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HEADER OXYGEN TRANSPORT 08-FEB-24 8VYL
TITLE THE STRUCTURE OF HUMAN HEMOGLOBIN IN COMPLEX WITH NANOBODY BTNBE11
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN SUBUNIT BETA;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: BETA-GLOBIN,HEMOGLOBIN BETA CHAIN;
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM: LAMA GLAMA;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9844
KEYWDS HEMOGLOBIN, NANOBODY, OXYGEN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GRINTER,S.BINKS,D.FOX
REVDAT 2 09-OCT-24 8VYL 1 JRNL
REVDAT 1 17-JUL-24 8VYL 0
JRNL AUTH D.R.FOX,I.SAMUELS,S.BINKS,R.GRINTER
JRNL TITL THE STRUCTURE OF A HAEMOGLOBIN-NANOBODY COMPLEX REVEALS
JRNL TITL 2 HUMAN BETA-SUBUNIT-SPECIFIC INTERACTIONS.
JRNL REF FEBS LETT. V. 598 2240 2024
JRNL REFN ISSN 0014-5793
JRNL PMID 38880764
JRNL DOI 10.1002/1873-3468.14958
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 52415
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 2698
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.8900 - 5.4000 1.00 2699 160 0.1689 0.1988
REMARK 3 2 5.4000 - 4.2900 1.00 2683 117 0.1772 0.2334
REMARK 3 3 4.2900 - 3.7500 1.00 2654 129 0.1745 0.2542
REMARK 3 4 3.7400 - 3.4000 1.00 2638 129 0.1910 0.2364
REMARK 3 5 3.4000 - 3.1600 1.00 2653 145 0.2221 0.2764
REMARK 3 6 3.1600 - 2.9700 1.00 2593 171 0.2246 0.2849
REMARK 3 7 2.9700 - 2.8200 1.00 2617 157 0.2231 0.2535
REMARK 3 8 2.8200 - 2.7000 1.00 2610 153 0.2293 0.3214
REMARK 3 9 2.7000 - 2.6000 1.00 2646 123 0.2420 0.3292
REMARK 3 10 2.6000 - 2.5100 1.00 2585 141 0.2408 0.2704
REMARK 3 11 2.5100 - 2.4300 1.00 2633 144 0.2288 0.3046
REMARK 3 12 2.4300 - 2.3600 1.00 2576 144 0.2259 0.2969
REMARK 3 13 2.3600 - 2.3000 1.00 2658 136 0.2325 0.2857
REMARK 3 14 2.3000 - 2.2400 1.00 2624 138 0.2285 0.2806
REMARK 3 15 2.2400 - 2.1900 1.00 2596 130 0.2358 0.3049
REMARK 3 16 2.1900 - 2.1400 1.00 2562 163 0.2428 0.2812
REMARK 3 17 2.1400 - 2.1000 1.00 2668 130 0.2632 0.3322
REMARK 3 18 2.1000 - 2.0600 1.00 2589 150 0.2717 0.3358
REMARK 3 19 2.0600 - 2.0200 0.93 2433 138 0.2810 0.3285
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 6583
REMARK 3 ANGLE : 0.723 9004
REMARK 3 CHIRALITY : 0.042 975
REMARK 3 PLANARITY : 0.006 1137
REMARK 3 DIHEDRAL : 10.684 895
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7926 -24.4751 3.8418
REMARK 3 T TENSOR
REMARK 3 T11: 0.2069 T22: 0.2319
REMARK 3 T33: 0.2748 T12: 0.0275
REMARK 3 T13: 0.0053 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.8071 L22: 0.8304
REMARK 3 L33: 0.4821 L12: -0.3495
REMARK 3 L13: -0.0163 L23: -0.1927
REMARK 3 S TENSOR
REMARK 3 S11: 0.0478 S12: 0.1371 S13: 0.3128
REMARK 3 S21: -0.0977 S22: -0.0808 S23: -0.2481
REMARK 3 S31: -0.0704 S32: 0.0260 S33: 0.0242
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 8VYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1000280379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : YES
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52426
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 49.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.26500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (1.20.1_4487: ???)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: FLAT PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1-0.3M NH4 ACET. PH 5.5, 0.1-0.3M NA
REMARK 280 ACET., 25% W/V PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 94.38050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.41850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 94.38050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.41850
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, F, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 SER A 138
REMARK 465 LYS A 139
REMARK 465 TYR A 140
REMARK 465 ARG A 141
REMARK 465 MET C 0
REMARK 465 ARG C 141
REMARK 465 MET B 0
REMARK 465 VAL B 1
REMARK 465 MET D 0
REMARK 465 MET F 1
REMARK 465 GLY F 2
REMARK 465 ALA F 3
REMARK 465 GLN F 4
REMARK 465 GLY F 130
REMARK 465 GLY F 131
REMARK 465 SER F 132
REMARK 465 LEU F 133
REMARK 465 GLU F 134
REMARK 465 HIS F 135
REMARK 465 HIS F 136
REMARK 465 HIS F 137
REMARK 465 HIS F 138
REMARK 465 HIS F 139
REMARK 465 HIS F 140
REMARK 465 MET E 1
REMARK 465 GLY E 2
REMARK 465 GLY E 130
REMARK 465 GLY E 131
REMARK 465 SER E 132
REMARK 465 LEU E 133
REMARK 465 GLU E 134
REMARK 465 HIS E 135
REMARK 465 HIS E 136
REMARK 465 HIS E 137
REMARK 465 HIS E 138
REMARK 465 HIS E 139
REMARK 465 HIS E 140
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 348 O HOH C 364 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU F 49 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 75 51.05 -146.90
REMARK 500 PHE A 117 53.43 -94.85
REMARK 500 ASP C 75 49.55 -143.78
REMARK 500 PHE C 117 50.15 -99.21
REMARK 500 LEU D 3 -159.97 -117.33
REMARK 500 GLU D 6 -8.11 76.15
REMARK 500 GLU D 7 -60.68 -107.65
REMARK 500 GLU F 49 118.25 -161.29
REMARK 500 SER F 91 66.29 -62.24
REMARK 500 ALA F 95 167.58 178.93
REMARK 500 ALA F 108 -35.53 62.53
REMARK 500 SER F 128 55.19 -104.73
REMARK 500 ALA E 95 170.91 179.57
REMARK 500 SER E 128 52.41 -105.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG F 48 GLU F 49 -145.36
REMARK 500 SER F 74 THR F 75 139.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 401 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH D 340 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH E 307 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH E 308 DISTANCE = 6.52 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 201 NA 84.0
REMARK 620 3 HEM A 201 NB 90.4 90.0
REMARK 620 4 HEM A 201 NC 97.2 177.9 91.7
REMARK 620 5 HEM A 201 ND 92.4 89.2 177.0 89.1
REMARK 620 6 HOH A 307 O 177.8 94.3 88.3 84.6 88.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HEM C 201 NA 88.7
REMARK 620 3 HEM C 201 NB 88.8 90.1
REMARK 620 4 HEM C 201 NC 90.8 178.8 91.0
REMARK 620 5 HEM C 201 ND 91.7 89.4 179.3 89.5
REMARK 620 6 HOH C 304 O 174.4 96.8 90.3 83.6 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 201 NA 86.7
REMARK 620 3 HEM B 201 NB 91.1 88.4
REMARK 620 4 HEM B 201 NC 94.4 177.8 89.7
REMARK 620 5 HEM B 201 ND 91.8 88.7 175.7 93.2
REMARK 620 6 HOH B 336 O 178.6 94.6 88.6 84.3 88.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HEM D 201 NA 81.7
REMARK 620 3 HEM D 201 NB 84.0 87.7
REMARK 620 4 HEM D 201 NC 97.5 176.9 89.2
REMARK 620 5 HEM D 201 ND 94.2 90.7 177.8 92.3
REMARK 620 6 HOH D 324 O 169.5 89.4 90.1 91.1 91.4
REMARK 620 N 1 2 3 4 5
DBREF 8VYL A 0 141 UNP P69905 HBA_HUMAN 1 142
DBREF 8VYL C 0 141 UNP P69905 HBA_HUMAN 1 142
DBREF 8VYL B 0 146 UNP P68871 HBB_HUMAN 1 147
DBREF 8VYL D 0 146 UNP P68871 HBB_HUMAN 1 147
DBREF 8VYL F 1 140 PDB 8VYL 8VYL 1 140
DBREF 8VYL E 1 140 PDB 8VYL 8VYL 1 140
SEQRES 1 A 142 MET VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA
SEQRES 2 A 142 ALA TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY
SEQRES 3 A 142 ALA GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR
SEQRES 4 A 142 THR LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY
SEQRES 5 A 142 SER ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP
SEQRES 6 A 142 ALA LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO
SEQRES 7 A 142 ASN ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS
SEQRES 8 A 142 LEU ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS
SEQRES 9 A 142 CYS LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU
SEQRES 10 A 142 PHE THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU
SEQRES 11 A 142 ALA SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 C 142 MET VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA
SEQRES 2 C 142 ALA TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY
SEQRES 3 C 142 ALA GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR
SEQRES 4 C 142 THR LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY
SEQRES 5 C 142 SER ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP
SEQRES 6 C 142 ALA LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO
SEQRES 7 C 142 ASN ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS
SEQRES 8 C 142 LEU ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS
SEQRES 9 C 142 CYS LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU
SEQRES 10 C 142 PHE THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU
SEQRES 11 C 142 ALA SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 147 MET VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR
SEQRES 2 B 147 ALA LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY
SEQRES 3 B 147 GLU ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR
SEQRES 4 B 147 GLN ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO
SEQRES 5 B 147 ASP ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY
SEQRES 6 B 147 LYS LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS
SEQRES 7 B 147 LEU ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU
SEQRES 8 B 147 LEU HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE
