B 488 8263 4507 6787 -843 -140 203 C ANISOU 3066 O LYS B 488 7904 4361 6536 -602 114 46 O ANISOU 3067 CB LYS B 488 8913 6073 7841 -1187 2 631 C ANISOU 3068 CG LYS B 488 8818 6274 7862 -1239 57 688 C ANISOU 3069 CD LYS B 488 8540 6796 7848 -1257 302 899 C ANISOU 3070 CE LYS B 488 9024 7582 8455 -1205 415 891 C ANISOU 3071 NZ LYS B 488 9817 9123 9441 -1160 627 1110 N ANISOU 3085 N GLN B 489 8589 4515 6919 -923 -345 204 N ANISOU 3086 CA GLN B 489 8878 4774 7124 -704 -220 9 C ANISOU 3087 C GLN B 489 8483 5041 7073 -790 17 103 C ANISOU 3088 O GLN B 489 7886 4698 6613 -1061 -81 339 O ANISOU 3089 CB GLN B 489 9570 4770 7378 -747 -579 -31 C ANISOU 3090 CG GLN B 489 9654 4773 7286 -504 -475 -230 C ANISOU 3091 CD GLN B 489 11073 5279 8066 -443 -878 -335 C ANISOU 3092 OE1 GLN B 489 11691 5299 8236 -141 -1003 -515 O ANISOU 3093 NE2 GLN B 489 11080 5153 7990 -704 -1103 -216 N ANISOU 3102 N TYR B 490 7547 4395 6270 -562 301 -46 N ANISOU 3103 CA TYR B 490 8101 5452 7062 -574 502 -4 C ANISOU 3104 C TYR B 490 7750 4946 6583 -491 480 -116 C ANISOU 3105 O TYR B 490 7650 4609 6311 -262 518 -290 O ANISOU 3106 CB TYR B 490 7351 4992 6468 -400 747 -85 C ANISOU 3107 CG TYR B 490 8048 5907 7253 -463 795 31 C ANISOU 3108 CD1 TYR B 490 8439 6081 7571 -492 700 50 C ANISOU 3109 CD2 TYR B 490 7361 5636 6671 -454 934 123 C ANISOU 3110 CE1 TYR B 490 7787 5636 6956 -539 749 163 C ANISOU 3111 CE2 TYR B 490 8394 6880 7694 -454 987 235 C ANISOU 3112 CZ TYR B 490 8609 6880 7837 -508 898 253 C ANISOU 3113 OH TYR B 490 8243 6707 7410 -488 955 358 O ANISOU 3123 N GLU B 491 7619 5009 6539 -654 430 8 N ANISOU 3124 CA GLU B 491 7760 4994 6537 -607 383 -78 C ANISOU 3125 C GLU B 491 7596 5191 6547 -427 656 -177 C ANISOU 3126 O GLU B 491 6727 4689 5904 -385 835 -145 O ANISOU 3127 CB GLU B 491 7782 5137 6637 -885 198 141 C ANISOU 3128 CG GLU B 491 8966 5865 7610 -1140 -180 295 C ANISOU 3129 CD GLU B 491 10857 6852 8923 -1008 -454 76 C ANISOU 3130 OE1 GLU B 491 11698 7516 9543 -782 -380 -126 O ANISOU 3131 OE2 GLU B 491 12204 7657 9992 -1096 -748 108 O ANISOU 3138 N ASP B 492 7655 5097 6442 -313 657 -291 N ANISOU 3139 CA ASP B 492 6830 4613 5784 -212 854 -329 C ANISOU 3140 C ASP B 492 6692 4697 5812 -70 1040 -370 C ANISOU 3141 O ASP B 492 6426 4710 5731 -70 1145 -334 O ANISOU 3142 CB ASP B 492 7669 5814 6855 -357 876 -189 C ANISOU 3143 CG ASP B 492 8366 6382 7462 -550 659 -78 C ANISOU 3144 OD1 ASP B 492 8609 6201 7388 -509 524 -186 O ANISOU 3145 OD2 ASP B 492 9180 7528 8496 -729 610 141 O ANISOU 3150 N MET B 493 6824 4666 5835 68 1047 -435 N ANISOU 3151 CA MET B 493 6643 4693 5829 155 1162 -416 C ANISOU 3152 C MET B 493 5871 4098 5077 329 1258 -414 C ANISOU 3153 O MET B 493 6496 4985 5919 318 1315 -324 O ANISOU 3154 CB MET B 493 6916 4794 6056 178 1104 -417 C ANISOU 3155 CG MET B 493 6346 4170 5517 -1 1029 -355 C ANISOU 3156 SD MET B 493 6936 5051 6293 -51 1128 -289 S ANISOU 3157 CE MET B 493 7539 5612 6952 35 1132 -292 C ANISOU 3167 N VAL B 494 6509 4605 5466 488 1251 -480 N ANISOU 3168 CA VAL B 494 6740 5102 5674 718 1371 -441 C ANISOU 3169 C VAL B 494 6854 5201 5610 752 1381 -479 C ANISOU 3170 O VAL B 494 7803 5729 6221 757 1254 -596 O ANISOU 3171 CB VAL B 494 6874 5050 5527 1017 1364 -505 C ANISOU 3172 CG1 VAL B 494 6946 5500 5529 1351 1521 -433 C ANISOU 3173 CG2 VAL B 494 7154 5325 5989 965 1332 -458 C ANISOU 3183 N VAL B 495 6484 5258 5428 775 1496 -357 N ANISOU 3184 CA VAL B 495 6794 5604 5584 805 1515 -370 C ANISOU 3185 C VAL B 495 6399 5135 4769 1161 1570 -436 C ANISOU 3186 O VAL B 495 7254 6363 5678 1404 1706 -328 O ANISOU 3187 CB VAL B 495 6552 5844 5684 686 1586 -177 C ANISOU 3188 CG1 VAL B 495 6946 6299 5890 746 1614 -176 C ANISOU 3189 CG2 VAL B 495 6550 5770 5940 422 1497 -154 C ANISOU 3199 N GLU B 496 7913 6152 5819 1223 1446 -598 N ANISOU 3200 CA GLU B 496 7997 6056 5338 1634 1475 -692 C ANISOU 3201 C GLU B 496 8272 6562 5483 1702 1554 -642 C ANISOU 3202 O GLU B 496 8287 6759 5160 2096 1686 -629 O ANISOU 3203 CB GLU B 496 9262 6438 5984 1714 1204 -916 C ANISOU 3204 CG GLU B 496 9668 6548 6431 1674 1092 -959 C ANISOU 3205 CD GLU B 496 9901 7028 6573 2105 1263 -945 C ANISOU 3206 OE1 GLU B 496 9857 7290 6298 2492 1438 -920 O ANISOU 3207 OE2 GLU B 496 9325 6398 6154 2084 1231 -933 O ANISOU 3214 N SER B 497 8436 6738 5870 1364 1480 -605 N ANISOU 3215 CA SER B 497 8398 6898 5721 1393 1531 -546 C ANISOU 3216 C SER B 497 7808 6604 5682 1003 1517 -410 C ANISOU 3217 O SER B 497 6895 5552 5045 752 1422 -430 O ANISOU 3218 CB SER B 497 9106 6940 5780 1475 1331 -732 C ANISOU 3219 OG SER B 497 11080 8575 7926 1093 1111 -763 O ANISOU 3225 N CYS B 498 7640 6852 5635 990 1609 -258 N ANISOU 3226 CA CYS B 498 7425 6906 5860 690 1579 -108 C ANISOU 3227 C CYS B 498 8056 7407 6247 659 1513 -135 C ANISOU 3228 O CYS B 498 7729 7001 5468 904 1553 -188 O ANISOU 3229 CB CYS B 498 7352 7465 6151 674 1695 172 C ANISOU 3230 SG CYS B 498 7282 7523 6446 610 1701 248 S ANISOU 3235 N GLY B 499 7391 6734 5843 399 1412 -87 N ANISOU 3236 CA GLY B 499 8293 7538 6559 345 1332 -88 C ANISOU 3237 C GLY B 499 7537 6880 6176 102 1244 8 C ANISOU 3238 O GLY B 499 6164 5526 5106 4 1222 26 O ANISOU 3242 N CYS B 500 6610 6005 5176 45 1192 79 N ANISOU 3243 CA CYS B 500 6907 6354 5754 -136 1085 174 C ANISOU 3244 C CYS B 500 6670 5863 5516 -213 962 73 C ANISOU 3245 O CYS B 500 7067 6053 5630 -201 896 -1 O ANISOU 3246 CB CYS B 500 7097 6765 5879 -167 1077 337 C ANISOU 3247 SG CYS B 500 7363 7537 6306 -139 1197 596 S ANISOU 3252 N ARG B 501 6494 5698 5623 -268 916 84 N ANISOU 3253 CA ARG B 501 6562 5707 5769 -318 828 63 C ANISOU 3254 C ARG B 501 7257 6503 6693 -308 767 137 C ANISOU 3255 O ARG B 501 6758 6086 6282 -338 684 194 O ANISOU 3256 CB ARG B 501 6426 5522 5678 -301 862 -2 C ANISOU 3257 CG ARG B 501 7296 6170 6255 -280 864 -93 C ANISOU 3258 CD ARG B 501 7419 6063 6134 -379 685 -90 C ANISOU 3259 NE ARG B 501 9415 7721 7645 -269 659 -204 N ANISOU 3260 CZ ARG B 501 10373 8348 8366 -255 565 -283 C ANISOU 3261 NH1 ARG B 501 11496 9530 9761 -386 513 -226 N ANISOU 3262 NH2 ARG B 501 9999 7572 7436 -78 517 -413 N ANISOU 3263 OXT ARG B 501 6894 6115 6395 -259 774 153 O TER 3277 ARG B 501 ANISOU 3278 N GLY C 25 15062 21012 15819 -4924 5102 -2426 N ANISOU 3279 CA GLY C 25 15156 20379 14933 -4571 5120 -2371 C ANISOU 3280 C GLY C 25 16520 20782 15578 -4213 4509 -2032 C ANISOU 3281 O GLY C 25 16872 20457 15001 -3958 4465 -1971 O ANISOU 3285 N CYS C 26 16593 20837 16094 -4187 4033 -1838 N ANISOU 3286 CA CYS C 26 15120 18522 14057 -3872 3454 -1519 C ANISOU 3287 C CYS C 26 14854 17365 12814 -4238 3469 -1132 C ANISOU 3288 O CYS C 26 13539 16194 11932 -4480 3341 -1020 O