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casp_data / casp15 /experiment_structures /T1104.pdb
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HEADER ANTIFUNGAL PROTEIN 30-JUL-21 7ROA
TITLE CRYSTAL STRUCTURE OF ENTV136 FROM ENTEROCOCCUS FAECALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTV;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS OG1RF;
SOURCE 3 ORGANISM_COMMON: STREPTOCOCCUS FAECALIS;
SOURCE 4 ORGANISM_TAXID: 474186;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: -GOLD;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALL ALPHA PROTEIN, ANTIFUNGAL, STRUCTURAL GENOMICS, CSGID, CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, NIAID, NATIONAL
KEYWDS 3 INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES, ANTIFUNGAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,E.EVDOKIMOVA,Y.KIM,D.GARSIN,A.SAVCHENKO,A.JOACHIMIAK,
AUTHOR 2 K.J.F.SATCHELL,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID),CENTER FOR STRUCTURAL BIOLOGY OF INFECTIOUS DISEASES (CSBID)
REVDAT 4 20-NOV-24 7ROA 1 REMARK
REVDAT 3 25-JAN-23 7ROA 1 AUTHOR
REVDAT 2 23-NOV-22 7ROA 1 JRNL
REVDAT 1 12-OCT-22 7ROA 0
JRNL AUTH M.R.CRUZ,S.CRISTY,S.GUHA,G.B.DE CESARE,E.EVDOKIMOVA,
JRNL AUTH 2 H.SANCHEZ,D.BOREK,P.MIRAMON,J.YANO,P.L.FIDEL JR.,
JRNL AUTH 3 A.SAVCHENKO,D.R.ANDES,P.J.STOGIOS,M.C.LORENZ,D.A.GARSIN
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF ENTV REVEALS A 12
JRNL TITL 2 AMINO ACID FRAGMENT PROTECTIVE AGAINST FUNGAL INFECTIONS.
JRNL REF NAT COMMUN V. 13 6047 2022
JRNL REFN ESSN 2041-1723
JRNL PMID 36229448
JRNL DOI 10.1038/S41467-022-33613-1
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.6
REMARK 3 NUMBER OF REFLECTIONS : 8823
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.560
REMARK 3 FREE R VALUE TEST SET COUNT : 685
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 31.1900 - 3.1000 0.94 3159 163 0.1582 0.1949
REMARK 3 2 3.1000 - 2.4600 0.96 3191 149 0.1790 0.2404
REMARK 3 3 2.4600 - 2.1500 0.91 3083 120 0.1906 0.2236
REMARK 3 4 2.1500 - 1.9600 0.84 2735 176 0.1876 0.2323
REMARK 3 5 1.9600 - 1.8200 0.63 2161 77 0.2049 0.2688
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.135
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.316
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.95
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 : 0.006 914
REMARK 3 ANGLE : 0.858 1232
REMARK 3 CHIRALITY : 0.048 144
REMARK 3 PLANARITY : 0.006 158
REMARK 3 DIHEDRAL : 21.195 333
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 58 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4585 18.6738 -14.8318
REMARK 3 T TENSOR
REMARK 3 T11: 0.1451 T22: 0.1188
REMARK 3 T33: 0.1363 T12: 0.0338
REMARK 3 T13: -0.0147 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 6.6491 L22: 4.5041
REMARK 3 L33: 4.2234 L12: 3.6949
REMARK 3 L13: 3.2834 L23: 4.2279
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: 0.0382 S13: 0.5220
REMARK 3 S21: -0.4869 S22: 0.1705 S23: -0.2691
REMARK 3 S31: -0.5185 S32: 0.1181 S33: 0.0387
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9644 5.1934 -18.8338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0684 T22: 0.1352
REMARK 3 T33: 0.1298 T12: 0.0073
REMARK 3 T13: 0.0109 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 4.1807 L22: 3.5687
REMARK 3 L33: 2.6358 L12: -0.5413
REMARK 3 L13: -0.0893 L23: -0.9505
REMARK 3 S TENSOR
REMARK 3 S11: -0.1289 S12: 0.2218 S13: -0.1219
REMARK 3 S21: -0.4477 S22: 0.0516 S23: -0.4491
REMARK 3 S31: 0.2316 S32: -0.1696 S33: -0.0037
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2928 1.4725 -5.5340
REMARK 3 T TENSOR
REMARK 3 T11: 0.2015 T22: 0.0421
REMARK 3 T33: 0.1282 T12: 0.0023
REMARK 3 T13: 0.0382 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 6.2865 L22: 4.8886
REMARK 3 L33: 4.0310 L12: -1.4045
REMARK 3 L13: -3.1750 L23: -1.6434
REMARK 3 S TENSOR
REMARK 3 S11: -0.1435 S12: 0.1133 S13: -0.3425
REMARK 3 S21: 0.3884 S22: 0.0266 S23: 0.1766
REMARK 3 S31: 0.3580 S32: -0.1615 S33: 0.1292
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1022 15.2186 -7.3665
REMARK 3 T TENSOR
REMARK 3 T11: 0.1174 T22: 0.1132
REMARK 3 T33: 0.0928 T12: 0.0484
REMARK 3 T13: 0.0233 T23: -0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 3.3239 L22: 5.2206
REMARK 3 L33: 5.2931 L12: 0.6141
REMARK 3 L13: 0.1648 L23: -0.4233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.2753 S13: 0.1000
REMARK 3 S21: 0.4415 S22: -0.0577 S23: 0.3353
REMARK 3 S31: 0.0454 S32: -0.3284 S33: 0.0226
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 169 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8501 7.4741 -10.3876
REMARK 3 T TENSOR
REMARK 3 T11: 0.0507 T22: 0.0362
REMARK 3 T33: 0.0718 T12: 0.0257
REMARK 3 T13: -0.0222 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 5.5777 L22: 4.2515
REMARK 3 L33: 6.0540 L12: -0.6013
REMARK 3 L13: -1.0043 L23: -0.6409
REMARK 3 S TENSOR
REMARK 3 S11: -0.0731 S12: -0.1765 S13: -0.1431
REMARK 3 S21: 0.4076 S22: -0.0040 S23: -0.2834
REMARK 3 S31: 0.2938 S32: -0.0088 S33: 0.0096
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 7ROA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1000258434.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8895
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXDE, MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 26.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8 AND 28% (W/V) PEG4K,
REMARK 280 CRYOPROTECTANT PARATONE-N OIL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 31.19700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.03200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 31.19700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.03200
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 249 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 257 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 267 LIES ON A SPECIAL POSITION.
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 SER A 56
REMARK 465 ASP A 57
REMARK 465 ALA A 111
REMARK 465 SER A 112
REMARK 465 THR A 113
REMARK 465 VAL A 114
REMARK 465 VAL A 115
REMARK 465 GLN A 116
REMARK 465 ALA A 117
REMARK 465 ARG A 118
REMARK 465 PHE A 119
REMARK 465 ASN A 120
REMARK 465 TRP A 121
REMARK 465 ASN A 122
REMARK 465 ALA A 123
REMARK 465 LEU A 124
REMARK 465 GLY A 125
REMARK 465 LEU A 190
REMARK 465 SER A 191
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP96499 RELATED DB: TARGETTRACK
DBREF1 7ROA A 56 191 UNP A0A1G1SCE7_ENTFL
DBREF2 7ROA A A0A1G1SCE7 35 170
SEQRES 1 A 136 SER ASP GLN LEU GLU ASP SER GLU VAL GLU ALA VAL ALA
SEQRES 2 A 136 LYS GLY LEU GLU GLU MSE TYR ALA ASN GLY VAL THR GLU
SEQRES 3 A 136 ASP ASN PHE LYS ASN TYR VAL LYS ASN ASN PHE ALA GLN
SEQRES 4 A 136 GLN GLU ILE SER SER VAL GLU GLU GLU LEU ASN VAL ASN
SEQRES 5 A 136 ILE SER ASP ALA SER THR VAL VAL GLN ALA ARG PHE ASN
SEQRES 6 A 136 TRP ASN ALA LEU GLY SER CYS VAL ALA ASN LYS ILE LYS
SEQRES 7 A 136 ASP GLU PHE PHE ALA MSE ILE SER ILE SER ALA ILE VAL
SEQRES 8 A 136 LYS ALA ALA GLN LYS LYS ALA TRP LYS GLU LEU ALA VAL
SEQRES 9 A 136 THR VAL LEU ARG PHE ALA LYS ALA ASN GLY LEU LYS THR
SEQRES 10 A 136 ASN ALA ILE ILE VAL ALA GLY GLN LEU ALA LEU TRP ALA
SEQRES 11 A 136 VAL GLN CYS GLY LEU SER
MODRES 7ROA MSE A 74 MET MODIFIED RESIDUE
MODRES 7ROA MSE A 139 MET MODIFIED RESIDUE
HET MSE A 74 8
HET MSE A 139 13
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 HOH *84(H2 O)
HELIX 1 AA1 GLU A 60 TYR A 75 1 16
HELIX 2 AA2 THR A 80 PHE A 92 1 13
HELIX 3 AA3 ALA A 93 ASN A 105 1 13
HELIX 4 AA4 ASN A 130 ILE A 140 1 11
HELIX 5 AA5 SER A 141 LYS A 151 1 11
HELIX 6 AA6 ALA A 153 ASN A 168 1 16
HELIX 7 AA7 ASN A 173 GLY A 189 1 17
LINK C GLU A 73 N MSE A 74 1555 1555 1.34
LINK C MSE A 74 N TYR A 75 1555 1555 1.33
LINK C ALA A 138 N MSE A 139 1555 1555 1.34
LINK C MSE A 139 N ILE A 140 1555 1555 1.33
CRYST1 62.394 32.064 49.992 90.00 90.86 90.00 C 1 2 1 4
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 0.016027 0.000000 0.000241 0.00000
SCALE2 0.000000 0.031188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020005 0.00000
ATOM 1 N GLN A 58 26.160 25.517 -1.781 1.00 46.11 N
ANISOU 1 N GLN A 58 4491 6576 6451 -162 -19 -1947 N
ATOM 2 CA GLN A 58 26.287 24.061 -1.793 1.00 51.41 C
ANISOU 2 CA GLN A 58 5306 7355 6873 -244 -150 -1641 C
ATOM 3 C GLN A 58 26.685 23.517 -3.164 1.00 51.14 C
ANISOU 3 C GLN A 58 5361 7087 6983 -169 -199 -1473 C
ATOM 4 O GLN A 58 27.867 23.313 -3.438 1.00 57.66 O
ANISOU 4 O GLN A 58 6184 7799 7927 -157 -224 -1444 O
ATOM 5 CB GLN A 58 24.978 23.399 -1.353 1.00 70.32 C
ANISOU 5 CB GLN A 58 7748 9984 8986 -334 -165 -1555 C
ATOM 6 CG GLN A 58 25.130 21.935 -0.957 1.00 53.71 C
ANISOU 6 CG GLN A 58 5814 7963 6630 -479 -350 -1235 C
ATOM 7 CD GLN A 58 23.812 21.287 -0.564 1.00 72.26 C
ANISOU 7 CD GLN A 58 8224 10512 8721 -606 -330 -1152 C
ATOM 8 OE1 GLN A 58 22.741 21.707 -1.011 1.00 66.73 O
ANISOU 8 OE1 GLN A 58 7440 9865 8048 -539 -190 -1292 O
ATOM 9 NE2 GLN A 58 23.885 20.253 0.272 1.00 67.82 N
ANISOU 9 NE2 GLN A 58 7799 10034 7936 -788 -488 -946 N
ATOM 10 N LEU A 59 25.688 23.276 -4.016 1.00 31.06 N
ANISOU 10 N LEU A 59 2873 4494 4436 -121 -202 -1396 N
ATOM 11 CA LEU A 59 25.900 22.661 -5.320 1.00 24.76 C
ANISOU 11 CA LEU A 59 2145 3527 3737 -71 -237 -1235 C
ATOM 12 C LEU A 59 26.283 23.702 -6.366 1.00 28.58 C
ANISOU 12 C LEU A 59 2634 3709 4518 -32 -109 -1286 C
ATOM 13 O LEU A 59 25.680 24.778 -6.434 1.00 34.71 O
ANISOU 13 O LEU A 59 3403 4347 5440 9 -75 -1394 O
ATOM 14 CB LEU A 59 24.631 21.930 -5.757 1.00 26.43 C
ANISOU 14 CB LEU A 59 2440 3823 3780 -42 -297 -1095 C
ATOM 15 CG LEU A 59 24.227 20.796 -4.815 1.00 38.11 C
ANISOU 15 CG LEU A 59 4018 5526 4935 -152 -392 -925 C
ATOM 16 CD1 LEU A 59 22.776 20.401 -5.027 1.00 27.57 C
ANISOU 16 CD1 LEU A 59 2740 4297 3438 -157 -376 -867 C
ATOM 17 CD2 LEU A 59 25.157 19.605 -5.025 1.00 25.41 C
ANISOU 17 CD2 LEU A 59 2503 3831 3320 -164 -548 -714 C
ATOM 18 N GLU A 60 27.280 23.374 -7.186 1.00 26.96 N
ANISOU 18 N GLU A 60 2483 3376 4383 -58 -42 -1193 N
ATOM 19 CA GLU A 60 27.684 24.274 -8.264 1.00 26.60 C
ANISOU 19 CA GLU A 60 2546 3062 4501 -119 115 -1154 C
ATOM 20 C GLU A 60 26.590 24.311 -9.327 1.00 21.99 C
ANISOU 20 C GLU A 60 2179 2333 3845 -62 100 -928 C
ATOM 21 O GLU A 60 26.171 23.264 -9.834 1.00 20.04 O
ANISOU 21 O GLU A 60 2000 2182 3432 -11 65 -777 O
ATOM 22 CB GLU A 60 29.015 23.838 -8.874 1.00 30.32 C
ANISOU 22 CB GLU A 60 2970 3533 5019 -229 228 -1194 C
ATOM 23 CG GLU A 60 29.428 24.688 -10.082 1.00 45.14 C
ANISOU 23 CG GLU A 60 4997 5196 6959 -415 422 -1128 C
ATOM 24 CD GLU A 60 30.608 24.115 -10.852 1.00 71.69 C
ANISOU 24 CD GLU A 60 8271 8653 10313 -577 584 -1238 C
ATOM 25 OE1 GLU A 60 30.750 22.873 -10.893 1.00 72.24 O
ANISOU 25 OE1 GLU A 60 8228 8884 10337 -472 507 -1285 O
ATOM 26 OE2 GLU A 60 31.391 24.913 -11.421 1.00 77.58 O
ANISOU 26 OE2 GLU A 60 9047 9314 11114 -833 779 -1311 O
ATOM 27 N ASP A 61 26.124 25.517 -9.663 1.00 23.49 N
ANISOU 27 N ASP A 61 2478 2260 4187 -66 81 -912 N
ATOM 28 CA ASP A 61 24.944 25.631 -10.513 1.00 21.31 C
ANISOU 28 CA ASP A 61 2397 1824 3876 24 -28 -723 C
ATOM 29 C ASP A 61 25.206 25.165 -11.937 1.00 26.33 C
ANISOU 29 C ASP A 61 3261 2392 4351 -100 51 -452 C
ATOM 30 O ASP A 61 24.275 24.714 -12.612 1.00 20.81 O
ANISOU 30 O ASP A 61 2692 1686 3527 -13 -36 -285 O
ATOM 31 CB ASP A 61 24.432 27.069 -10.523 1.00 24.11 C
ANISOU 31 CB ASP A 61 2816 1836 4508 64 -169 -786 C
ATOM 32 CG ASP A 61 22.985 27.156 -10.970 1.00 46.49 C
ANISOU 32 CG ASP A 61 5744 4542 7378 248 -384 -719 C
ATOM 33 OD1 ASP A 61 22.143 26.432 -10.389 1.00 32.78 O
ANISOU 33 OD1 ASP A 61 3840 3085 5530 386 -412 -854 O
ATOM 34 OD2 ASP A 61 22.690 27.942 -11.900 1.00 35.44 O
ANISOU 34 OD2 ASP A 61 4592 2766 6106 226 -547 -530 O
ATOM 35 N SER A 62 26.445 25.274 -12.424 1.00 19.85 N
ANISOU 35 N SER A 62 2467 1559 3517 -329 228 -450 N
ATOM 36 CA SER A 62 26.729 24.779 -13.766 1.00 20.38 C
ANISOU 36 CA SER A 62 2702 1659 3382 -512 346 -272 C
ATOM 37 C SER A 62 26.578 23.264 -13.828 1.00 25.18 C
ANISOU 37 C SER A 62 3181 2545 3842 -382 357 -302 C
ATOM 38 O SER A 62 26.042 22.724 -14.807 1.00 17.81 O
ANISOU 38 O SER A 62 2388 1645 2734 -396 354 -138 O
ATOM 39 CB SER A 62 28.128 25.211 -14.208 1.00 38.02 C
ANISOU 39 CB SER A 62 4924 3898 5622 -847 575 -366 C
ATOM 40 OG SER A 62 29.136 24.549 -13.464 1.00 34.50 O
ANISOU 40 OG SER A 62 4159 3687 5262 -809 679 -668 O
ATOM 41 N GLU A 63 27.026 22.563 -12.783 1.00 21.05 N
ANISOU 41 N GLU A 63 2406 2199 3392 -264 327 -502 N
ATOM 42 CA GLU A 63 26.848 21.115 -12.741 1.00 26.47 C
ANISOU 42 CA GLU A 63 2994 3072 3990 -139 248 -510 C
ATOM 43 C GLU A 63 25.380 20.748 -12.576 1.00 15.21 C
ANISOU 43 C GLU A 63 1668 1665 2446 29 93 -348 C
ATOM 44 O GLU A 63 24.911 19.764 -13.161 1.00 15.02 O
ANISOU 44 O GLU A 63 1686 1718 2304 82 56 -254 O
ATOM 45 CB GLU A 63 27.685 20.516 -11.614 1.00 33.76 C
ANISOU 45 CB GLU A 63 3677 4117 5033 -82 154 -718 C
ATOM 46 CG GLU A 63 27.486 19.018 -11.408 1.00 33.50 C
ANISOU 46 CG GLU A 63 3576 4196 4959 41 -37 -696 C
ATOM 47 CD GLU A 63 28.140 18.515 -10.124 1.00 62.83 C
ANISOU 47 CD GLU A 63 7123 7973 8776 86 -256 -827 C
ATOM 48 OE1 GLU A 63 28.256 19.307 -9.164 1.00 70.99 O
ANISOU 48 OE1 GLU A 63 8118 9030 9825 51 -267 -889 O
ATOM 49 OE2 GLU A 63 28.553 17.334 -10.080 1.00 48.33 O
ANISOU 49 OE2 GLU A 63 5232 6135 6997 151 -438 -859 O
ATOM 50 N VAL A 64 24.635 21.529 -11.791 1.00 13.53 N
ANISOU 50 N VAL A 64 1459 1403 2281 103 7 -372 N
ATOM 51 CA VAL A 64 23.202 21.292 -11.655 1.00 12.71 C
ANISOU 51 CA VAL A 64 1397 1350 2082 235 -116 -308 C
ATOM 52 C VAL A 64 22.517 21.414 -13.011 1.00 13.07 C
ANISOU 52 C VAL A 64 1651 1251 2064 258 -125 -115 C
ATOM 53 O VAL A 64 21.695 20.576 -13.388 1.00 14.72 O
ANISOU 53 O VAL A 64 1897 1558 2139 337 -181 -29 O
ATOM 54 CB VAL A 64 22.582 22.267 -10.634 1.00 16.59 C
ANISOU 54 CB VAL A 64 1783 1834 2688 291 -187 -493 C
ATOM 55 CG1 VAL A 64 21.074 22.123 -10.622 1.00 13.47 C
ANISOU 55 CG1 VAL A 64 1382 1510 2228 411 -295 -519 C
ATOM 56 CG2 VAL A 64 23.164 22.041 -9.232 1.00 20.84 C