SEQRES 9 B 147 ARG LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS
SEQRES 10 B 147 HIS PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA
SEQRES 11 B 147 TYR GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA
SEQRES 12 B 147 HIS LYS TYR HIS
SEQRES 1 D 147 MET VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR
SEQRES 2 D 147 ALA LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY
SEQRES 3 D 147 GLU ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR
SEQRES 4 D 147 GLN ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO
SEQRES 5 D 147 ASP ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY
SEQRES 6 D 147 LYS LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS
SEQRES 7 D 147 LEU ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU
SEQRES 8 D 147 LEU HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE
SEQRES 9 D 147 ARG LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS
SEQRES 10 D 147 HIS PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA
SEQRES 11 D 147 TYR GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA
SEQRES 12 D 147 HIS LYS TYR HIS
SEQRES 1 F 140 MET GLY ALA GLN VAL GLN LEU GLN GLU SER GLY GLY GLY
SEQRES 2 F 140 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA
SEQRES 3 F 140 ALA SER GLY PHE ILE PHE SER THR TYR SER MET GLY TRP
SEQRES 4 F 140 PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA
SEQRES 5 F 140 ALA SER THR TRP GLY GLY VAL THR THR ASN TYR ALA ASP
SEQRES 6 F 140 SER VAL LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA
SEQRES 7 F 140 LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU ASN SER
SEQRES 8 F 140 GLY ASP THR ALA VAL TYR TYR CYS ALA ALA ALA ARG PHE
SEQRES 9 F 140 LEU GLN ASN ALA ARG LEU THR THR GLY PRO TYR ASP TYR
SEQRES 10 F 140 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY GLY
SEQRES 11 F 140 GLY SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 140 MET GLY ALA GLN VAL GLN LEU GLN GLU SER GLY GLY GLY
SEQRES 2 E 140 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA
SEQRES 3 E 140 ALA SER GLY PHE ILE PHE SER THR TYR SER MET GLY TRP
SEQRES 4 E 140 PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA
SEQRES 5 E 140 ALA SER THR TRP GLY GLY VAL THR THR ASN TYR ALA ASP
SEQRES 6 E 140 SER VAL LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA
SEQRES 7 E 140 LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU ASN SER
SEQRES 8 E 140 GLY ASP THR ALA VAL TYR TYR CYS ALA ALA ALA ARG PHE
SEQRES 9 E 140 LEU GLN ASN ALA ARG LEU THR THR GLY PRO TYR ASP TYR
SEQRES 10 E 140 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY GLY
SEQRES 11 E 140 GLY SER LEU GLU HIS HIS HIS HIS HIS HIS
HET HEM A 201 73
HET ACE A 202 7
HET HEM C 201 43
HET HEM B 201 43
HET HEM D 201 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ACE ACETYL GROUP
HETSYN HEM HEME
FORMUL 7 HEM 4(C34 H32 FE N4 O4)
FORMUL 8 ACE C2 H4 O
FORMUL 12 HOH *440(H2 O)
HELIX 1 AA1 SER A 3 GLY A 15 1 13
HELIX 2 AA2 LYS A 16 ALA A 19 5 4
HELIX 3 AA3 HIS A 20 PHE A 36 1 17
HELIX 4 AA4 PRO A 37 PHE A 43 5 7
HELIX 5 AA5 SER A 52 HIS A 72 1 21
HELIX 6 AA6 ASP A 75 LEU A 80 1 6
HELIX 7 AA7 LEU A 80 HIS A 89 1 10
HELIX 8 AA8 PRO A 95 LEU A 113 1 19
HELIX 9 AA9 PRO A 114 PHE A 117 5 4
HELIX 10 AB1 THR A 118 THR A 137 1 20
HELIX 11 AB2 SER C 3 GLY C 15 1 13
HELIX 12 AB3 LYS C 16 ALA C 19 5 4
HELIX 13 AB4 HIS C 20 PHE C 36 1 17
HELIX 14 AB5 PRO C 37 PHE C 43 5 7
HELIX 15 AB6 SER C 52 HIS C 72 1 21
HELIX 16 AB7 ASP C 75 LEU C 80 1 6
HELIX 17 AB8 LEU C 80 HIS C 89 1 10
HELIX 18 AB9 PRO C 95 LEU C 113 1 19
HELIX 19 AC1 PRO C 114 PHE C 117 5 4
HELIX 20 AC2 THR C 118 THR C 137 1 20
HELIX 21 AC3 THR B 4 GLY B 16 1 13
HELIX 22 AC4 ASN B 19 TYR B 35 1 17
HELIX 23 AC5 PRO B 36 GLY B 46 5 11
HELIX 24 AC6 THR B 50 ASN B 57 1 8
HELIX 25 AC7 ASN B 57 ALA B 76 1 20
HELIX 26 AC8 ASN B 80 PHE B 85 1 6
HELIX 27 AC9 PHE B 85 LYS B 95 1 11
HELIX 28 AD1 PRO B 100 GLY B 119 1 20
HELIX 29 AD2 LYS B 120 PHE B 122 5 3
HELIX 30 AD3 THR B 123 ALA B 142 1 20
HELIX 31 AD4 HIS B 143 HIS B 146 5 4
HELIX 32 AD5 GLU D 7 GLY D 16 1 10
HELIX 33 AD6 ASN D 19 TYR D 35 1 17
HELIX 34 AD7 PRO D 36 GLY D 46 5 11
HELIX 35 AD8 THR D 50 ASN D 57 1 8
HELIX 36 AD9 ASN D 57 ALA D 76 1 20
HELIX 37 AE1 ASN D 80 PHE D 85 1 6
HELIX 38 AE2 PHE D 85 LYS D 95 1 11
HELIX 39 AE3 PRO D 100 GLY D 119 1 20
HELIX 40 AE4 LYS D 120 PHE D 122 5 3
HELIX 41 AE5 THR D 123 ALA D 142 1 20
HELIX 42 AE6 HIS D 143 HIS D 146 5 4
HELIX 43 AE7 ILE F 31 SER F 33 5 3
HELIX 44 AE8 TRP F 56 VAL F 59 5 4
HELIX 45 AE9 ILE E 31 SER E 33 5 3
HELIX 46 AF1 TRP E 56 VAL E 59 5 4
HELIX 47 AF2 ASN E 90 THR E 94 5 5
HELIX 48 AF3 GLN E 106 THR E 112 5 7
SHEET 1 AA1 4 GLN F 6 SER F 10 0
SHEET 2 AA1 4 LEU F 21 SER F 28 -1 O ALA F 26 N GLN F 8
SHEET 3 AA1 4 THR F 81 MET F 86 -1 O MET F 86 N LEU F 21
SHEET 4 AA1 4 PHE F 71 ILE F 73 -1 N THR F 72 O GLN F 85
SHEET 1 AA2 6 LEU F 14 VAL F 15 0
SHEET 2 AA2 6 THR F 122 VAL F 126 1 O THR F 125 N VAL F 15
SHEET 3 AA2 6 ALA F 95 ARG F 103 -1 N TYR F 97 O THR F 122
SHEET 4 AA2 6 TYR F 35 GLN F 42 -1 N PHE F 40 O TYR F 98
SHEET 5 AA2 6 ARG F 48 SER F 54 -1 O GLU F 49 N ARG F 41
SHEET 6 AA2 6 THR F 61 TYR F 63 -1 O ASN F 62 N ALA F 53
SHEET 1 AA3 4 LEU F 14 VAL F 15 0
SHEET 2 AA3 4 THR F 122 VAL F 126 1 O THR F 125 N VAL F 15
SHEET 3 AA3 4 ALA F 95 ARG F 103 -1 N TYR F 97 O THR F 122
SHEET 4 AA3 4 TYR F 117 TRP F 118 -1 O TYR F 117 N ALA F 101
SHEET 1 AA4 4 GLN E 6 SER E 10 0
SHEET 2 AA4 4 LEU E 21 SER E 28 -1 O ALA E 26 N GLN E 8
SHEET 3 AA4 4 THR E 81 MET E 86 -1 O MET E 86 N LEU E 21
SHEET 4 AA4 4 PHE E 71 ASP E 76 -1 N THR E 72 O GLN E 85
SHEET 1 AA5 6 LEU E 14 VAL E 15 0
SHEET 2 AA5 6 THR E 122 VAL E 126 1 O THR E 125 N VAL E 15
SHEET 3 AA5 6 ALA E 95 ARG E 103 -1 N ALA E 95 O VAL E 124
SHEET 4 AA5 6 TYR E 35 GLN E 42 -1 N SER E 36 O ALA E 102
SHEET 5 AA5 6 GLU E 49 SER E 54 -1 O ALA E 52 N TRP E 39
SHEET 6 AA5 6 THR E 61 TYR E 63 -1 O ASN E 62 N ALA E 53
SHEET 1 AA6 4 LEU E 14 VAL E 15 0
SHEET 2 AA6 4 THR E 122 VAL E 126 1 O THR E 125 N VAL E 15
SHEET 3 AA6 4 ALA E 95 ARG E 103 -1 N ALA E 95 O VAL E 124
SHEET 4 AA6 4 TYR E 117 TRP E 118 -1 O TYR E 117 N ALA E 101
SSBOND 1 CYS F 25 CYS F 99 1555 1555 2.03
SSBOND 2 CYS E 25 CYS E 99 1555 1555 2.02
LINK NE2 HIS A 87 FE HEM A 201 1555 1555 2.01
LINK FE HEM A 201 O HOH A 307 1555 1555 2.30
LINK NE2 HIS C 87 FE HEM C 201 1555 1555 2.07
LINK FE HEM C 201 O HOH C 304 1555 1555 2.46
LINK NE2 HIS B 92 FE HEM B 201 1555 1555 2.09
LINK FE HEM B 201 O HOH B 336 1555 1555 2.35
LINK NE2 HIS D 92 FE HEM D 201 1555 1555 2.42
LINK FE HEM D 201 O HOH D 324 1555 1555 2.13
CRYST1 188.761 74.837 57.875 90.00 91.44 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005298 0.000000 0.000133 0.00000
SCALE2 0.000000 0.013362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017284 0.00000
TER 1031 THR A 137
TER 2089 TYR C 140
ATOM 2090 N HIS B 2 -28.512 -44.612 -9.937 1.00 53.90 N
ATOM 2091 CA HIS B 2 -28.842 -44.215 -8.570 1.00 53.95 C
ATOM 2092 C HIS B 2 -28.239 -45.205 -7.570 1.00 49.69 C
ATOM 2093 O HIS B 2 -27.149 -44.982 -7.042 1.00 43.08 O
ATOM 2094 CB HIS B 2 -30.363 -44.120 -8.393 1.00 50.71 C
ATOM 2095 CG HIS B 2 -30.798 -43.168 -7.319 1.00 68.58 C
ATOM 2096 ND1 HIS B 2 -31.965 -42.437 -7.400 1.00 64.25 N
ATOM 2097 CD2 HIS B 2 -30.233 -42.840 -6.131 1.00 62.46 C
ATOM 2098 CE1 HIS B 2 -32.096 -41.696 -6.314 1.00 52.09 C
ATOM 2099 NE2 HIS B 2 -31.058 -41.922 -5.528 1.00 49.19 N
ATOM 2100 N LEU B 3 -28.925 -46.324 -7.356 1.00 50.10 N
ATOM 2101 CA LEU B 3 -28.537 -47.310 -6.357 1.00 52.17 C
ATOM 2102 C LEU B 3 -28.147 -48.611 -7.042 1.00 48.83 C
ATOM 2103 O LEU B 3 -28.878 -49.109 -7.906 1.00 46.44 O
ATOM 2104 CB LEU B 3 -29.685 -47.575 -5.371 1.00 42.16 C
ATOM 2105 CG LEU B 3 -29.639 -46.995 -3.956 1.00 45.67 C
ATOM 2106 CD1 LEU B 3 -29.504 -45.485 -3.989 1.00 39.13 C
ATOM 2107 CD2 LEU B 3 -30.884 -47.409 -3.179 1.00 41.13 C
ATOM 2108 N THR B 4 -26.993 -49.153 -6.665 1.00 50.00 N
ATOM 2109 CA THR B 4 -26.579 -50.427 -7.217 1.00 48.97 C
ATOM 2110 C THR B 4 -27.497 -51.518 -6.677 1.00 47.80 C
ATOM 2111 O THR B 4 -28.158 -51.332 -5.652 1.00 41.08 O
ATOM 2112 CB THR B 4 -25.133 -50.744 -6.843 1.00 48.64 C
ATOM 2113 OG1 THR B 4 -25.035 -50.919 -5.424 1.00 41.68 O
ATOM 2114 CG2 THR B 4 -24.207 -49.615 -7.273 1.00 54.39 C
ATOM 2115 N PRO B 5 -27.547 -52.672 -7.340 1.00 47.44 N
ATOM 2116 CA PRO B 5 -28.338 -53.780 -6.789 1.00 45.26 C
ATOM 2117 C PRO B 5 -28.033 -54.060 -5.328 1.00 42.58 C
ATOM 2118 O PRO B 5 -28.958 -54.315 -4.546 1.00 46.62 O
ATOM 2119 CB PRO B 5 -27.953 -54.960 -7.693 1.00 45.30 C
ATOM 2120 CG PRO B 5 -27.383 -54.320 -8.977 1.00 54.69 C
ATOM 2121 CD PRO B 5 -27.335 -52.827 -8.788 1.00 50.48 C
ATOM 2122 N GLU B 6 -26.763 -54.026 -4.932 1.00 41.55 N
ATOM 2123 CA GLU B 6 -26.406 -54.362 -3.560 1.00 44.71 C
ATOM 2124 C GLU B 6 -26.712 -53.227 -2.593 1.00 39.46 C
ATOM 2125 O GLU B 6 -26.775 -53.457 -1.381 1.00 39.20 O
ATOM 2126 CB GLU B 6 -24.918 -54.713 -3.477 1.00 50.57 C
ATOM 2127 CG GLU B 6 -24.422 -55.586 -4.626 1.00 54.49 C
ATOM 2128 CD GLU B 6 -23.884 -54.764 -5.792 1.00 58.12 C