ANISOU 3289 CB CYS C 26 14982 18843 14980 -3501 2896 -1543 C ANISOU 3290 SG CYS C 26 13230 16035 12572 -3215 2220 -1115 S ANISOU 3295 N ASN C 27 15538 17100 12131 -4233 3605 -935 N ANISOU 3296 CA ASN C 27 15625 16179 11074 -4500 3650 -546 C ANISOU 3297 C ASN C 27 14964 15069 10343 -4171 2977 -274 C ANISOU 3298 O ASN C 27 14972 14547 9669 -3796 2678 -167 O ANISOU 3299 CB ASN C 27 16416 16115 10353 -4524 4042 -437 C ANISOU 3300 CG ASN C 27 17250 15845 9912 -4820 4220 -39 C ANISOU 3301 OD1 ASN C 27 15979 14178 8569 -4778 3812 230 O ANISOU 3302 ND2 ASN C 27 18929 16953 10515 -5104 4862 6 N ANISOU 3309 N LYS C 28 13937 14298 10045 -4313 2738 -186 N ANISOU 3310 CA LYS C 28 14414 14399 10549 -3996 2120 60 C ANISOU 3311 C LYS C 28 14370 13190 9071 -3955 2023 440 C ANISOU 3312 O LYS C 28 13442 11907 7905 -3569 1561 581 O ANISOU 3313 CB LYS C 28 12968 13397 10030 -4173 1921 88 C ANISOU 3314 CG LYS C 28 13597 15268 12085 -4151 1995 -305 C ANISOU 3315 CD LYS C 28 13939 16143 13352 -4270 1745 -315 C ANISOU 3316 CE LYS C 28 12463 16000 13246 -4222 1852 -743 C ANISOU 3317 NZ LYS C 28 14190 18324 15813 -4348 1621 -797 N ANISOU 3331 N ALA C 29 15190 13388 8894 -4326 2472 598 N ANISOU 3332 CA ALA C 29 17093 14143 9325 -4196 2387 962 C ANISOU 3333 C ALA C 29 16398 13222 7891 -3757 2293 895 C ANISOU 3334 O ALA C 29 16978 13231 7738 -3400 1914 1099 O ANISOU 3335 CB ALA C 29 16804 13209 8248 -4595 2896 1098 C ANISOU 3341 N LEU C 30 16523 13817 8183 -3775 2639 589 N ANISOU 3342 CA LEU C 30 16830 13927 7744 -3379 2570 481 C ANISOU 3343 C LEU C 30 15650 13340 7471 -2965 2046 248 C ANISOU 3344 O LEU C 30 16287 13730 7502 -2594 1781 205 O ANISOU 3345 CB LEU C 30 17796 15116 8475 -3552 3171 230 C ANISOU 3346 CG LEU C 30 18598 15867 8606 -3177 3183 21 C ANISOU 3347 CD1 LEU C 30 19295 15572 7709 -2901 3095 300 C ANISOU 3348 CD2 LEU C 30 17166 14848 7308 -3407 3809 -264 C ANISOU 3360 N CYS C 31 14303 12766 7539 -3013 1913 71 N ANISOU 3361 CA CYS C 31 13508 12535 7618 -2663 1601 -225 C ANISOU 3362 C CYS C 31 11721 10714 6411 -2436 1042 -96 C ANISOU 3363 O CYS C 31 11669 10888 6828 -2127 772 -306 O ANISOU 3364 CB CYS C 31 12192 12110 7434 -2777 1897 -559 C ANISOU 3365 SG CYS C 31 14625 14665 9270 -3002 2595 -783 S ANISOU 3370 N ALA C 32 11951 10606 6562 -2587 889 232 N ANISOU 3371 CA ALA C 32 11298 10038 6660 -2399 428 325 C ANISOU 3372 C ALA C 32 10281 8731 5357 -2028 40 309 C ANISOU 3373 O ALA C 32 10419 9151 6294 -1794 -214 149 O ANISOU 3374 CB ALA C 32 10834 9173 5981 -2632 348 686 C ANISOU 3380 N SER C 33 11037 8916 4951 -1961 8 456 N ANISOU 3381 CA SER C 33 11264 8957 4897 -1623 -377 409 C ANISOU 3382 C SER C 33 11356 9542 5513 -1438 -381 -38 C ANISOU 3383 O SER C 33 10296 8678 5192 -1266 -647 -187 O ANISOU 3384 CB SER C 33 12419 9498 4632 -1531 -379 602 C ANISOU 3385 OG SER C 33 12510 9555 4519 -1191 -778 504 O ANISOU 3391 N ASP C 34 11293 9615 5011 -1475 -58 -261 N ANISOU 3392 CA ASP C 34 11532 10221 5558 -1278 -87 -701 C ANISOU 3393 C ASP C 34 10638 9837 5942 -1281 -20 -936 C ANISOU 3394 O ASP C 34 10318 9684 6106 -1094 -174 -1236 O ANISOU 3395 CB ASP C 34 12785 11468 5970 -1286 248 -888 C ANISOU 3396 CG ASP C 34 13554 11687 5346 -1151 140 -700 C ANISOU 3397 OD1 ASP C 34 15333 12990 6546 -1286 209 -297 O ANISOU 3398 OD2 ASP C 34 15561 13725 6822 -894 -22 -958 O ANISOU 3403 N VAL C 35 10369 9812 6219 -1479 212 -822 N ANISOU 3404 CA VAL C 35 9727 9655 6762 -1401 240 -1012 C ANISOU 3405 C VAL C 35 9434 9183 7023 -1221 -154 -895 C ANISOU 3406 O VAL C 35 8804 8689 7054 -1014 -221 -1134 O ANISOU 3407 CB VAL C 35 9666 9997 7156 -1637 537 -932 C ANISOU 3408 CG1 VAL C 35 9066 9892 7743 -1466 484 -1080 C ANISOU 3409 CG2 VAL C 35 10434 11028 7581 -1803 1004 -1130 C ANISOU 3419 N SER C 36 9050 8427 6340 -1293 -387 -524 N ANISOU 3420 CA SER C 36 8679 7832 6408 -1115 -738 -408 C ANISOU 3421 C SER C 36 9028 8009 6613 -926 -927 -635 C ANISOU 3422 O SER C 36 8863 7808 7081 -766 -1052 -754 O ANISOU 3423 CB SER C 36 8295 7058 5615 -1230 -926 21 C ANISOU 3424 OG SER C 36 8345 7352 5898 -1447 -720 136 O ANISOU 3430 N LYS C 37 8900 7775 5647 -937 -933 -723 N ANISOU 3431 CA LYS C 37 10131 9002 6796 -779 -1105 -1039 C ANISOU 3432 C LYS C 37 10653 9792 8082 -698 -952 -1464 C ANISOU 3433 O LYS C 37 9977 9046 7794 -598 -1096 -1690 O ANISOU 3434 CB LYS C 37 10034 8878 5659 -762 -1080 -1142 C ANISOU 3435 CG LYS C 37 9968 9004 5522 -621 -1185 -1610 C ANISOU 3436 CD LYS C 37 11392 10388 5776 -534 -1207 -1676 C ANISOU 3437 CE LYS C 37 13218 12398 7286 -572 -848 -1929 C ANISOU 3438 NZ LYS C 37 14065 13163 6922 -417 -895 -2032 N ANISOU 3452 N CYS C 38 9952 9379 7548 -744 -629 -1611 N ANISOU 3453 CA CYS C 38 9495 9121 7682 -630 -458 -2037 C ANISOU 3454 C CYS C 38 9905 9458 8999 -505 -478 -1976 C ANISOU 3455 O CYS C 38 9040 8481 8581 -373 -444 -2271 O ANISOU 3456 CB CYS C 38 9862 9836 7912 -683 -89 -2220 C ANISOU 3457 SG CYS C 38 11228 11155 8024 -767 -37 -2299 S ANISOU 3462 N LEU C 39 8581 8145 7892 -538 -527 -1602 N ANISOU 3463 CA LEU C 39 8949 8436 9027 -358 -565 -1516 C ANISOU 3464 C LEU C 39 8631 7632 8828 -261 -803 -1474 C ANISOU 3465 O LEU C 39 9035 7830 9760 -68 -739 -1614 O ANISOU 3466 CB LEU C 39 7860 7520 8075 -430 -605 -1153 C ANISOU 3467 CG LEU C 39 9053 9272 9346 -553 -318 -1227 C ANISOU 3468 CD1 LEU C 39 8143 8526 8593 -681 -396 -895 C ANISOU 3469 CD2 LEU C 39 9774 10341 10724 -310 -78 -1575 C ANISOU 3481 N ILE C 40 8750 7532 8438 -377 -1048 -1289 N ANISOU 3482 CA ILE C 40 9738 8113 9635 -297 -1244 -1240 C ANISOU 3483 C ILE C 40 8984 7308 8964 -290 -1181 -1705 C ANISOU 3484 O ILE C 40 9799 7786 10122 -238 -1222 -1790 O ANISOU 3485 CB ILE C 40 8715 6885 8129 -380 -1536 -907 C ANISOU 3486 CG1 ILE C 40 9396 7757 8039 -494 -1585 -993 C ANISOU 3487 CG2 ILE C 40 9115 7202 8505 -397 -1617 -456 C ANISOU 3488 CD1 ILE C 40 10377 8509 8534 -499 -1880 -731 C ANISOU 3500 N GLN C 41 9375 8011 9027 -358 -1059 -2029 N ANISOU 3501 CA GLN C 41 10523 9177 10316 -357 -941 -2554 C ANISOU 3502 C GLN C 41 11714 10263 12094 -220 -631 -2768 C ANISOU 3503 O GLN C 41 10824 9350 11299 -226 -468 -3234 O ANISOU 3504 CB GLN C 41 10411 9425 9559 -437 -926 -2829 C ANISOU 3505 CG GLN C 41 9608 8688 8094 -491 -1231 -2705 C ANISOU 3506 CD GLN C 41 10254 9634 8081 -498 -1243 -3056 C ANISOU 3507 OE1 GLN C 41 12268 11790 10249 -503 -1147 -3574 O ANISOU 3508 NE2 GLN C 41 10481 9908 7486 -484 -1354 -2779 N ANISOU 3517 N GLU C 42 10989 9498 11721 -75 -552 -2460 N ANISOU 3518 CA GLU C 42 12023 10429 13280 153 -277 -2619 C ANISOU 3519 C GLU C 42 11748 10548 12911 159 -14 -2969 C ANISOU 3520 O GLU C 42 11544 10193 12970 303 235 -3312 O ANISOU 3521 CB GLU C 42 11336 