ANISOU 56 CG2 VAL A 64 2124 2591 3202 222 -192 -677 C
ATOM 57 N GLU A 65 22.833 22.477 -13.760 1.00 14.97 N
ANISOU 57 N GLU A 65 2054 1249 2386 157 -96 -29 N
ATOM 58 CA GLU A 65 22.183 22.662 -15.057 1.00 16.04 C
ANISOU 58 CA GLU A 65 2439 1232 2422 132 -167 200 C
ATOM 59 C GLU A 65 22.608 21.602 -16.064 1.00 15.43 C
ANISOU 59 C GLU A 65 2414 1328 2121 9 -28 298 C
ATOM 60 O GLU A 65 21.792 21.184 -16.900 1.00 15.38 O
ANISOU 60 O GLU A 65 2536 1338 1968 53 -99 443 O
ATOM 61 CB GLU A 65 22.470 24.056 -15.600 1.00 19.31 C
ANISOU 61 CB GLU A 65 3075 1313 2950 -24 -230 322 C
ATOM 62 CG GLU A 65 21.813 25.149 -14.801 1.00 36.67 C
ANISOU 62 CG GLU A 65 5219 3271 5443 146 -445 190 C
ATOM 63 CD GLU A 65 20.634 25.745 -15.533 1.00 55.91 C
ANISOU 63 CD GLU A 65 7853 5440 7951 262 -740 336 C
ATOM 64 OE1 GLU A 65 20.298 25.222 -16.618 1.00 66.01 O
ANISOU 64 OE1 GLU A 65 9299 6798 8986 200 -739 554 O
ATOM 65 OE2 GLU A 65 20.053 26.734 -15.033 1.00 61.26 O
ANISOU 65 OE2 GLU A 65 8426 5991 8858 387 -907 173 O
ATOM 66 N ALA A 66 23.865 21.153 -16.009 1.00 16.98 N
ANISOU 66 N ALA A 66 2475 1664 2312 -136 157 167 N
ATOM 67 CA ALA A 66 24.277 20.064 -16.894 1.00 15.23 C
ANISOU 67 CA ALA A 66 2210 1637 1941 -230 281 137 C
ATOM 68 C ALA A 66 23.523 18.784 -16.569 1.00 12.97 C
ANISOU 68 C ALA A 66 1812 1484 1631 -6 161 118 C
ATOM 69 O ALA A 66 23.127 18.040 -17.476 1.00 14.50 O
ANISOU 69 O ALA A 66 2054 1769 1685 -11 174 174 O
ATOM 70 CB ALA A 66 25.785 19.834 -16.793 1.00 18.35 C
ANISOU 70 CB ALA A 66 2394 2153 2424 -396 466 -118 C
ATOM 71 N VAL A 67 23.318 18.509 -15.280 1.00 11.57 N
ANISOU 71 N VAL A 67 1498 1336 1563 146 38 39 N
ATOM 72 CA VAL A 67 22.538 17.344 -14.880 1.00 9.99 C
ANISOU 72 CA VAL A 67 1239 1250 1306 284 -101 61 C
ATOM 73 C VAL A 67 21.081 17.508 -15.298 1.00 10.20 C
ANISOU 73 C VAL A 67 1403 1259 1212 377 -173 197 C
ATOM 74 O VAL A 67 20.461 16.573 -15.819 1.00 10.91 O
ANISOU 74 O VAL A 67 1514 1432 1201 427 -213 252 O
ATOM 75 CB VAL A 67 22.669 17.128 -13.361 1.00 9.45 C
ANISOU 75 CB VAL A 67 1040 1246 1306 319 -226 -26 C
ATOM 76 CG1 VAL A 67 21.641 16.130 -12.862 1.00 10.39 C
ANISOU 76 CG1 VAL A 67 1163 1483 1301 369 -380 45 C
ATOM 77 CG2 VAL A 67 24.091 16.665 -13.019 1.00 10.11 C
ANISOU 77 CG2 VAL A 67 970 1333 1540 269 -243 -174 C
ATOM 78 N ALA A 68 20.513 18.695 -15.088 1.00 10.40 N
ANISOU 78 N ALA A 68 1499 1161 1291 415 -219 211 N
ATOM 79 CA ALA A 68 19.121 18.915 -15.472 1.00 10.63 C
ANISOU 79 CA ALA A 68 1614 1149 1276 539 -344 269 C
ATOM 80 C ALA A 68 18.935 18.731 -16.971 1.00 11.92 C
ANISOU 80 C ALA A 68 1946 1267 1316 477 -326 437 C
ATOM 81 O ALA A 68 17.924 18.177 -17.424 1.00 13.84 O
ANISOU 81 O ALA A 68 2119 1608 1531 465 -345 421 O
ATOM 82 CB ALA A 68 18.674 20.316 -15.050 1.00 12.26 C
ANISOU 82 CB ALA A 68 1830 1165 1665 610 -456 186 C
ATOM 83 N LYS A 69 19.900 19.195 -17.759 1.00 13.15 N
ANISOU 83 N LYS A 69 2252 1325 1418 309 -230 540 N
ATOM 84 CA LYS A 69 19.771 19.064 -19.204 1.00 21.08 C
ANISOU 84 CA LYS A 69 3448 2340 2220 178 -210 704 C
ATOM 85 C LYS A 69 19.859 17.604 -19.614 1.00 19.00 C
ANISOU 85 C LYS A 69 3062 2324 1833 184 -106 624 C
ATOM 86 O LYS A 69 19.102 17.151 -20.479 1.00 15.21 O
ANISOU 86 O LYS A 69 2546 1937 1295 165 -148 648 O
ATOM 87 CB LYS A 69 20.840 19.893 -19.906 1.00 20.37 C
ANISOU 87 CB LYS A 69 3532 2161 2047 -136 -87 799 C
ATOM 88 CG LYS A 69 20.842 19.763 -21.434 1.00 26.67 C
ANISOU 88 CG LYS A 69 4457 3077 2602 -355 -27 908 C
ATOM 89 CD LYS A 69 19.720 20.607 -22.037 1.00 47.77 C
ANISOU 89 CD LYS A 69 7237 5585 5327 -258 -258 1049 C
ATOM 90 CE LYS A 69 19.907 20.879 -23.537 1.00 44.10 C
ANISOU 90 CE LYS A 69 6961 5171 4623 -536 -238 1180 C
ATOM 91 NZ LYS A 69 20.781 19.894 -24.227 1.00 46.28 N
ANISOU 91 NZ LYS A 69 7165 5750 4668 -769 21 1064 N
ATOM 92 N GLY A 70 20.764 16.849 -18.988 1.00 12.95 N
ANISOU 92 N GLY A 70 2072 1674 1172 174 0 436 N
ATOM 93 CA GLY A 70 20.843 15.426 -19.273 1.00 11.61 C
ANISOU 93 CA GLY A 70 1753 1672 988 215 23 317 C
ATOM 94 C GLY A 70 19.567 14.691 -18.905 1.00 16.47 C
ANISOU 94 C GLY A 70 2346 2303 1610 383 -134 357 C
ATOM 95 O GLY A 70 19.092 13.837 -19.658 1.00 12.79 O
ANISOU 95 O GLY A 70 1853 1898 1108 366 -131 323 O
ATOM 96 N LEU A 71 19.000 15.001 -17.735 1.00 9.61 N
ANISOU 96 N LEU A 71 1408 1357 887 382 -206 310 N
ATOM 97 CA LEU A 71 17.737 14.376 -17.347 1.00 7.75 C
ANISOU 97 CA LEU A 71 1110 1131 703 344 -234 249 C
ATOM 98 C LEU A 71 16.647 14.691 -18.354 1.00 14.70 C
ANISOU 98 C LEU A 71 2054 2002 1528 376 -241 279 C
ATOM 99 O LEU A 71 15.875 13.805 -18.739 1.00 13.49 O
ANISOU 99 O LEU A 71 1882 1897 1348 401 -224 237 O
ATOM 100 CB LEU A 71 17.311 14.846 -15.959 1.00 7.29 C
ANISOU 100 CB LEU A 71 1006 1087 675 352 -264 203 C
ATOM 101 CG LEU A 71 18.160 14.353 -14.793 1.00 6.95 C
ANISOU 101 CG LEU A 71 904 1068 670 292 -300 189 C
ATOM 102 CD1 LEU A 71 17.815 15.100 -13.519 1.00 13.66 C
ANISOU 102 CD1 LEU A 71 1713 1976 1500 282 -335 142 C
ATOM 103 CD2 LEU A 71 17.950 12.842 -14.565 1.00 7.01 C
ANISOU 103 CD2 LEU A 71 898 1094 673 230 -342 199 C
ATOM 104 N GLU A 72 16.576 15.952 -18.789 1.00 9.41 N
ANISOU 104 N GLU A 72 1463 1256 858 374 -295 372 N
ATOM 105 CA GLU A 72 15.564 16.365 -19.753 1.00 10.88 C
ANISOU 105 CA GLU A 72 1717 1410 1009 407 -365 433 C
ATOM 106 C GLU A 72 15.726 15.622 -21.072 1.00 22.00 C
ANISOU 106 C GLU A 72 3176 2891 2292 323 -334 495 C
ATOM 107 O GLU A 72 14.736 15.218 -21.688 1.00 32.09 O
ANISOU 107 O GLU A 72 4462 4194 3536 367 -369 476 O
ATOM 108 CB GLU A 72 15.653 17.869 -19.997 1.00 19.87 C
ANISOU 108 CB GLU A 72 2941 2416 2191 427 -447 567 C
ATOM 109 CG GLU A 72 14.568 18.408 -20.915 1.00 27.84 C
ANISOU 109 CG GLU A 72 4049 3346 3182 496 -578 626 C
ATOM 110 CD GLU A 72 14.651 19.919 -21.121 1.00 36.29 C
ANISOU 110 CD GLU A 72 5290 4179 4320 529 -723 725 C
ATOM 111 OE1 GLU A 72 15.737 20.500 -20.897 1.00 44.14 O
ANISOU 111 OE1 GLU A 72 6391 5068 5313 447 -692 793 O
ATOM 112 OE2 GLU A 72 13.626 20.527 -21.502 1.00 48.14 O
ANISOU 112 OE2 GLU A 72 6852 5548 5888 618 -914 712 O
ATOM 113 N GLU A 73 16.965 15.452 -21.536 1.00 14.88 N
ANISOU 113 N GLU A 73 2318 2051 1287 195 -265 548 N
ATOM 114 CA GLU A 73 17.184 14.699 -22.768 1.00 19.64 C
ANISOU 114 CA GLU A 73 2977 2781 1705 84 -208 549 C
ATOM 115 C GLU A 73 16.901 13.209 -22.594 1.00 20.65 C
ANISOU 115 C GLU A 73 2992 2942 1911 191 -174 384 C
ATOM 116 O GLU A 73 16.311 12.597 -23.484 1.00 20.73 O
ANISOU 116 O GLU A 73 3016 3008 1854 176 -178 365 O
ATOM 117 CB GLU A 73 18.613 14.899 -23.267 1.00 19.02 C
ANISOU 117 CB GLU A 73 2943 2855 1428 -33 -21 562 C
ATOM 118 CG GLU A 73 18.904 16.306 -23.766 1.00 30.10 C
ANISOU 118 CG GLU A 73 4568 4136 2732 -83 18 734 C
ATOM 119 CD GLU A 73 20.351 16.475 -24.174 1.00 52.26 C
ANISOU 119 CD GLU A 73 7438 7027 5391 -422 228 649 C
ATOM 120 OE1 GLU A 73 21.059 15.448 -24.259 1.00 44.77 O
ANISOU 120 OE1 GLU A 73 6306 6294 4412 -507 397 406 O
ATOM 121 OE2 GLU A 73 20.774 17.626 -24.427 1.00 61.75 O
ANISOU 121 OE2 GLU A 73 8804 8113 6544 -630 227 772 O
HETATM 122 N MSE A 74 17.330 12.587 -21.491 1.00 11.48 N
ANISOU 122 N MSE A 74 1700 1780 882 300 -154 295 N
HETATM 123 CA MSE A 74 17.172 11.127 -21.436 1.00 12.69 C
ANISOU 123 CA MSE A 74 1732 1990 1101 371 -158 195 C
HETATM 124 C MSE A 74 15.700 10.802 -21.243 1.00 16.77 C
ANISOU 124 C MSE A 74 2236 2466 1671 411 -168 180 C
HETATM 125 O MSE A 74 15.198 9.792 -21.738 1.00 18.20 O
ANISOU 125 O MSE A 74 2377 2694 1846 439 -166 135 O
HETATM 126 CB MSE A 74 17.886 10.388 -20.295 1.00 19.46 C
ANISOU 126 CB MSE A 74 2486 2818 2091 412 -214 128 C
HETATM 127 CG MSE A 74 17.812 10.957 -18.914 1.00 22.10 C
ANISOU 127 CG MSE A 74 2835 3047 2514 355 -238 164 C
HETATM 128 SE MSE A 74 19.177 10.104 -17.805 0.52 10.58 SE
ANISOU 128 SE MSE A 74 1259 1528 1234 331 -358 134 SE
HETATM 129 CE MSE A 74 20.654 11.369 -17.973 1.00 19.54 C
ANISOU 129 CE MSE A 74 2327 2748 2348 465 -340 39 C
ATOM 130 N TYR A 75 15.006 11.633 -20.468 1.00 11.55 N
ANISOU 130 N TYR A 75 1600 1754 1034 429 -181 190 N
ATOM 131 CA TYR A 75 13.684 11.270 -19.977 1.00 10.88 C
ANISOU 131 CA TYR A 75 1486 1692 958 470 -184 135 C
ATOM 132 C TYR A 75 12.573 12.119 -20.568 1.00 18.55 C
ANISOU 132 C TYR A 75 2509 2654 1884 535 -230 136 C
ATOM 133 O TYR A 75 11.495 12.203 -19.975 1.00 16.28 O
ANISOU 133 O TYR A 75 2189 2398 1598 586 -251 61 O
ATOM 134 CB TYR A 75 13.641 11.354 -18.454 1.00 14.24 C
ANISOU 134 CB TYR A 75 1873 2119 1419 432 -197 114 C
ATOM 135 CG TYR A 75 14.511 10.334 -17.751 1.00 12.80 C
ANISOU 135 CG TYR A 75 1665 1914 1283 345 -233 140 C
ATOM 136 CD1 TYR A 75 14.616 9.034 -18.235 1.00 10.47 C
ANISOU 136 CD1 TYR A 75 1361 1608 1010 323 -269 143 C
ATOM 137 CD2 TYR A 75 15.194 10.667 -16.589 1.00 12.45 C
ANISOU 137 CD2 TYR A 75 1616 1846 1267 282 -278 167 C
ATOM 138 CE1 TYR A 75 15.389 8.092 -17.587 1.00 9.23 C
ANISOU 138 CE1 TYR A 75 1185 1395 929 242 -382 195 C
ATOM 139 CE2 TYR A 75 15.968 9.740 -15.934 1.00 7.43 C
ANISOU 139 CE2 TYR A 75 972 1162 687 190 -383 223 C
ATOM 140 CZ TYR A 75 16.066 8.454 -16.439 1.00 10.74 C
ANISOU 140 CZ TYR A 75 1355 1579 1146 178 -423 252 C
ATOM 141 OH TYR A 75 16.840 7.533 -15.781 1.00 10.31 O
ANISOU 141 OH TYR A 75 1280 1522 1115 217 -500 247 O
ATOM 142 N ALA A 76 12.815 12.756 -21.715 1.00 23.30 N
ANISOU 142 N ALA A 76 2434 3929 2489 223 -560 127 N
ATOM 143 CA ALA A 76 11.775 13.579 -22.321 1.00 41.64 C
ANISOU 143 CA ALA A 76 4707 6324 4790 277 -639 230 C
ATOM 144 C ALA A 76 10.536 12.761 -22.645 1.00 36.49 C
ANISOU 144 C ALA A 76 4016 5766 4083 201 -706 235 C
ATOM 145 O ALA A 76 9.416 13.282 -22.590 1.00 44.89 O
ANISOU 145 O ALA A 76 4983 6904 5168 254 -757 306 O
ATOM 146 CB ALA A 76 12.305 14.253 -23.584 1.00 30.18 C
ANISOU 146 CB ALA A 76 3302 4928 3239 307 -673 327 C
ATOM 147 N ASN A 77 10.713 11.481 -22.966 1.00 27.70 N
ANISOU 147 N ASN A 77 2953 4672 2899 85 -710 164 N
ATOM 148 CA ASN A 77 9.614 10.610 -23.359 1.00 29.92 C
ANISOU 148 CA ASN A 77 3185 5058 3125 -3 -793 162 C
ATOM 149 C ASN A 77 9.264 9.596 -22.278 1.00 40.87 C
ANISOU 149 C ASN A 77 4508 6440 4582 -58 -746 112 C
ATOM 150 O ASN A 77 8.577 8.608 -22.556 1.00 40.82 O
ANISOU 150 O ASN A 77 4471 6489 4548 -161 -816 90 O
ATOM 151 CB ASN A 77 9.952 9.890 -24.665 1.00 38.45 C
ANISOU 151 CB ASN A 77 4387 6160 4063 -97 -864 113 C
ATOM 152 CG ASN A 77 10.319 10.848 -25.773 1.00 60.56 C
ANISOU 152 CG ASN A 77 7254 9014 6740 -44 -898 189 C
ATOM 153 OD1 ASN A 77 11.429 11.370 -25.816 1.00 76.96 O
ANISOU 153 OD1 ASN A 77 9389 11051 8803 2 -815 203 O
ATOM 154 ND2 ASN A 77 9.369 11.114 -26.662 1.00 67.89 N
ANISOU 154 ND2 ASN A 77 8162 10057 7575 -46 -1024 259 N
ATOM 155 N GLY A 78 9.727 9.814 -21.055 1.00 26.73 N
ANISOU 155 N GLY A 78 2700 4584 2872 6 -640 94 N
ATOM 156 CA GLY A 78 9.376 8.945 -19.947 1.00 16.41 C
ANISOU 156 CA GLY A 78 1335 3287 1611 -28 -591 74 C
ATOM 157 C GLY A 78 10.619 8.483 -19.220 1.00 16.89 C
ANISOU 157 C GLY A 78 1474 3240 1704 -26 -500 4 C
ATOM 158 O GLY A 78 11.690 8.316 -19.809 1.00 17.62 O
ANISOU 158 O GLY A 78 1660 3252 1781 -50 -492 -45 O
ATOM 159 N VAL A 79 10.475 8.272 -17.917 1.00 18.13 N
ANISOU 159 N VAL A 79 1587 3406 1895 10 -435 7 N
ATOM 160 CA VAL A 79 11.539 7.707 -17.103 1.00 15.01 C
ANISOU 160 CA VAL A 79 1249 2927 1526 12 -368 -47 C
ATOM 161 C VAL A 79 11.416 6.192 -17.229 1.00 18.06 C
ANISOU 161 C VAL A 79 1634 3300 1928 -110 -401 -56 C
ATOM 162 O VAL A 79 10.590 5.574 -16.555 1.00 22.26 O
ANISOU 162 O VAL A 79 2087 3895 2477 -145 -407 -11 O
ATOM 163 CB VAL A 79 11.436 8.161 -15.648 1.00 15.20 C
ANISOU 163 CB VAL A 79 1241 2983 1550 109 -301 -42 C
ATOM 164 CG1 VAL A 79 12.546 7.526 -14.820 1.00 13.94 C
ANISOU 164 CG1 VAL A 79 1138 2749 1408 110 -255 -88 C
ATOM 165 CG2 VAL A 79 11.470 9.671 -15.562 1.00 15.75 C
ANISOU 165 CG2 VAL A 79 1318 3048 1619 226 -293 -54 C
ATOM 166 N THR A 80 12.226 5.590 -18.105 1.00 16.00 N
ANISOU 166 N THR A 80 1457 2958 1666 -177 -428 -116 N
ATOM 167 CA THR A 80 12.260 4.139 -18.275 1.00 19.64 C
ANISOU 167 CA THR A 80 1938 3369 2158 -294 -470 -155 C
ATOM 168 C THR A 80 13.705 3.652 -18.273 1.00 18.81 C
ANISOU 168 C THR A 80 1913 3164 2069 -298 -423 -226 C
ATOM 169 O THR A 80 14.637 4.404 -18.574 1.00 14.51 O
ANISOU 169 O THR A 80 1421 2586 1506 -232 -380 -249 O
ATOM 170 CB THR A 80 11.576 3.677 -19.576 1.00 21.39 C
ANISOU 170 CB THR A 80 2178 3620 2328 -401 -575 -193 C
ATOM 171 OG1 THR A 80 12.405 3.997 -20.704 1.00 16.04 O
ANISOU 171 OG1 THR A 80 1613 2914 1566 -397 -577 -256 O
ATOM 172 CG2 THR A 80 10.226 4.348 -19.743 1.00 35.62 C
ANISOU 172 CG2 THR A 80 3878 5551 4105 -389 -631 -117 C
ATOM 173 N GLU A 81 13.887 2.377 -17.924 1.00 16.95 N
ANISOU 173 N GLU A 81 1666 2894 1880 -389 -431 -260 N
ATOM 174 CA GLU A 81 15.239 1.827 -17.910 1.00 15.21 C
ANISOU 174 CA GLU A 81 1504 2589 1688 -404 -382 -341 C
ATOM 175 C GLU A 81 15.873 1.915 -19.287 1.00 13.63 C
ANISOU 175 C GLU A 81 1417 2353 1408 -436 -371 -448 C
ATOM 176 O GLU A 81 17.053 2.248 -19.415 1.00 15.62 O
ANISOU 176 O GLU A 81 1708 2567 1661 -381 -300 -502 O
ATOM 177 CB GLU A 81 15.213 0.381 -17.423 1.00 21.97 C
ANISOU 177 CB GLU A 81 2325 3387 2634 -529 -396 -365 C
ATOM 178 CG GLU A 81 16.586 -0.166 -17.077 1.00 33.35 C
ANISOU 178 CG GLU A 81 3791 4726 4153 -530 -329 -442 C
ATOM 179 CD GLU A 81 16.525 -1.294 -16.059 1.00 57.93 C
ANISOU 179 CD GLU A 81 6814 7789 7408 -619 -323 -387 C
ATOM 180 OE1 GLU A 81 15.773 -2.266 -16.285 1.00 54.08 O
ANISOU 180 OE1 GLU A 81 6329 7234 6984 -775 -357 -386 O
ATOM 181 OE2 GLU A 81 17.227 -1.209 -15.028 1.00 74.48 O
ANISOU 181 OE2 GLU A 81 8847 9886 9566 -511 -280 -314 O
ATOM 182 N ASP A 82 15.094 1.646 -20.337 1.00 16.42 N
ANISOU 182 N ASP A 82 1822 2731 1687 -520 -441 -483 N
ATOM 183 CA ASP A 82 15.652 1.691 -21.680 1.00 17.02 C
ANISOU 183 CA ASP A 82 2031 2787 1647 -542 -425 -585 C
ATOM 184 C ASP A 82 16.090 3.103 -22.059 1.00 17.21 C
ANISOU 184 C ASP A 82 2057 2877 1604 -430 -387 -527 C
ATOM 185 O ASP A 82 17.140 3.281 -22.691 1.00 13.88 O
ANISOU 185 O ASP A 82 1723 2431 1122 -408 -307 -596 O
ATOM 186 CB ASP A 82 14.631 1.159 -22.680 1.00 23.10 C