ATOM 2129 OE1 GLU B 6 -24.515 -54.772 -6.875 1.00 48.69 O
ATOM 2130 OE2 GLU B 6 -22.833 -54.103 -5.620 1.00 62.47 O
ATOM 2131 N GLU B 7 -27.032 -52.047 -3.111 1.00 42.34 N
ATOM 2132 CA GLU B 7 -27.449 -50.911 -2.305 1.00 38.30 C
ATOM 2133 C GLU B 7 -28.956 -50.942 -2.102 1.00 37.12 C
ATOM 2134 O GLU B 7 -29.446 -50.818 -0.972 1.00 34.05 O
ATOM 2135 CB GLU B 7 -27.018 -49.604 -2.982 1.00 39.89 C
ATOM 2136 CG GLU B 7 -25.530 -49.279 -2.826 1.00 42.40 C
ATOM 2137 CD GLU B 7 -25.159 -47.895 -3.351 1.00 42.48 C
ATOM 2138 OE1 GLU B 7 -25.549 -47.550 -4.492 1.00 43.16 O
ATOM 2139 OE2 GLU B 7 -24.472 -47.154 -2.613 1.00 36.78 O
ATOM 2140 N LYS B 8 -29.693 -51.140 -3.190 1.00 35.59 N
ATOM 2141 CA LYS B 8 -31.133 -51.317 -3.085 1.00 39.83 C
ATOM 2142 C LYS B 8 -31.473 -52.484 -2.164 1.00 38.71 C
ATOM 2143 O LYS B 8 -32.401 -52.394 -1.352 1.00 36.10 O
ATOM 2144 CB LYS B 8 -31.715 -51.536 -4.482 1.00 35.28 C
ATOM 2145 CG LYS B 8 -33.194 -51.847 -4.515 1.00 44.06 C
ATOM 2146 CD LYS B 8 -33.996 -50.751 -3.841 1.00 50.11 C
ATOM 2147 CE LYS B 8 -35.187 -50.354 -4.691 1.00 49.26 C
ATOM 2148 NZ LYS B 8 -36.110 -51.502 -4.892 1.00 55.04 N
ATOM 2149 N SER B 9 -30.695 -53.564 -2.226 1.00 38.15 N
ATOM 2150 CA SER B 9 -30.984 -54.703 -1.364 1.00 37.15 C
ATOM 2151 C SER B 9 -30.675 -54.383 0.095 1.00 39.14 C
ATOM 2152 O SER B 9 -31.420 -54.785 0.995 1.00 35.41 O
ATOM 2153 CB SER B 9 -30.192 -55.924 -1.838 1.00 39.11 C
ATOM 2154 OG SER B 9 -29.864 -56.775 -0.754 1.00 47.46 O
ATOM 2155 N ALA B 10 -29.608 -53.626 0.350 1.00 34.44 N
ATOM 2156 CA ALA B 10 -29.292 -53.254 1.723 1.00 32.67 C
ATOM 2157 C ALA B 10 -30.293 -52.240 2.270 1.00 31.61 C
ATOM 2158 O ALA B 10 -30.652 -52.280 3.454 1.00 36.30 O
ATOM 2159 CB ALA B 10 -27.871 -52.703 1.800 1.00 31.68 C
ATOM 2160 N VAL B 11 -30.740 -51.310 1.431 1.00 31.73 N
ATOM 2161 CA VAL B 11 -31.699 -50.311 1.880 1.00 23.49 C
ATOM 2162 C VAL B 11 -33.014 -50.975 2.274 1.00 31.07 C
ATOM 2163 O VAL B 11 -33.557 -50.730 3.362 1.00 25.44 O
ATOM 2164 CB VAL B 11 -31.901 -49.250 0.785 1.00 28.00 C
ATOM 2165 CG1 VAL B 11 -33.153 -48.428 1.057 1.00 28.99 C
ATOM 2166 CG2 VAL B 11 -30.672 -48.364 0.692 1.00 30.94 C
ATOM 2167 N THR B 12 -33.557 -51.805 1.381 1.00 25.94 N
ATOM 2168 CA THR B 12 -34.819 -52.483 1.661 1.00 33.42 C
ATOM 2169 C THR B 12 -34.714 -53.364 2.895 1.00 29.08 C
ATOM 2170 O THR B 12 -35.653 -53.437 3.696 1.00 39.20 O
ATOM 2171 CB THR B 12 -35.254 -53.316 0.456 1.00 33.24 C
ATOM 2172 OG1 THR B 12 -35.238 -52.500 -0.718 1.00 31.81 O
ATOM 2173 CG2 THR B 12 -36.661 -53.842 0.670 1.00 37.56 C
ATOM 2174 N ALA B 13 -33.573 -54.032 3.077 1.00 31.40 N
ATOM 2175 CA ALA B 13 -33.408 -54.890 4.246 1.00 35.32 C
ATOM 2176 C ALA B 13 -33.527 -54.076 5.527 1.00 29.11 C
ATOM 2177 O ALA B 13 -34.286 -54.430 6.438 1.00 31.69 O
ATOM 2178 CB ALA B 13 -32.069 -55.623 4.184 1.00 29.43 C
ATOM 2179 N LEU B 14 -32.767 -52.984 5.626 1.00 29.87 N
ATOM 2180 CA LEU B 14 -32.816 -52.185 6.844 1.00 26.34 C
ATOM 2181 C LEU B 14 -34.189 -51.550 7.042 1.00 25.33 C
ATOM 2182 O LEU B 14 -34.664 -51.432 8.178 1.00 27.05 O
ATOM 2183 CB LEU B 14 -31.724 -51.113 6.806 1.00 26.27 C
ATOM 2184 CG LEU B 14 -31.297 -50.526 8.152 1.00 26.83 C
ATOM 2185 CD1 LEU B 14 -30.386 -51.502 8.899 1.00 26.86 C
ATOM 2186 CD2 LEU B 14 -30.604 -49.170 7.977 1.00 27.03 C
ATOM 2187 N TRP B 15 -34.855 -51.160 5.958 1.00 24.74 N
ATOM 2188 CA TRP B 15 -36.156 -50.521 6.099 1.00 27.80 C
ATOM 2189 C TRP B 15 -37.218 -51.500 6.594 1.00 28.38 C
ATOM 2190 O TRP B 15 -38.157 -51.087 7.285 1.00 25.65 O
ATOM 2191 CB TRP B 15 -36.587 -49.887 4.773 1.00 27.16 C
ATOM 2192 CG TRP B 15 -37.558 -48.778 4.967 1.00 27.38 C
ATOM 2193 CD1 TRP B 15 -38.882 -48.782 4.641 1.00 26.03 C
ATOM 2194 CD2 TRP B 15 -37.294 -47.497 5.560 1.00 26.92 C
ATOM 2195 NE1 TRP B 15 -39.462 -47.585 4.996 1.00 27.32 N
ATOM 2196 CE2 TRP B 15 -38.505 -46.777 5.555 1.00 27.10 C
ATOM 2197 CE3 TRP B 15 -36.147 -46.887 6.084 1.00 25.97 C
ATOM 2198 CZ2 TRP B 15 -38.603 -45.472 6.047 1.00 29.42 C
ATOM 2199 CZ3 TRP B 15 -36.245 -45.590 6.576 1.00 27.12 C
ATOM 2200 CH2 TRP B 15 -37.465 -44.900 6.556 1.00 32.25 C
ATOM 2201 N GLY B 16 -37.099 -52.787 6.254 1.00 30.07 N
ATOM 2202 CA GLY B 16 -38.021 -53.775 6.802 1.00 26.74 C
ATOM 2203 C GLY B 16 -37.978 -53.885 8.316 1.00 30.29 C
ATOM 2204 O GLY B 16 -38.906 -54.439 8.920 1.00 29.18 O
ATOM 2205 N LYS B 17 -36.928 -53.358 8.944 1.00 27.56 N
ATOM 2206 CA LYS B 17 -36.746 -53.412 10.386 1.00 23.35 C
ATOM 2207 C LYS B 17 -37.118 -52.106 11.065 1.00 26.93 C
ATOM 2208 O LYS B 17 -36.933 -51.971 12.279 1.00 33.98 O
ATOM 2209 CB LYS B 17 -35.302 -53.778 10.727 1.00 27.79 C
ATOM 2210 CG LYS B 17 -34.890 -55.201 10.358 1.00 29.17 C
ATOM 2211 CD LYS B 17 -33.386 -55.356 10.532 1.00 29.37 C
ATOM 2212 CE LYS B 17 -32.805 -56.450 9.653 1.00 37.12 C
ATOM 2213 NZ LYS B 17 -31.532 -56.955 10.258 1.00 33.41 N
ATOM 2214 N VAL B 18 -37.660 -51.151 10.318 1.00 24.81 N
ATOM 2215 CA VAL B 18 -37.931 -49.815 10.825 1.00 26.83 C
ATOM 2216 C VAL B 18 -39.426 -49.691 11.075 1.00 30.34 C
ATOM 2217 O VAL B 18 -40.237 -50.062 10.220 1.00 32.06 O
ATOM 2218 CB VAL B 18 -37.447 -48.748 9.826 1.00 31.89 C
ATOM 2219 CG1 VAL B 18 -38.003 -47.383 10.179 1.00 25.19 C
ATOM 2220 CG2 VAL B 18 -35.918 -48.737 9.760 1.00 26.92 C
ATOM 2221 N ASN B 19 -39.794 -49.202 12.257 1.00 27.75 N
ATOM 2222 CA ASN B 19 -41.192 -48.895 12.548 1.00 35.14 C
ATOM 2223 C ASN B 19 -41.459 -47.500 12.002 1.00 38.52 C
ATOM 2224 O ASN B 19 -41.136 -46.501 12.651 1.00 32.37 O
ATOM 2225 CB ASN B 19 -41.469 -48.978 14.044 1.00 31.33 C
ATOM 2226 CG ASN B 19 -42.922 -48.684 14.382 1.00 42.10 C
ATOM 2227 OD1 ASN B 19 -43.673 -48.162 13.556 1.00 42.07 O
ATOM 2228 ND2 ASN B 19 -43.322 -49.011 15.606 1.00 43.67 N
ATOM 2229 N VAL B 20 -42.054 -47.429 10.804 1.00 39.77 N
ATOM 2230 CA VAL B 20 -42.144 -46.154 10.088 1.00 43.26 C
ATOM 2231 C VAL B 20 -42.850 -45.105 10.935 1.00 47.63 C
ATOM 2232 O VAL B 20 -42.426 -43.943 10.988 1.00 45.90 O
ATOM 2233 CB VAL B 20 -42.842 -46.338 8.726 1.00 43.59 C
ATOM 2234 CG1 VAL B 20 -41.900 -46.993 7.736 1.00 38.70 C
ATOM 2235 CG2 VAL B 20 -44.128 -47.146 8.884 1.00 48.98 C
ATOM 2236 N ASP B 21 -43.930 -45.496 11.614 1.00 35.88 N
ATOM 2237 CA ASP B 21 -44.607 -44.587 12.528 1.00 39.51 C
ATOM 2238 C ASP B 21 -43.616 -43.958 13.505 1.00 40.66 C
ATOM 2239 O ASP B 21 -43.422 -42.736 13.515 1.00 37.82 O
ATOM 2240 CB ASP B 21 -45.714 -45.333 13.278 1.00 40.49 C
ATOM 2241 CG ASP B 21 -47.007 -45.426 12.476 1.00 54.75 C
ATOM 2242 OD1 ASP B 21 -47.036 -44.942 11.321 1.00 52.57 O
ATOM 2243 OD2 ASP B 21 -47.994 -45.988 13.001 1.00 52.86 O
ATOM 2244 N GLU B 22 -42.941 -44.795 14.303 1.00 31.92 N
ATOM 2245 CA GLU B 22 -42.174 -44.292 15.441 1.00 34.60 C
ATOM 2246 C GLU B 22 -40.905 -43.579 14.989 1.00 28.23 C
ATOM 2247 O GLU B 22 -40.487 -42.596 15.612 1.00 28.52 O
ATOM 2248 CB GLU B 22 -41.821 -45.442 16.389 1.00 35.26 C
ATOM 2249 CG GLU B 22 -43.007 -46.082 17.095 1.00 36.91 C
ATOM 2250 CD GLU B 22 -43.667 -45.160 18.106 1.00 42.10 C
ATOM 2251 OE1 GLU B 22 -42.982 -44.253 18.634 1.00 44.17 O
ATOM 2252 OE2 GLU B 22 -44.874 -45.347 18.374 1.00 45.66 O
ATOM 2253 N VAL B 23 -40.257 -44.081 13.937 1.00 26.27 N
ATOM 2254 CA VAL B 23 -39.034 -43.455 13.446 1.00 29.66 C
ATOM 2255 C VAL B 23 -39.315 -42.024 13.008 1.00 28.36 C
ATOM 2256 O VAL B 23 -38.470 -41.135 13.163 1.00 27.75 O
ATOM 2257 CB VAL B 23 -38.427 -44.288 12.302 1.00 26.22 C
ATOM 2258 CG1 VAL B 23 -39.224 -44.106 11.023 1.00 30.06 C
ATOM 2259 CG2 VAL B 23 -36.962 -43.916 12.073 1.00 25.39 C
ATOM 2260 N GLY B 24 -40.506 -41.785 12.452 1.00 29.04 N
ATOM 2261 CA GLY B 24 -40.854 -40.451 11.986 1.00 26.98 C
ATOM 2262 C GLY B 24 -40.947 -39.441 13.112 1.00 25.92 C
ATOM 2263 O GLY B 24 -40.436 -38.323 13.002 1.00 25.89 O
ATOM 2264 N GLY B 25 -41.622 -39.812 14.203 1.00 26.91 N
ATOM 2265 CA GLY B 25 -41.705 -38.918 15.351 1.00 25.09 C
ATOM 2266 C GLY B 25 -40.342 -38.618 15.947 1.00 26.89 C
ATOM 2267 O GLY B 25 -40.044 -37.477 16.311 1.00 25.69 O
ATOM 2268 N GLU B 26 -39.484 -39.634 16.035 1.00 27.05 N
ATOM 2269 CA GLU B 26 -38.153 -39.419 16.591 1.00 27.65 C
ATOM 2270 C GLU B 26 -37.336 -38.469 15.721 1.00 22.05 C
ATOM 2271 O GLU B 26 -36.690 -37.547 16.231 1.00 22.58 O
ATOM 2272 CB GLU B 26 -37.433 -40.761 16.749 1.00 23.30 C
ATOM 2273 CG GLU B 26 -36.012 -40.656 17.296 1.00 27.39 C
ATOM 2274 CD GLU B 26 -35.981 -40.352 18.784 1.00 28.76 C
ATOM 2275 OE1 GLU B 26 -37.014 -40.539 19.456 1.00 33.50 O
ATOM 2276 OE2 GLU B 26 -34.923 -39.931 19.289 1.00 34.24 O
ATOM 2277 N ALA B 27 -37.355 -38.676 14.399 1.00 24.61 N
ATOM 2278 CA ALA B 27 -36.536 -37.849 13.512 1.00 25.48 C
ATOM 2279 C ALA B 27 -37.057 -36.416 13.437 1.00 25.01 C
ATOM 2280 O ALA B 27 -36.269 -35.461 13.473 1.00 19.52 O
ATOM 2281 CB ALA B 27 -36.471 -38.469 12.116 1.00 16.94 C
ATOM 2282 N LEU B 28 -38.378 -36.240 13.316 1.00 21.12 N
ATOM 2283 CA LEU B 28 -38.924 -34.885 13.294 1.00 20.56 C
ATOM 2284 C LEU B 28 -38.684 -34.193 14.628 1.00 21.51 C
ATOM 2285 O LEU B 28 -38.263 -33.030 14.667 1.00 25.04 O