9135 12915 241 -198 -2825 C ANISOU 3522 CG GLU C 42 13456 10808 15178 290 -389 -2451 C ANISOU 3523 CD GLU C 42 15049 11867 16880 189 -363 -2678 C ANISOU 3524 OE1 GLU C 42 13934 10456 15950 204 -88 -3101 O ANISOU 3525 OE2 GLU C 42 15251 11947 16980 82 -600 -2436 O ANISOU 3532 N LEU C 43 11495 10739 12218 2 -37 -2881 N ANISOU 3533 CA LEU C 43 11556 11196 12119 -6 234 -3160 C ANISOU 3534 C LEU C 43 11772 11849 12519 14 351 -2892 C ANISOU 3535 O LEU C 43 10892 10980 11717 -33 173 -2500 O ANISOU 3536 CB LEU C 43 10951 10727 10750 -205 170 -3324 C ANISOU 3537 CG LEU C 43 11732 11254 11296 -270 -28 -3606 C ANISOU 3538 CD1 LEU C 43 11509 11243 10239 -384 -135 -3750 C ANISOU 3539 CD2 LEU C 43 13067 12388 13069 -169 188 -4084 C ANISOU 3551 N CYS C 44 11985 12454 12822 71 663 -3138 N ANISOU 3552 CA CYS C 44 12505 13529 13621 68 833 -2983 C ANISOU 3553 C CYS C 44 12274 13347 14110 316 741 -2783 C ANISOU 3554 O CYS C 44 12624 14047 14652 239 672 -2510 O ANISOU 3555 CB CYS C 44 11966 13154 12534 -256 771 -2685 C ANISOU 3556 SG CYS C 44 13030 14033 12508 -482 806 -2821 S ANISOU 3561 N GLN C 45 13755 14436 15945 622 748 -2933 N ANISOU 3562 CA GLN C 45 13889 14492 16646 950 659 -2749 C ANISOU 3563 C GLN C 45 15334 16010 18552 1376 923 -3026 C ANISOU 3564 O GLN C 45 15107 15911 18786 1722 877 -2890 O ANISOU 3565 CB GLN C 45 13612 13453 16277 988 408 -2559 C ANISOU 3566 CG GLN C 45 12722 12454 14956 648 117 -2252 C ANISOU 3567 CD GLN C 45 13087 12215 15403 757 -121 -1989 C ANISOU 3568 OE1 GLN C 45 13626 12374 16285 1086 -46 -2026 O ANISOU 3569 NE2 GLN C 45 13381 12357 15328 509 -382 -1715 N ANISOU 3578 N CYS C 46 19582 20165 22646 1397 1190 -3416 N ANISOU 3579 CA CYS C 46 20314 20970 23755 1821 1479 -3689 C ANISOU 3580 C CYS C 46 19674 21314 23476 1897 1634 -3718 C ANISOU 3581 O CYS C 46 18646 20813 22230 1536 1699 -3727 O ANISOU 3582 CB CYS C 46 20670 20929 23800 1786 1734 -4127 C ANISOU 3583 SG CYS C 46 23602 24514 26303 1417 1912 -4364 S ANISOU 3588 N ARG C 47 19313 21197 23650 2381 1711 -3744 N ANISOU 3589 CA ARG C 47 18992 21938 23796 2469 1852 -3817 C ANISOU 3590 C ARG C 47 19661 22877 24440 2557 2256 -4231 C ANISOU 3591 O ARG C 47 19331 21884 23913 2791 2419 -4471 O ANISOU 3592 CB ARG C 47 18790 22033 24198 3012 1732 -3703 C ANISOU 3593 CG ARG C 47 19296 21809 24729 3621 1854 -3842 C ANISOU 3594 CD ARG C 47 19069 22124 25088 4258 1784 -3794 C ANISOU 3595 NE ARG C 47 19631 23091 25880 4155 1411 -3458 N ANISOU 3596 CZ ARG C 47 18430 22700 25242 4559 1260 -3416 C ANISOU 3597 NH1 ARG C 47 16884 21709 24120 5145 1439 -3672 N ANISOU 3598 NH2 ARG C 47 16948 21512 23898 4390 910 -3131 N ANISOU 3612 N PRO C 48 18628 22791 23583 2347 2458 -4340 N ANISOU 3613 CA PRO C 48 19019 23510 23971 2454 2870 -4732 C ANISOU 3614 C PRO C 48 18060 23075 23679 3072 3056 -4940 C ANISOU 3615 O PRO C 48 16484 22368 22438 3131 3355 -5174 O ANISOU 3616 CB PRO C 48 17456 22699 22272 1924 3025 -4711 C ANISOU 3617 CG PRO C 48 15624 21316 20814 1765 2744 -4374 C ANISOU 3618 CD PRO C 48 16378 21239 21463 1939 2341 -4104 C ANISOU 3626 N GLY C 49 18768 23189 24536 3582 2900 -4862 N ANISOU 3627 CA GLY C 49 17078 21863 23375 4284 3041 -5029 C ANISOU 3628 C GLY C 49 16442 20103 22432 4771 3174 -5168 C ANISOU 3629 O GLY C 49 16343 19102 22120 4901 2963 -4946 O ANISOU 3633 N CYS C 53 20032 21880 23589 2928 3617 -5956 N ANISOU 3634 CA CYS C 53 21957 23704 25273 2476 3247 -5627 C ANISOU 3635 C CYS C 53 21445 22368 24172 2186 3152 -5803 C ANISOU 3636 O CYS C 53 21922 22683 24280 2122 3376 -6198 O ANISOU 3637 CB CYS C 53 21358 23948 24560 2091 3249 -5490 C ANISOU 3638 SG CYS C 53 22034 24478 24896 1603 2812 -5046 S ANISOU 3643 N SER C 54 18312 18771 20964 2008 2818 -5540 N ANISOU 3644 CA SER C 54 18178 17927 20394 1747 2712 -5742 C ANISOU 3645 C SER C 54 18949 18963 20681 1285 2440 -5613 C ANISOU 3646 O SER C 54 18387 18480 19614 1080 2507 -5916 O ANISOU 3647 CB SER C 54 17861 16819 20308 1896 2584 -5595 C ANISOU 3648 OG SER C 54 17954 17125 20680 1943 2312 -5099 O ANISOU 3654 N CYS C 55 19992 20116 21812 1157 2132 -5165 N ANISOU 3655 CA CYS C 55 19280 19543 20598 780 1854 -4980 C ANISOU 3656 C CYS C 55 18532 19450 19508 613 1967 -4898 C ANISOU 3657 O CYS C 55 17626 18614 18094 342 1769 -4694 O ANISOU 3658 CB CYS C 55 19476 19572 20995 732 1524 -4516 C ANISOU 3659 SG CYS C 55 20729 21459 22715 855 1529 -4092 S ANISOU 3664 N CYS C 56 20086 21454 21294 776 2308 -5050 N ANISOU 3665 CA CYS C 56 19713 21684 20633 587 2489 -4968 C ANISOU 3666 C CYS C 56 18017 19835 18012 307 2432 -5061 C ANISOU 3667 O CYS C 56 17244 19331 16785 85 2495 -4858 O ANISOU 3668 CB CYS C 56 19778 22210 21032 816 2916 -5257 C ANISOU 3669 SG CYS C 56 22331 25448 24582 1089 3016 -5054 S ANISOU 3674 N LYS C 57 17490 18860 17167 325 2325 -5382 N ANISOU 3675 CA LYS C 57 16834 18116 15620 152 2259 -5570 C ANISOU 3676 C LYS C 57 16699 17684 15126 -5 1820 -5386 C ANISOU 3677 O LYS C 57 16401 17444 14071 -147 1708 -5238 O ANISOU 3678 CB LYS C 57 17270 18367 15918 272 2433 -6148 C ANISOU 3679 CG LYS C 57 17703 19009 16824 509 2865 -6360 C ANISOU 3680 CD LYS C 57 19208 20292 18049 612 3078 -6950 C ANISOU 3681 CE LYS C 57 16669 17936 15966 899 3522 -7154 C ANISOU 3682 NZ LYS C 57 16735 17722 15713 1001 3753 -7738 N ANISOU 3696 N GLU C 58 16234 16872 15149 40 1593 -5396 N ANISOU 3697 CA GLU C 58 15484 15908 14166 -99 1185 -5201 C ANISOU 3698 C GLU C 58 15562 16128 14069 -202 1046 -4637 C ANISOU 3699 O GLU C 58 14905 15372 12902 -312 752 -4449 O ANISOU 3700 CB GLU C 58 15856 15867 15183 -44 1050 -5259 C ANISOU 3701 CG GLU C 58 17999 17742 17412 -24 1162 -5846 C ANISOU 3702 CD GLU C 58 17200 16432 17153 -32 1070 -5909 C ANISOU 3703 OE1 GLU C 58 14919 14020 15133 -31 883 -5474 O ANISOU 3704 OE2 GLU C 58 18273 17191 18354 -54 1215 -6406 O ANISOU 3711 N CYS C 59 15502 16314 14439 -160 1255 -4386 N ANISOU 3712 CA CYS C 59 14031 14998 12785 -310 1190 -3908 C ANISOU 3713 C CYS C 59 14010 15085 11823 -467 1323 -3884 C ANISOU 3714 O CYS C 59 13405 14303 10603 -599 1134 -3577 O ANISOU 3715 CB CYS C 59 14153 15479 13660 -234 1400 -3749 C ANISOU 3716 SG CYS C 59 13948 15498 13344 -481 1359 -3229 S ANISOU 3721 N MET C 60 15668 16971 13288 -429 1673 -4196 N ANISOU 3722 CA MET C 60 15818 17140 12450 -550 1857 -4170 C ANISOU 3723 C MET C 60 15422 16406 11145 -525 1533 -4244 C ANISOU 3724 O MET C 60 14916 15727 9722 -604 1509 -3998 O ANISOU 3725 CB MET C 60 16290 17904 12924 -477 2302 -4537 C ANISOU 3726 CG MET C 60 16793 18354 12323 -558 2551 -4577 C ANISOU 3727 SD MET C 60 19531 21504 15164 -509 3175 -4924 S ANISOU 3728 CE MET C 60 15794 17913 12562 -250 3112 -5312 C ANISOU 3738 N LEU C 