ANISOU 186 CB ASP A 82 2853 3588 2337 -643 -538 -635 C
ATOM 187 CG ASP A 82 14.766 -0.339 -22.901 1.00 55.66 C
ANISOU 187 CG ASP A 82 7062 7584 6503 -772 -548 -777 C
ATOM 188 OD1 ASP A 82 13.836 -0.944 -23.479 1.00 45.17 O
ANISOU 188 OD1 ASP A 82 5747 6262 5152 -875 -666 -830 O
ATOM 189 OD2 ASP A 82 15.798 -0.912 -22.478 1.00 55.03 O
ANISOU 189 OD2 ASP A 82 7031 7378 6501 -769 -441 -844 O
ATOM 190 N ASN A 83 15.297 4.120 -21.702 1.00 13.14 N
ANISOU 190 N ASN A 83 1451 2433 1107 -362 -431 -408 N
ATOM 191 CA ASN A 83 15.672 5.494 -22.044 1.00 12.59 C
ANISOU 191 CA ASN A 83 1378 2408 998 -270 -406 -353 C
ATOM 192 C ASN A 83 16.950 5.908 -21.331 1.00 14.86 C
ANISOU 192 C ASN A 83 1638 2647 1363 -195 -316 -371 C
ATOM 193 O ASN A 83 17.801 6.601 -21.900 1.00 11.09 O
ANISOU 193 O ASN A 83 1186 2194 833 -158 -274 -390 O
ATOM 194 CB ASN A 83 14.533 6.457 -21.698 1.00 13.40 C
ANISOU 194 CB ASN A 83 1394 2563 1134 -210 -460 -244 C
ATOM 195 CG ASN A 83 13.369 6.351 -22.665 1.00 24.31 C
ANISOU 195 CG ASN A 83 2784 4026 2426 -267 -566 -225 C
ATOM 196 OD1 ASN A 83 13.512 5.819 -23.764 1.00 23.44 O
ANISOU 196 OD1 ASN A 83 2772 3940 2196 -337 -605 -292 O
ATOM 197 ND2 ASN A 83 12.212 6.854 -22.260 1.00 18.40 N
ANISOU 197 ND2 ASN A 83 1937 3331 1722 -235 -614 -147 N
ATOM 198 N PHE A 84 17.105 5.478 -20.083 1.00 10.12 N
ANISOU 198 N PHE A 84 979 1990 876 -171 -292 -366 N
ATOM 199 CA PHE A 84 18.323 5.750 -19.333 1.00 9.04 C
ANISOU 199 CA PHE A 84 806 1803 826 -97 -233 -397 C
ATOM 200 C PHE A 84 19.530 5.068 -19.972 1.00 10.54 C
ANISOU 200 C PHE A 84 1045 1954 1004 -142 -168 -531 C
ATOM 201 O PHE A 84 20.534 5.713 -20.295 1.00 10.92 O
ANISOU 201 O PHE A 84 1092 1993 1064 -93 -112 -579 O
ATOM 202 CB PHE A 84 18.136 5.278 -17.893 1.00 8.41 C
ANISOU 202 CB PHE A 84 683 1678 833 -68 -232 -355 C
ATOM 203 CG PHE A 84 19.398 5.293 -17.083 1.00 7.71 C
ANISOU 203 CG PHE A 84 570 1523 836 -1 -197 -390 C
ATOM 204 CD1 PHE A 84 20.047 6.497 -16.817 1.00 7.20 C
ANISOU 204 CD1 PHE A 84 505 1416 813 82 -188 -379 C
ATOM 205 CD2 PHE A 84 19.930 4.112 -16.577 1.00 8.27 C
ANISOU 205 CD2 PHE A 84 614 1555 974 -30 -189 -432 C
ATOM 206 CE1 PHE A 84 21.222 6.518 -16.051 1.00 7.14 C
ANISOU 206 CE1 PHE A 84 489 1320 903 124 -179 -396 C
ATOM 207 CE2 PHE A 84 21.097 4.124 -15.806 1.00 11.98 C
ANISOU 207 CE2 PHE A 84 1050 1948 1552 41 -173 -439 C
ATOM 208 CZ PHE A 84 21.745 5.329 -15.541 1.00 10.56 C
ANISOU 208 CZ PHE A 84 895 1720 1398 111 -172 -412 C
ATOM 209 N LYS A 85 19.447 3.753 -20.171 1.00 11.78 N
ANISOU 209 N LYS A 85 1266 2053 1156 -234 -150 -605 N
ATOM 210 CA LYS A 85 20.623 3.027 -20.633 1.00 10.87 C
ANISOU 210 CA LYS A 85 1236 1818 1076 -251 -24 -744 C
ATOM 211 C LYS A 85 21.023 3.451 -22.039 1.00 11.93 C
ANISOU 211 C LYS A 85 1493 1967 1075 -245 66 -777 C
ATOM 212 O LYS A 85 22.215 3.591 -22.334 1.00 12.17 O
ANISOU 212 O LYS A 85 1547 1911 1167 -177 221 -807 O
ATOM 213 CB LYS A 85 20.372 1.519 -20.575 1.00 14.88 C
ANISOU 213 CB LYS A 85 1808 2213 1632 -346 -14 -816 C
ATOM 214 CG LYS A 85 20.167 0.990 -19.154 1.00 15.71 C
ANISOU 214 CG LYS A 85 1794 2289 1886 -347 -68 -757 C
ATOM 215 CD LYS A 85 20.178 -0.556 -19.073 1.00 22.38 C
ANISOU 215 CD LYS A 85 2706 2957 2843 -436 -28 -817 C
ATOM 216 CE LYS A 85 18.943 -1.231 -19.684 1.00 44.80 C
ANISOU 216 CE LYS A 85 5609 5820 5592 -593 -119 -853 C
ATOM 217 NZ LYS A 85 18.724 -1.042 -21.153 1.00 45.30 N
ANISOU 217 NZ LYS A 85 5810 5917 5484 -609 -126 -919 N
ATOM 218 N ASN A 86 20.045 3.652 -22.923 1.00 12.89 N
ANISOU 218 N ASN A 86 1679 2184 1033 -296 -21 -735 N
ATOM 219 CA ASN A 86 20.378 3.998 -24.298 1.00 17.29 C
ANISOU 219 CA ASN A 86 2369 2778 1422 -284 54 -754 C
ATOM 220 C ASN A 86 20.949 5.401 -24.381 1.00 16.70 C
ANISOU 220 C ASN A 86 2238 2784 1323 -201 117 -671 C
ATOM 221 O ASN A 86 21.879 5.654 -25.155 1.00 18.09 O
ANISOU 221 O ASN A 86 2488 2942 1442 -158 286 -678 O
ATOM 222 CB ASN A 86 19.142 3.861 -25.180 1.00 19.36 C
ANISOU 222 CB ASN A 86 2704 3127 1527 -347 -82 -733 C
ATOM 223 CG ASN A 86 18.761 2.410 -25.398 1.00 30.07 C
ANISOU 223 CG ASN A 86 4144 4395 2886 -435 -119 -855 C
ATOM 224 OD1 ASN A 86 19.629 1.537 -25.476 1.00 33.68 O
ANISOU 224 OD1 ASN A 86 4682 4722 3393 -431 2 -971 O
ATOM 225 ND2 ASN A 86 17.466 2.143 -25.495 1.00 31.82 N
ANISOU 225 ND2 ASN A 86 4339 4673 3080 -506 -280 -832 N
ATOM 226 N TYR A 87 20.408 6.326 -23.586 1.00 12.43 N
ANISOU 226 N TYR A 87 1560 2323 839 -164 0 -579 N
ATOM 227 CA TYR A 87 20.988 7.661 -23.529 1.00 12.02 C
ANISOU 227 CA TYR A 87 1440 2251 876 -64 46 -454 C
ATOM 228 C TYR A 87 22.419 7.613 -23.019 1.00 13.22 C
ANISOU 228 C TYR A 87 1537 2229 1257 -7 188 -465 C
ATOM 229 O TYR A 87 23.315 8.240 -23.593 1.00 16.85 O
ANISOU 229 O TYR A 87 2001 2636 1766 35 320 -394 O
ATOM 230 CB TYR A 87 20.140 8.571 -22.646 1.00 13.71 C
ANISOU 230 CB TYR A 87 1524 2527 1159 -13 -110 -371 C
ATOM 231 CG TYR A 87 20.680 9.974 -22.582 1.00 13.98 C
ANISOU 231 CG TYR A 87 1499 2492 1320 82 -79 -255 C
ATOM 232 CD1 TYR A 87 20.323 10.912 -23.537 1.00 25.81 C
ANISOU 232 CD1 TYR A 87 3037 4062 2708 108 -86 -126 C
ATOM 233 CD2 TYR A 87 21.551 10.364 -21.571 1.00 14.65 C
ANISOU 233 CD2 TYR A 87 1489 2434 1643 139 -56 -268 C
ATOM 234 CE1 TYR A 87 20.814 12.203 -23.486 1.00 21.58 C
ANISOU 234 CE1 TYR A 87 2447 3424 2328 186 -53 -5 C
ATOM 235 CE2 TYR A 87 22.046 11.656 -21.514 1.00 16.56 C
ANISOU 235 CE2 TYR A 87 1676 2580 2036 203 -44 -178 C
ATOM 236 CZ TYR A 87 21.668 12.568 -22.479 1.00 21.50 C
ANISOU 236 CZ TYR A 87 2343 3246 2578 224 -33 -43 C
ATOM 237 OH TYR A 87 22.151 13.859 -22.438 1.00 24.74 O
ANISOU 237 OH TYR A 87 2701 3525 3176 280 -16 62 O
ATOM 238 N VAL A 88 22.662 6.866 -21.937 1.00 10.55 N
ANISOU 238 N VAL A 88 1131 1808 1069 -5 162 -531 N
ATOM 239 CA VAL A 88 24.012 6.803 -21.378 1.00 13.51 C
ANISOU 239 CA VAL A 88 1424 2034 1675 54 262 -528 C
ATOM 240 C VAL A 88 24.977 6.166 -22.369 1.00 11.72 C
ANISOU 240 C VAL A 88 1281 1731 1442 55 472 -570 C
ATOM 241 O VAL A 88 26.072 6.687 -22.615 1.00 12.32 O
ANISOU 241 O VAL A 88 1295 1734 1652 106 604 -505 O
ATOM 242 CB VAL A 88 24.005 6.064 -20.030 1.00 9.90 C
ANISOU 242 CB VAL A 88 886 1530 1347 65 177 -567 C
ATOM 243 CG1 VAL A 88 25.435 5.845 -19.533 1.00 12.32 C
ANISOU 243 CG1 VAL A 88 1099 1695 1885 126 264 -558 C
ATOM 244 CG2 VAL A 88 23.229 6.883 -19.016 1.00 9.17 C
ANISOU 244 CG2 VAL A 88 705 1522 1256 97 8 -525 C
ATOM 245 N LYS A 89 24.596 5.030 -22.957 1.00 12.80 N
ANISOU 245 N LYS A 89 1555 1876 1432 0 515 -683 N
ATOM 246 CA LYS A 89 25.514 4.393 -23.904 1.00 15.99 C
ANISOU 246 CA LYS A 89 2058 2202 1816 27 728 -741 C
ATOM 247 C LYS A 89 25.750 5.249 -25.139 1.00 17.51 C
ANISOU 247 C LYS A 89 2324 2488 1843 47 854 -673 C
ATOM 248 O LYS A 89 26.814 5.147 -25.763 1.00 18.18 O
ANISOU 248 O LYS A 89 2416 2514 1977 111 1024 -632 O
ATOM 249 CB LYS A 89 25.007 3.015 -24.328 1.00 16.59 C
ANISOU 249 CB LYS A 89 2286 2239 1780 -31 696 -859 C
ATOM 250 CG LYS A 89 24.796 2.062 -23.183 1.00 21.72 C
ANISOU 250 CG LYS A 89 2874 2783 2596 -58 611 -900 C
ATOM 251 CD LYS A 89 24.353 0.711 -23.717 1.00 40.19 C
ANISOU 251 CD LYS A 89 5362 5050 4859 -124 602 -1015 C
ATOM 252 CE LYS A 89 22.847 0.549 -23.644 1.00 43.12 C
ANISOU 252 CE LYS A 89 5766 5520 5097 -251 409 -1042 C
ATOM 253 NZ LYS A 89 22.471 -0.898 -23.631 1.00 53.35 N
ANISOU 253 NZ LYS A 89 7145 6685 6443 -325 381 -1142 N
ATOM 254 N ASN A 90 24.788 6.090 -25.511 1.00 15.56 N
ANISOU 254 N ASN A 90 2112 2391 1409 7 732 -605 N
ATOM 255 CA ASN A 90 24.974 6.911 -26.704 1.00 17.18 C
ANISOU 255 CA ASN A 90 2394 2695 1437 31 847 -498 C
ATOM 256 C ASN A 90 25.768 8.182 -26.442 1.00 20.42 C
ANISOU 256 C ASN A 90 2649 3039 2069 93 912 -307 C
ATOM 257 O ASN A 90 26.193 8.827 -27.405 1.00 21.40 O
ANISOU 257 O ASN A 90 2817 3212 2104 120 1063 -180 O
ATOM 258 CB ASN A 90 23.617 7.289 -27.312 1.00 19.81 C
ANISOU 258 CB ASN A 90 2826 3220 1482 -26 671 -468 C
ATOM 259 CG ASN A 90 22.928 6.112 -27.967 1.00 31.55 C
ANISOU 259 CG ASN A 90 4479 4733 2775 -80 587 -612 C
ATOM 260 OD1 ASN A 90 23.587 5.172 -28.393 1.00 38.44 O
ANISOU 260 OD1 ASN A 90 5433 5516 3657 -49 707 -714 O
ATOM 261 ND2 ASN A 90 21.600 6.158 -28.052 1.00 38.42 N
ANISOU 261 ND2 ASN A 90 5366 5698 3533 -143 360 -596 N
ATOM 262 N ASN A 91 25.976 8.568 -25.180 1.00 15.14 N
ANISOU 262 N ASN A 91 1808 2263 1681 109 799 -280 N
ATOM 263 CA ASN A 91 26.514 9.893 -24.884 1.00 17.16 C
ANISOU 263 CA ASN A 91 1924 2444 2153 141 799 -121 C
ATOM 264 C ASN A 91 27.748 9.911 -23.993 1.00 19.93 C
ANISOU 264 C ASN A 91 2096 2630 2848 167 846 -120 C
ATOM 265 O ASN A 91 28.320 10.991 -23.802 1.00 21.97 O
ANISOU 265 O ASN A 91 2230 2800 3318 172 849 0 O
ATOM 266 CB ASN A 91 25.433 10.774 -24.229 1.00 16.20 C
ANISOU 266 CB ASN A 91 1762 2361 2032 141 566 -80 C
ATOM 267 CG ASN A 91 24.342 11.204 -25.208 1.00 26.12 C
ANISOU 267 CG ASN A 91 3141 3778 3007 131 514 2 C
ATOM 268 OD1 ASN A 91 24.487 12.206 -25.908 1.00 29.66 O
ANISOU 268 OD1 ASN A 91 3596 4228 3444 156 576 172 O
ATOM 269 ND2 ASN A 91 23.241 10.443 -25.256 1.00 18.42 N
ANISOU 269 ND2 ASN A 91 2248 2935 1816 91 390 -101 N
ATOM 270 N PHE A 92 28.167 8.779 -23.426 1.00 14.26 N
ANISOU 270 N PHE A 92 1349 1859 2210 178 865 -240 N
ATOM 271 CA PHE A 92 29.304 8.743 -22.515 1.00 15.30 C
ANISOU 271 CA PHE A 92 1334 1863 2617 195 814 -215 C
ATOM 272 C PHE A 92 30.261 7.627 -22.900 1.00 17.33 C
ANISOU 272 C PHE A 92 1629 2070 2885 217 942 -238 C
ATOM 273 O PHE A 92 29.851 6.562 -23.368 1.00 17.76 O
ANISOU 273 O PHE A 92 1813 2160 2776 224 1004 -335 O
ATOM 274 CB PHE A 92 28.859 8.553 -21.051 1.00 12.43 C
ANISOU 274 CB PHE A 92 930 1489 2304 188 569 -277 C
ATOM 275 CG PHE A 92 27.967 9.658 -20.554 1.00 11.51 C
ANISOU 275 CG PHE A 92 777 1413 2183 185 414 -269 C
ATOM 276 CD1 PHE A 92 28.507 10.773 -19.927 1.00 21.58 C
ANISOU 276 CD1 PHE A 92 1980 2601 3620 174 308 -212 C
ATOM 277 CD2 PHE A 92 26.592 9.596 -20.741 1.00 12.96 C
ANISOU 277 CD2 PHE A 92 1048 1718 2158 179 345 -315 C
ATOM 278 CE1 PHE A 92 27.681 11.804 -19.481 1.00 13.55 C
ANISOU 278 CE1 PHE A 92 961 1596 2592 185 167 -217 C
ATOM 279 CE2 PHE A 92 25.765 10.630 -20.306 1.00 16.41 C
ANISOU 279 CE2 PHE A 92 1470 2192 2574 195 191 -289 C
ATOM 280 CZ PHE A 92 26.317 11.730 -19.669 1.00 19.12 C
ANISOU 280 CZ PHE A 92 1709 2425 3131 217 119 -255 C
ATOM 281 N ALA A 93 31.543 7.877 -22.667 1.00 18.43 N
ANISOU 281 N ALA A 93 1653 2116 3235 224 967 -154 N
ATOM 282 CA ALA A 93 32.564 6.885 -22.943 1.00 19.36 C
ANISOU 282 CA ALA A 93 1768 2179 3411 262 1089 -161 C
ATOM 283 C ALA A 93 32.444 5.714 -21.975 1.00 20.95 C
ANISOU 283 C ALA A 93 1984 2347 3631 273 968 -240 C
ATOM 284 O ALA A 93 31.973 5.859 -20.842 1.00 16.91 O
ANISOU 284 O ALA A 93 1439 1844 3142 248 772 -253 O
ATOM 285 CB ALA A 93 33.949 7.513 -22.844 1.00 21.97 C
ANISOU 285 CB ALA A 93 1945 2421 3983 262 1135 -41 C
ATOM 286 N GLN A 94 32.865 4.539 -22.446 1.00 23.11 N
ANISOU 286 N GLN A 94 2313 2581 3885 318 1096 -287 N
ATOM 287 CA GLN A 94 32.799 3.321 -21.640 1.00 20.80 C
ANISOU 287 CA GLN A 94 2034 2235 3635 335 1019 -338 C
ATOM 288 C GLN A 94 33.415 3.517 -20.261 1.00 24.34 C
ANISOU 288 C GLN A 94 2342 2650 4256 328 852 -262 C
ATOM 289 O GLN A 94 32.848 3.098 -19.247 1.00 24.31 O
ANISOU 289 O GLN A 94 2346 2659 4232 317 703 -280 O
ATOM 290 CB GLN A 94 33.496 2.178 -22.382 1.00 24.60 C
ANISOU 290 CB GLN A 94 2566 2645 4136 398 1205 -380 C
ATOM 291 CG GLN A 94 32.788 0.852 -22.231 1.00 37.97 C
ANISOU 291 CG GLN A 94 4378 4288 5763 404 1188 -488 C
ATOM 292 CD GLN A 94 31.277 0.997 -22.258 1.00 47.69 C
ANISOU 292 CD GLN A 94 5727 5590 6804 334 1087 -573 C
ATOM 293 OE1 GLN A 94 30.595 0.797 -21.249 1.00 49.46 O
ANISOU 293 OE1 GLN A 94 5926 5813 7054 300 936 -572 O
ATOM 294 NE2 GLN A 94 30.745 1.335 -23.427 1.00 45.02 N
ANISOU 294 NE2 GLN A 94 5517 5328 6260 313 1173 -642 N
ATOM 295 N GLN A 95 34.589 4.145 -20.214 1.00 22.62 N
ANISOU 295 N GLN A 95 1998 2396 4202 334 879 -174 N
ATOM 296 CA GLN A 95 35.281 4.397 -18.956 1.00 27.27 C
ANISOU 296 CA GLN A 95 2464 2961 4938 322 716 -116 C
ATOM 297 C GLN A 95 34.398 5.146 -17.966 1.00 26.57 C
ANISOU 297 C GLN A 95 2401 2936 4760 272 502 -143 C
ATOM 298 O GLN A 95 34.313 4.773 -16.788 1.00 28.77 O
ANISOU 298 O GLN A 95 2668 3238 5026 280 356 -146 O
ATOM 299 CB GLN A 95 36.556 5.187 -19.245 1.00 36.10 C
ANISOU 299 CB GLN A 95 3442 4026 6250 317 784 -26 C
ATOM 300 CG GLN A 95 37.189 5.833 -18.044 1.00 33.12 C
ANISOU 300 CG GLN A 95 2943 3629 6012 284 595 15 C
ATOM 301 CD GLN A 95 38.194 6.885 -18.462 1.00 65.49 C
ANISOU 301 CD GLN A 95 6910 7663 10312 254 654 100 C
ATOM 302 OE1 GLN A 95 37.816 7.995 -18.842 1.00 66.82 O
ANISOU 302 OE1 GLN A 95 7092 7820 10476 207 650 111 O
ATOM 303 NE2 GLN A 95 39.479 6.541 -18.409 1.00 58.72 N
ANISOU 303 NE2 GLN A 95 5908 6753 9652 287 714 176 N
ATOM 304 N GLU A 96 33.742 6.219 -18.426 1.00 23.30 N
ANISOU 304 N GLU A 96 2022 2554 4276 234 493 -156 N
ATOM 305 CA GLU A 96 32.840 6.973 -17.558 1.00 23.60 C
ANISOU 305 CA GLU A 96 2096 2648 4222 201 309 -191 C
ATOM 306 C GLU A 96 31.704 6.090 -17.057 1.00 21.01 C
ANISOU 306 C GLU A 96 1864 2392 3728 216 243 -246 C
ATOM 307 O GLU A 96 31.339 6.132 -15.876 1.00 17.45 O
ANISOU 307 O GLU A 96 1427 1986 3218 215 95 -254 O
ATOM 308 CB GLU A 96 32.253 8.172 -18.304 1.00 23.96 C
ANISOU 308 CB GLU A 96 2159 2705 4238 173 338 -187 C
ATOM 309 CG GLU A 96 33.198 9.324 -18.540 1.00 36.59 C
ANISOU 309 CG GLU A 96 3653 4214 6035 143 364 -118 C
ATOM 310 CD GLU A 96 32.555 10.425 -19.378 1.00 61.03 C
ANISOU 310 CD GLU A 96 6760 7310 9119 126 421 -84 C
ATOM 311 OE1 GLU A 96 32.274 11.504 -18.814 1.00 58.52 O
ANISOU 311 OE1 GLU A 96 6421 6950 8864 99 287 -95 O
ATOM 312 OE2 GLU A 96 32.328 10.219 -20.595 1.00 49.20 O
ANISOU 312 OE2 GLU A 96 5298 5853 7543 146 608 -46 O
ATOM 313 N ILE A 97 31.131 5.288 -17.950 1.00 15.45 N
ANISOU 313 N ILE A 97 1229 1696 2947 229 365 -284 N
ATOM 314 CA ILE A 97 30.042 4.397 -17.571 1.00 14.01 C
ANISOU 314 CA ILE A 97 1117 1552 2653 230 318 -337 C
ATOM 315 C ILE A 97 30.522 3.376 -16.547 1.00 14.22 C