ATOM 2286 CB LEU B 28 -40.414 -34.909 12.946 1.00 20.32 C
ATOM 2287 CG LEU B 28 -41.112 -33.544 12.836 1.00 28.46 C
ATOM 2288 CD1 LEU B 28 -40.561 -32.693 11.676 1.00 18.73 C
ATOM 2289 CD2 LEU B 28 -42.627 -33.709 12.715 1.00 21.27 C
ATOM 2290 N GLY B 29 -38.933 -34.893 15.734 1.00 23.78 N
ATOM 2291 CA GLY B 29 -38.601 -34.333 17.036 1.00 20.99 C
ATOM 2292 C GLY B 29 -37.155 -33.890 17.119 1.00 23.07 C
ATOM 2293 O GLY B 29 -36.852 -32.771 17.547 1.00 22.36 O
ATOM 2294 N ARG B 30 -36.236 -34.758 16.690 1.00 19.82 N
ATOM 2295 CA ARG B 30 -34.816 -34.419 16.752 1.00 25.10 C
ATOM 2296 C ARG B 30 -34.481 -33.225 15.867 1.00 21.33 C
ATOM 2297 O ARG B 30 -33.658 -32.382 16.241 1.00 21.51 O
ATOM 2298 CB ARG B 30 -33.965 -35.628 16.359 1.00 20.99 C
ATOM 2299 CG ARG B 30 -33.318 -36.314 17.558 1.00 26.26 C
ATOM 2300 CD ARG B 30 -32.772 -37.695 17.215 1.00 29.93 C
ATOM 2301 NE ARG B 30 -32.735 -38.541 18.406 1.00 31.17 N
ATOM 2302 CZ ARG B 30 -31.751 -38.542 19.297 1.00 28.34 C
ATOM 2303 NH1 ARG B 30 -30.669 -37.794 19.133 1.00 23.56 N
ATOM 2304 NH2 ARG B 30 -31.854 -39.313 20.379 1.00 23.69 N
ATOM 2305 N LEU B 31 -35.112 -33.124 14.694 1.00 23.07 N
ATOM 2306 CA LEU B 31 -34.903 -31.955 13.842 1.00 23.36 C
ATOM 2307 C LEU B 31 -35.252 -30.666 14.582 1.00 23.76 C
ATOM 2308 O LEU B 31 -34.495 -29.685 14.552 1.00 22.89 O
ATOM 2309 CB LEU B 31 -35.746 -32.080 12.568 1.00 21.06 C
ATOM 2310 CG LEU B 31 -35.614 -30.942 11.549 1.00 24.88 C
ATOM 2311 CD1 LEU B 31 -34.448 -31.169 10.560 1.00 19.99 C
ATOM 2312 CD2 LEU B 31 -36.926 -30.740 10.808 1.00 19.48 C
ATOM 2313 N LEU B 32 -36.404 -30.660 15.259 1.00 21.32 N
ATOM 2314 CA LEU B 32 -36.866 -29.472 15.964 1.00 21.99 C
ATOM 2315 C LEU B 32 -35.996 -29.157 17.168 1.00 25.40 C
ATOM 2316 O LEU B 32 -35.893 -27.991 17.569 1.00 25.15 O
ATOM 2317 CB LEU B 32 -38.318 -29.655 16.402 1.00 24.15 C
ATOM 2318 CG LEU B 32 -39.309 -29.806 15.254 1.00 24.95 C
ATOM 2319 CD1 LEU B 32 -40.597 -30.491 15.728 1.00 30.04 C
ATOM 2320 CD2 LEU B 32 -39.607 -28.448 14.659 1.00 28.46 C
ATOM 2321 N VAL B 33 -35.380 -30.176 17.769 1.00 23.25 N
ATOM 2322 CA VAL B 33 -34.513 -29.931 18.912 1.00 24.96 C
ATOM 2323 C VAL B 33 -33.139 -29.479 18.445 1.00 24.95 C
ATOM 2324 O VAL B 33 -32.587 -28.496 18.959 1.00 23.80 O
ATOM 2325 CB VAL B 33 -34.419 -31.191 19.789 1.00 27.95 C
ATOM 2326 CG1 VAL B 33 -33.384 -30.987 20.871 1.00 22.20 C
ATOM 2327 CG2 VAL B 33 -35.785 -31.533 20.398 1.00 24.80 C
ATOM 2328 N VAL B 34 -32.591 -30.156 17.431 1.00 22.69 N
ATOM 2329 CA VAL B 34 -31.215 -29.908 17.015 1.00 24.36 C
ATOM 2330 C VAL B 34 -31.095 -28.614 16.210 1.00 23.19 C
ATOM 2331 O VAL B 34 -30.053 -27.958 16.260 1.00 25.94 O
ATOM 2332 CB VAL B 34 -30.675 -31.111 16.219 1.00 25.09 C
ATOM 2333 CG1 VAL B 34 -29.299 -30.786 15.617 1.00 21.07 C
ATOM 2334 CG2 VAL B 34 -30.593 -32.362 17.104 1.00 22.46 C
ATOM 2335 N TYR B 35 -32.135 -28.228 15.461 1.00 21.95 N
ATOM 2336 CA TYR B 35 -32.140 -27.001 14.650 1.00 27.05 C
ATOM 2337 C TYR B 35 -33.395 -26.212 14.996 1.00 24.89 C
ATOM 2338 O TYR B 35 -34.398 -26.274 14.274 1.00 23.15 O
ATOM 2339 CB TYR B 35 -32.081 -27.314 13.152 1.00 22.78 C
ATOM 2340 CG TYR B 35 -31.014 -28.308 12.792 1.00 27.16 C
ATOM 2341 CD1 TYR B 35 -29.673 -27.928 12.715 1.00 24.86 C
ATOM 2342 CD2 TYR B 35 -31.338 -29.637 12.543 1.00 24.46 C
ATOM 2343 CE1 TYR B 35 -28.696 -28.850 12.394 1.00 21.70 C
ATOM 2344 CE2 TYR B 35 -30.374 -30.558 12.228 1.00 20.88 C
ATOM 2345 CZ TYR B 35 -29.056 -30.165 12.152 1.00 26.93 C
ATOM 2346 OH TYR B 35 -28.091 -31.098 11.831 1.00 25.51 O
ATOM 2347 N PRO B 36 -33.370 -25.451 16.092 1.00 23.76 N
ATOM 2348 CA PRO B 36 -34.631 -24.926 16.648 1.00 26.79 C
ATOM 2349 C PRO B 36 -35.371 -23.971 15.732 1.00 25.82 C
ATOM 2350 O PRO B 36 -36.583 -23.791 15.908 1.00 25.28 O
ATOM 2351 CB PRO B 36 -34.182 -24.222 17.940 1.00 26.34 C
ATOM 2352 CG PRO B 36 -32.863 -24.862 18.284 1.00 30.46 C
ATOM 2353 CD PRO B 36 -32.216 -25.176 16.965 1.00 22.24 C
ATOM 2354 N TRP B 37 -34.705 -23.350 14.759 1.00 23.88 N
ATOM 2355 CA TRP B 37 -35.448 -22.455 13.878 1.00 23.63 C
ATOM 2356 C TRP B 37 -36.520 -23.194 13.088 1.00 24.64 C
ATOM 2357 O TRP B 37 -37.500 -22.568 12.669 1.00 21.24 O
ATOM 2358 CB TRP B 37 -34.505 -21.720 12.924 1.00 24.79 C
ATOM 2359 CG TRP B 37 -33.838 -22.609 11.932 1.00 24.74 C
ATOM 2360 CD1 TRP B 37 -34.345 -23.035 10.739 1.00 23.92 C
ATOM 2361 CD2 TRP B 37 -32.534 -23.189 12.043 1.00 22.82 C
ATOM 2362 NE1 TRP B 37 -33.442 -23.838 10.104 1.00 22.47 N
ATOM 2363 CE2 TRP B 37 -32.319 -23.947 10.880 1.00 23.38 C
ATOM 2364 CE3 TRP B 37 -31.531 -23.141 13.013 1.00 22.75 C
ATOM 2365 CZ2 TRP B 37 -31.147 -24.657 10.660 1.00 25.73 C
ATOM 2366 CZ3 TRP B 37 -30.360 -23.844 12.788 1.00 21.60 C
ATOM 2367 CH2 TRP B 37 -30.183 -24.594 11.625 1.00 25.59 C
ATOM 2368 N THR B 38 -36.362 -24.508 12.875 1.00 23.25 N
ATOM 2369 CA THR B 38 -37.380 -25.262 12.151 1.00 22.09 C
ATOM 2370 C THR B 38 -38.705 -25.307 12.900 1.00 24.77 C
ATOM 2371 O THR B 38 -39.748 -25.561 12.282 1.00 24.25 O
ATOM 2372 CB THR B 38 -36.894 -26.686 11.862 1.00 23.70 C
ATOM 2373 OG1 THR B 38 -36.655 -27.383 13.089 1.00 22.23 O
ATOM 2374 CG2 THR B 38 -35.603 -26.650 11.049 1.00 22.03 C
ATOM 2375 N GLN B 39 -38.691 -25.085 14.216 1.00 21.38 N
ATOM 2376 CA GLN B 39 -39.939 -24.997 14.964 1.00 29.00 C
ATOM 2377 C GLN B 39 -40.839 -23.886 14.452 1.00 28.87 C
ATOM 2378 O GLN B 39 -42.059 -23.959 14.641 1.00 21.99 O
ATOM 2379 CB GLN B 39 -39.666 -24.768 16.455 1.00 23.97 C
ATOM 2380 CG GLN B 39 -38.783 -25.815 17.111 1.00 21.61 C
ATOM 2381 CD GLN B 39 -38.340 -25.394 18.492 1.00 27.85 C
ATOM 2382 OE1 GLN B 39 -38.975 -24.548 19.123 1.00 31.37 O
ATOM 2383 NE2 GLN B 39 -37.250 -25.980 18.976 1.00 25.12 N
ATOM 2384 N ARG B 40 -40.275 -22.854 13.814 1.00 25.25 N
ATOM 2385 CA ARG B 40 -41.118 -21.756 13.358 1.00 27.38 C
ATOM 2386 C ARG B 40 -42.156 -22.232 12.348 1.00 27.76 C
ATOM 2387 O ARG B 40 -43.256 -21.678 12.285 1.00 26.99 O
ATOM 2388 CB ARG B 40 -40.272 -20.638 12.762 1.00 25.57 C
ATOM 2389 CG ARG B 40 -41.111 -19.453 12.250 1.00 27.42 C
ATOM 2390 CD ARG B 40 -40.243 -18.254 11.899 1.00 28.28 C
ATOM 2391 NE ARG B 40 -41.030 -17.120 11.427 1.00 35.29 N
ATOM 2392 CZ ARG B 40 -41.502 -16.995 10.192 1.00 38.36 C
ATOM 2393 NH1 ARG B 40 -41.263 -17.908 9.263 1.00 29.38 N
ATOM 2394 NH2 ARG B 40 -42.212 -15.915 9.874 1.00 39.33 N
ATOM 2395 N PHE B 41 -41.833 -23.256 11.558 1.00 23.72 N
ATOM 2396 CA PHE B 41 -42.787 -23.745 10.569 1.00 27.74 C
ATOM 2397 C PHE B 41 -43.942 -24.505 11.197 1.00 25.09 C
ATOM 2398 O PHE B 41 -44.920 -24.792 10.503 1.00 26.69 O
ATOM 2399 CB PHE B 41 -42.077 -24.645 9.559 1.00 27.95 C
ATOM 2400 CG PHE B 41 -41.127 -23.909 8.670 1.00 26.85 C
ATOM 2401 CD1 PHE B 41 -41.598 -23.137 7.625 1.00 28.17 C
ATOM 2402 CD2 PHE B 41 -39.762 -23.959 8.905 1.00 28.41 C
ATOM 2403 CE1 PHE B 41 -40.722 -22.447 6.806 1.00 28.98 C
ATOM 2404 CE2 PHE B 41 -38.881 -23.264 8.094 1.00 24.48 C
ATOM 2405 CZ PHE B 41 -39.363 -22.512 7.044 1.00 24.12 C
ATOM 2406 N PHE B 42 -43.872 -24.799 12.488 1.00 29.07 N
ATOM 2407 CA PHE B 42 -44.842 -25.646 13.173 1.00 31.47 C
ATOM 2408 C PHE B 42 -45.479 -24.930 14.359 1.00 32.75 C
ATOM 2409 O PHE B 42 -45.696 -25.536 15.410 1.00 32.59 O
ATOM 2410 CB PHE B 42 -44.193 -26.955 13.626 1.00 30.38 C
ATOM 2411 CG PHE B 42 -43.590 -27.753 12.499 1.00 28.92 C
ATOM 2412 CD1 PHE B 42 -44.385 -28.536 11.683 1.00 28.97 C
ATOM 2413 CD2 PHE B 42 -42.229 -27.705 12.249 1.00 23.62 C
ATOM 2414 CE1 PHE B 42 -43.825 -29.263 10.640 1.00 26.46 C
ATOM 2415 CE2 PHE B 42 -41.665 -28.430 11.207 1.00 28.28 C
ATOM 2416 CZ PHE B 42 -42.461 -29.206 10.403 1.00 25.99 C
ATOM 2417 N GLU B 43 -45.783 -23.627 14.211 1.00 49.95 N
ATOM 2418 CA GLU B 43 -46.321 -22.865 15.341 1.00 53.00 C
ATOM 2419 C GLU B 43 -47.542 -23.554 15.912 1.00 52.61 C
ATOM 2420 O GLU B 43 -47.719 -23.633 17.135 1.00 54.00 O
ATOM 2421 CB GLU B 43 -46.808 -21.467 14.939 1.00 71.09 C
ATOM 2422 CG GLU B 43 -46.643 -20.996 13.511 1.00 78.48 C
ATOM 2423 CD GLU B 43 -47.644 -19.881 13.205 1.00 96.42 C
ATOM 2424 OE1 GLU B 43 -48.754 -19.922 13.789 1.00 92.33 O
ATOM 2425 OE2 GLU B 43 -47.344 -18.987 12.385 1.00109.52 O
ATOM 2426 N SER B 44 -48.405 -24.046 15.025 1.00 38.63 N
ATOM 2427 CA SER B 44 -49.697 -24.611 15.376 1.00 38.02 C
ATOM 2428 C SER B 44 -49.601 -25.940 16.099 1.00 32.55 C
ATOM 2429 O SER B 44 -50.643 -26.470 16.488 1.00 33.58 O
ATOM 2430 CB SER B 44 -50.537 -24.776 14.109 1.00 37.42 C
ATOM 2431 OG SER B 44 -50.008 -25.818 13.304 1.00 33.69 O
ATOM 2432 N PHE B 45 -48.405 -26.499 16.274 1.00 32.36 N
ATOM 2433 CA PHE B 45 -48.269 -27.806 16.903 1.00 33.56 C
ATOM 2434 C PHE B 45 -48.231 -27.714 18.418 1.00 29.46 C
ATOM 2435 O PHE B 45 -48.173 -28.750 19.082 1.00 27.06 O
ATOM 2436 CB PHE B 45 -47.010 -28.526 16.392 1.00 26.67 C
ATOM 2437 CG PHE B 45 -47.188 -29.177 15.035 1.00 26.91 C
ATOM 2438 CD1 PHE B 45 -48.211 -28.780 14.189 1.00 31.36 C
ATOM 2439 CD2 PHE B 45 -46.324 -30.172 14.603 1.00 30.26 C
ATOM 2440 CE1 PHE B 45 -48.379 -29.375 12.935 1.00 33.06 C