61 15347 16231 11301 -405 1293 -4598 N ANISOU 3739 CA LEU C 61 15684 16392 10927 -365 931 -4732 C ANISOU 3740 C LEU C 61 15428 15939 10446 -427 594 -4260 C ANISOU 3741 O LEU C 61 14385 14770 8451 -384 411 -4154 O ANISOU 3742 CB LEU C 61 15148 15832 10913 -296 761 -5222 C ANISOU 3743 CG LEU C 61 15671 16334 10916 -263 356 -5480 C ANISOU 3744 CD1 LEU C 61 15664 16456 9841 -159 393 -5792 C ANISOU 3745 CD2 LEU C 61 15474 16085 11485 -292 224 -5928 C ANISOU 3757 N CYS C 62 14039 14493 9870 -485 508 -3974 N ANISOU 3758 CA CYS C 62 13798 14035 9461 -536 190 -3539 C ANISOU 3759 C CYS C 62 13804 13928 8747 -646 339 -3101 C ANISOU 3760 O CYS C 62 13964 13823 8216 -636 102 -2817 O ANISOU 3761 CB CYS C 62 13600 13772 10293 -549 92 -3371 C ANISOU 3762 SG CYS C 62 12358 12239 8988 -598 -290 -2850 S ANISOU 3767 N LEU C 63 14071 14377 9140 -751 754 -3060 N ANISOU 3768 CA LEU C 63 13611 13771 8036 -925 975 -2676 C ANISOU 3769 C LEU C 63 15621 15566 8762 -877 1134 -2746 C ANISOU 3770 O LEU C 63 16759 16342 9038 -972 1226 -2392 O ANISOU 3771 CB LEU C 63 13424 13944 8539 -1091 1387 -2637 C ANISOU 3772 CG LEU C 63 13108 13857 9406 -1095 1254 -2525 C ANISOU 3773 CD1 LEU C 63 13682 14925 10629 -1232 1648 -2527 C ANISOU 3774 CD2 LEU C 63 11720 12111 7856 -1168 913 -2104 C ANISOU 3786 N GLY C 64 16446 16547 9379 -720 1193 -3195 N ANISOU 3787 CA GLY C 64 17572 17443 9182 -606 1300 -3278 C ANISOU 3788 C GLY C 64 17649 17358 8647 -788 1833 -3034 C ANISOU 3789 O GLY C 64 17011 17050 8667 -947 2238 -3128 O ANISOU 3793 N ALA C 65 18651 17831 8351 -755 1857 -2728 N ANISOU 3794 CA ALA C 65 19808 18686 8690 -935 2432 -2521 C ANISOU 3795 C ALA C 65 20211 19257 9968 -1321 2747 -2257 C ANISOU 3796 O ALA C 65 19805 18904 9447 -1557 3318 -2243 O ANISOU 3797 CB ALA C 65 20205 18330 7459 -791 2385 -2191 C ANISOU 3803 N LEU C 66 17712 16883 8361 -1389 2390 -2076 N ANISOU 3804 CA LEU C 66 17392 16758 8888 -1723 2576 -1834 C ANISOU 3805 C LEU C 66 16422 16566 9376 -1766 2688 -2133 C ANISOU 3806 O LEU C 66 15855 16316 9689 -1979 2754 -1997 O ANISOU 3807 CB LEU C 66 16118 15194 7766 -1727 2120 -1483 C ANISOU 3808 CG LEU C 66 16849 15128 7184 -1775 2118 -1061 C ANISOU 3809 CD1 LEU C 66 15380 13437 5990 -1738 1638 -758 C ANISOU 3810 CD2 LEU C 66 18398 16448 8343 -2171 2722 -855 C ANISOU 3822 N TRP C 67 16398 16847 9594 -1543 2704 -2552 N ANISOU 3823 CA TRP C 67 16133 17257 10560 -1536 2893 -2837 C ANISOU 3824 C TRP C 67 16558 18036 11172 -1831 3471 -2804 C ANISOU 3825 O TRP C 67 15915 17969 11648 -1928 3556 -2828 O ANISOU 3826 CB TRP C 67 16674 17942 11105 -1263 2899 -3302 C ANISOU 3827 CG TRP C 67 16937 18825 12442 -1203 3173 -3609 C ANISOU 3828 CD1 TRP C 67 16346 18558 11794 -1223 3677 -3868 C ANISOU 3829 CD2 TRP C 67 16106 18338 12852 -1061 2972 -3690 C ANISOU 3830 NE1 TRP C 67 16362 19143 12967 -1084 3783 -4116 N ANISOU 3831 CE2 TRP C 67 16362 19132 13738 -967 3355 -4005 C ANISOU 3832 CE3 TRP C 67 15981 18077 13305 -975 2526 -3521 C ANISOU 3833 CZ2 TRP C 67 15370 18521 13888 -747 3287 -4148 C ANISOU 3834 CZ3 TRP C 67 15411 17837 13838 -779 2481 -3657 C ANISOU 3835 CH2 TRP C 67 15052 17988 14039 -648 2850 -3963 C ANISOU 3846 N ASP C 68 17683 18844 11203 -1962 3888 -2772 N ANISOU 3847 CA ASP C 68 18285 19722 11894 -2315 4509 -2737 C ANISOU 3848 C ASP C 68 17345 18868 11485 -2653 4484 -2415 C ANISOU 3849 O ASP C 68 15603 17874 10917 -2810 4642 -2527 O ANISOU 3850 CB ASP C 68 18116 18926 10195 -2402 4944 -2661 C ANISOU 3851 CG ASP C 68 20473 21264 12020 -2078 5005 -3020 C ANISOU 3852 OD1 ASP C 68 21037 22398 13542 -1874 4872 -3371 O ANISOU 3853 OD2 ASP C 68 21955 22126 12081 -2012 5204 -2959 O ANISOU 3858 N GLU C 69 17148 17934 10443 -2731 4251 -2033 N ANISOU 3859 CA GLU C 69 16860 17530 10331 -3103 4306 -1709 C ANISOU 3860 C GLU C 69 15809 16933 10535 -3034 3815 -1663 C ANISOU 3861 O GLU C 69 14276 15497 9396 -3347 3854 -1472 O ANISOU 3862 CB GLU C 69 17216 16813 9174 -3144 4246 -1313 C ANISOU 3863 CG GLU C 69 19582 18557 10062 -3209 4800 -1289 C ANISOU 3864 CD GLU C 69 20390 19274 10212 -2757 4666 -1548 C ANISOU 3865 OE1 GLU C 69 19491 18737 9966 -2429 4144 -1748 O ANISOU 3866 OE2 GLU C 69 22172 20607 10804 -2736 5101 -1575 O ANISOU 3873 N CYS C 70 14972 16351 10312 -2640 3386 -1854 N ANISOU 3874 CA CYS C 70 14310 15909 10608 -2509 2901 -1766 C ANISOU 3875 C CYS C 70 13305 15607 10806 -2222 2799 -2100 C ANISOU 3876 O CYS C 70 11238 13665 9487 -2061 2417 -2028 O ANISOU 3877 CB CYS C 70 13110 14023 8798 -2281 2375 -1550 C ANISOU 3878 SG CYS C 70 13823 13778 7988 -2483 2394 -1106 S ANISOU 3883 N CYS C 71 13340 16036 10984 -2125 3143 -2452 N ANISOU 3884 CA CYS C 71 12994 16290 11721 -1812 3082 -2765 C ANISOU 3885 C CYS C 71 12618 16612 12481 -1873 3068 -2729 C ANISOU 3886 O CYS C 71 12338 16585 13030 -1545 2793 -2817 O ANISOU 3887 CB CYS C 71 13551 17167 12188 -1729 3525 -3144 C ANISOU 3888 SG CYS C 71 15075 19490 14114 -2089 4190 -3258 S ANISOU 3893 N ASP C 72 13512 17805 13396 -2282 3371 -2618 N ANISOU 3894 CA ASP C 72 13443 18552 14452 -2357 3358 -2656 C ANISOU 3895 C ASP C 72 13269 18098 14543 -2238 2808 -2375 C ANISOU 3896 O ASP C 72 13128 18567 15397 -2050 2617 -2445 O ANISOU 3897 CB ASP C 72 15158 20623 16104 -2905 3832 -2638 C ANISOU 3898 CG ASP C 72 15659 22215 17904 -2992 3852 -2798 C ANISOU 3899 OD1 ASP C 72 13383 20414 16522 -2556 3502 -2911 O ANISOU 3900 OD2 ASP C 72 18176 25101 20512 -3496 4233 -2826 O ANISOU 3905 N CYS C 73 12037 15954 12406 -2299 2543 -2064 N ANISOU 3906 CA CYS C 73 11020 14611 11577 -2179 2039 -1788 C ANISOU 3907 C CYS C 73 10745 14484 12038 -1679 1719 -1925 C ANISOU 3908 O CYS C 73 10218 13942 11973 -1530 1369 -1763 O ANISOU 3909 CB CYS C 73 11155 13767 10598 -2254 1821 -1476 C ANISOU 3910 SG CYS C 73 14841 17006 13263 -2796 2151 -1204 S ANISOU 3915 N VAL C 74 11561 15363 12903 -1411 1853 -2218 N ANISOU 3916 CA VAL C 74 11699 15595 13720 -937 1658 -2386 C ANISOU 3917 C VAL C 74 12466 17130 15163 -732 1995 -2762 C ANISOU 3918 O VAL C 74 11634 16303 14772 -302 1926 -2947 O ANISOU 3919 CB VAL C 74 12187 15309 13653 -749 1458 -2415 C ANISOU 3920 CG1 VAL C 74 11388 13861 12422 -840 1061 -2053 C ANISOU 3921 CG2 VAL C 74 12036 15022 12733 -896 1757 -2620 C ANISOU 3931 N GLY C 75 14616 19882 17359 -1032 2397 -2886 N ANISOU 3932 CA GLY C 75 14798 20919 18244 -853 2743 -3250 C ANISOU 3933 C GLY C 75 15365 21281 18549 -588 2954 -3551 C ANISOU 3934 O GLY C 75 16357 22936 20129 -358 3232 -3865 O ANISOU 3938 N MET C 76 12652 17715 14977 -607 2832 -3495 N ANISOU 3939 CA MET C 76 12775 17596 14803 -376 3004 -3819 C ANISOU 3940 C MET C 76 13403 18496 14944 -621 3497 -4007 C ANISOU 3941 O MET C 76 14324 