ANISOU 315 C ILE A 97 1108 1540 2754 261 265 -304 C
ATOM 316 O ILE A 97 29.854 3.128 -15.537 1.00 18.07 O
ANISOU 316 O ILE A 97 1607 2079 3180 263 148 -297 O
ATOM 317 CB ILE A 97 29.463 3.721 -18.827 1.00 14.93 C
ANISOU 317 CB ILE A 97 1328 1659 2685 226 475 -416 C
ATOM 318 CG1 ILE A 97 28.917 4.776 -19.794 1.00 12.04 C
ANISOU 318 CG1 ILE A 97 999 1364 2212 204 525 -436 C
ATOM 319 CG2 ILE A 97 28.358 2.772 -18.446 1.00 16.22 C
ANISOU 319 CG2 ILE A 97 1550 1835 2778 206 428 -487 C
ATOM 320 CD1 ILE A 97 28.460 4.188 -21.106 1.00 17.75 C
ANISOU 320 CD1 ILE A 97 1859 2103 2780 191 685 -525 C
ATOM 321 N SER A 98 31.699 2.787 -16.779 1.00 20.23 N
ANISOU 321 N SER A 98 1816 2219 3650 296 360 -269 N
ATOM 322 CA SER A 98 32.215 1.750 -15.886 1.00 24.13 C
ANISOU 322 CA SER A 98 2264 2669 4236 342 324 -222 C
ATOM 323 C SER A 98 32.433 2.274 -14.467 1.00 21.30 C
ANISOU 323 C SER A 98 1847 2385 3861 348 143 -168 C
ATOM 324 O SER A 98 32.216 1.547 -13.486 1.00 18.68 O
ANISOU 324 O SER A 98 1508 2076 3512 384 68 -130 O
ATOM 325 CB SER A 98 33.524 1.187 -16.448 1.00 24.72 C
ANISOU 325 CB SER A 98 2275 2646 4470 389 464 -188 C
ATOM 326 OG SER A 98 33.280 0.356 -17.571 1.00 31.82 O
ANISOU 326 OG SER A 98 3262 3473 5353 406 642 -254 O
ATOM 327 N SER A 99 32.888 3.522 -14.342 1.00 17.12 N
ANISOU 327 N SER A 99 1277 1886 3340 317 80 -165 N
ATOM 328 CA SER A 99 33.090 4.123 -13.025 1.00 17.55 C
ANISOU 328 CA SER A 99 1294 2007 3368 319 -82 -147 C
ATOM 329 C SER A 99 31.787 4.214 -12.246 1.00 17.70 C
ANISOU 329 C SER A 99 1398 2123 3204 316 -174 -171 C
ATOM 330 O SER A 99 31.759 3.957 -11.036 1.00 15.87 O
ANISOU 330 O SER A 99 1145 1959 2926 350 -273 -139 O
ATOM 331 CB SER A 99 33.713 5.505 -13.177 1.00 23.08 C
ANISOU 331 CB SER A 99 1940 2672 4159 274 -121 -166 C
ATOM 332 OG SER A 99 34.857 5.423 -14.005 1.00 34.99 O
ANISOU 332 OG SER A 99 3357 4098 5841 276 -8 -122 O
ATOM 333 N VAL A 100 30.699 4.586 -12.918 1.00 11.82 N
ANISOU 333 N VAL A 100 739 1401 2350 281 -136 -215 N
ATOM 334 CA VAL A 100 29.401 4.654 -12.247 1.00 10.65 C
ANISOU 334 CA VAL A 100 659 1343 2043 278 -202 -227 C
ATOM 335 C VAL A 100 28.919 3.262 -11.876 1.00 10.59 C
ANISOU 335 C VAL A 100 652 1362 2009 312 -183 -178 C
ATOM 336 O VAL A 100 28.378 3.043 -10.785 1.00 13.53 O
ANISOU 336 O VAL A 100 1027 1829 2286 335 -250 -125 O
ATOM 337 CB VAL A 100 28.379 5.384 -13.135 1.00 10.20 C
ANISOU 337 CB VAL A 100 673 1303 1901 238 -170 -277 C
ATOM 338 CG1 VAL A 100 27.013 5.445 -12.440 1.00 12.90 C
ANISOU 338 CG1 VAL A 100 1073 1733 2094 236 -227 -286 C
ATOM 339 CG2 VAL A 100 28.860 6.786 -13.447 1.00 13.89 C
ANISOU 339 CG2 VAL A 100 1125 1726 2426 216 -192 -312 C
ATOM 340 N GLU A 101 29.104 2.296 -12.777 1.00 11.01 N
ANISOU 340 N GLU A 101 693 1314 2176 318 -83 -197 N
ATOM 341 CA GLU A 101 28.684 0.933 -12.488 1.00 15.39 C
ANISOU 341 CA GLU A 101 1234 1827 2785 349 -60 -167 C
ATOM 342 C GLU A 101 29.374 0.409 -11.237 1.00 13.85 C
ANISOU 342 C GLU A 101 980 1662 2620 417 -134 -64 C
ATOM 343 O GLU A 101 28.753 -0.288 -10.425 1.00 15.31 O
ANISOU 343 O GLU A 101 1154 1892 2773 450 -181 2 O
ATOM 344 CB GLU A 101 28.984 0.028 -13.685 1.00 14.68 C
ANISOU 344 CB GLU A 101 1157 1573 2847 344 96 -220 C
ATOM 345 CG GLU A 101 28.109 0.295 -14.915 1.00 14.80 C
ANISOU 345 CG GLU A 101 1240 1582 2800 284 180 -340 C
ATOM 346 CD GLU A 101 28.476 -0.596 -16.098 1.00 31.11 C
ANISOU 346 CD GLU A 101 3374 3499 4946 280 364 -415 C
ATOM 347 OE1 GLU A 101 29.678 -0.887 -16.282 1.00 34.49 O
ANISOU 347 OE1 GLU A 101 3776 3857 5473 325 436 -369 O
ATOM 348 OE2 GLU A 101 27.567 -1.016 -16.842 1.00 26.50 O
ANISOU 348 OE2 GLU A 101 2887 2879 4302 227 434 -532 O
ATOM 349 N GLU A 102 30.657 0.741 -11.059 1.00 14.99 N
ANISOU 349 N GLU A 102 1069 1792 2833 442 -150 -42 N
ATOM 350 CA GLU A 102 31.372 0.239 -9.892 1.00 19.68 C
ANISOU 350 CA GLU A 102 1592 2429 3454 516 -231 48 C
ATOM 351 C GLU A 102 30.939 0.984 -8.638 1.00 21.39 C
ANISOU 351 C GLU A 102 1813 2840 3474 530 -357 72 C
ATOM 352 O GLU A 102 30.795 0.379 -7.570 1.00 21.24 O
ANISOU 352 O GLU A 102 1768 2914 3390 602 -428 148 O
ATOM 353 CB GLU A 102 32.888 0.342 -10.123 1.00 23.59 C
ANISOU 353 CB GLU A 102 1999 2854 4109 535 -212 64 C
ATOM 354 CG GLU A 102 33.850 -0.183 -9.004 1.00 43.37 C
ANISOU 354 CG GLU A 102 4403 5399 6677 620 -307 161 C
ATOM 355 CD GLU A 102 33.670 0.413 -7.597 1.00 61.42 C
ANISOU 355 CD GLU A 102 6667 7875 8793 650 -473 183 C
ATOM 356 OE1 GLU A 102 33.873 -0.327 -6.603 1.00 46.71 O
ANISOU 356 OE1 GLU A 102 4762 6080 6904 740 -552 269 O
ATOM 357 OE2 GLU A 102 33.380 1.628 -7.480 1.00 53.96 O
ANISOU 357 OE2 GLU A 102 5744 6997 7761 587 -527 118 O
ATOM 358 N GLU A 103 30.747 2.301 -8.738 1.00 14.26 N
ANISOU 358 N GLU A 103 936 1968 2512 465 -392 6 N
ATOM 359 CA GLU A 103 30.349 3.070 -7.566 1.00 15.66 C
ANISOU 359 CA GLU A 103 1117 2267 2566 460 -506 16 C
ATOM 360 C GLU A 103 28.968 2.668 -7.069 1.00 21.23 C
ANISOU 360 C GLU A 103 1871 3062 3136 455 -498 84 C
ATOM 361 O GLU A 103 28.759 2.506 -5.861 1.00 21.68 O
ANISOU 361 O GLU A 103 1900 3206 3132 473 -586 177 O
ATOM 362 CB GLU A 103 30.359 4.565 -7.869 1.00 15.91 C
ANISOU 362 CB GLU A 103 1191 2245 2610 399 -544 -111 C
ATOM 363 CG GLU A 103 30.411 5.402 -6.615 1.00 30.12 C
ANISOU 363 CG GLU A 103 2988 4122 4335 412 -683 -152 C
ATOM 364 CD GLU A 103 30.736 6.845 -6.895 1.00 44.56 C
ANISOU 364 CD GLU A 103 4836 5868 6225 380 -729 -292 C
ATOM 365 OE1 GLU A 103 31.688 7.372 -6.270 1.00 29.89 O
ANISOU 365 OE1 GLU A 103 2910 4008 4438 386 -844 -323 O
ATOM 366 OE2 GLU A 103 30.006 7.453 -7.714 1.00 28.09 O
ANISOU 366 OE2 GLU A 103 2826 3723 4122 353 -660 -360 O
ATOM 367 N LEU A 104 28.000 2.540 -7.980 1.00 12.19 N
ANISOU 367 N LEU A 104 789 1872 1969 411 -413 48 N
ATOM 368 CA LEU A 104 26.618 2.291 -7.602 1.00 12.03 C
ANISOU 368 CA LEU A 104 804 1896 1872 379 -421 99 C
ATOM 369 C LEU A 104 26.239 0.817 -7.568 1.00 16.11 C
ANISOU 369 C LEU A 104 1285 2425 2409 420 -379 190 C
ATOM 370 O LEU A 104 25.133 0.503 -7.119 1.00 13.55 O
ANISOU 370 O LEU A 104 983 2047 2118 392 -457 170 O
ATOM 371 CB LEU A 104 25.655 3.000 -8.563 1.00 11.51 C
ANISOU 371 CB LEU A 104 822 1801 1751 324 -374 -21 C
ATOM 372 CG LEU A 104 25.752 4.525 -8.676 1.00 19.98 C
ANISOU 372 CG LEU A 104 1954 2865 2771 322 -402 -162 C
ATOM 373 CD1 LEU A 104 24.611 5.051 -9.529 1.00 9.05 C
ANISOU 373 CD1 LEU A 104 636 1485 1317 291 -351 -229 C
ATOM 374 CD2 LEU A 104 25.735 5.168 -7.307 1.00 20.24 C
ANISOU 374 CD2 LEU A 104 1997 2978 2715 372 -490 -197 C
ATOM 375 N ASN A 105 27.110 -0.078 -8.024 1.00 13.64 N
ANISOU 375 N ASN A 105 2166 1059 1958 370 117 386 N
ATOM 376 CA ASN A 105 26.805 -1.498 -8.212 1.00 12.29 C
ANISOU 376 CA ASN A 105 2101 773 1795 389 270 348 C
ATOM 377 C ASN A 105 25.563 -1.684 -9.083 1.00 12.19 C
ANISOU 377 C ASN A 105 2188 700 1743 320 376 200 C
ATOM 378 O ASN A 105 24.589 -2.339 -8.708 1.00 15.69 O
ANISOU 378 O ASN A 105 2706 1060 2196 229 440 126 O
ATOM 379 CB ASN A 105 26.646 -2.243 -6.890 1.00 13.30 C
ANISOU 379 CB ASN A 105 2280 848 1924 386 276 413 C
ATOM 380 CG ASN A 105 26.559 -3.751 -7.094 1.00 17.64 C
ANISOU 380 CG ASN A 105 2921 1248 2533 414 472 396 C
ATOM 381 OD1 ASN A 105 27.113 -4.290 -8.067 1.00 19.62 O
ANISOU 381 OD1 ASN A 105 3188 1435 2830 463 586 365 O
ATOM 382 ND2 ASN A 105 25.843 -4.437 -6.202 1.00 23.39 N
ANISOU 382 ND2 ASN A 105 3714 1902 3271 386 549 417 N
ATOM 383 N VAL A 106 25.627 -1.116 -10.283 1.00 11.93 N
ANISOU 383 N VAL A 106 2153 709 1669 367 403 155 N
ATOM 384 CA VAL A 106 24.554 -1.232 -11.260 1.00 13.77 C
ANISOU 384 CA VAL A 106 2471 948 1815 297 465 -42 C
ATOM 385 C VAL A 106 25.166 -1.674 -12.572 1.00 24.94 C
ANISOU 385 C VAL A 106 3925 2391 3159 387 566 -140 C
ATOM 386 O VAL A 106 26.376 -1.572 -12.787 1.00 19.21 O
ANISOU 386 O VAL A 106 3181 1626 2492 561 629 9 O
ATOM 387 CB VAL A 106 23.758 0.081 -11.453 1.00 13.98 C
ANISOU 387 CB VAL A 106 2350 1218 1745 256 341 -14 C
ATOM 388 CG1 VAL A 106 23.208 0.548 -10.143 1.00 15.35 C
ANISOU 388 CG1 VAL A 106 2520 1336 1978 192 288 73 C
ATOM 389 CG2 VAL A 106 24.639 1.180 -12.093 1.00 10.75 C
ANISOU 389 CG2 VAL A 106 1823 940 1321 415 322 139 C
ATOM 390 N ASN A 107 24.312 -2.211 -13.432 1.00 16.03 N
ANISOU 390 N ASN A 107 2846 1341 1903 262 587 -403 N
ATOM 391 CA ASN A 107 24.685 -2.594 -14.785 1.00 18.90 C
ANISOU 391 CA ASN A 107 3283 1789 2108 333 678 -565 C
ATOM 392 C ASN A 107 24.001 -1.629 -15.741 1.00 24.54 C
ANISOU 392 C ASN A 107 3858 2900 2567 334 536 -601 C
ATOM 393 O ASN A 107 22.774 -1.491 -15.709 1.00 25.63 O
ANISOU 393 O ASN A 107 3906 3203 2629 160 404 -719 O
ATOM 394 CB ASN A 107 24.289 -4.038 -15.090 1.00 21.91 C
ANISOU 394 CB ASN A 107 3821 1987 2517 173 790 -871 C
ATOM 395 CG ASN A 107 24.752 -4.474 -16.454 1.00 35.26 C
ANISOU 395 CG ASN A 107 5587 3778 4031 251 867 -1041 C
ATOM 396 OD1 ASN A 107 23.951 -4.621 -17.378 1.00 43.29 O
ANISOU 396 OD1 ASN A 107 6612 5016 4822 132 776 -1325 O
ATOM 397 ND2 ASN A 107 26.053 -4.700 -16.589 1.00 34.27 N
ANISOU 397 ND2 ASN A 107 5501 3521 4000 453 1017 -855 N
ATOM 398 N ILE A 108 24.797 -0.933 -16.553 1.00 20.32 N
ANISOU 398 N ILE A 108 3274 2525 1920 554 582 -448 N
ATOM 399 CA ILE A 108 24.296 0.021 -17.536 1.00 21.61 C
ANISOU 399 CA ILE A 108 3301 3083 1824 635 497 -398 C
ATOM 400 C ILE A 108 24.627 -0.425 -18.955 1.00 31.65 C
ANISOU 400 C ILE A 108 4690 4539 2796 758 594 -560 C
ATOM 401 O ILE A 108 23.757 -0.452 -19.831 1.00 31.84 O
ANISOU 401 O ILE A 108 4684 4892 2520 686 479 -744 O
ATOM 402 CB ILE A 108 24.847 1.440 -17.272 1.00 19.72 C
ANISOU 402 CB ILE A 108 2887 2892 1716 813 508 -28 C
ATOM 403 CG1 ILE A 108 24.386 1.937 -15.900 1.00 17.54 C
ANISOU 403 CG1 ILE A 108 2530 2467 1667 679 409 70 C
ATOM 404 CG2 ILE A 108 24.425 2.378 -18.421 1.00 25.12 C
ANISOU 404 CG2 ILE A 108 3436 3973 2135 968 496 90 C
ATOM 405 CD1 ILE A 108 25.025 3.264 -15.457 1.00 23.23 C
ANISOU 405 CD1 ILE A 108 3111 3136 2580 798 438 365 C
ATOM 406 N SER A 109 25.880 -0.785 -19.199 1.00 24.09 N
ANISOU 406 N SER A 109 3836 3379 1938 921 788 -476 N
ATOM 407 CA SER A 109 26.311 -1.316 -20.488 1.00 37.32 C
ANISOU 407 CA SER A 109 5610 5147 3424 984 888 -607 C
ATOM 408 C SER A 109 26.616 -2.800 -20.323 1.00 61.21 C
ANISOU 408 C SER A 109 8830 7855 6572 868 1018 -877 C
ATOM 409 O SER A 109 27.543 -3.172 -19.596 1.00 71.09 O
ANISOU 409 O SER A 109 10108 8780 8122 942 1140 -697 O
ATOM 410 CB SER A 109 27.537 -0.568 -21.008 1.00 49.23 C
ANISOU 410 CB SER A 109 7032 6657 5014 1255 1012 -252 C
ATOM 411 OG SER A 109 28.641 -0.757 -20.137 1.00 46.06 O
ANISOU 411 OG SER A 109 6623 5918 4958 1320 1122 -44 O
ATOM 412 N ASP A 110 25.846 -3.641 -20.999 1.00 69.72 N
ANISOU 412 N ASP A 110 10001 9045 7443 682 978 -1285 N
ATOM 413 CA ASP A 110 25.946 -5.077 -20.792 1.00 73.23 C
ANISOU 413 CA ASP A 110 10596 9165 8062 583 1066 -1534 C
ATOM 414 C ASP A 110 27.113 -5.673 -21.566 1.00 64.47 C
ANISOU 414 C ASP A 110 9614 7928 6956 759 1301 -1516 C
ATOM 415 O ASP A 110 28.049 -6.202 -20.970 1.00 74.02 O
ANISOU 415 O ASP A 110 10882 8784 8460 845 1476 -1309 O
ATOM 416 CB ASP A 110 24.635 -5.748 -21.190 1.00 87.91 C
ANISOU 416 CB ASP A 110 12525 11138 9739 374 870 -1937 C
ATOM 417 CG ASP A 110 23.435 -5.119 -20.504 1.00 83.89 C
ANISOU 417 CG ASP A 110 11905 10740 9230 184 645 -1887 C
ATOM 418 OD1 ASP A 110 22.718 -5.836 -19.772 1.00 83.67 O
ANISOU 418 OD1 ASP A 110 11864 10480 9445 -77 608 -2004 O
ATOM 419 OD2 ASP A 110 23.219 -3.901 -20.692 1.00 75.47 O
ANISOU 419 OD2 ASP A 110 10748 9975 7952 264 556 -1684 O
ATOM 420 N SER A 126 13.482 -5.562 -12.807 1.00 44.41 N
ANISOU 420 N SER A 126 5447 5287 6138 -1712 199 -1629 N
ATOM 421 CA SER A 126 13.561 -4.113 -12.661 1.00 56.68 C
ANISOU 421 CA SER A 126 6877 7126 7533 -1592 99 -1431 C
ATOM 422 C SER A 126 14.178 -3.733 -11.323 1.00 64.65 C
ANISOU 422 C SER A 126 8061 7828 8676 -1394 302 -1118 C
ATOM 423 O SER A 126 15.259 -3.145 -11.271 1.00 59.56 O
ANISOU 423 O SER A 126 7577 7178 7874 -1138 303 -966 O
ATOM 424 CB SER A 126 12.174 -3.470 -12.795 1.00 53.68 C
ANISOU 424 CB SER A 126 6110 7123 7163 -1715 -62 -1354 C
ATOM 425 OG SER A 126 11.836 -3.235 -14.153 1.00 61.59 O
ANISOU 425 OG SER A 126 6939 8590 7871 -1739 -325 -1509 O
ATOM 426 N CYS A 127 13.483 -4.082 -10.244 1.00 61.41 N
ANISOU 426 N CYS A 127 7617 7192 8526 -1450 460 -973 N
ATOM 427 CA CYS A 127 13.852 -3.690 -8.888 1.00 60.97 C
ANISOU 427 CA CYS A 127 7715 6914 8536 -1240 635 -655 C
ATOM 428 C CYS A 127 14.458 -4.896 -8.183 1.00 54.76 C
ANISOU 428 C CYS A 127 7151 5813 7842 -1119 797 -605 C
ATOM 429 O CYS A 127 13.769 -5.898 -7.961 1.00 71.04 O
ANISOU 429 O CYS A 127 9163 7737 10092 -1235 899 -660 O
ATOM 430 CB CYS A 127 12.633 -3.177 -8.123 1.00 64.61 C
ANISOU 430 CB CYS A 127 7977 7442 9131 -1270 706 -450 C
ATOM 431 SG CYS A 127 11.408 -2.323 -9.144 1.00 97.01 S
ANISOU 431 SG CYS A 127 11650 12046 13165 -1398 480 -485 S
ATOM 432 N VAL A 128 15.745 -4.810 -7.846 1.00 25.22 N
ANISOU 432 N VAL A 128 3609 1994 3978 -891 818 -487 N
ATOM 433 CA VAL A 128 16.386 -5.777 -6.963 1.00 27.51 C
ANISOU 433 CA VAL A 128 4037 2092 4322 -736 964 -355 C
ATOM 434 C VAL A 128 17.229 -5.022 -5.941 1.00 20.18 C
ANISOU 434 C VAL A 128 3203 1230 3233 -488 929 -109 C
ATOM 435 O VAL A 128 17.535 -3.840 -6.101 1.00 23.10 O
ANISOU 435 O VAL A 128 3567 1744 3464 -428 800 -68 O
ATOM 436 CB VAL A 128 17.251 -6.810 -7.714 1.00 26.80 C
ANISOU 436 CB VAL A 128 4041 1887 4255 -736 1013 -500 C
ATOM 437 CG1 VAL A 128 16.431 -7.541 -8.785 1.00 30.88 C
ANISOU 437 CG1 VAL A 128 4475 2373 4886 -1002 1012 -811 C
ATOM 438 CG2 VAL A 128 18.461 -6.126 -8.304 1.00 27.63 C
ANISOU 438 CG2 VAL A 128 4218 2103 4179 -597 894 -487 C
ATOM 439 N ALA A 129 17.616 -5.746 -4.889 1.00 21.26 N
ANISOU 439 N ALA A 129 3416 1270 3392 -356 1049 37 N
ATOM 440 CA ALA A 129 18.302 -5.151 -3.749 1.00 19.12 C
ANISOU 440 CA ALA A 129 3213 1096 2956 -159 1000 229 C
ATOM 441 C ALA A 129 19.560 -4.416 -4.180 1.00 25.40 C
ANISOU 441 C ALA A 129 4029 2014 3608 -68 824 232 C
ATOM 442 O ALA A 129 20.320 -4.891 -5.026 1.00 17.28 O
ANISOU 442 O ALA A 129 3012 942 2614 -67 817 164 O