ATOM 2441 CE2 PHE B 45 -46.481 -30.763 13.347 1.00 26.53 C
ATOM 2442 CZ PHE B 45 -47.511 -30.360 12.516 1.00 25.23 C
ATOM 2443 N GLY B 46 -48.234 -26.506 18.975 1.00 30.88 N
ATOM 2444 CA GLY B 46 -48.288 -26.333 20.413 1.00 28.24 C
ATOM 2445 C GLY B 46 -46.948 -26.122 21.084 1.00 27.09 C
ATOM 2446 O GLY B 46 -46.099 -25.377 20.588 1.00 26.02 O
ATOM 2447 N ASP B 47 -46.742 -26.798 22.214 1.00 28.75 N
ATOM 2448 CA ASP B 47 -45.600 -26.546 23.088 1.00 30.16 C
ATOM 2449 C ASP B 47 -44.349 -27.212 22.521 1.00 30.28 C
ATOM 2450 O ASP B 47 -44.241 -28.444 22.507 1.00 27.93 O
ATOM 2451 CB ASP B 47 -45.909 -27.053 24.495 1.00 29.10 C
ATOM 2452 CG ASP B 47 -44.803 -26.752 25.482 1.00 32.78 C
ATOM 2453 OD1 ASP B 47 -43.780 -26.143 25.090 1.00 33.42 O
ATOM 2454 OD2 ASP B 47 -44.954 -27.139 26.662 1.00 34.82 O
ATOM 2455 N LEU B 48 -43.407 -26.396 22.047 1.00 29.15 N
ATOM 2456 CA LEU B 48 -42.091 -26.834 21.588 1.00 33.65 C
ATOM 2457 C LEU B 48 -40.986 -26.063 22.305 1.00 31.50 C
ATOM 2458 O LEU B 48 -39.936 -25.771 21.728 1.00 32.31 O
ATOM 2459 CB LEU B 48 -41.960 -26.672 20.074 1.00 27.27 C
ATOM 2460 CG LEU B 48 -43.139 -27.137 19.215 1.00 28.11 C
ATOM 2461 CD1 LEU B 48 -43.069 -26.514 17.828 1.00 31.07 C
ATOM 2462 CD2 LEU B 48 -43.195 -28.663 19.126 1.00 23.66 C
ATOM 2463 N SER B 49 -41.186 -25.765 23.591 1.00 29.77 N
ATOM 2464 CA SER B 49 -40.315 -24.848 24.318 1.00 33.80 C
ATOM 2465 C SER B 49 -39.084 -25.512 24.924 1.00 34.60 C
ATOM 2466 O SER B 49 -38.158 -24.803 25.332 1.00 36.02 O
ATOM 2467 CB SER B 49 -41.117 -24.147 25.427 1.00 34.09 C
ATOM 2468 OG SER B 49 -41.938 -25.076 26.127 1.00 34.78 O
ATOM 2469 N THR B 50 -39.055 -26.837 25.011 1.00 35.90 N
ATOM 2470 CA THR B 50 -37.918 -27.563 25.550 1.00 33.81 C
ATOM 2471 C THR B 50 -37.789 -28.873 24.791 1.00 30.06 C
ATOM 2472 O THR B 50 -38.764 -29.342 24.189 1.00 28.54 O
ATOM 2473 CB THR B 50 -38.053 -27.821 27.056 1.00 33.15 C
ATOM 2474 OG1 THR B 50 -39.184 -28.662 27.302 1.00 30.64 O
ATOM 2475 CG2 THR B 50 -38.219 -26.505 27.806 1.00 30.78 C
ATOM 2476 N PRO B 51 -36.602 -29.481 24.785 1.00 28.30 N
ATOM 2477 CA PRO B 51 -36.463 -30.808 24.158 1.00 30.83 C
ATOM 2478 C PRO B 51 -37.488 -31.817 24.641 1.00 28.56 C
ATOM 2479 O PRO B 51 -38.088 -32.522 23.822 1.00 29.80 O
ATOM 2480 CB PRO B 51 -35.035 -31.211 24.537 1.00 34.25 C
ATOM 2481 CG PRO B 51 -34.317 -29.900 24.685 1.00 34.15 C
ATOM 2482 CD PRO B 51 -35.316 -28.949 25.267 1.00 31.65 C
ATOM 2483 N ASP B 52 -37.695 -31.914 25.957 1.00 30.46 N
ATOM 2484 CA ASP B 52 -38.728 -32.801 26.493 1.00 31.17 C
ATOM 2485 C ASP B 52 -40.109 -32.458 25.940 1.00 29.77 C
ATOM 2486 O ASP B 52 -40.883 -33.356 25.588 1.00 29.65 O
ATOM 2487 CB ASP B 52 -38.730 -32.738 28.020 1.00 30.99 C
ATOM 2488 CG ASP B 52 -37.522 -33.432 28.633 1.00 34.51 C
ATOM 2489 OD1 ASP B 52 -36.868 -34.215 27.925 1.00 39.20 O
ATOM 2490 OD2 ASP B 52 -37.225 -33.195 29.819 1.00 36.09 O
ATOM 2491 N ALA B 53 -40.451 -31.170 25.877 1.00 28.27 N
ATOM 2492 CA ALA B 53 -41.743 -30.792 25.307 1.00 29.74 C
ATOM 2493 C ALA B 53 -41.842 -31.224 23.846 1.00 28.66 C
ATOM 2494 O ALA B 53 -42.862 -31.781 23.417 1.00 27.06 O
ATOM 2495 CB ALA B 53 -41.967 -29.283 25.448 1.00 26.73 C
ATOM 2496 N VAL B 54 -40.795 -30.959 23.058 1.00 27.39 N
ATOM 2497 CA VAL B 54 -40.811 -31.360 21.651 1.00 27.50 C
ATOM 2498 C VAL B 54 -40.995 -32.870 21.532 1.00 26.16 C
ATOM 2499 O VAL B 54 -41.869 -33.349 20.799 1.00 24.19 O
ATOM 2500 CB VAL B 54 -39.530 -30.896 20.933 1.00 29.00 C
ATOM 2501 CG1 VAL B 54 -39.453 -31.524 19.537 1.00 25.62 C
ATOM 2502 CG2 VAL B 54 -39.481 -29.381 20.847 1.00 30.54 C
ATOM 2503 N MET B 55 -40.171 -33.644 22.245 1.00 25.21 N
ATOM 2504 CA MET B 55 -40.210 -35.094 22.075 1.00 29.26 C
ATOM 2505 C MET B 55 -41.500 -35.706 22.608 1.00 31.86 C
ATOM 2506 O MET B 55 -41.840 -36.827 22.225 1.00 37.24 O
ATOM 2507 CB MET B 55 -39.007 -35.750 22.759 1.00 33.94 C
ATOM 2508 CG MET B 55 -37.627 -35.406 22.159 1.00 22.93 C
ATOM 2509 SD MET B 55 -37.533 -35.343 20.357 1.00 28.69 S
ATOM 2510 CE MET B 55 -37.291 -37.079 19.971 1.00 29.00 C
ATOM 2511 N GLY B 56 -42.210 -35.015 23.502 1.00 26.95 N
ATOM 2512 CA GLY B 56 -43.507 -35.481 23.953 1.00 34.56 C
ATOM 2513 C GLY B 56 -44.694 -34.930 23.188 1.00 33.24 C
ATOM 2514 O GLY B 56 -45.827 -35.378 23.396 1.00 32.59 O
ATOM 2515 N ASN B 57 -44.463 -33.973 22.305 1.00 25.00 N
ATOM 2516 CA ASN B 57 -45.552 -33.295 21.608 1.00 27.44 C
ATOM 2517 C ASN B 57 -46.306 -34.257 20.696 1.00 25.28 C
ATOM 2518 O ASN B 57 -45.688 -34.873 19.818 1.00 26.20 O
ATOM 2519 CB ASN B 57 -44.996 -32.114 20.814 1.00 25.28 C
ATOM 2520 CG ASN B 57 -46.085 -31.276 20.188 1.00 26.27 C
ATOM 2521 OD1 ASN B 57 -46.819 -31.746 19.324 1.00 24.06 O
ATOM 2522 ND2 ASN B 57 -46.204 -30.028 20.632 1.00 28.08 N
ATOM 2523 N PRO B 58 -47.624 -34.424 20.862 1.00 28.43 N
ATOM 2524 CA PRO B 58 -48.352 -35.392 20.022 1.00 25.96 C
ATOM 2525 C PRO B 58 -48.548 -34.955 18.580 1.00 27.36 C
ATOM 2526 O PRO B 58 -48.689 -35.817 17.702 1.00 28.86 O
ATOM 2527 CB PRO B 58 -49.698 -35.539 20.745 1.00 27.66 C
ATOM 2528 CG PRO B 58 -49.888 -34.222 21.424 1.00 31.86 C
ATOM 2529 CD PRO B 58 -48.510 -33.735 21.817 1.00 26.82 C
ATOM 2530 N LYS B 59 -48.585 -33.650 18.302 1.00 24.59 N
ATOM 2531 CA LYS B 59 -48.693 -33.215 16.912 1.00 26.48 C
ATOM 2532 C LYS B 59 -47.400 -33.490 16.159 1.00 25.81 C
ATOM 2533 O LYS B 59 -47.433 -33.837 14.976 1.00 23.14 O
ATOM 2534 CB LYS B 59 -49.068 -31.735 16.849 1.00 25.14 C
ATOM 2535 CG LYS B 59 -50.516 -31.481 17.233 1.00 31.14 C
ATOM 2536 CD LYS B 59 -51.154 -30.433 16.354 1.00 34.60 C
ATOM 2537 CE LYS B 59 -52.580 -30.154 16.780 1.00 33.49 C
ATOM 2538 NZ LYS B 59 -52.991 -28.772 16.406 1.00 38.58 N
ATOM 2539 N VAL B 60 -46.260 -33.360 16.838 1.00 25.14 N
ATOM 2540 CA VAL B 60 -44.990 -33.763 16.246 1.00 29.45 C
ATOM 2541 C VAL B 60 -45.011 -35.251 15.918 1.00 24.98 C
ATOM 2542 O VAL B 60 -44.722 -35.659 14.789 1.00 23.77 O
ATOM 2543 CB VAL B 60 -43.827 -33.418 17.195 1.00 25.89 C
ATOM 2544 CG1 VAL B 60 -42.525 -33.963 16.638 1.00 20.18 C
ATOM 2545 CG2 VAL B 60 -43.743 -31.902 17.422 1.00 22.88 C
ATOM 2546 N LYS B 61 -45.366 -36.085 16.900 1.00 27.72 N
ATOM 2547 CA LYS B 61 -45.429 -37.526 16.668 1.00 30.28 C
ATOM 2548 C LYS B 61 -46.321 -37.859 15.478 1.00 28.63 C
ATOM 2549 O LYS B 61 -45.957 -38.667 14.617 1.00 27.16 O
ATOM 2550 CB LYS B 61 -45.923 -38.246 17.924 1.00 26.98 C
ATOM 2551 CG LYS B 61 -44.858 -38.456 18.978 1.00 39.09 C
ATOM 2552 CD LYS B 61 -45.309 -39.449 20.041 1.00 44.01 C
ATOM 2553 CE LYS B 61 -45.377 -38.794 21.413 1.00 43.28 C
ATOM 2554 NZ LYS B 61 -44.055 -38.760 22.098 1.00 43.54 N
ATOM 2555 N ALA B 62 -47.494 -37.228 15.408 1.00 31.46 N
ATOM 2556 CA ALA B 62 -48.432 -37.544 14.337 1.00 29.50 C
ATOM 2557 C ALA B 62 -47.915 -37.064 12.986 1.00 31.08 C
ATOM 2558 O ALA B 62 -48.013 -37.781 11.981 1.00 25.22 O
ATOM 2559 CB ALA B 62 -49.796 -36.921 14.643 1.00 26.47 C
ATOM 2560 N HIS B 63 -47.378 -35.846 12.937 1.00 26.23 N
ATOM 2561 CA HIS B 63 -46.863 -35.335 11.677 1.00 23.77 C
ATOM 2562 C HIS B 63 -45.616 -36.095 11.234 1.00 22.68 C
ATOM 2563 O HIS B 63 -45.387 -36.255 10.034 1.00 20.99 O
ATOM 2564 CB HIS B 63 -46.572 -33.839 11.798 1.00 26.23 C
ATOM 2565 CG HIS B 63 -46.053 -33.234 10.533 1.00 27.19 C
ATOM 2566 ND1 HIS B 63 -46.838 -33.076 9.411 1.00 25.94 N
ATOM 2567 CD2 HIS B 63 -44.821 -32.779 10.202 1.00 23.11 C
ATOM 2568 CE1 HIS B 63 -46.115 -32.534 8.446 1.00 27.98 C
ATOM 2569 NE2 HIS B 63 -44.887 -32.348 8.898 1.00 25.71 N
ATOM 2570 N GLY B 64 -44.812 -36.575 12.187 1.00 23.18 N
ATOM 2571 CA GLY B 64 -43.672 -37.414 11.842 1.00 21.65 C
ATOM 2572 C GLY B 64 -44.068 -38.667 11.082 1.00 26.43 C
ATOM 2573 O GLY B 64 -43.382 -39.076 10.141 1.00 24.05 O
ATOM 2574 N LYS B 65 -45.159 -39.314 11.504 1.00 26.49 N
ATOM 2575 CA LYS B 65 -45.675 -40.470 10.776 1.00 27.46 C
ATOM 2576 C LYS B 65 -45.921 -40.125 9.311 1.00 25.64 C
ATOM 2577 O LYS B 65 -45.611 -40.918 8.416 1.00 24.42 O
ATOM 2578 CB LYS B 65 -46.967 -40.983 11.424 1.00 27.96 C
ATOM 2579 CG LYS B 65 -46.814 -41.570 12.828 1.00 42.64 C
ATOM 2580 CD LYS B 65 -48.031 -42.425 13.205 1.00 47.49 C
ATOM 2581 CE LYS B 65 -48.322 -42.442 14.714 1.00 50.10 C
ATOM 2582 NZ LYS B 65 -47.224 -41.886 15.565 1.00 42.69 N
ATOM 2583 N LYS B 66 -46.500 -38.950 9.045 1.00 27.33 N
ATOM 2584 CA LYS B 66 -46.769 -38.576 7.658 1.00 22.01 C
ATOM 2585 C LYS B 66 -45.473 -38.323 6.896 1.00 24.17 C
ATOM 2586 O LYS B 66 -45.335 -38.739 5.739 1.00 23.30 O
ATOM 2587 CB LYS B 66 -47.658 -37.333 7.598 1.00 21.88 C
ATOM 2588 CG LYS B 66 -49.073 -37.539 8.116 1.00 35.34 C
ATOM 2589 CD LYS B 66 -49.866 -36.231 8.086 1.00 36.50 C
ATOM 2590 CE LYS B 66 -51.321 -36.446 8.498 1.00 40.66 C
ATOM 2591 NZ LYS B 66 -51.969 -35.167 8.923 1.00 54.49 N
ATOM 2592 N VAL B 67 -44.517 -37.638 7.522 1.00 24.51 N
ATOM 2593 CA VAL B 67 -43.242 -37.379 6.863 1.00 18.86 C
ATOM 2594 C VAL B 67 -42.575 -38.691 6.479 1.00 22.94 C
ATOM 2595 O VAL B 67 -42.101 -38.861 5.353 1.00 22.62 O
ATOM 2596 CB VAL B 67 -42.330 -36.533 7.765 1.00 28.59 C