18891 14926 -743 3564 -4039 O ANISOU 3942 CB MET C 76 13114 17027 14456 -329 2670 -3741 C ANISOU 3943 CG MET C 76 12869 16425 14664 -74 2249 -3585 C ANISOU 3944 SD MET C 76 14826 17678 16453 235 2129 -3874 S ANISOU 3945 CE MET C 76 13464 16048 15821 580 1821 -3697 C ANISOU 3955 N CYS C 77 15372 21337 17571 -667 3854 -4156 N ANISOU 3956 CA CYS C 77 16217 22513 18062 -896 4402 -4356 C ANISOU 3957 C CYS C 77 16490 23908 19317 -950 4752 -4530 C ANISOU 3958 O CYS C 77 16216 24214 20021 -585 4615 -4663 O ANISOU 3959 CB CYS C 77 17037 22784 17796 -1363 4506 -4089 C ANISOU 3960 SG CYS C 77 17678 23330 18526 -1740 4225 -3633 S TER 3965 CYS C 77 ANISOU 3966 N GLY D 25 12679 13574 15477 3076 3973 -1033 N ANISOU 3967 CA GLY D 25 10797 11394 13853 3104 3513 -620 C ANISOU 3968 C GLY D 25 12188 12658 14492 2734 3119 -387 C ANISOU 3969 O GLY D 25 11533 12342 13406 2483 3157 -308 O ANISOU 3973 N CYS D 26 10429 10415 12615 2701 2749 -254 N ANISOU 3974 CA CYS D 26 10847 10684 12413 2388 2362 -64 C ANISOU 3975 C CYS D 26 10200 9364 11302 2359 2198 -292 C ANISOU 3976 O CYS D 26 10058 8926 11462 2456 1998 -181 O ANISOU 3977 CB CYS D 26 9389 9562 11392 2314 2029 377 C ANISOU 3978 SG CYS D 26 9512 9432 10865 1948 1546 543 S ANISOU 3983 N ASN D 27 9895 8880 10263 2216 2293 -608 N ANISOU 3984 CA ASN D 27 9522 7980 9376 2120 2109 -845 C ANISOU 3985 C ASN D 27 7795 6153 7415 1934 1643 -536 C ANISOU 3986 O ASN D 27 8358 6861 7502 1744 1494 -414 O ANISOU 3987 CB ASN D 27 10470 8974 9598 2004 2319 -1247 C ANISOU 3988 CG ASN D 27 10686 8752 9304 1900 2186 -1603 C ANISOU 3989 OD1 ASN D 27 10178 7944 8742 1824 1844 -1466 O ANISOU 3990 ND2 ASN D 27 12893 11021 11114 1865 2464 -2092 N ANISOU 3997 N LYS D 28 7689 5786 7637 1984 1418 -413 N ANISOU 3998 CA LYS D 28 7933 6023 7703 1800 1000 -172 C ANISOU 3999 C LYS D 28 7963 5811 6982 1615 840 -393 C ANISOU 4000 O LYS D 28 7630 5569 6380 1454 572 -236 O ANISOU 4001 CB LYS D 28 8270 6198 8484 1876 816 -8 C ANISOU 4002 CG LYS D 28 9025 7181 10023 2135 999 204 C ANISOU 4003 CD LYS D 28 8966 7234 10447 2195 746 566 C ANISOU 4004 CE LYS D 28 9163 7841 11503 2503 916 854 C ANISOU 4005 NZ LYS D 28 10419 9566 13223 2528 612 1312 N ANISOU 4019 N ALA D 29 8913 6463 7642 1636 987 -774 N ANISOU 4020 CA ALA D 29 9415 6858 7447 1467 811 -990 C ANISOU 4021 C ALA D 29 8667 6431 6226 1398 850 -916 C ANISOU 4022 O ALA D 29 8516 6325 5721 1282 580 -770 O ANISOU 4023 CB ALA D 29 9570 6720 7404 1466 986 -1470 C ANISOU 4029 N LEU D 30 8177 6185 5781 1476 1193 -974 N ANISOU 4030 CA LEU D 30 8357 6701 5453 1393 1273 -878 C ANISOU 4031 C LEU D 30 8301 6805 5578 1319 1128 -395 C ANISOU 4032 O LEU D 30 9074 7676 5902 1215 1030 -204 O ANISOU 4033 CB LEU D 30 8780 7402 5892 1474 1718 -1119 C ANISOU 4034 CG LEU D 30 11376 10395 7788 1375 1865 -1166 C ANISOU 4035 CD1 LEU D 30 11638 10613 7374 1295 1730 -1517 C ANISOU 4036 CD2 LEU D 30 11024 10415 7610 1451 2343 -1376 C ANISOU 4048 N CYS D 31 8359 6893 6309 1366 1099 -192 N ANISOU 4049 CA CYS D 31 7884 6675 6128 1273 1074 182 C ANISOU 4050 C CYS D 31 7619 6299 6083 1156 707 397 C ANISOU 4051 O CYS D 31 7280 6103 5864 1018 668 654 O ANISOU 4052 CB CYS D 31 7316 6435 6241 1392 1342 237 C ANISOU 4053 SG CYS D 31 8296 7691 7088 1511 1851 -28 S ANISOU 4058 N ALA D 32 6962 5424 5526 1186 467 285 N ANISOU 4059 CA ALA D 32 7061 5564 5946 1074 160 448 C ANISOU 4060 C ALA D 32 6636 5052 5248 903 -31 562 C ANISOU 4061 O ALA D 32 6928 5510 5901 765 -123 737 O ANISOU 4062 CB ALA D 32 7030 5325 5938 1119 -35 294 C ANISOU 4068 N SER D 33 6675 4855 4704 909 -91 462 N ANISOU 4069 CA SER D 33 6519 4570 4362 800 -277 605 C ANISOU 4070 C SER D 33 7621 5773 5535 715 -80 899 C ANISOU 4071 O SER D 33 7323 5409 5496 574 -182 1071 O ANISOU 4072 CB SER D 33 7206 5073 4423 867 -394 455 C ANISOU 4073 OG SER D 33 8140 5864 5220 818 -578 625 O ANISOU 4079 N ASP D 34 7552 5852 5218 773 213 943 N ANISOU 4080 CA ASP D 34 7715 6125 5407 658 415 1263 C ANISOU 4081 C ASP D 34 7416 6087 5820 533 531 1374 C ANISOU 4082 O ASP D 34 7680 6322 6313 349 552 1614 O ANISOU 4083 CB ASP D 34 7909 6512 5088 733 702 1258 C ANISOU 4084 CG ASP D 34 10091 8539 6541 792 551 1276 C ANISOU 4085 OD1 ASP D 34 11594 9869 7904 728 442 1604 O ANISOU 4086 OD2 ASP D 34 10699 9187 6767 902 510 962 O ANISOU 4091 N VAL D 35 6840 5771 5647 624 591 1209 N ANISOU 4092 CA VAL D 35 6934 6251 6448 521 662 1311 C ANISOU 4093 C VAL D 35 7124 6379 6972 342 356 1333 C ANISOU 4094 O VAL D 35 6209 5656 6468 123 402 1467 O ANISOU 4095 CB VAL D 35 6478 6104 6363 722 770 1166 C ANISOU 4096 CG1 VAL D 35 6339 6457 6998 662 717 1257 C ANISOU 4097 CG2 VAL D 35 6598 6411 6345 861 1162 1106 C ANISOU 4107 N SER D 36 6455 5487 6160 403 64 1164 N ANISOU 4108 CA SER D 36 6077 5071 6036 226 -221 1115 C ANISOU 4109 C SER D 36 5779 4465 5659 50 -218 1243 C ANISOU 4110 O SER D 36 6911 5722 7261 -178 -260 1251 O ANISOU 4111 CB SER D 36 5779 4568 5471 327 -490 911 C ANISOU 4112 OG SER D 36 5644 4695 5526 467 -450 865 O ANISOU 4118 N LYS D 37 6192 4507 5521 144 -149 1357 N ANISOU 4119 CA LYS D 37 6610 4598 5888 14 -105 1586 C ANISOU 4120 C LYS D 37 7975 6180 7744 -223 143 1773 C ANISOU 4121 O LYS D 37 6906 4922 7042 -444 120 1836 O ANISOU 4122 CB LYS D 37 7365 5127 5953 176 -8 1768 C ANISOU 4123 CG LYS D 37 7692 5141 6184 78 98 2139 C ANISOU 4124 CD LYS D 37 10082 7481 7830 245 193 2370 C ANISOU 4125 CE LYS D 37 10881 8720 8369 264 526 2409 C ANISOU 4126 NZ LYS D 37 12356 10296 9042 412 603 2548 N ANISOU 4140 N CYS D 38 7211 5812 7019 -190 408 1842 N ANISOU 4141 CA CYS D 38 7533 6424 7789 -424 683 2025 C ANISOU 4142 C CYS D 38 7267 6542 8268 -629 573 1852 C ANISOU 4143 O CYS D 38 6775 6096 8218 -928 677 1933 O ANISOU 4144 CB CYS D 38 7757 7062 7882 -304 997 2085 C ANISOU 4145 SG CYS D 38 8666 7657 7862 -158 1172 2308 S ANISOU 4150 N LEU D 39 6197 5790 7349 -488 376 1622 N ANISOU 4151 CA LEU D 39 6482 6570 8286 -676 229 1462 C ANISOU 4152 C LEU D 39 6637 6423 8618 -932 42 1332 C ANISOU 4153 O LEU D 39 5702 5828 8263 -1239 76 1252 O ANISOU 4154 CB LEU D 39 5950 6371 7793 -458 21 1310 C ANISOU 4155 CG LEU D 39 5323 6128 7247 -214 219 1396 C ANISOU 4156 CD1 LEU D 39 6449 7442 8419 18 -1 1300 C ANISOU 4157 CD2 LEU D 39 5631 7082 8152 -364 429 1490 C ANISOU 4169 N ILE D 40 6059 5270 7612 -817 -157 1257 N ANISOU 4170 CA ILE D 40 6671 5709 8543 -1050 -335 1045 C ANISOU 4171 C ILE D 40 7340 5933 9408 -1278 -124 1221 C ANISOU 4172 O ILE D 40 7591 6108 10153 -1565 -158 1032 O ANISOU 4173 CB ILE D 40 5714 4347 7239 -899 -616 858 C ANISOU 4174 CG1 ILE D 40 7843 5832 8791 -682 -560 1091 C ANISOU 4175 CG2 ILE D 40 6430 5456 7812 -740 -826 682 C ANISOU 4176 