ATOM 443 CB ALA A 129 18.663 -6.236 -2.733 1.00 21.25 C
ANISOU 443 CB ALA A 129 3554 1248 3271 -38 1172 367 C
ATOM 444 N ASN A 130 19.773 -3.244 -3.588 1.00 17.04 N
ANISOU 444 N ASN A 130 2974 1098 2403 7 703 303 N
ATOM 445 CA ASN A 130 20.948 -2.424 -3.860 1.00 19.20 C
ANISOU 445 CA ASN A 130 3236 1482 2576 79 539 314 C
ATOM 446 C ASN A 130 21.196 -1.545 -2.647 1.00 16.62 C
ANISOU 446 C ASN A 130 2955 1249 2112 160 467 399 C
ATOM 447 O ASN A 130 20.317 -0.761 -2.278 1.00 16.46 O
ANISOU 447 O ASN A 130 2944 1266 2042 132 488 381 O
ATOM 448 CB ASN A 130 20.741 -1.567 -5.114 1.00 12.45 C
ANISOU 448 CB ASN A 130 2315 690 1724 7 463 211 C
ATOM 449 CG ASN A 130 21.987 -0.819 -5.518 1.00 16.64 C
ANISOU 449 CG ASN A 130 2810 1308 2203 84 332 232 C
ATOM 450 OD1 ASN A 130 22.361 0.151 -4.867 1.00 18.57 O
ANISOU 450 OD1 ASN A 130 3038 1635 2383 124 243 280 O
ATOM 451 ND2 ASN A 130 22.629 -1.251 -6.601 1.00 13.02 N
ANISOU 451 ND2 ASN A 130 2344 815 1789 99 344 185 N
ATOM 452 N LYS A 131 22.354 -1.731 -2.005 1.00 15.78 N
ANISOU 452 N LYS A 131 2887 1166 1942 262 402 494 N
ATOM 453 CA LYS A 131 22.871 -0.834 -0.972 1.00 22.73 C
ANISOU 453 CA LYS A 131 3839 2137 2659 330 294 552 C
ATOM 454 C LYS A 131 22.518 0.628 -1.124 1.00 25.27 C
ANISOU 454 C LYS A 131 4173 2510 2919 274 225 453 C
ATOM 455 O LYS A 131 21.875 1.233 -0.254 1.00 15.50 O
ANISOU 455 O LYS A 131 3058 1276 1556 290 269 440 O
ATOM 456 CB LYS A 131 24.394 -0.922 -0.932 1.00 29.09 C
ANISOU 456 CB LYS A 131 4604 2998 3449 406 153 646 C
ATOM 457 CG LYS A 131 25.016 -0.642 0.403 1.00 27.04 C
ANISOU 457 CG LYS A 131 4440 2850 2984 509 41 764 C
ATOM 458 CD LYS A 131 24.421 -1.294 1.588 1.00 41.52 C
ANISOU 458 CD LYS A 131 6394 4687 4693 595 160 861 C
ATOM 459 CE LYS A 131 25.524 -1.380 2.621 1.00 55.02 C
ANISOU 459 CE LYS A 131 8127 6574 6203 720 -1 1023 C
ATOM 460 NZ LYS A 131 26.435 -0.206 2.488 1.00 43.22 N
ANISOU 460 NZ LYS A 131 6592 5224 4605 678 -265 956 N
ATOM 461 N ILE A 132 23.022 1.213 -2.202 1.00 14.66 N
ANISOU 461 N ILE A 132 2717 1194 1660 228 140 394 N
ATOM 462 CA ILE A 132 22.933 2.650 -2.363 1.00 12.64 C
ANISOU 462 CA ILE A 132 2466 959 1376 192 86 327 C
ATOM 463 C ILE A 132 21.488 3.058 -2.566 1.00 14.53 C
ANISOU 463 C ILE A 132 2684 1198 1639 143 211 280 C
ATOM 464 O ILE A 132 21.042 4.088 -2.045 1.00 14.07 O
ANISOU 464 O ILE A 132 2707 1122 1517 145 251 251 O
ATOM 465 CB ILE A 132 23.827 3.093 -3.534 1.00 17.34 C
ANISOU 465 CB ILE A 132 2911 1582 2097 178 5 317 C
ATOM 466 CG1 ILE A 132 25.295 3.102 -3.093 1.00 35.00 C
ANISOU 466 CG1 ILE A 132 5165 3821 4314 235 -143 390 C
ATOM 467 CG2 ILE A 132 23.414 4.471 -4.029 1.00 20.70 C
ANISOU 467 CG2 ILE A 132 3285 2008 2571 139 24 266 C
ATOM 468 CD1 ILE A 132 25.605 4.139 -2.037 1.00 47.49 C
ANISOU 468 CD1 ILE A 132 6936 5363 5746 225 -306 362 C
ATOM 469 N LYS A 133 20.734 2.252 -3.320 1.00 13.82 N
ANISOU 469 N LYS A 133 2506 1104 1640 103 283 278 N
ATOM 470 CA LYS A 133 19.326 2.548 -3.540 1.00 10.38 C
ANISOU 470 CA LYS A 133 2029 671 1244 61 391 274 C
ATOM 471 C LYS A 133 18.570 2.596 -2.221 1.00 16.19 C
ANISOU 471 C LYS A 133 2867 1371 1912 97 505 306 C
ATOM 472 O LYS A 133 17.716 3.468 -2.011 1.00 13.44 O
ANISOU 472 O LYS A 133 2509 1032 1564 111 593 312 O
ATOM 473 CB LYS A 133 18.693 1.505 -4.458 1.00 10.73 C
ANISOU 473 CB LYS A 133 2016 668 1393 -19 451 260 C
ATOM 474 CG LYS A 133 17.180 1.674 -4.575 1.00 12.95 C
ANISOU 474 CG LYS A 133 2224 946 1750 -90 575 292 C
ATOM 475 CD LYS A 133 16.590 0.710 -5.572 1.00 21.51 C
ANISOU 475 CD LYS A 133 3234 1970 2970 -256 635 231 C
ATOM 476 CE LYS A 133 16.694 -0.712 -5.065 1.00 31.36 C
ANISOU 476 CE LYS A 133 4543 3085 4286 -282 690 186 C
ATOM 477 NZ LYS A 133 16.111 -1.691 -6.015 1.00 41.13 N
ANISOU 477 NZ LYS A 133 5692 4247 5687 -490 740 35 N
ATOM 478 N ASP A 134 18.869 1.669 -1.315 1.00 15.60 N
ANISOU 478 N ASP A 134 2894 1250 1782 142 535 348 N
ATOM 479 CA ASP A 134 18.145 1.671 -0.055 1.00 15.70 C
ANISOU 479 CA ASP A 134 3028 1226 1713 209 673 397 C
ATOM 480 C ASP A 134 18.515 2.875 0.792 1.00 17.49 C
ANISOU 480 C ASP A 134 3435 1456 1754 276 652 360 C
ATOM 481 O ASP A 134 17.643 3.470 1.433 1.00 17.20 O
ANISOU 481 O ASP A 134 3481 1381 1672 322 795 359 O
ATOM 482 CB ASP A 134 18.384 0.375 0.696 1.00 15.76 C
ANISOU 482 CB ASP A 134 3103 1182 1703 271 738 488 C
ATOM 483 CG ASP A 134 17.569 -0.762 0.121 1.00 35.68 C
ANISOU 483 CG ASP A 134 5507 3622 4426 194 857 509 C
ATOM 484 OD1 ASP A 134 16.370 -0.550 -0.167 1.00 38.00 O
ANISOU 484 OD1 ASP A 134 5713 3898 4828 129 950 497 O
ATOM 485 OD2 ASP A 134 18.123 -1.859 -0.065 1.00 38.36 O
ANISOU 485 OD2 ASP A 134 5842 3900 4834 197 869 538 O
ATOM 486 N GLU A 135 19.793 3.271 0.796 1.00 16.08 N
ANISOU 486 N GLU A 135 3342 1296 1473 282 484 329 N
ATOM 487 CA GLU A 135 20.167 4.472 1.539 1.00 19.25 C
ANISOU 487 CA GLU A 135 3987 1655 1672 308 445 265 C
ATOM 488 C GLU A 135 19.563 5.713 0.904 1.00 18.22 C
ANISOU 488 C GLU A 135 3805 1467 1649 253 545 194 C
ATOM 489 O GLU A 135 19.152 6.638 1.607 1.00 15.91 O
ANISOU 489 O GLU A 135 3731 1076 1238 281 676 144 O
ATOM 490 CB GLU A 135 21.686 4.593 1.635 1.00 21.81 C
ANISOU 490 CB GLU A 135 4398 2029 1862 303 190 256 C
ATOM 491 CG GLU A 135 22.330 3.394 2.321 1.00 35.82 C
ANISOU 491 CG GLU A 135 6146 3919 3543 396 108 369 C
ATOM 492 CD GLU A 135 23.837 3.345 2.143 1.00 50.59 C
ANISOU 492 CD GLU A 135 7949 5899 5372 398 -160 396 C
ATOM 493 OE1 GLU A 135 24.322 3.536 1.005 1.00 46.89 O
ANISOU 493 OE1 GLU A 135 7334 5377 5106 336 -227 384 O
ATOM 494 OE2 GLU A 135 24.537 3.096 3.148 1.00 61.24 O
ANISOU 494 OE2 GLU A 135 9343 7420 6504 471 -302 441 O
ATOM 495 N PHE A 136 19.478 5.731 -0.425 1.00 13.99 N
ANISOU 495 N PHE A 136 2980 1003 1333 192 507 204 N
ATOM 496 CA PHE A 136 18.814 6.816 -1.144 1.00 12.27 C
ANISOU 496 CA PHE A 136 2619 794 1250 180 607 197 C
ATOM 497 C PHE A 136 17.347 6.939 -0.741 1.00 19.32 C
ANISOU 497 C PHE A 136 3499 1675 2168 236 819 239 C
ATOM 498 O PHE A 136 16.870 8.034 -0.416 1.00 18.84 O
ANISOU 498 O PHE A 136 3506 1546 2107 284 984 224 O
ATOM 499 CB PHE A 136 18.975 6.548 -2.649 1.00 15.04 C
ANISOU 499 CB PHE A 136 2706 1244 1763 144 510 235 C
ATOM 500 CG PHE A 136 18.266 7.509 -3.545 1.00 17.10 C
ANISOU 500 CG PHE A 136 2805 1546 2146 174 606 284 C
ATOM 501 CD1 PHE A 136 18.502 8.874 -3.463 1.00 19.83 C
ANISOU 501 CD1 PHE A 136 3168 1830 2538 201 687 268 C
ATOM 502 CD2 PHE A 136 17.400 7.036 -4.520 1.00 14.17 C
ANISOU 502 CD2 PHE A 136 2268 1266 1850 178 628 365 C
ATOM 503 CE1 PHE A 136 17.855 9.755 -4.319 1.00 20.22 C
ANISOU 503 CE1 PHE A 136 3044 1926 2711 275 813 353 C
ATOM 504 CE2 PHE A 136 16.750 7.913 -5.378 1.00 17.77 C
ANISOU 504 CE2 PHE A 136 2556 1796 2401 250 712 462 C
ATOM 505 CZ PHE A 136 16.983 9.270 -5.278 1.00 14.82 C
ANISOU 505 CZ PHE A 136 2177 1370 2082 324 812 461 C
ATOM 506 N PHE A 137 16.611 5.818 -0.744 1.00 13.22 N
ANISOU 506 N PHE A 137 2635 940 1448 233 841 298 N
ATOM 507 CA PHE A 137 15.194 5.860 -0.382 1.00 14.43 C
ANISOU 507 CA PHE A 137 2733 1070 1680 288 1025 365 C
ATOM 508 C PHE A 137 14.983 6.198 1.091 1.00 20.42 C
ANISOU 508 C PHE A 137 3753 1712 2293 394 1188 345 C
ATOM 509 O PHE A 137 13.930 6.730 1.452 1.00 17.65 O
ANISOU 509 O PHE A 137 3391 1302 2013 479 1375 392 O
ATOM 510 CB PHE A 137 14.518 4.525 -0.698 1.00 20.02 C
ANISOU 510 CB PHE A 137 3301 1806 2498 225 1021 437 C
ATOM 511 CG PHE A 137 14.290 4.281 -2.164 1.00 24.21 C
ANISOU 511 CG PHE A 137 3617 2418 3163 124 932 468 C
ATOM 512 CD1 PHE A 137 14.616 5.242 -3.109 1.00 21.91 C
ANISOU 512 CD1 PHE A 137 3236 2202 2888 136 866 468 C
ATOM 513 CD2 PHE A 137 13.761 3.072 -2.593 1.00 33.94 C
ANISOU 513 CD2 PHE A 137 4751 3637 4507 12 948 501 C
ATOM 514 CE1 PHE A 137 14.411 4.995 -4.461 1.00 18.09 C
ANISOU 514 CE1 PHE A 137 2570 1822 2479 61 810 523 C
ATOM 515 CE2 PHE A 137 13.545 2.822 -3.934 1.00 28.54 C
ANISOU 515 CE2 PHE A 137 3892 3030 3922 -117 897 511 C
ATOM 516 CZ PHE A 137 13.870 3.783 -4.869 1.00 21.44 C
ANISOU 516 CZ PHE A 137 2903 2256 2987 -83 829 535 C
ATOM 517 N ALA A 138 15.948 5.890 1.954 1.00 16.95 N
ANISOU 517 N ALA A 138 3566 1228 1648 411 1118 298 N
ATOM 518 CA ALA A 138 15.784 6.232 3.364 1.00 19.38 C
ANISOU 518 CA ALA A 138 4182 1413 1770 522 1246 291 C
ATOM 519 C ALA A 138 15.968 7.725 3.629 1.00 20.50 C
ANISOU 519 C ALA A 138 4551 1400 1839 518 1319 214 C
ATOM 520 O ALA A 138 15.410 8.238 4.603 1.00 22.75 O
ANISOU 520 O ALA A 138 5022 1589 2033 584 1471 241 O
ATOM 521 CB ALA A 138 16.757 5.413 4.220 1.00 20.46 C
ANISOU 521 CB ALA A 138 4494 1602 1677 550 1099 310 C
HETATM 522 N MSE A 139 16.701 8.437 2.767 1.00 19.07 N
ANISOU 522 N MSE A 139 4287 1257 1701 402 1213 158 N
HETATM 523 CA AMSE A 139 16.997 9.857 2.985 0.52 24.89 C
ANISOU 523 CA AMSE A 139 5151 1921 2387 330 1281 77 C
HETATM 524 CA BMSE A 139 17.023 9.858 2.969 0.48 24.90 C
ANISOU 524 CA BMSE A 139 5149 1924 2388 328 1276 74 C
HETATM 525 C MSE A 139 16.191 10.822 2.120 1.00 20.08 C
ANISOU 525 C MSE A 139 4310 1311 2009 335 1497 166 C
HETATM 526 O MSE A 139 15.841 11.918 2.560 1.00 22.15 O
ANISOU 526 O MSE A 139 4666 1447 2303 339 1670 137 O
HETATM 527 CB AMSE A 139 18.495 10.103 2.775 0.52 26.36 C
ANISOU 527 CB AMSE A 139 5317 2164 2536 220 990 -133 C
HETATM 528 CB BMSE A 139 18.507 10.116 2.669 0.48 26.22 C
ANISOU 528 CB BMSE A 139 5277 2146 2537 217 989 -128 C
HETATM 529 CG AMSE A 139 19.357 9.125 3.545 0.52 31.56 C
ANISOU 529 CG AMSE A 139 6134 2932 2925 234 752 -197 C
HETATM 530 CG BMSE A 139 18.881 11.604 2.678 0.48 30.35 C
ANISOU 530 CG BMSE A 139 5772 2580 3181 128 1017 -307 C
HETATM 531 SE AMSE A 139 18.931 9.357 5.437 0.31 57.94 SE
ANISOU 531 SE AMSE A 139 9767 6308 5938 316 833 -286 SE
HETATM 532 SE BMSE A 139 20.762 12.013 2.343 0.45 57.71 SE
ANISOU 532 SE BMSE A 139 9137 6056 6734 -40 669 -560 SE
HETATM 533 CE AMSE A 139 18.957 7.514 6.018 0.52 44.35 C
ANISOU 533 CE AMSE A 139 8058 4748 4044 468 752 -65 C
HETATM 534 CE BMSE A 139 21.538 10.337 2.977 0.48 27.13 C
ANISOU 534 CE BMSE A 139 5419 2379 2508 -8 359 -545 C
ATOM 535 N ILE A 140 15.895 10.420 0.893 1.00 15.32 N
ANISOU 535 N ILE A 140 3299 1260 1262 -14 335 -381 N
ATOM 536 CA ILE A 140 15.254 11.281 -0.093 1.00 14.90 C
ANISOU 536 CA ILE A 140 2943 1361 1357 24 376 -461 C
ATOM 537 C ILE A 140 13.860 10.748 -0.386 1.00 17.56 C
ANISOU 537 C ILE A 140 3246 1708 1719 -62 564 -514 C
ATOM 538 O ILE A 140 13.685 9.546 -0.624 1.00 18.98 O
ANISOU 538 O ILE A 140 3506 1818 1888 -146 595 -520 O
ATOM 539 CB ILE A 140 16.094 11.357 -1.381 1.00 14.23 C
ANISOU 539 CB ILE A 140 2625 1379 1404 101 223 -489 C
ATOM 540 CG1 ILE A 140 17.545 11.706 -1.052 1.00 23.00 C
ANISOU 540 CG1 ILE A 140 3807 2454 2478 148 83 -431 C
ATOM 541 CG2 ILE A 140 15.491 12.331 -2.362 1.00 20.40 C
ANISOU 541 CG2 ILE A 140 3183 2287 2283 142 246 -549 C
ATOM 542 CD1 ILE A 140 17.723 13.127 -0.587 1.00 23.33 C
ANISOU 542 CD1 ILE A 140 3870 2501 2492 157 74 -422 C
ATOM 543 N SER A 141 12.876 11.642 -0.385 1.00 15.54 N
ANISOU 543 N SER A 141 2873 1527 1503 -50 701 -559 N
ATOM 544 CA SER A 141 11.491 11.264 -0.630 1.00 17.43 C
ANISOU 544 CA SER A 141 3026 1804 1793 -151 928 -623 C
ATOM 545 C SER A 141 11.314 10.816 -2.075 1.00 22.85 C
ANISOU 545 C SER A 141 3507 2582 2592 -159 860 -683 C
ATOM 546 O SER A 141 11.579 11.588 -3.003 1.00 20.48 O
ANISOU 546 O SER A 141 3033 2389 2360 -26 724 -685 O
ATOM 547 CB SER A 141 10.573 12.449 -0.332 1.00 17.69 C
ANISOU 547 CB SER A 141 2925 1925 1871 -74 1072 -651 C
ATOM 548 OG SER A 141 9.289 12.269 -0.901 1.00 27.44 O
ANISOU 548 OG SER A 141 3921 3279 3225 -129 1252 -711 O
ATOM 549 N ILE A 142 10.860 9.572 -2.263 1.00 18.29 N
ANISOU 549 N ILE A 142 2987 1946 2015 -343 964 -742 N
ATOM 550 CA ILE A 142 10.474 9.105 -3.594 1.00 20.99 C
ANISOU 550 CA ILE A 142 3134 2384 2458 -412 928 -853 C
ATOM 551 C ILE A 142 9.385 9.995 -4.172 1.00 18.75 C
ANISOU 551 C ILE A 142 2498 2322 2303 -387 1044 -922 C
ATOM 552 O ILE A 142 9.406 10.350 -5.357 1.00 19.19 O
ANISOU 552 O ILE A 142 2337 2521 2433 -313 911 -969 O
ATOM 553 CB ILE A 142 10.012 7.637 -3.538 1.00 26.90 C
ANISOU 553 CB ILE A 142 4033 3006 3183 -681 1034 -939 C
ATOM 554 CG1 ILE A 142 11.195 6.692 -3.335 1.00 25.52 C
ANISOU 554 CG1 ILE A 142 4125 2640 2930 -613 826 -822 C
ATOM 555 CG2 ILE A 142 9.241 7.271 -4.794 1.00 19.24 C
ANISOU 555 CG2 ILE A 142 2767 2193 2349 -808 960 -1020 C
ATOM 556 CD1 ILE A 142 10.808 5.432 -2.582 1.00 40.59 C
ANISOU 556 CD1 ILE A 142 6316 4339 4766 -849 955 -803 C
ATOM 557 N SER A 143 8.411 10.365 -3.340 1.00 19.59 N
ANISOU 557 N SER A 143 2521 2478 2446 -425 1263 -890 N
ATOM 558 CA SER A 143 7.321 11.219 -3.791 1.00 20.36 C
ANISOU 558 CA SER A 143 2243 2786 2706 -339 1308 -875 C
ATOM 559 C SER A 143 7.836 12.554 -4.324 1.00 21.32 C
ANISOU 559 C SER A 143 2317 2940 2843 -67 1123 -811 C
ATOM 560 O SER A 143 7.327 13.066 -5.328 1.00 23.45 O
ANISOU 560 O SER A 143 2305 3371 3234 13 1036 -797 O
ATOM 561 CB SER A 143 6.341 11.435 -2.639 1.00 24.46 C
ANISOU 561 CB SER A 143 2739 3318 3234 -364 1544 -824 C
ATOM 562 OG SER A 143 6.238 10.278 -1.822 1.00 53.96 O
ANISOU 562 OG SER A 143 6687 6939 6878 -615 1713 -836 O
ATOM 563 N ALA A 144 8.842 13.138 -3.665 1.00 17.21 N
ANISOU 563 N ALA A 144 2070 2275 2195 53 1040 -750 N
ATOM 564 CA ALA A 144 9.392 14.403 -4.148 1.00 20.51 C
ANISOU 564 CA ALA A 144 2474 2706 2611 257 884 -686 C
ATOM 565 C ALA A 144 10.038 14.238 -5.517 1.00 19.72 C
ANISOU 565 C ALA A 144 2298 2656 2540 264 705 -684 C
ATOM 566 O ALA A 144 9.896 15.110 -6.384 1.00 20.58 O
ANISOU 566 O ALA A 144 2260 2840 2720 372 638 -638 O
ATOM 567 CB ALA A 144 10.403 14.966 -3.149 1.00 18.64 C
ANISOU 567 CB ALA A 144 2496 2342 2246 312 799 -658 C
ATOM 568 N ILE A 145 10.758 13.131 -5.727 1.00 13.29 N
ANISOU 568 N ILE A 145 1596 1790 1664 152 624 -726 N
ATOM 569 CA ILE A 145 11.417 12.890 -7.014 1.00 16.11 C
ANISOU 569 CA ILE A 145 1894 2209 2019 157 460 -744 C
ATOM 570 C ILE A 145 10.391 12.669 -8.119 1.00 24.74 C
ANISOU 570 C ILE A 145 2677 3521 3200 102 456 -863 C
ATOM 571 O ILE A 145 10.469 13.283 -9.190 1.00 16.34 O