ATOM 2597 CG1 VAL B 67 -40.895 -36.517 7.206 1.00 22.95 C
ATOM 2598 CG2 VAL B 67 -42.892 -35.114 7.911 1.00 23.39 C
ATOM 2599 N LEU B 68 -42.517 -39.636 7.418 1.00 23.62 N
ATOM 2600 CA LEU B 68 -41.834 -40.893 7.148 1.00 24.47 C
ATOM 2601 C LEU B 68 -42.634 -41.791 6.220 1.00 22.13 C
ATOM 2602 O LEU B 68 -42.043 -42.596 5.492 1.00 24.47 O
ATOM 2603 CB LEU B 68 -41.536 -41.617 8.460 1.00 25.56 C
ATOM 2604 CG LEU B 68 -40.101 -41.430 8.953 1.00 34.21 C
ATOM 2605 CD1 LEU B 68 -39.157 -42.368 8.210 1.00 36.15 C
ATOM 2606 CD2 LEU B 68 -39.652 -39.977 8.806 1.00 29.64 C
ATOM 2607 N GLY B 69 -43.957 -41.639 6.185 1.00 26.76 N
ATOM 2608 CA GLY B 69 -44.732 -42.346 5.180 1.00 23.14 C
ATOM 2609 C GLY B 69 -44.349 -41.931 3.771 1.00 31.59 C
ATOM 2610 O GLY B 69 -44.275 -42.767 2.866 1.00 26.69 O
ATOM 2611 N ALA B 70 -44.079 -40.635 3.573 1.00 27.89 N
ATOM 2612 CA ALA B 70 -43.646 -40.143 2.269 1.00 29.70 C
ATOM 2613 C ALA B 70 -42.242 -40.631 1.917 1.00 27.54 C
ATOM 2614 O ALA B 70 -41.974 -40.974 0.759 1.00 31.07 O
ATOM 2615 CB ALA B 70 -43.711 -38.612 2.246 1.00 27.20 C
ATOM 2616 N PHE B 71 -41.332 -40.671 2.895 1.00 27.30 N
ATOM 2617 CA PHE B 71 -40.020 -41.271 2.660 1.00 26.14 C
ATOM 2618 C PHE B 71 -40.174 -42.711 2.195 1.00 31.46 C
ATOM 2619 O PHE B 71 -39.564 -43.132 1.207 1.00 25.20 O
ATOM 2620 CB PHE B 71 -39.179 -41.234 3.939 1.00 27.71 C
ATOM 2621 CG PHE B 71 -38.279 -40.037 4.054 1.00 40.36 C
ATOM 2622 CD1 PHE B 71 -37.050 -40.007 3.409 1.00 35.48 C
ATOM 2623 CD2 PHE B 71 -38.654 -38.942 4.826 1.00 33.31 C
ATOM 2624 CE1 PHE B 71 -36.212 -38.896 3.526 1.00 32.44 C
ATOM 2625 CE2 PHE B 71 -37.822 -37.835 4.945 1.00 34.88 C
ATOM 2626 CZ PHE B 71 -36.596 -37.816 4.292 1.00 35.48 C
ATOM 2627 N SER B 72 -40.998 -43.478 2.910 1.00 28.70 N
ATOM 2628 CA SER B 72 -41.287 -44.849 2.517 1.00 32.82 C
ATOM 2629 C SER B 72 -41.829 -44.903 1.093 1.00 38.09 C
ATOM 2630 O SER B 72 -41.431 -45.766 0.300 1.00 31.22 O
ATOM 2631 CB SER B 72 -42.279 -45.459 3.513 1.00 29.38 C
ATOM 2632 OG SER B 72 -41.778 -46.657 4.072 1.00 37.44 O
ATOM 2633 N ASP B 73 -42.723 -43.972 0.741 1.00 33.58 N
ATOM 2634 CA ASP B 73 -43.215 -43.908 -0.633 1.00 34.54 C
ATOM 2635 C ASP B 73 -42.084 -43.607 -1.609 1.00 33.33 C
ATOM 2636 O ASP B 73 -42.049 -44.150 -2.719 1.00 36.33 O
ATOM 2637 CB ASP B 73 -44.295 -42.835 -0.752 1.00 40.56 C
ATOM 2638 CG ASP B 73 -45.594 -43.239 -0.097 1.00 46.05 C
ATOM 2639 OD1 ASP B 73 -45.749 -44.436 0.238 1.00 47.60 O
ATOM 2640 OD2 ASP B 73 -46.453 -42.348 0.098 1.00 47.25 O
ATOM 2641 N GLY B 74 -41.141 -42.755 -1.210 1.00 33.57 N
ATOM 2642 CA GLY B 74 -39.995 -42.500 -2.064 1.00 33.56 C
ATOM 2643 C GLY B 74 -39.185 -43.754 -2.342 1.00 36.71 C
ATOM 2644 O GLY B 74 -38.678 -43.942 -3.450 1.00 29.64 O
ATOM 2645 N LEU B 75 -39.082 -44.647 -1.353 1.00 30.77 N
ATOM 2646 CA LEU B 75 -38.278 -45.850 -1.534 1.00 31.62 C
ATOM 2647 C LEU B 75 -38.870 -46.796 -2.562 1.00 31.76 C
ATOM 2648 O LEU B 75 -38.130 -47.585 -3.157 1.00 33.00 O
ATOM 2649 CB LEU B 75 -38.118 -46.578 -0.199 1.00 32.65 C
ATOM 2650 CG LEU B 75 -37.192 -45.942 0.831 1.00 35.01 C
ATOM 2651 CD1 LEU B 75 -37.323 -46.665 2.157 1.00 36.05 C
ATOM 2652 CD2 LEU B 75 -35.750 -45.972 0.353 1.00 30.96 C
ATOM 2653 N ALA B 76 -40.174 -46.710 -2.809 1.00 29.39 N
ATOM 2654 CA ALA B 76 -40.829 -47.512 -3.830 1.00 37.86 C
ATOM 2655 C ALA B 76 -40.823 -46.866 -5.212 1.00 38.14 C
ATOM 2656 O ALA B 76 -41.273 -47.499 -6.174 1.00 39.17 O
ATOM 2657 CB ALA B 76 -42.277 -47.802 -3.416 1.00 40.63 C
ATOM 2658 N HIS B 77 -40.334 -45.633 -5.343 1.00 39.29 N
ATOM 2659 CA HIS B 77 -40.309 -44.938 -6.632 1.00 33.95 C
ATOM 2660 C HIS B 77 -38.984 -44.207 -6.811 1.00 33.85 C
ATOM 2661 O HIS B 77 -38.936 -43.052 -7.232 1.00 35.39 O
ATOM 2662 CB HIS B 77 -41.473 -43.955 -6.761 1.00 38.13 C
ATOM 2663 CG HIS B 77 -42.820 -44.563 -6.516 1.00 41.01 C
ATOM 2664 ND1 HIS B 77 -43.350 -44.717 -5.252 1.00 38.58 N
ATOM 2665 CD2 HIS B 77 -43.753 -45.038 -7.375 1.00 39.43 C
ATOM 2666 CE1 HIS B 77 -44.545 -45.274 -5.343 1.00 41.72 C
ATOM 2667 NE2 HIS B 77 -44.813 -45.480 -6.620 1.00 41.91 N
ATOM 2668 N LEU B 78 -37.880 -44.903 -6.535 1.00 35.76 N
ATOM 2669 CA LEU B 78 -36.570 -44.262 -6.549 1.00 38.23 C
ATOM 2670 C LEU B 78 -36.199 -43.679 -7.909 1.00 44.75 C
ATOM 2671 O LEU B 78 -35.330 -42.802 -7.976 1.00 44.19 O
ATOM 2672 CB LEU B 78 -35.503 -45.255 -6.102 1.00 37.41 C
ATOM 2673 CG LEU B 78 -35.419 -45.457 -4.586 1.00 35.96 C
ATOM 2674 CD1 LEU B 78 -34.228 -46.332 -4.222 1.00 36.75 C
ATOM 2675 CD2 LEU B 78 -35.366 -44.122 -3.843 1.00 30.54 C
ATOM 2676 N ASP B 79 -36.818 -44.131 -8.994 1.00 38.65 N
ATOM 2677 CA ASP B 79 -36.477 -43.599 -10.305 1.00 44.83 C
ATOM 2678 C ASP B 79 -37.389 -42.468 -10.758 1.00 43.63 C
ATOM 2679 O ASP B 79 -37.162 -41.906 -11.833 1.00 49.31 O
ATOM 2680 CB ASP B 79 -36.473 -44.724 -11.342 1.00 51.02 C
ATOM 2681 CG ASP B 79 -35.405 -45.764 -11.054 1.00 68.17 C
ATOM 2682 OD1 ASP B 79 -34.206 -45.403 -11.068 1.00 66.22 O
ATOM 2683 OD2 ASP B 79 -35.762 -46.936 -10.802 1.00 79.05 O
ATOM 2684 N ASN B 80 -38.400 -42.105 -9.968 1.00 38.89 N
ATOM 2685 CA ASN B 80 -39.244 -40.957 -10.274 1.00 38.62 C
ATOM 2686 C ASN B 80 -39.648 -40.264 -8.974 1.00 36.31 C
ATOM 2687 O ASN B 80 -40.819 -40.150 -8.617 1.00 38.82 O
ATOM 2688 CB ASN B 80 -40.471 -41.345 -11.093 1.00 43.32 C
ATOM 2689 CG ASN B 80 -41.195 -40.131 -11.643 1.00 42.00 C
ATOM 2690 OD1 ASN B 80 -40.638 -39.031 -11.694 1.00 36.80 O
ATOM 2691 ND2 ASN B 80 -42.440 -40.321 -12.050 1.00 45.60 N
ATOM 2692 N LEU B 81 -38.646 -39.775 -8.247 1.00 36.05 N
ATOM 2693 CA LEU B 81 -38.928 -39.096 -6.992 1.00 37.00 C
ATOM 2694 C LEU B 81 -39.514 -37.717 -7.255 1.00 34.06 C
ATOM 2695 O LEU B 81 -40.401 -37.260 -6.524 1.00 36.61 O
ATOM 2696 CB LEU B 81 -37.656 -39.002 -6.153 1.00 33.90 C
ATOM 2697 CG LEU B 81 -37.156 -40.292 -5.498 1.00 34.01 C
ATOM 2698 CD1 LEU B 81 -35.723 -40.101 -5.031 1.00 31.44 C
ATOM 2699 CD2 LEU B 81 -38.053 -40.707 -4.340 1.00 30.97 C
ATOM 2700 N LYS B 82 -39.052 -37.050 -8.313 1.00 29.00 N
ATOM 2701 CA LYS B 82 -39.593 -35.736 -8.631 1.00 33.82 C
ATOM 2702 C LYS B 82 -41.090 -35.810 -8.903 1.00 37.30 C
ATOM 2703 O LYS B 82 -41.844 -34.902 -8.527 1.00 35.88 O
ATOM 2704 CB LYS B 82 -38.854 -35.143 -9.826 1.00 38.99 C
ATOM 2705 CG LYS B 82 -37.401 -34.818 -9.552 1.00 37.93 C
ATOM 2706 CD LYS B 82 -36.725 -34.307 -10.812 1.00 47.36 C
ATOM 2707 CE LYS B 82 -35.219 -34.282 -10.644 1.00 56.80 C
ATOM 2708 NZ LYS B 82 -34.586 -35.502 -11.219 1.00 58.28 N
ATOM 2709 N GLY B 83 -41.545 -36.895 -9.527 1.00 35.06 N
ATOM 2710 CA GLY B 83 -42.960 -37.067 -9.799 1.00 35.78 C
ATOM 2711 C GLY B 83 -43.753 -37.478 -8.575 1.00 34.55 C
ATOM 2712 O GLY B 83 -44.869 -36.995 -8.358 1.00 35.49 O
ATOM 2713 N THR B 84 -43.184 -38.373 -7.762 1.00 31.65 N
ATOM 2714 CA THR B 84 -43.873 -38.807 -6.549 1.00 33.65 C
ATOM 2715 C THR B 84 -44.064 -37.653 -5.568 1.00 34.61 C
ATOM 2716 O THR B 84 -45.061 -37.615 -4.837 1.00 33.50 O
ATOM 2717 CB THR B 84 -43.099 -39.947 -5.879 1.00 30.28 C
ATOM 2718 OG1 THR B 84 -42.989 -41.050 -6.785 1.00 36.53 O
ATOM 2719 CG2 THR B 84 -43.804 -40.410 -4.611 1.00 39.36 C
ATOM 2720 N PHE B 85 -43.132 -36.702 -5.544 1.00 30.42 N
ATOM 2721 CA PHE B 85 -43.140 -35.612 -4.577 1.00 33.36 C
ATOM 2722 C PHE B 85 -43.621 -34.297 -5.185 1.00 28.01 C
ATOM 2723 O PHE B 85 -43.379 -33.229 -4.612 1.00 28.98 O
ATOM 2724 CB PHE B 85 -41.751 -35.442 -3.965 1.00 28.51 C
ATOM 2725 CG PHE B 85 -41.359 -36.562 -3.048 1.00 33.84 C
ATOM 2726 CD1 PHE B 85 -42.161 -36.911 -1.976 1.00 39.85 C
ATOM 2727 CD2 PHE B 85 -40.204 -37.288 -3.275 1.00 35.95 C
ATOM 2728 CE1 PHE B 85 -41.804 -37.953 -1.129 1.00 39.05 C
ATOM 2729 CE2 PHE B 85 -39.839 -38.328 -2.433 1.00 37.12 C
ATOM 2730 CZ PHE B 85 -40.640 -38.662 -1.358 1.00 33.22 C
ATOM 2731 N ALA B 86 -44.316 -34.358 -6.321 1.00 27.72 N
ATOM 2732 CA ALA B 86 -44.699 -33.140 -7.025 1.00 28.44 C
ATOM 2733 C ALA B 86 -45.619 -32.273 -6.173 1.00 34.30 C
ATOM 2734 O ALA B 86 -45.522 -31.041 -6.197 1.00 30.00 O
ATOM 2735 CB ALA B 86 -45.364 -33.492 -8.353 1.00 30.29 C
ATOM 2736 N THR B 87 -46.532 -32.895 -5.427 1.00 29.10 N
ATOM 2737 CA THR B 87 -47.428 -32.122 -4.575 1.00 29.92 C
ATOM 2738 C THR B 87 -46.702 -31.572 -3.356 1.00 25.98 C
ATOM 2739 O THR B 87 -46.871 -30.399 -3.001 1.00 24.50 O
ATOM 2740 CB THR B 87 -48.603 -32.992 -4.137 1.00 31.03 C
ATOM 2741 OG1 THR B 87 -49.403 -33.308 -5.283 1.00 32.81 O
ATOM 2742 CG2 THR B 87 -49.448 -32.262 -3.103 1.00 28.21 C
ATOM 2743 N LEU B 88 -45.877 -32.400 -2.712 1.00 20.64 N
ATOM 2744 CA LEU B 88 -45.137 -31.948 -1.537 1.00 23.48 C
ATOM 2745 C LEU B 88 -44.150 -30.842 -1.892 1.00 29.39 C
ATOM 2746 O LEU B 88 -43.912 -29.929 -1.089 1.00 27.68 O
ATOM 2747 CB LEU B 88 -44.422 -33.133 -0.890 1.00 25.59 C
ATOM 2748 CG LEU B 88 -45.370 -34.167 -0.269 1.00 32.42 C
ATOM 2749 CD1 LEU B 88 -44.604 -35.359 0.283 1.00 29.98 C
ATOM 2750 CD2 LEU B 88 -46.218 -33.516 0.832 1.00 25.56 C
ATOM 2751 N SER B 89 -43.551 -30.915 -3.082 1.00 23.72 N
ATOM 2752 CA SER B 89 -42.665 -29.849 -3.536 1.00 28.16 C