CD1 ILE D 40 8040 5708 8783 -568 -830 885 C ANISOU 4188 N GLN D 41 6774 5088 8478 -1177 122 1582 N ANISOU 4189 CA GLN D 41 8308 6279 10245 -1428 379 1840 C ANISOU 4190 C GLN D 41 8370 6940 10905 -1734 601 1816 C ANISOU 4191 O GLN D 41 7930 6281 10628 -1956 878 2076 O ANISOU 4192 CB GLN D 41 7951 5510 9283 -1259 583 2288 C ANISOU 4193 CG GLN D 41 8431 5473 9161 -954 367 2351 C ANISOU 4194 CD GLN D 41 8756 5488 8856 -803 546 2831 C ANISOU 4195 OE1 GLN D 41 9362 5861 9577 -985 796 3200 O ANISOU 4196 NE2 GLN D 41 8850 5636 8287 -492 421 2816 N ANISOU 4205 N GLU D 42 7578 6921 10452 -1755 496 1554 N ANISOU 4206 CA GLU D 42 8261 8339 11797 -2054 671 1494 C ANISOU 4207 C GLU D 42 7786 8079 11209 -2012 1021 1815 C ANISOU 4208 O GLU D 42 8522 9210 12441 -2318 1270 1872 O ANISOU 4209 CB GLU D 42 9341 9277 13490 -2516 736 1337 C ANISOU 4210 CG GLU D 42 10585 10353 14937 -2618 433 933 C ANISOU 4211 CD GLU D 42 13284 12685 18250 -3081 571 760 C ANISOU 4212 OE1 GLU D 42 15181 14799 20606 -3420 862 853 O ANISOU 4213 OE2 GLU D 42 13195 12077 18226 -3114 411 509 O ANISOU 4220 N LEU D 43 8362 8437 11142 -1663 1069 1999 N ANISOU 4221 CA LEU D 43 8612 9037 11293 -1606 1409 2223 C ANISOU 4222 C LEU D 43 8857 9914 11593 -1299 1350 2062 C ANISOU 4223 O LEU D 43 8858 9897 11507 -1094 1049 1869 O ANISOU 4224 CB LEU D 43 8982 8800 10907 -1456 1563 2535 C ANISOU 4225 CG LEU D 43 9444 8462 11194 -1624 1550 2772 C ANISOU 4226 CD1 LEU D 43 8890 7394 9807 -1390 1596 3096 C ANISOU 4227 CD2 LEU D 43 9784 8912 12071 -2047 1862 2957 C ANISOU 4239 N CYS D 44 8345 9931 11220 -1253 1660 2161 N ANISOU 4240 CA CYS D 44 8128 10264 11116 -916 1678 2043 C ANISOU 4241 C CYS D 44 8717 11536 12403 -929 1451 1871 C ANISOU 4242 O CYS D 44 7346 10430 11102 -602 1330 1791 O ANISOU 4243 CB CYS D 44 8464 10112 10789 -535 1541 1966 C ANISOU 4244 SG CYS D 44 9515 10503 10906 -463 1737 2137 S ANISOU 4249 N GLN D 45 8584 11709 12799 -1311 1392 1817 N ANISOU 4250 CA GLN D 45 7950 11865 12807 -1372 1153 1648 C ANISOU 4251 C GLN D 45 8393 13286 14012 -1604 1372 1657 C ANISOU 4252 O GLN D 45 8859 14426 15065 -1866 1211 1501 O ANISOU 4253 CB GLN D 45 7739 11368 12624 -1643 851 1457 C ANISOU 4254 CG GLN D 45 8286 11083 12493 -1409 612 1418 C ANISOU 4255 CD GLN D 45 8766 11563 13112 -1601 276 1160 C ANISOU 4256 OE1 GLN D 45 8222 11808 13150 -1832 158 990 O ANISOU 4257 NE2 GLN D 45 9050 11044 12870 -1513 120 1103 N ANISOU 4266 N CYS D 46 8290 13363 13921 -1529 1743 1808 N ANISOU 4267 CA CYS D 46 8897 15028 15281 -1669 1974 1812 C ANISOU 4268 C CYS D 46 9835 16463 16340 -1173 2083 1860 C ANISOU 4269 O CYS D 46 9447 15580 15494 -769 1966 1866 O ANISOU 4270 CB CYS D 46 9218 15226 15629 -2070 2377 1935 C ANISOU 4271 SG CYS D 46 11535 16854 17122 -1862 2776 2186 S ANISOU 4276 N ARG D 47 11445 19054 18618 -1208 2337 1874 N ANISOU 4277 CA ARG D 47 10911 19045 18346 -726 2485 1896 C ANISOU 4278 C ARG D 47 11697 20560 19569 -834 2942 1916 C ANISOU 4279 O ARG D 47 12140 21564 20471 -1296 3054 1908 O ANISOU 4280 CB ARG D 47 11190 20130 19260 -473 2146 1882 C ANISOU 4281 CG ARG D 47 12699 22852 21635 -838 2086 1830 C ANISOU 4282 CD ARG D 47 14834 26054 24465 -482 1822 1870 C ANISOU 4283 NE ARG D 47 13138 24203 22573 -419 1338 1868 N ANISOU 4284 CZ ARG D 47 11504 23102 21168 -214 1008 1846 C ANISOU 4285 NH1 ARG D 47 10906 23257 21090 -31 1078 1832 N ANISOU 4286 NH2 ARG D 47 7274 18647 16622 -202 608 1850 N ANISOU 4300 N PRO D 48 12612 21508 20378 -446 3238 1906 N ANISOU 4301 CA PRO D 48 10227 20014 18520 -512 3682 1888 C ANISOU 4302 C PRO D 48 8307 19424 17692 -396 3613 1852 C ANISOU 4303 O PRO D 48 9310 21162 19134 -609 3908 1780 O ANISOU 4304 CB PRO D 48 10135 19584 18016 -73 3980 1809 C ANISOU 4305 CG PRO D 48 11137 19829 18638 344 3627 1771 C ANISOU 4306 CD PRO D 48 11294 19382 18420 5 3221 1862 C ANISOU 4314 N CYS D 53 12291 21615 19990 -2416 4716 2336 N ANISOU 4315 CA CYS D 53 11926 20178 18982 -2222 4300 2347 C ANISOU 4316 C CYS D 53 11793 18967 18187 -2589 4310 2581 C ANISOU 4317 O CYS D 53 11468 18077 17107 -2523 4518 2778 O ANISOU 4318 CB CYS D 53 12030 19941 18525 -1635 4269 2279 C ANISOU 4319 SG CYS D 53 14883 21541 20575 -1428 3794 2284 S ANISOU 4324 N SER D 54 13115 20024 19805 -2955 4077 2550 N ANISOU 4325 CA SER D 54 14491 20501 20825 -3379 4178 2795 C ANISOU 4326 C SER D 54 13113 17977 18500 -3090 3969 2944 C ANISOU 4327 O SER D 54 13296 17648 18022 -3097 4206 3253 O ANISOU 4328 CB SER D 54 13941 19981 20938 -3839 3995 2627 C ANISOU 4329 OG SER D 54 12455 18541 19558 -3576 3520 2344 O ANISOU 4335 N CYS D 55 11205 15740 16511 -2838 3521 2732 N ANISOU 4336 CA CYS D 55 11011 14509 15508 -2600 3284 2828 C ANISOU 4337 C CYS D 55 10566 13962 14341 -2150 3370 2890 C ANISOU 4338 O CYS D 55 9591 12244 12689 -1925 3158 2934 O ANISOU 4339 CB CYS D 55 9428 12724 14056 -2460 2802 2548 C ANISOU 4340 SG CYS D 55 9790 13551 14320 -1854 2557 2315 S ANISOU 4345 N CYS D 56 11256 15413 15193 -2028 3683 2853 N ANISOU 4346 CA CYS D 56 11487 15630 14832 -1603 3783 2793 C ANISOU 4347 C CYS D 56 11206 14617 13601 -1618 3869 3064 C ANISOU 4348 O CYS D 56 10824 13873 12588 -1284 3734 2967 O ANISOU 4349 CB CYS D 56 11814 16927 15558 -1532 4190 2701 C ANISOU 4350 SG CYS D 56 14660 20574 19185 -1076 4045 2328 S ANISOU 4355 N LYS D 57 11742 14956 14027 -2004 4096 3420 N ANISOU 4356 CA LYS D 57 12509 15253 13875 -1970 4227 3739 C ANISOU 4357 C LYS D 57 12581 14338 13471 -1912 3854 3900 C ANISOU 4358 O LYS D 57 12878 14296 12951 -1700 3800 4032 O ANISOU 4359 CB LYS D 57 13963 17015 15361 -2375 4695 4125 C ANISOU 4360 CG LYS D 57 14007 18179 15836 -2384 5107 3916 C ANISOU 4361 CD LYS D 57 13250 17826 15048 -2795 5611 4289 C ANISOU 4362 CE LYS D 57 11845 17578 14262 -2822 5983 4021 C ANISOU 4363 NZ LYS D 57 13696 19647 15974 -3251 6339 4194 N ANISOU 4377 N GLU D 58 11422 12781 12819 -2080 3587 3846 N ANISOU 4378 CA GLU D 58 11940 12417 12957 -1972 3230 3927 C ANISOU 4379 C GLU D 58 10488 10903 11225 -1553 2875 3559 C ANISOU 4380 O GLU D 58 10082 9929 10234 -1354 2641 3622 O ANISOU 4381 CB GLU D 58 12205 12292 13887 -2302 3090 3915 C ANISOU 4382 CG GLU D 58 15098 14887 16937 -2730 3422 4371 C ANISOU 4383 CD GLU D 58 16235 15452 18707 -3054 3293 4324 C ANISOU 4384 OE1 GLU D 58 14209 13287 16892 -2917 2919 3932 O ANISOU 4385 OE2 GLU D 58 16417 15338 19167 -3451 3580 4656 O ANISOU 4392 N CYS D 59 9938 10955 11107 -1411 2842 3199 N ANISOU 4393 CA CYS D 59 9156 10140 10050 -1014 2587 2889 C ANISOU 4394 C CYS D 59 10112 11087 10224 -768 2750 2912 C ANISOU 4395 O CYS D 59 9266 9861 8850 -524 2518 2788 O ANISOU 4396 CB CYS D 59 9085 10753 10663 -903 2574 2589 C ANISOU 4397 