ANISOU 571 O ILE A 145 1470 2590 2147 190 327 -838 O
ATOM 572 CB ILE A 145 12.391 11.699 -6.920 1.00 15.21 C
ANISOU 572 CB ILE A 145 1985 1978 1819 96 374 -737 C
ATOM 573 CG1 ILE A 145 13.524 11.985 -5.929 1.00 25.58 C
ANISOU 573 CG1 ILE A 145 3519 3159 3042 197 302 -621 C
ATOM 574 CG2 ILE A 145 12.939 11.315 -8.305 1.00 13.99 C
ANISOU 574 CG2 ILE A 145 1763 1898 1654 97 244 -763 C
ATOM 575 CD1 ILE A 145 13.914 10.771 -5.125 1.00 31.25 C
ANISOU 575 CD1 ILE A 145 4355 3787 3730 143 263 -655 C
ATOM 576 N VAL A 146 9.438 11.762 -7.888 1.00 23.75 N
ANISOU 576 N VAL A 146 2449 3448 3128 -71 571 -955 N
ATOM 577 CA VAL A 146 8.446 11.432 -8.909 1.00 22.72 C
ANISOU 577 CA VAL A 146 2030 3521 3081 -185 471 -978 C
ATOM 578 C VAL A 146 7.622 12.662 -9.287 1.00 24.17 C
ANISOU 578 C VAL A 146 1899 3890 3393 -26 451 -892 C
ATOM 579 O VAL A 146 7.300 12.874 -10.463 1.00 21.72 O
ANISOU 579 O VAL A 146 1420 3741 3092 -9 253 -852 O
ATOM 580 CB VAL A 146 7.557 10.278 -8.414 1.00 25.48 C
ANISOU 580 CB VAL A 146 2346 3850 3483 -455 586 -1032 C
ATOM 581 CG1 VAL A 146 6.391 10.054 -9.370 1.00 36.31 C
ANISOU 581 CG1 VAL A 146 3362 5464 4971 -603 467 -1051 C
ATOM 582 CG2 VAL A 146 8.385 9.007 -8.242 1.00 22.50 C
ANISOU 582 CG2 VAL A 146 2319 3248 2983 -592 555 -1102 C
ATOM 583 N LYS A 147 7.259 13.485 -8.297 1.00 18.52 N
ANISOU 583 N LYS A 147 1232 3072 2730 98 605 -792 N
ATOM 584 CA LYS A 147 6.566 14.743 -8.573 1.00 20.50 C
ANISOU 584 CA LYS A 147 1320 3382 3086 291 575 -647 C
ATOM 585 C LYS A 147 7.394 15.666 -9.464 1.00 20.53 C
ANISOU 585 C LYS A 147 1407 3358 3037 439 396 -570 C
ATOM 586 O LYS A 147 6.864 16.293 -10.387 1.00 21.84 O
ANISOU 586 O LYS A 147 1395 3627 3275 520 266 -472 O
ATOM 587 CB LYS A 147 6.235 15.455 -7.260 1.00 29.28 C
ANISOU 587 CB LYS A 147 2533 4375 4217 414 799 -589 C
ATOM 588 CG LYS A 147 5.941 16.945 -7.430 1.00 30.80 C
ANISOU 588 CG LYS A 147 2670 4546 4485 667 796 -454 C
ATOM 589 CD LYS A 147 5.671 17.626 -6.100 1.00 38.42 C
ANISOU 589 CD LYS A 147 3772 5451 5377 811 993 -461 C
ATOM 590 CE LYS A 147 5.089 19.018 -6.299 1.00 35.81 C
ANISOU 590 CE LYS A 147 3346 5159 5102 1058 968 -392 C
ATOM 591 NZ LYS A 147 4.658 19.620 -5.006 1.00 59.98 N
ANISOU 591 NZ LYS A 147 6469 8214 8108 1157 1110 -563 N
ATOM 592 N ALA A 148 8.693 15.795 -9.181 1.00 17.32 N
ANISOU 592 N ALA A 148 1276 2799 2506 460 385 -589 N
ATOM 593 CA ALA A 148 9.538 16.641 -10.018 1.00 17.54 C
ANISOU 593 CA ALA A 148 1375 2809 2481 555 239 -511 C
ATOM 594 C ALA A 148 9.573 16.137 -11.456 1.00 15.84 C
ANISOU 594 C ALA A 148 1032 2794 2192 502 49 -533 C
ATOM 595 O ALA A 148 9.525 16.934 -12.402 1.00 18.88 O
ANISOU 595 O ALA A 148 1361 3244 2569 582 -75 -422 O
ATOM 596 CB ALA A 148 10.952 16.711 -9.440 1.00 17.41 C
ANISOU 596 CB ALA A 148 1640 2619 2357 538 254 -520 C
ATOM 597 N ALA A 149 9.670 14.817 -11.641 1.00 14.96 N
ANISOU 597 N ALA A 149 902 2768 2014 356 27 -679 N
ATOM 598 CA ALA A 149 9.739 14.275 -12.994 1.00 15.44 C
ANISOU 598 CA ALA A 149 895 3009 1962 281 -153 -720 C
ATOM 599 C ALA A 149 8.401 14.420 -13.705 1.00 19.52 C
ANISOU 599 C ALA A 149 1195 3669 2551 239 -264 -640 C
ATOM 600 O ALA A 149 8.356 14.679 -14.913 1.00 25.22 O
ANISOU 600 O ALA A 149 1907 4494 3180 246 -429 -566 O
ATOM 601 CB ALA A 149 10.172 12.810 -12.951 1.00 15.03 C
ANISOU 601 CB ALA A 149 976 2914 1822 107 -140 -891 C
ATOM 602 N GLN A 150 7.303 14.257 -12.963 1.00 22.04 N
ANISOU 602 N GLN A 150 1343 3994 3037 191 -166 -640 N
ATOM 603 CA GLN A 150 5.969 14.430 -13.533 1.00 22.59 C
ANISOU 603 CA GLN A 150 1155 4201 3229 165 -274 -544 C
ATOM 604 C GLN A 150 5.789 15.838 -14.085 1.00 23.82 C
ANISOU 604 C GLN A 150 1257 4347 3446 375 -365 -358 C
ATOM 605 O GLN A 150 5.159 16.032 -15.132 1.00 30.57 O
ANISOU 605 O GLN A 150 1977 5322 4316 368 -565 -272 O
ATOM 606 CB GLN A 150 4.926 14.129 -12.453 1.00 33.52 C
ANISOU 606 CB GLN A 150 2354 5581 4801 102 -90 -558 C
ATOM 607 CG GLN A 150 3.493 14.516 -12.749 1.00 46.96 C
ANISOU 607 CG GLN A 150 3727 7408 6707 129 -152 -430 C
ATOM 608 CD GLN A 150 2.508 13.464 -12.252 1.00 58.75 C
ANISOU 608 CD GLN A 150 5023 8988 8311 -102 -63 -492 C
ATOM 609 OE1 GLN A 150 2.875 12.582 -11.472 1.00 65.56 O
ANISOU 609 OE1 GLN A 150 6027 9775 9108 -264 95 -622 O
ATOM 610 NE2 GLN A 150 1.251 13.571 -12.673 1.00 48.52 N
ANISOU 610 NE2 GLN A 150 3397 7834 7205 -128 -163 -389 N
ATOM 611 N LYS A 151 6.329 16.836 -13.391 1.00 28.58 N
ANISOU 611 N LYS A 151 1985 4784 4092 548 -234 -299 N
ATOM 612 CA LYS A 151 6.217 18.222 -13.820 1.00 23.95 C
ANISOU 612 CA LYS A 151 1378 4135 3588 736 -306 -140 C
ATOM 613 C LYS A 151 7.322 18.643 -14.776 1.00 24.36 C
ANISOU 613 C LYS A 151 1626 4182 3447 755 -444 -86 C
ATOM 614 O LYS A 151 7.337 19.801 -15.205 1.00 26.87 O
ANISOU 614 O LYS A 151 1960 4438 3811 893 -522 51 O
ATOM 615 CB LYS A 151 6.231 19.157 -12.613 1.00 22.99 C
ANISOU 615 CB LYS A 151 1320 3804 3612 891 -94 -118 C
ATOM 616 CG LYS A 151 5.048 18.987 -11.690 1.00 39.34 C
ANISOU 616 CG LYS A 151 3185 5879 5881 912 90 -134 C
ATOM 617 CD LYS A 151 5.481 19.174 -10.260 1.00 43.70 C
ANISOU 617 CD LYS A 151 3944 6244 6417 954 360 -194 C
ATOM 618 CE LYS A 151 5.949 20.603 -10.069 1.00 49.01 C
ANISOU 618 CE LYS A 151 4768 6691 7164 1119 377 -168 C
ATOM 619 NZ LYS A 151 7.188 20.676 -9.266 1.00 47.68 N
ANISOU 619 NZ LYS A 151 4930 6348 6840 1068 467 -242 N
ATOM 620 N LYS A 152 8.247 17.742 -15.106 1.00 20.04 N
ANISOU 620 N LYS A 152 1227 3693 2694 626 -462 -190 N
ATOM 621 CA LYS A 152 9.421 18.065 -15.919 1.00 24.87 C
ANISOU 621 CA LYS A 152 2022 4312 3115 636 -530 -144 C
ATOM 622 C LYS A 152 10.227 19.197 -15.287 1.00 21.32 C
ANISOU 622 C LYS A 152 1706 3680 2715 761 -437 -63 C
ATOM 623 O LYS A 152 10.847 20.009 -15.982 1.00 25.16 O
ANISOU 623 O LYS A 152 2282 4158 3121 810 -509 61 O
ATOM 624 CB LYS A 152 9.030 18.404 -17.360 1.00 24.94 C
ANISOU 624 CB LYS A 152 1987 4455 3033 630 -737 -23 C
ATOM 625 CG LYS A 152 8.900 17.175 -18.250 1.00 28.49 C
ANISOU 625 CG LYS A 152 2444 5068 3314 458 -840 -133 C
ATOM 626 CD LYS A 152 7.876 17.412 -19.349 1.00 47.80 C
ANISOU 626 CD LYS A 152 4771 7636 5754 440 -1073 -27 C
ATOM 627 CE LYS A 152 8.413 18.359 -20.408 1.00 49.16 C
ANISOU 627 CE LYS A 152 5082 7824 5771 511 -1186 133 C
ATOM 628 NZ LYS A 152 7.796 18.145 -21.756 1.00 49.94 N
ANISOU 628 NZ LYS A 152 5178 8069 5726 432 -1436 176 N
ATOM 629 N ALA A 153 10.196 19.258 -13.954 1.00 21.04 N
ANISOU 629 N ALA A 153 1701 3491 2803 795 -276 -130 N
ATOM 630 CA ALA A 153 11.011 20.192 -13.179 1.00 16.34 C
ANISOU 630 CA ALA A 153 1271 2695 2244 876 -186 -96 C
ATOM 631 C ALA A 153 12.399 19.575 -13.012 1.00 15.30 C
ANISOU 631 C ALA A 153 1295 2552 1967 786 -160 -177 C
ATOM 632 O ALA A 153 12.803 19.145 -11.932 1.00 17.08 O
ANISOU 632 O ALA A 153 1624 2659 2205 737 -55 -274 O
ATOM 633 CB ALA A 153 10.356 20.482 -11.836 1.00 19.68 C
ANISOU 633 CB ALA A 153 1694 2954 2829 929 -19 -146 C
ATOM 634 N TRP A 154 13.125 19.505 -14.135 1.00 14.43 N
ANISOU 634 N TRP A 154 1200 2573 1710 755 -258 -126 N
ATOM 635 CA TRP A 154 14.356 18.719 -14.157 1.00 13.85 C
ANISOU 635 CA TRP A 154 1209 2539 1514 678 -228 -216 C
ATOM 636 C TRP A 154 15.428 19.325 -13.269 1.00 11.55 C
ANISOU 636 C TRP A 154 1035 2083 1269 704 -170 -197 C
ATOM 637 O TRP A 154 16.289 18.602 -12.760 1.00 10.25 O
ANISOU 637 O TRP A 154 935 1883 1076 644 -124 -293 O
ATOM 638 CB TRP A 154 14.867 18.577 -15.588 1.00 16.46 C
ANISOU 638 CB TRP A 154 1530 3061 1663 637 -304 -160 C
ATOM 639 CG TRP A 154 13.910 17.837 -16.448 1.00 17.86 C
ANISOU 639 CG TRP A 154 1633 3383 1770 580 -378 -212 C
ATOM 640 CD1 TRP A 154 13.289 18.300 -17.569 1.00 27.16 C
ANISOU 640 CD1 TRP A 154 2773 4665 2881 578 -496 -92 C
ATOM 641 CD2 TRP A 154 13.443 16.503 -16.249 1.00 17.32 C
ANISOU 641 CD2 TRP A 154 1531 3355 1696 501 -364 -393 C
ATOM 642 NE1 TRP A 154 12.462 17.333 -18.084 1.00 25.74 N
ANISOU 642 NE1 TRP A 154 2530 4592 2656 492 -565 -192 N
ATOM 643 CE2 TRP A 154 12.541 16.218 -17.292 1.00 26.00 C
ANISOU 643 CE2 TRP A 154 2566 4584 2730 436 -478 -377 C
ATOM 644 CE3 TRP A 154 13.697 15.518 -15.285 1.00 22.58 C
ANISOU 644 CE3 TRP A 154 2226 3946 2408 467 -286 -560 C
ATOM 645 CZ2 TRP A 154 11.897 14.987 -17.406 1.00 19.57 C
ANISOU 645 CZ2 TRP A 154 1718 3818 1901 318 -508 -526 C
ATOM 646 CZ3 TRP A 154 13.055 14.294 -15.399 1.00 25.24 C
ANISOU 646 CZ3 TRP A 154 2541 4318 2730 355 -304 -703 C
ATOM 647 CH2 TRP A 154 12.165 14.041 -16.453 1.00 21.79 C
ANISOU 647 CH2 TRP A 154 2040 4003 2238 273 -409 -685 C
ATOM 648 N LYS A 155 15.400 20.637 -13.054 1.00 19.06 N
ANISOU 648 N LYS A 155 2044 2899 2300 778 -181 -72 N
ATOM 649 CA LYS A 155 16.456 21.188 -12.214 1.00 12.71 C
ANISOU 649 CA LYS A 155 1396 1907 1528 725 -145 -65 C
ATOM 650 C LYS A 155 16.118 20.994 -10.739 1.00 14.15 C
ANISOU 650 C LYS A 155 1674 1918 1786 750 -60 -198 C
ATOM 651 O LYS A 155 17.020 20.785 -9.921 1.00 9.94 O
ANISOU 651 O LYS A 155 1259 1288 1231 669 -54 -258 O
ATOM 652 CB LYS A 155 16.682 22.665 -12.565 1.00 21.34 C
ANISOU 652 CB LYS A 155 2578 2871 2659 748 -193 114 C
ATOM 653 CG LYS A 155 17.832 23.306 -11.819 1.00 18.87 C
ANISOU 653 CG LYS A 155 2425 2368 2378 637 -189 127 C
ATOM 654 CD LYS A 155 18.213 24.632 -12.454 1.00 33.59 C
ANISOU 654 CD LYS A 155 4382 4122 4258 596 -243 328 C
ATOM 655 CE LYS A 155 19.262 25.356 -11.630 1.00 46.28 C
ANISOU 655 CE LYS A 155 6156 5510 5918 446 -262 331 C
ATOM 656 NZ LYS A 155 19.352 26.800 -11.998 1.00 32.37 N
ANISOU 656 NZ LYS A 155 4556 3532 4210 412 -307 514 N
ATOM 657 N GLU A 156 14.826 21.037 -10.388 1.00 11.43 N
ANISOU 657 N GLU A 156 1279 1546 1520 805 6 -224 N
ATOM 658 CA GLU A 156 14.397 20.586 -9.066 1.00 15.55 C
ANISOU 658 CA GLU A 156 1879 1956 2072 728 125 -319 C
ATOM 659 C GLU A 156 14.844 19.152 -8.809 1.00 16.14 C
ANISOU 659 C GLU A 156 1972 2096 2066 593 125 -385 C
ATOM 660 O GLU A 156 15.407 18.841 -7.750 1.00 18.66 O
ANISOU 660 O GLU A 156 2427 2306 2356 505 159 -415 O
ATOM 661 CB GLU A 156 12.880 20.698 -8.957 1.00 24.32 C
ANISOU 661 CB GLU A 156 2859 3085 3297 792 214 -318 C
ATOM 662 CG GLU A 156 12.312 20.220 -7.644 1.00 35.43 C
ANISOU 662 CG GLU A 156 4324 4403 4735 721 378 -406 C
ATOM 663 CD GLU A 156 10.977 20.876 -7.314 1.00 64.52 C
ANISOU 663 CD GLU A 156 7882 8057 8576 822 485 -433 C
ATOM 664 OE1 GLU A 156 10.564 21.809 -8.046 1.00 41.69 O
ANISOU 664 OE1 GLU A 156 4886 5171 5784 966 418 -361 O
ATOM 665 OE2 GLU A 156 10.338 20.455 -6.323 1.00 62.93 O
ANISOU 665 OE2 GLU A 156 7667 7879 8365 763 563 -556 O
ATOM 666 N LEU A 157 14.591 18.256 -9.773 1.00 11.41 N
ANISOU 666 N LEU A 157 1246 1663 1427 573 72 -403 N
ATOM 667 CA LEU A 157 15.010 16.866 -9.624 1.00 9.39 C
ANISOU 667 CA LEU A 157 1031 1423 1115 464 63 -458 C
ATOM 668 C LEU A 157 16.517 16.775 -9.432 1.00 14.05 C
ANISOU 668 C LEU A 157 1710 1964 1663 432 13 -437 C
ATOM 669 O LEU A 157 17.000 16.074 -8.536 1.00 11.85 O
ANISOU 669 O LEU A 157 1530 1591 1383 366 32 -437 O
ATOM 670 CB LEU A 157 14.571 16.055 -10.841 1.00 9.30 C
ANISOU 670 CB LEU A 157 885 1595 1055 457 2 -518 C
ATOM 671 CG LEU A 157 14.291 14.559 -10.659 1.00 23.40 C
ANISOU 671 CG LEU A 157 2691 3370 2831 360 23 -605 C
ATOM 672 CD1 LEU A 157 13.662 14.030 -11.917 1.00 21.74 C
ANISOU 672 CD1 LEU A 157 2327 3373 2562 355 -42 -717 C
ATOM 673 CD2 LEU A 157 15.563 13.781 -10.371 1.00 17.53 C
ANISOU 673 CD2 LEU A 157 2085 2511 2065 315 14 -566 C
ATOM 674 N ALA A 158 17.274 17.525 -10.234 1.00 10.31 N
ANISOU 674 N ALA A 158 1189 1572 1157 497 -45 -414 N
ATOM 675 CA ALA A 158 18.729 17.434 -10.182 1.00 7.99 C
ANISOU 675 CA ALA A 158 914 1286 836 493 -87 -420 C
ATOM 676 C ALA A 158 19.260 17.829 -8.815 1.00 7.84 C
ANISOU 676 C ALA A 158 1035 1098 847 471 -107 -430 C
ATOM 677 O ALA A 158 20.116 17.133 -8.253 1.00 13.22 O
ANISOU 677 O ALA A 158 1750 1753 1521 442 -152 -448 O
ATOM 678 CB ALA A 158 19.362 18.310 -11.269 1.00 9.55 C
ANISOU 678 CB ALA A 158 1017 1610 1002 525 -110 -339 C
ATOM 679 N VAL A 159 18.772 18.942 -8.257 1.00 9.84 N
ANISOU 679 N VAL A 159 1389 1221 1129 494 -87 -417 N
ATOM 680 CA VAL A 159 19.322 19.377 -6.972 1.00 12.32 C
ANISOU 680 CA VAL A 159 1879 1367 1434 430 -124 -429 C
ATOM 681 C VAL A 159 18.990 18.374 -5.888 1.00 16.48 C
ANISOU 681 C VAL A 159 2445 1878 1939 346 -60 -430 C
ATOM 682 O VAL A 159 19.785 18.163 -4.959 1.00 16.23 O
ANISOU 682 O VAL A 159 2512 1789 1866 301 -131 -432 O
ATOM 683 CB VAL A 159 18.848 20.787 -6.575 1.00 9.81 C
ANISOU 683 CB VAL A 159 1696 882 1151 449 -94 -412 C
ATOM 684 CG1 VAL A 159 19.337 21.800 -7.566 1.00 17.46 C
ANISOU 684 CG1 VAL A 159 2622 1843 2169 449 -165 -309 C
ATOM 685 CG2 VAL A 159 17.328 20.872 -6.392 1.00 18.04 C
ANISOU 685 CG2 VAL A 159 2676 1934 2243 490 54 -412 C
ATOM 686 N THR A 160 17.837 17.717 -5.997 1.00 10.48 N
ANISOU 686 N THR A 160 1618 1159 1207 327 52 -434 N
ATOM 687 CA THR A 160 17.439 16.757 -4.969 1.00 21.10 C
ANISOU 687 CA THR A 160 3004 2475 2538 253 114 -466 C
ATOM 688 C THR A 160 18.342 15.524 -4.987 1.00 22.34 C
ANISOU 688 C THR A 160 3177 2651 2659 244 37 -447 C
ATOM 689 O THR A 160 18.878 15.117 -3.947 1.00 21.55 O
ANISOU 689 O THR A 160 3185 2495 2510 235 -16 -443 O
ATOM 690 CB THR A 160 15.969 16.380 -5.157 1.00 17.06 C
ANISOU 690 CB THR A 160 2419 1991 2071 242 237 -510 C
ATOM 691 OG1 THR A 160 15.159 17.560 -5.087 1.00 19.16 O
ANISOU 691 OG1 THR A 160 2644 2240 2395 300 291 -530 O
ATOM 692 CG2 THR A 160 15.501 15.411 -4.055 1.00 22.06 C
ANISOU 692 CG2 THR A 160 3087 2636 2660 231 232 -576 C
ATOM 693 N VAL A 161 18.558 14.932 -6.165 1.00 11.05 N
ANISOU 693 N VAL A 161 1657 1296 1245 272 13 -434 N
ATOM 694 CA VAL A 161 19.404 13.744 -6.199 1.00 15.69 C
ANISOU 694 CA VAL A 161 2254 1886 1822 296 -47 -439 C
ATOM 695 C VAL A 161 20.887 14.106 -6.092 1.00 18.99 C
ANISOU 695 C VAL A 161 2669 2317 2228 387 -194 -444 C
ATOM 696 O VAL A 161 21.675 13.323 -5.552 1.00 19.04 O
ANISOU 696 O VAL A 161 2736 2278 2219 444 -285 -457 O
ATOM 697 CB VAL A 161 19.099 12.893 -7.447 1.00 15.09 C
ANISOU 697 CB VAL A 161 2095 1881 1758 311 -28 -463 C
ATOM 698 CG1 VAL A 161 17.631 12.498 -7.443 1.00 18.66 C