ATOM 2753 C SER B 89 -43.407 -28.526 -3.649 1.00 28.32 C
ATOM 2754 O SER B 89 -42.943 -27.495 -3.148 1.00 27.30 O
ATOM 2755 CB SER B 89 -42.034 -30.220 -4.875 1.00 27.90 C
ATOM 2756 OG SER B 89 -41.016 -29.292 -5.190 1.00 31.21 O
ATOM 2757 N GLU B 90 -44.544 -28.530 -4.312 1.00 24.04 N
ATOM 2758 CA GLU B 90 -45.324 -27.282 -4.401 1.00 29.44 C
ATOM 2759 C GLU B 90 -45.603 -26.759 -2.987 1.00 32.00 C
ATOM 2760 O GLU B 90 -45.432 -25.560 -2.757 1.00 28.24 O
ATOM 2761 CB GLU B 90 -46.625 -27.532 -5.151 1.00 30.00 C
ATOM 2762 CG GLU B 90 -47.409 -26.259 -5.444 1.00 30.00 C
ATOM 2763 CD GLU B 90 -48.714 -26.564 -6.151 1.00 30.00 C
ATOM 2764 OE1 GLU B 90 -49.762 -26.636 -5.484 1.00 30.00 O
ATOM 2765 OE2 GLU B 90 -48.672 -26.735 -7.381 1.00 30.00 O
ATOM 2766 N LEU B 91 -46.018 -27.646 -2.093 1.00 26.40 N
ATOM 2767 CA LEU B 91 -46.381 -27.202 -0.749 1.00 27.00 C
ATOM 2768 C LEU B 91 -45.185 -26.616 -0.006 1.00 30.59 C
ATOM 2769 O LEU B 91 -45.281 -25.537 0.597 1.00 24.15 O
ATOM 2770 CB LEU B 91 -46.970 -28.367 0.046 1.00 26.16 C
ATOM 2771 CG LEU B 91 -47.098 -28.112 1.549 1.00 28.61 C
ATOM 2772 CD1 LEU B 91 -48.232 -27.151 1.829 1.00 27.17 C
ATOM 2773 CD2 LEU B 91 -47.319 -29.427 2.296 1.00 27.09 C
ATOM 2774 N HIS B 92 -44.058 -27.330 -0.010 1.00 21.89 N
ATOM 2775 CA HIS B 92 -42.898 -26.901 0.768 1.00 28.38 C
ATOM 2776 C HIS B 92 -42.206 -25.699 0.146 1.00 23.92 C
ATOM 2777 O HIS B 92 -41.646 -24.871 0.870 1.00 24.60 O
ATOM 2778 CB HIS B 92 -41.896 -28.045 0.914 1.00 24.24 C
ATOM 2779 CG HIS B 92 -42.357 -29.126 1.834 1.00 27.76 C
ATOM 2780 ND1 HIS B 92 -43.236 -30.109 1.437 1.00 22.90 N
ATOM 2781 CD2 HIS B 92 -42.083 -29.367 3.137 1.00 24.98 C
ATOM 2782 CE1 HIS B 92 -43.473 -30.919 2.453 1.00 28.82 C
ATOM 2783 NE2 HIS B 92 -42.793 -30.485 3.499 1.00 30.04 N
ATOM 2784 N CYS B 93 -42.207 -25.603 -1.179 1.00 20.35 N
ATOM 2785 CA CYS B 93 -41.475 -24.540 -1.858 1.00 29.41 C
ATOM 2786 C CYS B 93 -42.352 -23.334 -2.178 1.00 34.31 C
ATOM 2787 O CYS B 93 -41.978 -22.199 -1.875 1.00 35.64 O
ATOM 2788 CB CYS B 93 -40.838 -25.082 -3.141 1.00 33.04 C
ATOM 2789 SG CYS B 93 -39.769 -26.529 -2.876 1.00 33.57 S
ATOM 2790 N ASP B 94 -43.509 -23.561 -2.799 1.00 28.74 N
ATOM 2791 CA ASP B 94 -44.333 -22.466 -3.289 1.00 37.05 C
ATOM 2792 C ASP B 94 -45.274 -21.908 -2.230 1.00 34.20 C
ATOM 2793 O ASP B 94 -45.682 -20.749 -2.339 1.00 39.10 O
ATOM 2794 CB ASP B 94 -45.139 -22.910 -4.519 1.00 35.80 C
ATOM 2795 CG ASP B 94 -44.249 -23.286 -5.709 1.00 41.07 C
ATOM 2796 OD1 ASP B 94 -43.109 -22.781 -5.802 1.00 41.97 O
ATOM 2797 OD2 ASP B 94 -44.694 -24.086 -6.561 1.00 38.85 O
ATOM 2798 N LYS B 95 -45.617 -22.688 -1.207 1.00 33.86 N
ATOM 2799 CA LYS B 95 -46.532 -22.246 -0.164 1.00 27.55 C
ATOM 2800 C LYS B 95 -45.839 -21.998 1.167 1.00 33.30 C
ATOM 2801 O LYS B 95 -46.062 -20.957 1.793 1.00 32.22 O
ATOM 2802 CB LYS B 95 -47.657 -23.273 0.028 1.00 32.76 C
ATOM 2803 CG LYS B 95 -48.611 -23.381 -1.148 1.00 40.14 C
ATOM 2804 CD LYS B 95 -49.816 -24.257 -0.800 1.00 40.95 C
ATOM 2805 CE LYS B 95 -50.382 -24.935 -2.041 1.00 46.26 C
ATOM 2806 NZ LYS B 95 -49.396 -25.883 -2.653 1.00 42.55 N
ATOM 2807 N LEU B 96 -44.998 -22.927 1.621 1.00 27.16 N
ATOM 2808 CA LEU B 96 -44.353 -22.816 2.924 1.00 31.24 C
ATOM 2809 C LEU B 96 -43.022 -22.082 2.863 1.00 33.22 C
ATOM 2810 O LEU B 96 -42.579 -21.530 3.875 1.00 32.62 O
ATOM 2811 CB LEU B 96 -44.136 -24.209 3.524 1.00 30.91 C
ATOM 2812 CG LEU B 96 -45.434 -24.952 3.844 1.00 31.66 C
ATOM 2813 CD1 LEU B 96 -45.171 -26.345 4.398 1.00 28.24 C
ATOM 2814 CD2 LEU B 96 -46.271 -24.130 4.818 1.00 34.23 C
ATOM 2815 N HIS B 97 -42.359 -22.098 1.710 1.00 31.35 N
ATOM 2816 CA HIS B 97 -41.084 -21.413 1.529 1.00 31.76 C
ATOM 2817 C HIS B 97 -40.052 -21.915 2.536 1.00 31.74 C
ATOM 2818 O HIS B 97 -39.350 -21.145 3.191 1.00 27.80 O
ATOM 2819 CB HIS B 97 -41.275 -19.898 1.601 1.00 34.67 C
ATOM 2820 CG HIS B 97 -42.184 -19.374 0.530 1.00 35.04 C
ATOM 2821 ND1 HIS B 97 -41.824 -19.349 -0.802 1.00 39.42 N
ATOM 2822 CD2 HIS B 97 -43.451 -18.897 0.585 1.00 36.00 C
ATOM 2823 CE1 HIS B 97 -42.822 -18.858 -1.516 1.00 33.59 C
ATOM 2824 NE2 HIS B 97 -43.821 -18.579 -0.699 1.00 37.27 N
ATOM 2825 N VAL B 98 -39.964 -23.238 2.643 1.00 28.13 N
ATOM 2826 CA VAL B 98 -38.928 -23.886 3.436 1.00 21.89 C
ATOM 2827 C VAL B 98 -37.622 -23.798 2.663 1.00 27.88 C
ATOM 2828 O VAL B 98 -37.532 -24.272 1.523 1.00 27.70 O
ATOM 2829 CB VAL B 98 -39.288 -25.351 3.729 1.00 25.92 C
ATOM 2830 CG1 VAL B 98 -38.124 -26.052 4.410 1.00 20.29 C
ATOM 2831 CG2 VAL B 98 -40.553 -25.438 4.570 1.00 24.56 C
ATOM 2832 N ASP B 99 -36.611 -23.184 3.269 1.00 23.28 N
ATOM 2833 CA ASP B 99 -35.306 -23.165 2.633 1.00 24.95 C
ATOM 2834 C ASP B 99 -34.860 -24.599 2.364 1.00 25.71 C
ATOM 2835 O ASP B 99 -34.954 -25.449 3.261 1.00 25.70 O
ATOM 2836 CB ASP B 99 -34.263 -22.470 3.500 1.00 26.89 C
ATOM 2837 CG ASP B 99 -32.956 -22.297 2.772 1.00 30.22 C
ATOM 2838 OD1 ASP B 99 -32.871 -21.367 1.951 1.00 37.20 O
ATOM 2839 OD2 ASP B 99 -32.032 -23.112 2.979 1.00 32.03 O
ATOM 2840 N PRO B 100 -34.366 -24.905 1.165 1.00 24.57 N
ATOM 2841 CA PRO B 100 -34.064 -26.308 0.836 1.00 28.54 C
ATOM 2842 C PRO B 100 -32.965 -26.917 1.685 1.00 26.96 C
ATOM 2843 O PRO B 100 -32.908 -28.147 1.789 1.00 27.43 O
ATOM 2844 CB PRO B 100 -33.661 -26.255 -0.648 1.00 25.82 C
ATOM 2845 CG PRO B 100 -33.488 -24.810 -0.977 1.00 29.92 C
ATOM 2846 CD PRO B 100 -34.321 -24.028 -0.018 1.00 27.74 C
ATOM 2847 N GLU B 101 -32.090 -26.116 2.298 1.00 25.01 N
ATOM 2848 CA GLU B 101 -31.082 -26.712 3.166 1.00 25.98 C
ATOM 2849 C GLU B 101 -31.730 -27.477 4.310 1.00 24.40 C
ATOM 2850 O GLU B 101 -31.150 -28.444 4.810 1.00 24.83 O
ATOM 2851 CB GLU B 101 -30.127 -25.643 3.705 1.00 28.83 C
ATOM 2852 CG GLU B 101 -29.277 -26.111 4.896 1.00 29.09 C
ATOM 2853 CD GLU B 101 -28.110 -27.005 4.489 1.00 34.46 C
ATOM 2854 OE1 GLU B 101 -27.998 -27.352 3.293 1.00 30.90 O
ATOM 2855 OE2 GLU B 101 -27.303 -27.363 5.372 1.00 39.48 O
ATOM 2856 N ASN B 102 -32.937 -27.072 4.725 1.00 22.80 N
ATOM 2857 CA ASN B 102 -33.628 -27.796 5.785 1.00 21.31 C
ATOM 2858 C ASN B 102 -34.036 -29.198 5.342 1.00 22.57 C
ATOM 2859 O ASN B 102 -34.113 -30.102 6.178 1.00 21.80 O
ATOM 2860 CB ASN B 102 -34.848 -27.006 6.264 1.00 24.07 C
ATOM 2861 CG ASN B 102 -34.471 -25.655 6.864 1.00 21.78 C
ATOM 2862 OD1 ASN B 102 -33.683 -25.583 7.804 1.00 21.16 O
ATOM 2863 ND2 ASN B 102 -35.035 -24.585 6.323 1.00 20.35 N
ATOM 2864 N PHE B 103 -34.332 -29.395 4.049 1.00 22.56 N
ATOM 2865 CA PHE B 103 -34.593 -30.747 3.557 1.00 23.92 C
ATOM 2866 C PHE B 103 -33.374 -31.638 3.769 1.00 26.64 C
ATOM 2867 O PHE B 103 -33.504 -32.820 4.112 1.00 24.56 O
ATOM 2868 CB PHE B 103 -34.952 -30.729 2.069 1.00 23.60 C
ATOM 2869 CG PHE B 103 -36.097 -29.828 1.710 1.00 20.39 C
ATOM 2870 CD1 PHE B 103 -37.161 -29.644 2.572 1.00 21.96 C
ATOM 2871 CD2 PHE B 103 -36.115 -29.185 0.486 1.00 24.42 C
ATOM 2872 CE1 PHE B 103 -38.220 -28.823 2.228 1.00 22.48 C
ATOM 2873 CE2 PHE B 103 -37.179 -28.366 0.127 1.00 24.08 C
ATOM 2874 CZ PHE B 103 -38.225 -28.177 1.004 1.00 26.23 C
ATOM 2875 N ARG B 104 -32.182 -31.098 3.508 1.00 23.00 N
ATOM 2876 CA ARG B 104 -30.953 -31.848 3.731 1.00 24.23 C
ATOM 2877 C ARG B 104 -30.784 -32.188 5.207 1.00 22.62 C
ATOM 2878 O ARG B 104 -30.454 -33.328 5.557 1.00 22.13 O
ATOM 2879 CB ARG B 104 -29.767 -31.035 3.208 1.00 27.07 C
ATOM 2880 CG ARG B 104 -28.417 -31.730 3.242 1.00 32.05 C
ATOM 2881 CD ARG B 104 -27.299 -30.726 2.942 1.00 32.52 C
ATOM 2882 NE ARG B 104 -26.929 -29.956 4.126 1.00 33.72 N
ATOM 2883 CZ ARG B 104 -26.230 -30.445 5.142 1.00 33.91 C
ATOM 2884 NH1 ARG B 104 -25.746 -31.675 5.117 1.00 37.10 N
ATOM 2885 NH2 ARG B 104 -25.997 -29.676 6.201 1.00 35.97 N
ATOM 2886 N LEU B 105 -31.045 -31.220 6.091 1.00 18.98 N
ATOM 2887 CA LEU B 105 -30.905 -31.455 7.525 1.00 23.18 C
ATOM 2888 C LEU B 105 -31.826 -32.575 8.003 1.00 25.87 C
ATOM 2889 O LEU B 105 -31.423 -33.413 8.820 1.00 20.14 O
ATOM 2890 CB LEU B 105 -31.190 -30.164 8.296 1.00 23.85 C
ATOM 2891 CG LEU B 105 -30.208 -29.020 8.035 1.00 22.69 C
ATOM 2892 CD1 LEU B 105 -30.617 -27.760 8.796 1.00 23.40 C
ATOM 2893 CD2 LEU B 105 -28.782 -29.446 8.397 1.00 25.35 C
ATOM 2894 N LEU B 106 -33.076 -32.598 7.526 1.00 21.49 N
ATOM 2895 CA LEU B 106 -33.999 -33.631 7.994 1.00 23.56 C
ATOM 2896 C LEU B 106 -33.555 -35.007 7.515 1.00 22.83 C
ATOM 2897 O LEU B 106 -33.611 -35.984 8.270 1.00 21.27 O
ATOM 2898 CB LEU B 106 -35.430 -33.332 7.532 1.00 19.26 C
ATOM 2899 CG LEU B 106 -36.487 -34.381 7.895 1.00 24.18 C
ATOM 2900 CD1 LEU B 106 -36.467 -34.671 9.386 1.00 20.52 C
ATOM 2901 CD2 LEU B 106 -37.895 -33.958 7.458 1.00 24.36 C
ATOM 2902 N GLY B 107 -33.110 -35.102 6.263 1.00 20.64 N
ATOM 2903 CA GLY B 107 -32.584 -36.367 5.779 1.00 20.77 C
ATOM 2904 C GLY B 107 -31.408 -36.855 6.601 1.00 23.64 C
ATOM 2905 O GLY B 107 -31.268 -38.055 6.852 1.00 25.85 O
ATOM 2906 N ASN B 108 -30.537 -35.931 7.018 1.00 20.74 N
ATOM 2907 CA ASN B 108 -29.372 -36.305 7.811 1.00 20.61 C