SG CYS D 59 9778 11393 11146 -423 2318 2244 S ANISOU 4402 N MET D 60 9464 10947 9511 -841 3160 3019 N ANISOU 4403 CA MET D 60 10779 12359 10060 -650 3341 2994 C ANISOU 4404 C MET D 60 10599 11610 9086 -684 3210 3325 C ANISOU 4405 O MET D 60 11297 12169 9136 -450 3086 3186 O ANISOU 4406 CB MET D 60 11133 13438 10513 -778 3835 3060 C ANISOU 4407 CG MET D 60 12922 15456 11460 -670 4088 3057 C ANISOU 4408 SD MET D 60 17768 21339 16565 -753 4693 2934 S ANISOU 4409 CE MET D 60 13157 16844 12542 -1227 4863 3415 C ANISOU 4419 N LEU D 61 10801 11502 9359 -974 3249 3771 N ANISOU 4420 CA LEU D 61 11572 11688 9482 -964 3089 4154 C ANISOU 4421 C LEU D 61 10876 10471 8624 -707 2623 3916 C ANISOU 4422 O LEU D 61 11627 11007 8676 -531 2469 4024 O ANISOU 4423 CB LEU D 61 11977 11689 10233 -1305 3174 4634 C ANISOU 4424 CG LEU D 61 15081 14839 12821 -1483 3493 5234 C ANISOU 4425 CD1 LEU D 61 14901 14359 11712 -1220 3279 5494 C ANISOU 4426 CD2 LEU D 61 14202 14840 11904 -1592 3944 5164 C ANISOU 4438 N CYS D 62 10194 9649 8581 -704 2390 3609 N ANISOU 4439 CA CYS D 62 10224 9214 8500 -507 1965 3395 C ANISOU 4440 C CYS D 62 10473 9657 8290 -197 1863 3025 C ANISOU 4441 O CYS D 62 10574 9441 7906 -27 1602 2977 O ANISOU 4442 CB CYS D 62 9424 8337 8498 -629 1771 3163 C ANISOU 4443 SG CYS D 62 9170 7633 8170 -416 1267 2843 S ANISOU 4448 N LEU D 63 9796 9494 7834 -119 2067 2734 N ANISOU 4449 CA LEU D 63 9562 9401 7240 152 2040 2350 C ANISOU 4450 C LEU D 63 10150 10159 6997 208 2218 2424 C ANISOU 4451 O LEU D 63 11046 11023 7428 391 2106 2134 O ANISOU 4452 CB LEU D 63 8818 9128 7049 246 2248 2044 C ANISOU 4453 CG LEU D 63 9384 9670 8378 251 2025 1924 C ANISOU 4454 CD1 LEU D 63 8956 9750 8485 401 2239 1698 C ANISOU 4455 CD2 LEU D 63 8957 8782 7769 390 1630 1736 C ANISOU 4467 N GLY D 64 10545 10789 7187 31 2500 2801 N ANISOU 4468 CA GLY D 64 12060 12483 7824 64 2594 2967 C ANISOU 4469 C GLY D 64 12120 13058 7548 215 2809 2487 C ANISOU 4470 O GLY D 64 11701 13074 7505 204 3136 2259 O ANISOU 4474 N ALA D 65 12350 13273 7101 355 2636 2297 N ANISOU 4475 CA ALA D 65 13100 14492 7514 467 2850 1763 C ANISOU 4476 C ALA D 65 12423 13672 7485 623 2858 1216 C ANISOU 4477 O ALA D 65 13016 14616 8023 712 3126 737 O ANISOU 4478 CB ALA D 65 13519 14966 7107 550 2629 1641 C ANISOU 4484 N LEU D 66 10611 11382 6300 656 2591 1279 N ANISOU 4485 CA LEU D 66 10208 10826 6501 818 2552 866 C ANISOU 4486 C LEU D 66 10665 11562 7754 815 2799 901 C ANISOU 4487 O LEU D 66 9526 10318 7222 966 2742 678 O ANISOU 4488 CB LEU D 66 9863 9921 6361 857 2102 898 C ANISOU 4489 CG LEU D 66 10601 10390 6508 925 1826 693 C ANISOU 4490 CD1 LEU D 66 10209 9511 6364 933 1397 761 C ANISOU 4491 CD2 LEU D 66 10768 10655 6560 1056 1984 135 C ANISOU 4503 N TRP D 67 10351 11656 7464 648 3080 1193 N ANISOU 4504 CA TRP D 67 9844 11511 7763 621 3302 1238 C ANISOU 4505 C TRP D 67 10327 12301 8658 869 3561 768 C ANISOU 4506 O TRP D 67 9159 11171 8275 1003 3512 699 O ANISOU 4507 CB TRP D 67 10125 12243 7931 374 3623 1584 C ANISOU 4508 CG TRP D 67 10362 13022 8955 354 3917 1542 C ANISOU 4509 CD1 TRP D 67 10653 13988 9371 400 4378 1325 C ANISOU 4510 CD2 TRP D 67 10833 13522 10253 274 3781 1697 C ANISOU 4511 NE1 TRP D 67 10310 14081 9922 375 4522 1365 N ANISOU 4512 CE2 TRP D 67 10229 13639 10269 288 4151 1596 C ANISOU 4513 CE3 TRP D 67 11092 13341 10808 188 3382 1870 C ANISOU 4514 CZ2 TRP D 67 10129 13870 11060 216 4112 1691 C ANISOU 4515 CZ3 TRP D 67 11073 13652 11638 89 3358 1937 C ANISOU 4516 CH2 TRP D 67 10019 13355 11180 104 3709 1860 C ANISOU 4527 N ASP D 68 10554 12819 8410 930 3866 450 N ANISOU 4528 CA ASP D 68 11150 13655 9450 1180 4163 -56 C ANISOU 4529 C ASP D 68 11383 13321 10071 1416 3879 -289 C ANISOU 4530 O ASP D 68 10424 12419 9924 1630 3957 -404 O ANISOU 4531 CB ASP D 68 11980 14830 9597 1173 4495 -455 C ANISOU 4532 CG ASP D 68 14258 17817 11528 945 4856 -230 C ANISOU 4533 OD1 ASP D 68 13702 17609 11570 876 5024 26 O ANISOU 4534 OD2 ASP D 68 15400 19235 11806 821 4973 -304 O ANISOU 4539 N GLU D 69 10928 12351 9054 1380 3548 -326 N ANISOU 4540 CA GLU D 69 11737 12639 10100 1566 3334 -598 C ANISOU 4541 C GLU D 69 10176 10834 9192 1612 3012 -283 C ANISOU 4542 O GLU D 69 10246 10606 9702 1806 2921 -443 O ANISOU 4543 CB GLU D 69 11230 11759 8794 1480 3080 -751 C ANISOU 4544 CG GLU D 69 13646 14505 10495 1427 3368 -1151 C ANISOU 4545 CD GLU D 69 14339 15694 10523 1216 3461 -816 C ANISOU 4546 OE1 GLU D 69 15916 17368 12313 1113 3420 -312 O ANISOU 4547 OE2 GLU D 69 15255 16939 10704 1137 3588 -1050 O ANISOU 4554 N CYS D 70 9414 10220 8519 1422 2856 156 N ANISOU 4555 CA CYS D 70 8565 9192 8144 1389 2495 426 C ANISOU 4556 C CYS D 70 8886 10011 9161 1308 2571 708 C ANISOU 4557 O CYS D 70 7856 8968 8587 1280 2288 876 O ANISOU 4558 CB CYS D 70 8854 9086 7882 1190 2136 620 C ANISOU 4559 SG CYS D 70 8332 8090 6582 1261 1984 290 S ANISOU 4564 N CYS D 71 8788 10421 9153 1240 2939 749 N ANISOU 4565 CA CYS D 71 9116 11294 10172 1120 3020 992 C ANISOU 4566 C CYS D 71 8829 11266 10759 1362 2923 951 C ANISOU 4567 O CYS D 71 7630 10458 10138 1245 2794 1166 O ANISOU 4568 CB CYS D 71 9136 11891 10186 1039 3490 982 C ANISOU 4569 SG CYS D 71 9330 12411 10616 1400 3912 523 S ANISOU 4574 N ASP D 72 8512 10770 10581 1693 2990 687 N ANISOU 4575 CA ASP D 72 8217 10699 11123 1964 2888 734 C ANISOU 4576 C ASP D 72 9383 11608 12356 1893 2408 942 C ANISOU 4577 O ASP D 72 8190 10804 11866 2031 2265 1108 O ANISOU 4578 CB ASP D 72 9203 11417 12262 2336 3095 421 C ANISOU 4579 CG ASP D 72 11008 13612 15065 2678 3127 520 C ANISOU 4580 OD1 ASP D 72 9525 12892 14184 2712 3323 619 O ANISOU 4581 OD2 ASP D 72 12466 14641 16721 2913 2959 524 O ANISOU 4586 N CYS D 73 8440 10084 10714 1703 2152 931 N ANISOU 4587 CA CYS D 73 6769 8254 9124 1617 1720 1086 C ANISOU 4588 C CYS D 73 7871 9881 10621 1353 1570 1320 C ANISOU 4589 O CYS D 73 7586 9690 10557 1282 1236 1424 O ANISOU 4590 CB CYS D 73 7497 8328 9081 1459 1481 1004 C ANISOU 4591 SG CYS D 73 7891 8144 8806 1609 1641 673 S ANISOU 4596 N VAL D 74 7017 9354 9798 1152 1809 1381 N ANISOU 4597 CA VAL D 74 7470 10326 10702 857 1722 1552 C ANISOU 4598 C VAL D 74 8149 11836 12066 893 2029 1604 C ANISOU 4599 O VAL D 74 8373 12550 12659 592 2045 1711 O ANISOU 4600 CB VAL D 74 8214 10682 10940 490 1703 1626 C ANISOU 4601 CG1 VAL D 74 7171 8982 9414 438 1342 1580 C ANISOU 4602 CG2 VAL D 74 7779 10053 9967 491 2070 1621 C ANISOU 4612 N GLY D 75 8072 11921 12171 1232 2307 1493 N ANISOU 4613 CA GLY D 75 8711 13421 13546 1334 2610 1511 C ANISOU 4614 C GLY D 75 9058 14112 13815 1004 2933 1550 C ANISOU 4615 O GLY D 75 9689 15556 15116 866 3040 1636 O ANISOU 4619 