ANISOU 698 CG1 VAL A 161 2577 2308 2205 246 67 -492 C
ATOM 699 CG2 VAL A 161 19.466 13.639 -8.718 1.00 17.03 C
ANISOU 699 CG2 VAL A 161 2210 2255 2006 362 -68 -460 C
ATOM 700 N LEU A 162 21.303 15.295 -6.541 1.00 13.96 N
ANISOU 700 N LEU A 162 1977 1728 1601 418 -244 -458 N
ATOM 701 CA LEU A 162 22.711 15.661 -6.387 1.00 13.29 C
ANISOU 701 CA LEU A 162 1876 1654 1520 480 -411 -512 C
ATOM 702 C LEU A 162 23.059 15.943 -4.933 1.00 19.24 C
ANISOU 702 C LEU A 162 2814 2260 2237 410 -521 -477 C
ATOM 703 O LEU A 162 24.201 15.728 -4.510 1.00 16.57 O
ANISOU 703 O LEU A 162 2461 1926 1908 420 -711 -476 O
ATOM 704 CB LEU A 162 23.061 16.884 -7.241 1.00 20.24 C
ANISOU 704 CB LEU A 162 2616 2631 2444 426 -411 -452 C
ATOM 705 CG LEU A 162 23.114 16.660 -8.756 1.00 22.09 C
ANISOU 705 CG LEU A 162 2645 3061 2688 473 -312 -435 C
ATOM 706 CD1 LEU A 162 23.401 17.969 -9.502 1.00 17.32 C
ANISOU 706 CD1 LEU A 162 1948 2527 2107 381 -300 -316 C
ATOM 707 CD2 LEU A 162 24.152 15.606 -9.100 1.00 23.13 C
ANISOU 707 CD2 LEU A 162 2628 3307 2853 560 -323 -466 C
ATOM 708 N ARG A 163 22.096 16.420 -4.153 1.00 17.18 N
ANISOU 708 N ARG A 163 2683 1911 1932 328 -407 -434 N
ATOM 709 CA ARG A 163 22.357 16.622 -2.736 1.00 15.49 C
ANISOU 709 CA ARG A 163 2654 1586 1644 266 -478 -409 C
ATOM 710 C ARG A 163 22.637 15.289 -2.053 1.00 17.79 C
ANISOU 710 C ARG A 163 3031 1840 1888 312 -541 -389 C
ATOM 711 O ARG A 163 23.520 15.193 -1.192 1.00 22.06 O
ANISOU 711 O ARG A 163 3697 2306 2381 304 -722 -369 O
ATOM 712 CB ARG A 163 21.162 17.321 -2.095 1.00 29.11 C
ANISOU 712 CB ARG A 163 4462 3265 3334 210 -314 -411 C
ATOM 713 CG ARG A 163 21.368 17.732 -0.651 1.00 40.97 C
ANISOU 713 CG ARG A 163 6179 4660 4728 153 -369 -404 C
ATOM 714 CD ARG A 163 20.040 18.103 -0.039 1.00 29.44 C
ANISOU 714 CD ARG A 163 4776 3174 3236 145 -186 -435 C
ATOM 715 NE ARG A 163 19.535 17.010 0.781 1.00 52.21 N
ANISOU 715 NE ARG A 163 7754 6044 6040 140 -128 -419 N
ATOM 716 CZ ARG A 163 18.320 16.490 0.690 1.00 43.75 C
ANISOU 716 CZ ARG A 163 6635 5000 4985 154 28 -438 C
ATOM 717 NH1 ARG A 163 17.484 16.840 -0.279 1.00 38.97 N
ANISOU 717 NH1 ARG A 163 5845 4467 4494 189 121 -477 N
ATOM 718 NH2 ARG A 163 17.940 15.588 1.589 1.00 34.63 N
ANISOU 718 NH2 ARG A 163 5636 3794 3728 123 80 -416 N
ATOM 719 N PHE A 164 21.913 14.240 -2.442 1.00 18.93 N
ANISOU 719 N PHE A 164 3124 2021 2049 343 -419 -391 N
ATOM 720 CA PHE A 164 22.213 12.913 -1.913 1.00 19.63 C
ANISOU 720 CA PHE A 164 3334 2036 2088 402 -497 -374 C
ATOM 721 C PHE A 164 23.590 12.431 -2.361 1.00 21.24 C
ANISOU 721 C PHE A 164 3486 2241 2345 554 -722 -414 C
ATOM 722 O PHE A 164 24.342 11.856 -1.564 1.00 24.30 O
ANISOU 722 O PHE A 164 4027 2517 2689 624 -922 -399 O
ATOM 723 CB PHE A 164 21.131 11.918 -2.329 1.00 21.38 C
ANISOU 723 CB PHE A 164 3507 2281 2336 368 -323 -385 C
ATOM 724 CG PHE A 164 21.481 10.487 -2.023 1.00 23.81 C
ANISOU 724 CG PHE A 164 3958 2487 2600 439 -403 -373 C
ATOM 725 CD1 PHE A 164 21.453 10.016 -0.717 1.00 24.69 C
ANISOU 725 CD1 PHE A 164 4354 2453 2574 425 -468 -315 C
ATOM 726 CD2 PHE A 164 21.840 9.615 -3.036 1.00 25.89 C
ANISOU 726 CD2 PHE A 164 4113 2782 2941 523 -412 -418 C
ATOM 727 CE1 PHE A 164 21.774 8.698 -0.433 1.00 27.55 C
ANISOU 727 CE1 PHE A 164 4903 2687 2878 498 -563 -293 C
ATOM 728 CE2 PHE A 164 22.159 8.296 -2.757 1.00 24.93 C
ANISOU 728 CE2 PHE A 164 4142 2537 2793 601 -481 -414 C
ATOM 729 CZ PHE A 164 22.128 7.840 -1.451 1.00 27.26 C
ANISOU 729 CZ PHE A 164 4731 2672 2954 592 -568 -348 C
ATOM 730 N ALA A 165 23.946 12.662 -3.628 1.00 13.48 N
ANISOU 730 N ALA A 165 2276 1388 1459 621 -707 -482 N
ATOM 731 CA ALA A 165 25.180 12.088 -4.165 1.00 14.20 C
ANISOU 731 CA ALA A 165 2190 1555 1649 782 -847 -513 C
ATOM 732 C ALA A 165 26.415 12.729 -3.538 1.00 28.69 C
ANISOU 732 C ALA A 165 3922 3439 3541 711 -1028 -418 C
ATOM 733 O ALA A 165 27.334 12.028 -3.097 1.00 20.67 O
ANISOU 733 O ALA A 165 2860 2415 2580 779 -1140 -364 O
ATOM 734 CB ALA A 165 25.216 12.239 -5.690 1.00 18.68 C
ANISOU 734 CB ALA A 165 2488 2306 2302 821 -685 -555 C
ATOM 735 N LYS A 166 26.460 14.066 -3.496 1.00 21.07 N
ANISOU 735 N LYS A 166 2917 2519 2571 552 -1039 -387 N
ATOM 736 CA LYS A 166 27.640 14.738 -2.960 1.00 28.31 C
ANISOU 736 CA LYS A 166 3724 3489 3544 437 -1201 -296 C
ATOM 737 C LYS A 166 27.828 14.410 -1.486 1.00 38.06 C
ANISOU 737 C LYS A 166 5203 4578 4680 403 -1354 -264 C
ATOM 738 O LYS A 166 28.964 14.290 -1.008 1.00 51.08 O
ANISOU 738 O LYS A 166 6734 6292 6383 389 -1525 -189 O
ATOM 739 CB LYS A 166 27.535 16.252 -3.170 1.00 38.97 C
ANISOU 739 CB LYS A 166 5056 4860 4891 256 -1191 -284 C
ATOM 740 CG LYS A 166 27.704 16.738 -4.617 1.00 44.30 C
ANISOU 740 CG LYS A 166 5445 5712 5674 253 -1088 -267 C
ATOM 741 CD LYS A 166 28.697 15.901 -5.428 1.00 53.81 C
ANISOU 741 CD LYS A 166 6327 7114 7004 376 -1038 -222 C
ATOM 742 CE LYS A 166 28.523 16.151 -6.928 1.00 59.38 C
ANISOU 742 CE LYS A 166 6829 7979 7752 402 -841 -226 C
ATOM 743 NZ LYS A 166 29.696 15.698 -7.730 1.00 58.09 N
ANISOU 743 NZ LYS A 166 6354 8006 7709 463 -757 -160 N
ATOM 744 N ALA A 167 26.722 14.246 -0.752 1.00 24.18 N
ANISOU 744 N ALA A 167 3770 2643 2774 388 -1277 -304 N
ATOM 745 CA ALA A 167 26.822 13.870 0.653 1.00 27.98 C
ANISOU 745 CA ALA A 167 4513 2984 3132 354 -1392 -260 C
ATOM 746 C ALA A 167 27.523 12.531 0.815 1.00 41.09 C
ANISOU 746 C ALA A 167 6136 4640 4835 498 -1529 -220 C
ATOM 747 O ALA A 167 28.384 12.369 1.688 1.00 50.67 O
ANISOU 747 O ALA A 167 7375 5848 6030 477 -1726 -147 O
ATOM 748 CB ALA A 167 25.429 13.816 1.286 1.00 31.46 C
ANISOU 748 CB ALA A 167 5254 3279 3421 320 -1202 -274 C
ATOM 749 N ASN A 168 27.185 11.567 -0.035 1.00 31.06 N
ANISOU 749 N ASN A 168 4803 3375 3624 655 -1430 -265 N
ATOM 750 CA ASN A 168 27.610 10.190 0.133 1.00 20.68 C
ANISOU 750 CA ASN A 168 3519 2000 2338 811 -1508 -232 C
ATOM 751 C ASN A 168 28.856 9.856 -0.670 1.00 29.22 C
ANISOU 751 C ASN A 168 4217 3257 3627 947 -1546 -190 C
ATOM 752 O ASN A 168 29.157 8.675 -0.870 1.00 35.11 O
ANISOU 752 O ASN A 168 4942 3959 4438 1117 -1541 -178 O
ATOM 753 CB ASN A 168 26.461 9.266 -0.246 1.00 32.92 C
ANISOU 753 CB ASN A 168 5272 3425 3811 882 -1349 -304 C
ATOM 754 CG ASN A 168 25.284 9.427 0.673 1.00 43.12 C
ANISOU 754 CG ASN A 168 6950 4542 4891 750 -1281 -310 C
ATOM 755 OD1 ASN A 168 24.802 10.543 0.881 1.00 46.17 O
ANISOU 755 OD1 ASN A 168 7343 4952 5249 627 -1186 -290 O
ATOM 756 ND2 ASN A 168 24.803 8.321 1.225 1.00 56.54 N
ANISOU 756 ND2 ASN A 168 8921 6104 6458 755 -1266 -287 N
ATOM 757 N GLY A 169 29.586 10.865 -1.133 1.00 33.04 N
ANISOU 757 N GLY A 169 3831 5051 3672 10 -1697 -228 N
ATOM 758 CA GLY A 169 30.821 10.607 -1.848 1.00 38.32 C
ANISOU 758 CA GLY A 169 4213 5818 4529 19 -1735 -125 C
ATOM 759 C GLY A 169 30.630 9.894 -3.163 1.00 42.94 C
ANISOU 759 C GLY A 169 4753 6242 5320 151 -1521 -9 C
ATOM 760 O GLY A 169 31.530 9.178 -3.612 1.00 34.06 O
ANISOU 760 O GLY A 169 3429 5225 4286 259 -1511 136 O
ATOM 761 N LEU A 170 29.467 10.049 -3.786 1.00 24.28 N
ANISOU 761 N LEU A 170 2566 3647 3012 153 -1346 -70 N
ATOM 762 CA LEU A 170 29.250 9.491 -5.113 1.00 20.74 C
ANISOU 762 CA LEU A 170 2087 3061 2733 232 -1149 4 C
ATOM 763 C LEU A 170 29.846 10.483 -6.099 1.00 37.91 C
ANISOU 763 C LEU A 170 4116 5198 5090 111 -1105 -70 C
ATOM 764 O LEU A 170 29.205 11.451 -6.513 1.00 36.56 O
ANISOU 764 O LEU A 170 4030 4876 4984 12 -1044 -171 O
ATOM 765 CB LEU A 170 27.768 9.252 -5.361 1.00 17.45 C
ANISOU 765 CB LEU A 170 1883 2469 2277 262 -1007 -21 C
ATOM 766 CG LEU A 170 27.025 8.355 -4.371 1.00 20.36 C
ANISOU 766 CG LEU A 170 2419 2861 2458 352 -1025 58 C
ATOM 767 CD1 LEU A 170 25.585 8.175 -4.842 1.00 17.60 C
ANISOU 767 CD1 LEU A 170 2224 2366 2098 357 -869 30 C
ATOM 768 CD2 LEU A 170 27.725 6.999 -4.245 1.00 23.49 C
ANISOU 768 CD2 LEU A 170 2744 3315 2864 494 -1036 259 C
ATOM 769 N LYS A 171 31.101 10.255 -6.468 1.00 24.45 N
ANISOU 769 N LYS A 171 2179 3644 3466 136 -1133 0 N
ATOM 770 CA LYS A 171 31.848 11.246 -7.228 1.00 24.91 C
ANISOU 770 CA LYS A 171 2069 3711 3686 -7 -1114 -57 C
ATOM 771 C LYS A 171 31.969 10.917 -8.709 1.00 35.22 C
ANISOU 771 C LYS A 171 3316 4956 5110 66 -908 11 C
ATOM 772 O LYS A 171 32.576 11.695 -9.451 1.00 33.13 O
ANISOU 772 O LYS A 171 2909 4698 4979 -46 -863 -5 O
ATOM 773 CB LYS A 171 33.233 11.439 -6.602 1.00 35.22 C
ANISOU 773 CB LYS A 171 3110 5285 4989 -72 -1300 -62 C
ATOM 774 CG LYS A 171 33.147 12.062 -5.214 1.00 54.32 C
ANISOU 774 CG LYS A 171 5600 7782 7259 -214 -1518 -176 C
ATOM 775 CD LYS A 171 32.760 13.543 -5.319 1.00 65.20 C
ANISOU 775 CD LYS A 171 7084 8966 8722 -457 -1510 -354 C
ATOM 776 CE LYS A 171 33.306 14.373 -4.162 1.00 59.59 C
ANISOU 776 CE LYS A 171 6338 8400 7905 -678 -1738 -517 C
ATOM 777 NZ LYS A 171 32.641 14.051 -2.865 1.00 55.09 N
ANISOU 777 NZ LYS A 171 5980 7894 7058 -615 -1859 -567 N
ATOM 778 N THR A 172 31.385 9.810 -9.168 1.00 20.36 N
ANISOU 778 N THR A 172 1552 3016 3169 230 -777 77 N
ATOM 779 CA THR A 172 31.416 9.508 -10.585 1.00 15.85 C
ANISOU 779 CA THR A 172 960 2388 2673 285 -601 101 C
ATOM 780 C THR A 172 30.465 10.453 -11.322 1.00 19.34 C
ANISOU 780 C THR A 172 1528 2672 3149 162 -500 57 C
ATOM 781 O THR A 172 29.809 11.307 -10.718 1.00 24.29 O
ANISOU 781 O THR A 172 2251 3209 3770 61 -563 -1 O
ATOM 782 CB THR A 172 31.103 8.025 -10.812 1.00 23.59 C
ANISOU 782 CB THR A 172 2039 3339 3586 479 -518 152 C
ATOM 783 OG1 THR A 172 29.848 7.685 -10.207 1.00 21.46 O
ANISOU 783 OG1 THR A 172 1984 2948 3223 465 -515 148 O
ATOM 784 CG2 THR A 172 32.176 7.180 -10.171 1.00 19.79 C
ANISOU 784 CG2 THR A 172 1415 3017 3086 660 -612 218 C
ATOM 785 N ASN A 173 30.435 10.329 -12.647 1.00 17.55 N
ANISOU 785 N ASN A 173 1288 2424 2956 191 -352 83 N
ATOM 786 CA ASN A 173 29.718 11.237 -13.531 1.00 14.82 C
ANISOU 786 CA ASN A 173 1015 1980 2636 107 -255 83 C
ATOM 787 C ASN A 173 28.328 11.577 -13.005 1.00 17.02 C
ANISOU 787 C ASN A 173 1483 2138 2846 77 -276 36 C
ATOM 788 O ASN A 173 27.486 10.699 -12.844 1.00 10.55 O
ANISOU 788 O ASN A 173 784 1302 1924 136 -255 17 O
ATOM 789 CB ASN A 173 29.612 10.605 -14.913 1.00 18.99 C
ANISOU 789 CB ASN A 173 1549 2544 3121 188 -109 109 C
ATOM 790 CG ASN A 173 29.090 11.566 -15.941 1.00 27.51 C
ANISOU 790 CG ASN A 173 2658 3582 4212 125 -13 148 C
ATOM 791 OD1 ASN A 173 27.908 11.909 -15.944 1.00 17.39 O
ANISOU 791 OD1 ASN A 173 1512 2224 2870 106 -7 137 O
ATOM 792 ND2 ASN A 173 29.973 12.025 -16.818 1.00 25.99 N
ANISOU 792 ND2 ASN A 173 2319 3457 4099 101 71 211 N
ATOM 793 N ALA A 174 28.089 12.865 -12.742 1.00 12.85 N
ANISOU 793 N ALA A 174 957 1509 2417 -17 -320 15 N
ATOM 794 CA ALA A 174 26.879 13.255 -12.028 1.00 12.47 C
ANISOU 794 CA ALA A 174 1048 1349 2340 -14 -368 -55 C
ATOM 795 C ALA A 174 25.636 13.095 -12.886 1.00 9.44 C
ANISOU 795 C ALA A 174 762 955 1870 31 -242 -27 C
ATOM 796 O ALA A 174 24.534 12.929 -12.351 1.00 10.35 O
ANISOU 796 O ALA A 174 976 1058 1897 56 -254 -80 O
ATOM 797 CB ALA A 174 27.004 14.703 -11.554 1.00 13.54 C
ANISOU 797 CB ALA A 174 1156 1365 2624 -116 -454 -111 C
ATOM 798 N ILE A 175 25.779 13.197 -14.210 1.00 8.43 N
ANISOU 798 N ILE A 175 592 876 1736 37 -128 54 N
ATOM 799 CA ILE A 175 24.622 13.042 -15.084 1.00 5.91 C
ANISOU 799 CA ILE A 175 348 613 1283 78 -40 77 C
ATOM 800 C ILE A 175 24.156 11.597 -15.086 1.00 8.76 C
ANISOU 800 C ILE A 175 767 1050 1513 119 -37 31 C
ATOM 801 O ILE A 175 22.959 11.312 -14.997 1.00 7.90 O
ANISOU 801 O ILE A 175 723 968 1308 132 -29 6 O
ATOM 802 CB ILE A 175 24.972 13.523 -16.500 1.00 6.75 C
ANISOU 802 CB ILE A 175 387 761 1415 90 56 177 C
ATOM 803 CG1 ILE A 175 25.420 14.980 -16.451 1.00 14.40 C
ANISOU 803 CG1 ILE A 175 1260 1564 2646 34 77 289 C
ATOM 804 CG2 ILE A 175 23.747 13.366 -17.419 1.00 12.91 C
ANISOU 804 CG2 ILE A 175 1227 1626 2054 144 108 196 C
ATOM 805 CD1 ILE A 175 26.129 15.427 -17.712 1.00 22.20 C
ANISOU 805 CD1 ILE A 175 2151 2594 3690 36 194 442 C
ATOM 806 N ILE A 176 25.096 10.660 -15.190 1.00 9.25 N
ANISOU 806 N ILE A 176 782 1145 1587 150 -38 26 N
ATOM 807 CA ILE A 176 24.740 9.251 -15.139 1.00 5.45 C
ANISOU 807 CA ILE A 176 352 688 1032 199 -30 -9 C
ATOM 808 C ILE A 176 24.186 8.903 -13.766 1.00 10.65 C
ANISOU 808 C ILE A 176 1080 1289 1677 178 -97 -36 C
ATOM 809 O ILE A 176 23.154 8.234 -13.642 1.00 6.32 O
ANISOU 809 O ILE A 176 594 736 1070 177 -81 -58 O
ATOM 810 CB ILE A 176 25.965 8.381 -15.484 1.00 8.13 C
ANISOU 810 CB ILE A 176 616 1065 1409 282 -9 -2 C
ATOM 811 CG1 ILE A 176 26.522 8.771 -16.857 1.00 7.71 C
ANISOU 811 CG1 ILE A 176 472 1097 1360 307 68 3 C
ATOM 812 CG2 ILE A 176 25.573 6.894 -15.499 1.00 9.06 C
ANISOU 812 CG2 ILE A 176 810 1149 1483 359 21 -32 C
ATOM 813 CD1 ILE A 176 27.703 7.933 -17.269 1.00 12.17 C
ANISOU 813 CD1 ILE A 176 940 1717 1966 413 107 -19 C
ATOM 814 N VAL A 177 24.875 9.336 -12.709 1.00 5.88 N
ANISOU 814 N VAL A 177 452 660 1124 170 -179 -36 N
ATOM 815 CA VAL A 177 24.393 9.049 -11.360 1.00 6.19 C
ANISOU 815 CA VAL A 177 560 680 1111 181 -250 -55 C
ATOM 816 C VAL A 177 22.977 9.586 -11.168 1.00 6.48 C
ANISOU 816 C VAL A 177 667 711 1083 151 -223 -90 C
ATOM 817 O VAL A 177 22.078 8.865 -10.706 1.00 7.34 O
ANISOU 817 O VAL A 177 832 824 1131 173 -215 -89 O
ATOM 818 CB VAL A 177 25.365 9.611 -10.309 1.00 8.66 C
ANISOU 818 CB VAL A 177 826 1004 1462 182 -375 -60 C
ATOM 819 CG1 VAL A 177 24.748 9.530 -8.912 1.00 14.11 C
ANISOU 819 CG1 VAL A 177 1615 1682 2065 206 -483 -97 C
ATOM 820 CG2 VAL A 177 26.708 8.847 -10.380 1.00 8.54 C
ANISOU 820 CG2 VAL A 177 701 1056 1489 248 -404 3 C
ATOM 821 N ALA A 178 22.751 10.857 -11.516 1.00 6.20 N
ANISOU 821 N ALA A 178 614 660 1082 122 -209 -107 N
ATOM 822 CA ALA A 178 21.419 11.427 -11.341 1.00 7.03 C
ANISOU 822 CA ALA A 178 758 781 1131 137 -176 -124 C
ATOM 823 C ALA A 178 20.387 10.652 -12.141 1.00 8.19 C
ANISOU 823 C ALA A 178 906 998 1209 140 -92 -88 C
ATOM 824 O ALA A 178 19.258 10.442 -11.681 1.00 4.58 O
ANISOU 824 O ALA A 178 464 577 700 159 -63 -91 O
ATOM 825 CB ALA A 178 21.404 12.894 -11.769 1.00 4.87 C
ANISOU 825 CB ALA A 178 455 458 937 138 -162 -121 C
ATOM 826 N GLY A 179 20.748 10.243 -13.352 1.00 6.37 N