N MET D 76 9803 14308 13761 862 3093 1508 N ANISOU 4620 CA MET D 76 9864 14609 13638 521 3400 1622 C ANISOU 4621 C MET D 76 9996 14910 13476 664 3850 1460 C ANISOU 4622 O MET D 76 11178 16310 14406 385 4143 1578 O ANISOU 4623 CB MET D 76 10278 14321 13339 189 3222 1799 C ANISOU 4624 CG MET D 76 10487 14320 13782 7 2804 1890 C ANISOU 4625 SD MET D 76 11374 15788 15305 -482 2912 2066 S ANISOU 4626 CE MET D 76 12027 16294 16274 -592 2386 2008 C ANISOU 4636 N CYS D 77 8749 13578 12264 1071 3936 1182 N ANISOU 4637 CA CYS D 77 10343 15284 13465 1173 4367 937 C ANISOU 4638 C CYS D 77 9874 15728 13448 1054 4817 948 C ANISOU 4639 O CYS D 77 11347 17394 14459 990 5199 812 O ANISOU 4640 CB CYS D 77 8647 13366 11926 1629 4423 570 C ANISOU 4641 SG CYS D 77 10524 14194 13235 1749 3962 501 S ANISOU 4646 N ASN D 78 10610 17116 15068 1008 4788 1090 N ANISOU 4647 CA ASN D 78 10598 18083 15617 917 5223 1064 C ANISOU 4648 C ASN D 78 10103 17917 15264 1296 5642 669 C ANISOU 4649 O ASN D 78 10286 18314 16179 1728 5633 485 O ANISOU 4650 CB ASN D 78 11901 19466 16387 396 5432 1312 C ANISOU 4651 CG ASN D 78 10534 18294 15454 -10 5231 1630 C ANISOU 4652 OD1 ASN D 78 10778 17870 15422 -155 4837 1795 O ANISOU 4653 ND2 ASN D 78 12244 20954 17858 -221 5528 1676 N TER 4660 ASN D 78 HETATM 4661 CA CA A 601 -16.364 22.412 -36.679 1.00 78.48 CA HETATM 4665 O HOH A 701 -24.606 5.879 -43.185 1.00 63.08 O HETATM 4666 O HOH A 702 -15.774 22.575 -39.349 1.00 81.96 O HETATM 4667 O HOH A 703 -18.954 26.708 -34.750 1.00 72.53 O HETATM 4668 O HOH A 704 -9.446 15.975 7.074 1.00 68.31 O HETATM 4669 O HOH A 705 -22.819 5.812 -16.745 1.00 67.77 O HETATM 4670 O HOH A 706 -23.390 27.351 -16.007 1.00 57.95 O HETATM 4671 O HOH A 707 -2.963 19.522 -0.276 1.00 52.34 O HETATM 4672 O HOH A 708 -28.214 25.912 -18.462 1.00 59.50 O HETATM 4673 O HOH A 709 11.603 24.843 3.494 1.00 59.80 O HETATM 4674 O HOH A 710 -8.057 26.677 -11.613 1.00 63.29 O HETATM 4675 O HOH A 711 0.867 21.849 9.979 1.00 57.68 O HETATM 4676 O HOH A 712 -14.999 13.941 -3.669 1.00 50.03 O HETATM 4677 O HOH A 713 -1.770 13.004 -3.760 1.00 47.91 O HETATM 4678 O HOH A 714 -25.630 21.599 -35.011 1.00 73.02 O HETATM 4679 O HOH A 715 -25.509 13.500 -16.184 1.00 51.22 O HETATM 4680 O HOH A 716 -4.671 10.542 -4.850 1.00 43.20 O HETATM 4681 O HOH A 717 -4.202 22.608 -5.225 1.00 50.86 O HETATM 4682 O HOH A 718 0.286 14.059 -6.453 1.00 42.20 O HETATM 4683 O HOH A 719 -1.429 18.130 -6.945 1.00 53.17 O HETATM 4684 O HOH A 720 -27.031 9.481 -20.902 1.00 61.93 O HETATM 4685 O HOH A 721 13.032 21.515 0.197 1.00 64.43 O HETATM 4686 O HOH A 722 -11.287 23.348 -12.924 1.00 47.39 O HETATM 4687 O HOH A 723 -12.373 13.177 -1.829 1.00 61.11 O HETATM 4688 O HOH A 724 -22.340 23.798 -14.894 1.00 49.30 O HETATM 4689 O HOH A 725 -28.552 14.996 -23.393 1.00 64.17 O HETATM 4690 O HOH A 726 -1.675 21.177 3.365 1.00 47.04 O HETATM 4691 O HOH A 727 7.027 18.692 2.975 1.00 51.42 O HETATM 4692 O HOH A 728 -19.646 26.131 -5.661 1.00 58.81 O HETATM 4693 O HOH A 729 7.657 26.533 4.675 1.00 63.56 O HETATM 4694 O HOH A 730 -11.809 12.781 -12.948 1.00 45.81 O HETATM 4695 O HOH A 731 -15.868 28.992 -12.040 1.00 58.03 O HETATM 4696 O HOH A 732 -6.705 22.363 -6.284 1.00 41.86 O HETATM 4697 O HOH A 733 -26.849 27.598 -15.894 1.00 62.71 O HETATM 4698 O HOH A 734 -20.305 8.677 -16.592 1.00 49.87 O HETATM 4699 O HOH A 735 -17.451 8.612 -12.179 1.00 49.18 O HETATM 4700 O HOH A 736 -9.139 22.749 3.801 1.00 64.55 O HETATM 4701 O HOH A 737 -8.706 22.391 -10.096 1.00 48.13 O HETATM 4702 O HOH A 738 -18.248 7.590 -23.519 1.00 56.01 O HETATM 4703 O HOH A 739 3.047 24.733 -2.206 1.00 58.44 O HETATM 4704 O HOH A 740 -28.378 19.910 -21.866 1.00 63.59 O HETATM 4705 O HOH A 741 -14.421 9.299 -20.313 1.00 56.05 O HETATM 4706 O HOH A 742 1.532 25.051 6.640 1.00 55.40 O HETATM 4707 O HOH A 743 -25.920 18.593 -16.437 1.00 56.44 O HETATM 4708 O HOH A 744 -1.930 15.487 -7.260 1.00 49.59 O HETATM 4709 O HOH A 745 -26.676 19.831 -9.943 1.00 54.10 O HETATM 4710 O HOH A 746 -8.027 23.974 -8.033 1.00 45.42 O HETATM 4711 O HOH A 747 -4.504 24.121 -3.140 1.00 53.84 O HETATM 4712 O HOH A 748 -23.658 30.019 -24.103 1.00 69.39 O HETATM 4713 O HOH A 749 -11.497 28.609 -5.568 1.00 64.39 O HETATM 4714 O HOH A 750 -17.882 13.063 -36.575 1.00 72.31 O HETATM 4715 O HOH A 751 -18.121 17.095 -4.155 1.00 58.13 O HETATM 4716 O HOH A 752 -6.534 16.011 5.833 1.00 48.47 O HETATM 4717 O HOH A 753 -28.747 13.190 -21.612 1.00 55.92 O HETATM 4718 O HOH A 754 -27.168 20.065 -18.651 1.00 58.53 O HETATM 4719 O HOH A 755 -18.038 25.758 -24.540 1.00 64.87 O HETATM 4720 O HOH A 756 -8.990 21.529 1.355 1.00 52.19 O HETATM 4721 O HOH A 757 -25.584 17.434 -11.252 1.00 64.40 O HETATM 4722 O HOH A 758 -17.652 24.484 -36.863 1.00 73.98 O HETATM 4723 O HOH A 759 -11.206 19.398 0.831 1.00 57.28 O HETATM 4724 O HOH A 760 0.641 25.231 -0.834 1.00 59.70 O HETATM 4725 O HOH A 761 -28.295 5.531 -26.399 1.00 72.90 O HETATM 4726 O HOH A 762 -20.697 29.053 -16.845 1.00 61.84 O HETATM 4727 O HOH A 763 -11.516 17.280 -0.609 1.00 56.19 O HETATM 4728 O HOH A 764 6.723 23.186 -3.715 1.00 67.78 O HETATM 4729 O HOH A 765 -15.149 24.303 -37.103 1.00 85.09 O HETATM 4730 O HOH A 766 -1.813 22.233 -7.513 1.00 65.85 O HETATM 4731 O HOH A 767 -2.371 25.313 -1.536 1.00 66.80 O CONECT 62 1092 CONECT 274 4661 CONECT 320 4661 CONECT 321 4661 CONECT 532 1616 CONECT 597 1633 CONECT 1082 2696 CONECT 1092 62 CONECT 1616 532 CONECT 1633 597 CONECT 1690 2706 CONECT 1902 4662 CONECT 1948 4662 CONECT 1949 4662 CONECT 2160 3230 CONECT 2211 3247 CONECT 2696 1082 CONECT 2706 1690 CONECT 3230 2160 CONECT 3247 2211 CONECT 3290 3910 CONECT 3365 3878 CONECT 3457 3762 CONECT 3556 3716 CONECT 3583 3659 CONECT 3638 3669 CONECT 3659 3583 CONECT 3669 3638 CONECT 3716 3556 CONECT 3762 3457 CONECT 3796 4663 CONECT 3866 4663 CONECT 3878 3365 CONECT 3888 3960 CONECT 3910 3290 CONECT 3960 3888 CONECT 3978 4591 CONECT 4053 4559 CONECT 4145 4443 CONECT 4244 4397 CONECT 4271 4340 CONECT 4319 4350 CONECT 4340 4271 CONECT 4350 4319 CONECT 4397 4244 CONECT 4443 4145 CONECT 4477 4664 CONECT 4546 4664 CONECT 4547 4664 CONECT 4559 4053 CONECT 4569 4641 CONECT 4591 3978 CONECT 4641 4569 CONECT 4661 274 320 321 4666 CONECT 4661 4722 4729 4794 4796 CONECT 4662 1902 1948 1949 4771 CONECT 4662 4778 4785 4808 4809 CONECT 4663 3796 3866 CONECT 4664 4477 4546 4547 4807 CONECT 4664 4813 CONECT 4666 4661 CONECT 4722 4661 CONECT 4729 4661 CONECT 4771 4662 CONECT 4778 4662 CONECT 4785 4662 CONECT 4794 4661 CONECT 4796 4661 CONECT 4807 4664 CONECT 4808 4662 CONECT 4809 4662 CONECT 4813 4664 MASTER 444 0 4 13 14 0 0 6 2527 4 72 32 END