ANISOU 826 N GLY A 179 642 790 988 130 -58 -63 N
ATOM 827 CA GLY A 179 19.819 9.460 -14.147 1.00 6.96 C
ANISOU 827 CA GLY A 179 706 925 1014 126 -16 -62 C
ATOM 828 C GLY A 179 19.435 8.160 -13.468 1.00 6.58 C
ANISOU 828 C GLY A 179 676 857 969 118 -24 -111 C
ATOM 829 O GLY A 179 18.272 7.758 -13.495 1.00 6.69 O
ANISOU 829 O GLY A 179 646 940 955 86 4 -166 O
ATOM 830 N GLN A 180 20.417 7.468 -12.878 1.00 5.11 N
ANISOU 830 N GLN A 180 524 587 833 146 -59 -112 N
ATOM 831 CA GLN A 180 20.124 6.212 -12.202 1.00 4.49 C
ANISOU 831 CA GLN A 180 520 392 795 168 -63 -140 C
ATOM 832 C GLN A 180 19.279 6.440 -10.956 1.00 7.26 C
ANISOU 832 C GLN A 180 939 768 1050 135 -67 -103 C
ATOM 833 O GLN A 180 18.384 5.639 -10.644 1.00 8.07 O
ANISOU 833 O GLN A 180 1108 856 1103 39 7 -82 O
ATOM 834 CB GLN A 180 21.425 5.492 -11.842 1.00 5.65 C
ANISOU 834 CB GLN A 180 716 466 965 230 -84 -71 C
ATOM 835 CG GLN A 180 21.204 4.171 -11.089 1.00 6.29 C
ANISOU 835 CG GLN A 180 949 375 1066 251 -64 -22 C
ATOM 836 CD GLN A 180 20.541 3.106 -11.945 1.00 7.98 C
ANISOU 836 CD GLN A 180 1258 463 1312 167 24 -107 C
ATOM 837 OE1 GLN A 180 19.340 2.845 -11.823 1.00 16.36 O
ANISOU 837 OE1 GLN A 180 2360 1503 2354 6 90 -135 O
ATOM 838 NE2 GLN A 180 21.307 2.501 -12.816 1.00 8.53 N
ANISOU 838 NE2 GLN A 180 1340 505 1395 234 42 -150 N
ATOM 839 N LEU A 181 19.567 7.504 -10.205 1.00 6.11 N
ANISOU 839 N LEU A 181 789 665 869 195 -137 -97 N
ATOM 840 CA LEU A 181 18.771 7.766 -9.010 1.00 7.88 C
ANISOU 840 CA LEU A 181 1099 946 951 187 -112 -82 C
ATOM 841 C LEU A 181 17.322 8.066 -9.382 1.00 8.39 C
ANISOU 841 C LEU A 181 1084 1132 971 135 14 -102 C
ATOM 842 O LEU A 181 16.387 7.585 -8.727 1.00 7.54 O
ANISOU 842 O LEU A 181 1010 1088 768 77 107 -61 O
ATOM 843 CB LEU A 181 19.382 8.924 -8.215 1.00 7.42 C
ANISOU 843 CB LEU A 181 1074 895 850 255 -217 -134 C
ATOM 844 CG LEU A 181 20.757 8.614 -7.585 1.00 12.74 C
ANISOU 844 CG LEU A 181 1784 1524 1531 295 -382 -106 C
ATOM 845 CD1 LEU A 181 21.354 9.876 -6.952 1.00 13.87 C
ANISOU 845 CD1 LEU A 181 1932 1678 1658 290 -488 -208 C
ATOM 846 CD2 LEU A 181 20.682 7.473 -6.556 1.00 13.68 C
ANISOU 846 CD2 LEU A 181 2046 1648 1505 323 -391 8 C
ATOM 847 N ALA A 182 17.115 8.867 -10.433 1.00 4.99 N
ANISOU 847 N ALA A 182 527 763 607 163 24 -139 N
ATOM 848 CA ALA A 182 15.748 9.184 -10.856 1.00 7.06 C
ANISOU 848 CA ALA A 182 679 1172 831 141 108 -127 C
ATOM 849 C ALA A 182 15.021 7.936 -11.336 1.00 9.02 C
ANISOU 849 C ALA A 182 860 1501 1067 -10 158 -132 C
ATOM 850 O ALA A 182 13.831 7.745 -11.049 1.00 11.34 O
ANISOU 850 O ALA A 182 1106 1881 1321 -72 213 -99 O
ATOM 851 CB ALA A 182 15.779 10.239 -11.969 1.00 9.89 C
ANISOU 851 CB ALA A 182 1029 1477 1252 158 67 -84 C
ATOM 852 N LEU A 183 15.723 7.072 -12.074 1.00 9.05 N
ANISOU 852 N LEU A 183 900 1409 1131 -78 120 -171 N
ATOM 853 CA LEU A 183 15.129 5.819 -12.533 1.00 7.34 C
ANISOU 853 CA LEU A 183 678 1187 922 -266 159 -218 C
ATOM 854 C LEU A 183 14.709 4.950 -11.356 1.00 13.31 C
ANISOU 854 C LEU A 183 1545 1846 1667 -377 237 -146 C
ATOM 855 O LEU A 183 13.595 4.414 -11.326 1.00 13.61 O
ANISOU 855 O LEU A 183 1506 1972 1695 -555 310 -144 O
ATOM 856 CB LEU A 183 16.124 5.066 -13.417 1.00 11.59 C
ANISOU 856 CB LEU A 183 1304 1572 1527 -269 124 -296 C
ATOM 857 CG LEU A 183 15.652 3.699 -13.910 1.00 13.11 C
ANISOU 857 CG LEU A 183 1561 1674 1745 -466 164 -393 C
ATOM 858 CD1 LEU A 183 14.424 3.838 -14.794 1.00 14.75 C
ANISOU 858 CD1 LEU A 183 1626 2119 1860 -538 145 -432 C
ATOM 859 CD2 LEU A 183 16.773 3.016 -14.671 1.00 11.01 C
ANISOU 859 CD2 LEU A 183 1416 1236 1533 -378 155 -462 C
ATOM 860 N TRP A 184 15.591 4.817 -10.363 1.00 8.81 N
ANISOU 860 N TRP A 184 1142 1118 1089 -274 217 -66 N
ATOM 861 CA TRP A 184 15.263 4.016 -9.189 1.00 8.84 C
ANISOU 861 CA TRP A 184 1280 1037 1041 -348 300 56 C
ATOM 862 C TRP A 184 13.987 4.514 -8.532 1.00 16.45 C
ANISOU 862 C TRP A 184 2134 2221 1894 -404 414 100 C
ATOM 863 O TRP A 184 13.091 3.727 -8.210 1.00 17.42 O
ANISOU 863 O TRP A 184 2242 2360 2015 -590 541 172 O
ATOM 864 CB TRP A 184 16.421 4.057 -8.202 1.00 8.60 C
ANISOU 864 CB TRP A 184 1417 894 958 -177 220 148 C
ATOM 865 CG TRP A 184 17.469 3.025 -8.432 1.00 10.92 C
ANISOU 865 CG TRP A 184 1840 946 1363 -130 172 188 C
ATOM 866 CD1 TRP A 184 17.354 1.866 -9.149 1.00 16.92 C
ANISOU 866 CD1 TRP A 184 2668 1510 2253 -245 240 158 C
ATOM 867 CD2 TRP A 184 18.799 3.050 -7.914 1.00 9.31 C
ANISOU 867 CD2 TRP A 184 1710 671 1156 62 46 258 C
ATOM 868 NE1 TRP A 184 18.546 1.168 -9.108 1.00 16.62 N
ANISOU 868 NE1 TRP A 184 2738 1277 2300 -88 182 211 N
ATOM 869 CE2 TRP A 184 19.446 1.882 -8.359 1.00 14.49 C
ANISOU 869 CE2 TRP A 184 2456 1096 1953 103 61 292 C
ATOM 870 CE3 TRP A 184 19.504 3.948 -7.107 1.00 12.68 C
ANISOU 870 CE3 TRP A 184 2122 1221 1476 198 -89 279 C
ATOM 871 CZ2 TRP A 184 20.754 1.589 -8.016 1.00 14.84 C
ANISOU 871 CZ2 TRP A 184 2454 1135 2048 275 -46 356 C
ATOM 872 CZ3 TRP A 184 20.806 3.664 -6.786 1.00 13.96 C
ANISOU 872 CZ3 TRP A 184 2293 1337 1676 344 -218 344 C
ATOM 873 CH2 TRP A 184 21.420 2.495 -7.236 1.00 15.66 C
ANISOU 873 CH2 TRP A 184 2492 1408 2048 377 -176 391 C
ATOM 874 N ALA A 185 13.878 5.829 -8.347 1.00 12.76 N
ANISOU 874 N ALA A 185 1581 1914 1352 -244 393 60 N
ATOM 875 CA ALA A 185 12.694 6.392 -7.703 1.00 16.90 C
ANISOU 875 CA ALA A 185 2004 2627 1789 -212 510 90 C
ATOM 876 C ALA A 185 11.422 6.052 -8.474 1.00 20.02 C
ANISOU 876 C ALA A 185 2206 3108 2294 -325 527 81 C
ATOM 877 O ALA A 185 10.414 5.655 -7.877 1.00 21.53 O
ANISOU 877 O ALA A 185 2343 3364 2474 -396 639 150 O
ATOM 878 CB ALA A 185 12.842 7.910 -7.559 1.00 13.51 C
ANISOU 878 CB ALA A 185 1569 2228 1336 0 458 12 C
ATOM 879 N VAL A 186 11.451 6.180 -9.802 1.00 16.93 N
ANISOU 879 N VAL A 186 1719 2734 1980 -341 413 0 N
ATOM 880 CA VAL A 186 10.228 5.993 -10.585 1.00 22.46 C
ANISOU 880 CA VAL A 186 2254 3564 2716 -426 390 -21 C
ATOM 881 C VAL A 186 9.898 4.516 -10.744 1.00 30.87 C
ANISOU 881 C VAL A 186 3322 4572 3833 -682 421 -33 C
ATOM 882 O VAL A 186 8.746 4.093 -10.571 1.00 30.40 O
ANISOU 882 O VAL A 186 3139 4611 3801 -804 481 1 O
ATOM 883 CB VAL A 186 10.349 6.686 -11.954 1.00 24.05 C
ANISOU 883 CB VAL A 186 2405 3820 2912 -335 261 -82 C
ATOM 884 CG1 VAL A 186 9.273 6.165 -12.909 1.00 23.91 C
ANISOU 884 CG1 VAL A 186 2243 3961 2880 -469 222 -123 C
ATOM 885 CG2 VAL A 186 10.234 8.193 -11.800 1.00 17.60 C
ANISOU 885 CG2 VAL A 186 1581 3026 2079 -120 252 -42 C
ATOM 886 N GLN A 187 10.891 3.704 -11.092 1.00 25.36 N
ANISOU 886 N GLN A 187 2775 3685 3174 -772 389 -87 N
ATOM 887 CA GLN A 187 10.600 2.308 -11.386 1.00 28.32 C
ANISOU 887 CA GLN A 187 3206 3923 3630 -1003 408 -124 C
ATOM 888 C GLN A 187 10.525 1.437 -10.137 1.00 41.26 C
ANISOU 888 C GLN A 187 4970 5393 5313 -1108 537 21 C
ATOM 889 O GLN A 187 9.874 0.387 -10.175 1.00 43.49 O
ANISOU 889 O GLN A 187 5251 5588 5684 -1310 579 32 O
ATOM 890 CB GLN A 187 11.623 1.767 -12.398 1.00 39.18 C
ANISOU 890 CB GLN A 187 4720 5123 5044 -1010 333 -255 C
ATOM 891 CG GLN A 187 12.968 1.327 -11.847 1.00 50.12 C
ANISOU 891 CG GLN A 187 6340 6220 6484 -936 362 -209 C
ATOM 892 CD GLN A 187 13.806 0.563 -12.873 1.00 62.39 C
ANISOU 892 CD GLN A 187 8019 7584 8102 -913 311 -338 C
ATOM 893 OE1 GLN A 187 14.892 0.067 -12.558 1.00 40.01 O
ANISOU 893 OE1 GLN A 187 5363 4506 5332 -800 319 -296 O
ATOM 894 NE2 GLN A 187 13.283 0.434 -14.094 1.00 36.56 N
ANISOU 894 NE2 GLN A 187 4653 4441 4798 -990 258 -481 N
ATOM 895 N CYS A 188 11.125 1.860 -9.024 1.00 25.91 N
ANISOU 895 N CYS A 188 3140 3412 3292 -974 601 147 N
ATOM 896 CA CYS A 188 11.103 1.075 -7.799 1.00 29.21 C
ANISOU 896 CA CYS A 188 3707 3694 3697 -1025 720 332 C
ATOM 897 C CYS A 188 10.298 1.717 -6.680 1.00 38.80 C
ANISOU 897 C CYS A 188 4822 5130 4788 -941 845 462 C
ATOM 898 O CYS A 188 10.104 1.081 -5.639 1.00 42.72 O
ANISOU 898 O CYS A 188 5413 5575 5245 -979 962 644 O
ATOM 899 CB CYS A 188 12.534 0.817 -7.304 1.00 35.93 C
ANISOU 899 CB CYS A 188 4832 4307 4513 -894 683 408 C
ATOM 900 SG CYS A 188 13.663 0.294 -8.620 1.00 48.08 S
ANISOU 900 SG CYS A 188 6478 5590 6201 -868 556 240 S
ATOM 901 N GLY A 189 9.825 2.947 -6.861 1.00 31.78 N
ANISOU 901 N GLY A 189 3765 4470 3840 -796 833 380 N
ATOM 902 CA GLY A 189 9.055 3.622 -5.832 1.00 35.00 C
ANISOU 902 CA GLY A 189 4118 5040 4141 -668 980 453 C
ATOM 903 C GLY A 189 7.567 3.344 -5.904 1.00 41.40 C
ANISOU 903 C GLY A 189 4704 5983 5042 -800 1094 481 C
ATOM 904 O GLY A 189 6.946 3.511 -6.955 1.00 49.55 O
ANISOU 904 O GLY A 189 5538 7116 6171 -864 998 377 O
TER 905 GLY A 189
HETATM 906 O HOH A 201 28.103 20.249 -7.169 1.00 45.94 O
HETATM 907 O HOH A 202 8.565 19.427 -8.012 1.00 44.49 O
HETATM 908 O HOH A 203 17.458 -3.780 -11.450 1.00 41.95 O
HETATM 909 O HOH A 204 28.561 1.639 -24.093 1.00 36.00 O
HETATM 910 O HOH A 205 20.972 29.621 -12.048 1.00 25.54 O
HETATM 911 O HOH A 206 20.485 20.898 -1.346 1.00 47.00 O
HETATM 912 O HOH A 207 21.194 16.666 2.557 1.00 47.73 O
HETATM 913 O HOH A 208 20.006 -0.999 -23.366 1.00 42.58 O
HETATM 914 O HOH A 209 17.335 -2.272 -2.407 1.00 30.38 O
HETATM 915 O HOH A 210 11.443 2.938 -22.792 1.00 38.67 O
HETATM 916 O HOH A 211 11.340 19.660 -20.797 1.00 34.71 O
HETATM 917 O HOH A 212 9.996 17.369 -22.915 1.00 25.54 O
HETATM 918 O HOH A 213 17.041 -0.980 -24.797 1.00 47.31 O
HETATM 919 O HOH A 214 31.735 -2.520 -15.990 1.00 45.14 O
HETATM 920 O HOH A 215 20.880 0.612 -14.627 1.00 24.85 O
HETATM 921 O HOH A 216 29.409 4.287 -24.686 1.00 23.14 O
HETATM 922 O HOH A 217 21.154 -7.391 -5.530 1.00 27.91 O
HETATM 923 O HOH A 218 5.362 19.206 -22.179 1.00 47.90 O
HETATM 924 O HOH A 219 21.981 -3.813 -7.321 1.00 45.86 O
HETATM 925 O HOH A 220 24.963 -0.296 -4.063 1.00 20.61 O
HETATM 926 O HOH A 221 13.039 10.071 -23.481 1.00 31.66 O
HETATM 927 O HOH A 222 24.313 17.793 -19.992 1.00 25.54 O
HETATM 928 O HOH A 223 33.832 4.140 -9.174 1.00 25.82 O
HETATM 929 O HOH A 224 12.268 -6.825 -10.632 1.00 53.11 O
HETATM 930 O HOH A 225 15.108 2.548 2.244 1.00 24.18 O
HETATM 931 O HOH A 226 11.579 0.892 -17.178 1.00 31.26 O
HETATM 932 O HOH A 227 17.746 0.307 -12.498 1.00 27.74 O
HETATM 933 O HOH A 228 7.954 -1.696 -10.613 1.00 46.96 O
HETATM 934 O HOH A 229 11.538 7.721 -0.061 1.00 28.39 O
HETATM 935 O HOH A 230 2.269 18.069 -4.603 1.00 46.65 O
HETATM 936 O HOH A 231 31.447 20.078 -11.162 1.00 55.66 O
HETATM 937 O HOH A 232 32.876 11.016 -16.001 1.00 53.50 O
HETATM 938 O HOH A 233 32.244 8.509 -14.039 1.00 34.17 O
HETATM 939 O HOH A 234 21.996 22.084 -25.741 1.00 39.88 O
HETATM 940 O HOH A 235 22.443 14.211 -26.523 1.00 45.59 O
HETATM 941 O HOH A 236 14.013 -3.867 -23.533 1.00 50.35 O
HETATM 942 O HOH A 237 11.667 21.205 -18.537 1.00 50.64 O
HETATM 943 O HOH A 238 9.167 17.835 -5.555 1.00 37.66 O
HETATM 944 O HOH A 239 15.021 3.774 -25.659 1.00 47.11 O
HETATM 945 O HOH A 240 12.580 16.851 -6.335 1.00 44.01 O
HETATM 946 O HOH A 241 7.668 6.026 -16.377 1.00 40.18 O
HETATM 947 O HOH A 242 22.962 25.136 -7.573 1.00 27.48 O
HETATM 948 O HOH A 243 27.960 27.732 -13.292 1.00 48.80 O
HETATM 949 O HOH A 244 16.385 -4.483 -14.311 1.00 50.90 O
HETATM 950 O HOH A 245 7.806 9.189 -16.745 1.00 40.52 O
HETATM 951 O HOH A 246 12.330 0.343 -20.529 1.00 33.30 O
HETATM 952 O HOH A 247 30.147 3.471 -3.303 1.00 46.50 O
HETATM 953 O HOH A 248 24.552 -3.196 -3.583 1.00 23.32 O
HETATM 954 O HOH A 249 31.197 16.153 0.000 0.50 54.52 O
HETATM 955 O HOH A 250 31.038 12.899 -21.392 1.00 53.12 O
HETATM 956 O HOH A 251 8.243 10.731 1.570 1.00 25.54 O
HETATM 957 O AHOH A 252 16.802 8.334 -24.306 0.66 27.16 O
HETATM 958 O BHOH A 252 17.513 9.605 -25.536 0.34 27.16 O
HETATM 959 O HOH A 253 18.647 19.850 -2.568 1.00 30.04 O
HETATM 960 O AHOH A 254 19.613 8.273 -26.792 0.46 26.83 O
HETATM 961 O BHOH A 254 20.698 9.984 -27.149 0.54 23.42 O
HETATM 962 O HOH A 255 13.068 22.714 -12.432 1.00 24.11 O
HETATM 963 O HOH A 256 18.954 2.349 4.105 1.00 34.66 O
HETATM 964 O HOH A 257 31.197 6.384 0.000 0.48 52.32 O
HETATM 965 O HOH A 258 30.500 -2.842 -7.334 1.00 25.54 O
HETATM 966 O HOH A 259 8.235 12.342 -17.161 1.00 44.46 O
HETATM 967 O HOH A 260 10.152 2.831 -14.866 1.00 45.42 O
HETATM 968 O HOH A 261 35.139 11.523 -21.699 1.00 56.61 O
HETATM 969 O AHOH A 262 13.947 22.834 -15.037 0.49 18.86 O
HETATM 970 O BHOH A 262 12.664 22.120 -16.495 0.51 22.63 O
HETATM 971 O HOH A 263 8.718 8.889 0.179 1.00 35.24 O
HETATM 972 O HOH A 264 30.614 14.814 -13.792 1.00 44.77 O
HETATM 973 O HOH A 265 12.885 -1.595 -5.037 1.00 48.31 O
HETATM 974 O HOH A 266 16.063 6.422 -25.997 1.00 47.93 O
HETATM 975 O HOH A 267 31.493 11.581 -25.046 0.93 61.61 O
HETATM 976 O HOH A 268 39.423 10.541 -20.586 1.00 53.61 O
HETATM 977 O HOH A 269 29.383 -1.324 -4.859 1.00 42.90 O
HETATM 978 O HOH A 270 21.371 16.361 -27.645 1.00 25.54 O
HETATM 979 O HOH A 271 29.816 -3.666 -10.469 1.00 25.54 O
HETATM 980 O HOH A 272 26.462 23.996 -18.155 1.00 53.80 O
HETATM 981 O HOH A 273 30.344 -5.288 -6.288 1.00 42.31 O
HETATM 982 O HOH A 274 7.214 10.289 -13.402 1.00 25.94 O
HETATM 983 O HOH A 275 8.339 -2.323 -6.643 1.00 25.54 O
HETATM 984 O HOH A 276 16.020 22.371 -16.670 1.00 34.91 O
HETATM 985 O HOH A 277 29.203 16.274 -14.732 1.00 49.43 O
HETATM 986 O HOH A 278 33.522 16.944 -6.223 1.00 52.74 O
HETATM 987 O HOH A 279 30.094 19.802 -14.261 1.00 51.27 O
HETATM 988 O HOH A 280 8.092 1.713 -14.434 1.00 52.32 O
HETATM 989 O HOH A 281 25.879 21.053 -20.359 1.00 58.25 O
HETATM 990 O HOH A 282 30.951 17.062 -17.195 1.00 61.49 O
HETATM 991 O HOH A 283 27.480 15.444 -21.333 1.00 49.30 O
HETATM 992 O HOH A 284 5.903 7.373 -15.192 1.00 49.90 O
CONECT 115 122
CONECT 122 115 123
CONECT 123 122 124 126
CONECT 124 123 125 130
CONECT 125 124
CONECT 126 123 127
CONECT 127 126 128
CONECT 128 127 129
CONECT 129 128
CONECT 130 124
CONECT 519 522
CONECT 522 519 523 524
CONECT 523 522 525 527
CONECT 524 522 525 528
CONECT 525 523 524 526 535
CONECT 526 525
CONECT 527 523 529
CONECT 528 524 530
CONECT 529 527 531
CONECT 530 528 532
CONECT 531 529 533
CONECT 532 530 534
CONECT 533 531
CONECT 534 532
CONECT 535 525
MASTER 308 0 2 7 0 0 0 6 983 1 25 11
END