ATOM 2908 C ASN B 108 -29.740 -36.660 9.243 1.00 22.48 C
ATOM 2909 O ASN B 108 -29.125 -37.561 9.835 1.00 18.85 O
ATOM 2910 CB ASN B 108 -28.344 -35.177 7.781 1.00 20.74 C
ATOM 2911 CG ASN B 108 -27.553 -35.162 6.489 1.00 28.82 C
ATOM 2912 OD1 ASN B 108 -27.721 -36.040 5.637 1.00 26.87 O
ATOM 2913 ND2 ASN B 108 -26.677 -34.185 6.342 1.00 24.98 N
ATOM 2914 N VAL B 109 -30.746 -35.996 9.813 1.00 19.10 N
ATOM 2915 CA VAL B 109 -31.217 -36.404 11.131 1.00 19.69 C
ATOM 2916 C VAL B 109 -31.768 -37.827 11.080 1.00 22.89 C
ATOM 2917 O VAL B 109 -31.531 -38.632 11.990 1.00 22.07 O
ATOM 2918 CB VAL B 109 -32.248 -35.399 11.678 1.00 21.42 C
ATOM 2919 CG1 VAL B 109 -32.913 -35.945 12.926 1.00 21.72 C
ATOM 2920 CG2 VAL B 109 -31.563 -34.066 11.972 1.00 20.36 C
ATOM 2921 N LEU B 110 -32.526 -38.157 10.032 1.00 18.48 N
ATOM 2922 CA LEU B 110 -33.035 -39.519 9.905 1.00 19.75 C
ATOM 2923 C LEU B 110 -31.893 -40.526 9.849 1.00 26.92 C
ATOM 2924 O LEU B 110 -31.963 -41.596 10.470 1.00 23.58 O
ATOM 2925 CB LEU B 110 -33.922 -39.642 8.667 1.00 24.57 C
ATOM 2926 CG LEU B 110 -34.367 -41.052 8.260 1.00 23.90 C
ATOM 2927 CD1 LEU B 110 -35.076 -41.732 9.421 1.00 27.68 C
ATOM 2928 CD2 LEU B 110 -35.283 -40.974 7.054 1.00 27.39 C
ATOM 2929 N VAL B 111 -30.837 -40.203 9.096 1.00 21.11 N
ATOM 2930 CA VAL B 111 -29.661 -41.066 9.049 1.00 21.81 C
ATOM 2931 C VAL B 111 -29.069 -41.231 10.441 1.00 20.37 C
ATOM 2932 O VAL B 111 -28.627 -42.325 10.815 1.00 20.71 O
ATOM 2933 CB VAL B 111 -28.630 -40.513 8.046 1.00 20.94 C
ATOM 2934 CG1 VAL B 111 -27.260 -41.154 8.261 1.00 18.12 C
ATOM 2935 CG2 VAL B 111 -29.121 -40.751 6.614 1.00 22.87 C
ATOM 2936 N CYS B 112 -29.057 -40.152 11.235 1.00 19.79 N
ATOM 2937 CA CYS B 112 -28.553 -40.244 12.602 1.00 19.49 C
ATOM 2938 C CYS B 112 -29.409 -41.188 13.441 1.00 23.48 C
ATOM 2939 O CYS B 112 -28.881 -41.984 14.228 1.00 21.85 O
ATOM 2940 CB CYS B 112 -28.511 -38.856 13.249 1.00 20.97 C
ATOM 2941 SG CYS B 112 -27.134 -37.801 12.730 1.00 21.78 S
ATOM 2942 N VAL B 113 -30.732 -41.121 13.278 1.00 21.63 N
ATOM 2943 CA VAL B 113 -31.618 -42.005 14.028 1.00 22.60 C
ATOM 2944 C VAL B 113 -31.372 -43.457 13.640 1.00 21.23 C
ATOM 2945 O VAL B 113 -31.326 -44.343 14.500 1.00 26.00 O
ATOM 2946 CB VAL B 113 -33.090 -41.603 13.817 1.00 24.64 C
ATOM 2947 CG1 VAL B 113 -34.023 -42.640 14.449 1.00 22.76 C
ATOM 2948 CG2 VAL B 113 -33.358 -40.216 14.406 1.00 24.62 C
ATOM 2949 N LEU B 114 -31.234 -43.729 12.340 1.00 20.51 N
ATOM 2950 CA LEU B 114 -30.959 -45.093 11.895 1.00 20.92 C
ATOM 2951 C LEU B 114 -29.658 -45.616 12.491 1.00 24.78 C
ATOM 2952 O LEU B 114 -29.609 -46.741 13.003 1.00 25.93 O
ATOM 2953 CB LEU B 114 -30.910 -45.148 10.368 1.00 17.54 C
ATOM 2954 CG LEU B 114 -32.217 -44.830 9.638 1.00 24.25 C
ATOM 2955 CD1 LEU B 114 -32.007 -44.793 8.132 1.00 19.22 C
ATOM 2956 CD2 LEU B 114 -33.321 -45.825 10.023 1.00 25.54 C
ATOM 2957 N ALA B 115 -28.599 -44.799 12.466 1.00 22.49 N
ATOM 2958 CA ALA B 115 -27.342 -45.209 13.083 1.00 22.45 C
ATOM 2959 C ALA B 115 -27.519 -45.432 14.581 1.00 22.96 C
ATOM 2960 O ALA B 115 -26.945 -46.366 15.158 1.00 25.72 O
ATOM 2961 CB ALA B 115 -26.261 -44.158 12.824 1.00 22.99 C
ATOM 2962 N HIS B 116 -28.313 -44.579 15.223 1.00 20.27 N
ATOM 2963 CA HIS B 116 -28.545 -44.696 16.656 1.00 23.73 C
ATOM 2964 C HIS B 116 -29.122 -46.065 17.005 1.00 26.76 C
ATOM 2965 O HIS B 116 -28.618 -46.754 17.900 1.00 25.24 O
ATOM 2966 CB HIS B 116 -29.482 -43.581 17.112 1.00 22.66 C
ATOM 2967 CG HIS B 116 -29.476 -43.352 18.591 1.00 23.44 C
ATOM 2968 ND1 HIS B 116 -30.517 -42.739 19.251 1.00 22.13 N
ATOM 2969 CD2 HIS B 116 -28.557 -43.657 19.539 1.00 25.01 C
ATOM 2970 CE1 HIS B 116 -30.235 -42.662 20.540 1.00 23.12 C
ATOM 2971 NE2 HIS B 116 -29.053 -43.218 20.742 1.00 25.31 N
ATOM 2972 N HIS B 117 -30.156 -46.493 16.279 1.00 23.51 N
ATOM 2973 CA HIS B 117 -30.858 -47.722 16.621 1.00 26.57 C
ATOM 2974 C HIS B 117 -30.223 -48.984 16.045 1.00 25.14 C
ATOM 2975 O HIS B 117 -30.372 -50.054 16.646 1.00 26.69 O
ATOM 2976 CB HIS B 117 -32.317 -47.623 16.166 1.00 24.44 C
ATOM 2977 CG HIS B 117 -33.143 -46.734 17.039 1.00 25.71 C
ATOM 2978 ND1 HIS B 117 -33.933 -47.218 18.059 1.00 20.84 N
ATOM 2979 CD2 HIS B 117 -33.262 -45.384 17.077 1.00 23.15 C
ATOM 2980 CE1 HIS B 117 -34.525 -46.205 18.672 1.00 24.63 C
ATOM 2981 NE2 HIS B 117 -34.133 -45.081 18.096 1.00 22.76 N
ATOM 2982 N PHE B 118 -29.480 -48.890 14.940 1.00 24.50 N
ATOM 2983 CA PHE B 118 -28.918 -50.072 14.296 1.00 25.70 C
ATOM 2984 C PHE B 118 -27.442 -50.290 14.614 1.00 26.77 C
ATOM 2985 O PHE B 118 -26.920 -51.375 14.340 1.00 26.12 O
ATOM 2986 CB PHE B 118 -29.102 -49.987 12.774 1.00 21.63 C
ATOM 2987 CG PHE B 118 -30.525 -50.209 12.325 1.00 24.29 C
ATOM 2988 CD1 PHE B 118 -31.073 -51.480 12.317 1.00 25.40 C
ATOM 2989 CD2 PHE B 118 -31.321 -49.143 11.935 1.00 24.41 C
ATOM 2990 CE1 PHE B 118 -32.386 -51.685 11.921 1.00 26.58 C
ATOM 2991 CE2 PHE B 118 -32.634 -49.344 11.535 1.00 26.84 C
ATOM 2992 CZ PHE B 118 -33.167 -50.611 11.529 1.00 22.22 C
ATOM 2993 N GLY B 119 -26.759 -49.287 15.158 1.00 26.86 N
ATOM 2994 CA GLY B 119 -25.372 -49.468 15.557 1.00 25.19 C
ATOM 2995 C GLY B 119 -24.498 -50.008 14.450 1.00 27.63 C
ATOM 2996 O GLY B 119 -24.559 -49.564 13.293 1.00 28.61 O
ATOM 2997 N LYS B 120 -23.667 -50.993 14.815 1.00 26.35 N
ATOM 2998 CA LYS B 120 -22.697 -51.567 13.889 1.00 29.24 C
ATOM 2999 C LYS B 120 -23.337 -51.997 12.573 1.00 26.99 C
ATOM 3000 O LYS B 120 -22.698 -51.927 11.519 1.00 27.79 O
ATOM 3001 CB LYS B 120 -21.995 -52.749 14.558 1.00 32.22 C
ATOM 3002 CG LYS B 120 -20.910 -53.382 13.715 1.00 42.95 C
ATOM 3003 CD LYS B 120 -20.189 -54.481 14.482 1.00 59.63 C
ATOM 3004 CE LYS B 120 -18.751 -54.653 13.996 1.00 64.24 C
ATOM 3005 NZ LYS B 120 -17.989 -53.366 14.006 1.00 57.51 N
ATOM 3006 N GLU B 121 -24.596 -52.435 12.610 1.00 27.79 N
ATOM 3007 CA GLU B 121 -25.274 -52.852 11.387 1.00 26.43 C
ATOM 3008 C GLU B 121 -25.380 -51.710 10.374 1.00 28.24 C
ATOM 3009 O GLU B 121 -25.437 -51.958 9.164 1.00 23.13 O
ATOM 3010 CB GLU B 121 -26.667 -53.390 11.722 1.00 23.47 C
ATOM 3011 CG GLU B 121 -27.436 -53.870 10.516 1.00 28.16 C
ATOM 3012 CD GLU B 121 -28.651 -54.699 10.871 1.00 35.37 C
ATOM 3013 OE1 GLU B 121 -29.021 -54.749 12.065 1.00 33.99 O
ATOM 3014 OE2 GLU B 121 -29.249 -55.287 9.942 1.00 39.09 O
ATOM 3015 N PHE B 122 -25.431 -50.460 10.843 1.00 25.49 N
ATOM 3016 CA PHE B 122 -25.509 -49.297 9.951 1.00 26.47 C
ATOM 3017 C PHE B 122 -24.101 -48.952 9.463 1.00 23.44 C
ATOM 3018 O PHE B 122 -23.485 -47.963 9.864 1.00 23.98 O
ATOM 3019 CB PHE B 122 -26.167 -48.121 10.668 1.00 20.75 C
ATOM 3020 CG PHE B 122 -26.618 -47.022 9.744 1.00 26.62 C
ATOM 3021 CD1 PHE B 122 -27.657 -47.229 8.854 1.00 27.48 C
ATOM 3022 CD2 PHE B 122 -25.988 -45.790 9.751 1.00 24.27 C
ATOM 3023 CE1 PHE B 122 -28.069 -46.219 7.987 1.00 26.46 C
ATOM 3024 CE2 PHE B 122 -26.395 -44.776 8.896 1.00 24.96 C
ATOM 3025 CZ PHE B 122 -27.431 -44.992 8.005 1.00 23.60 C
ATOM 3026 N THR B 123 -23.596 -49.800 8.566 1.00 22.66 N
ATOM 3027 CA THR B 123 -22.207 -49.724 8.138 1.00 24.47 C
ATOM 3028 C THR B 123 -21.970 -48.545 7.198 1.00 24.22 C
ATOM 3029 O THR B 123 -22.908 -47.999 6.613 1.00 23.09 O
ATOM 3030 CB THR B 123 -21.790 -51.004 7.418 1.00 23.89 C
ATOM 3031 OG1 THR B 123 -22.567 -51.142 6.220 1.00 27.35 O
ATOM 3032 CG2 THR B 123 -21.991 -52.233 8.308 1.00 28.25 C
ATOM 3033 N PRO B 124 -20.711 -48.154 7.024 1.00 22.40 N
ATOM 3034 CA PRO B 124 -20.383 -47.061 6.106 1.00 24.05 C
ATOM 3035 C PRO B 124 -21.037 -47.255 4.749 1.00 22.84 C
ATOM 3036 O PRO B 124 -21.661 -46.324 4.227 1.00 27.27 O
ATOM 3037 CB PRO B 124 -18.852 -47.135 6.017 1.00 22.56 C
ATOM 3038 CG PRO B 124 -18.457 -47.615 7.386 1.00 23.39 C
ATOM 3039 CD PRO B 124 -19.520 -48.642 7.744 1.00 23.97 C
ATOM 3040 N PRO B 125 -20.942 -48.448 4.148 1.00 23.97 N
ATOM 3041 CA PRO B 125 -21.625 -48.645 2.857 1.00 21.92 C
ATOM 3042 C PRO B 125 -23.139 -48.568 2.966 1.00 24.98 C
ATOM 3043 O PRO B 125 -23.798 -48.050 2.054 1.00 22.89 O
ATOM 3044 CB PRO B 125 -21.147 -50.037 2.413 1.00 31.51 C
ATOM 3045 CG PRO B 125 -19.911 -50.305 3.222 1.00 25.13 C
ATOM 3046 CD PRO B 125 -20.181 -49.643 4.547 1.00 27.60 C
ATOM 3047 N VAL B 126 -23.721 -49.056 4.062 1.00 24.28 N
ATOM 3048 CA VAL B 126 -25.166 -48.939 4.228 1.00 26.66 C
ATOM 3049 C VAL B 126 -25.565 -47.473 4.363 1.00 24.80 C
ATOM 3050 O VAL B 126 -26.506 -47.008 3.711 1.00 25.48 O
ATOM 3051 CB VAL B 126 -25.646 -49.777 5.428 1.00 25.96 C
ATOM 3052 CG1 VAL B 126 -27.065 -49.369 5.823 1.00 20.49 C
ATOM 3053 CG2 VAL B 126 -25.609 -51.265 5.079 1.00 27.46 C
ATOM 3054 N GLN B 127 -24.848 -46.718 5.200 1.00 27.09 N
ATOM 3055 CA GLN B 127 -25.137 -45.292 5.308 1.00 26.64 C
ATOM 3056 C GLN B 127 -25.021 -44.604 3.952 1.00 22.41 C
ATOM 3057 O GLN B 127 -25.852 -43.757 3.606 1.00 27.11 O
ATOM 3058 CB GLN B 127 -24.205 -44.626 6.321 1.00 23.59 C
ATOM 3059 CG GLN B 127 -24.233 -43.109 6.210 1.00 23.82 C
ATOM 3060 CD GLN B 127 -23.146 -42.430 6.999 1.00 23.33 C
ATOM 3061 OE1 GLN B 127 -22.276 -43.080 7.585 1.00 24.74 O
ATOM 3062 NE2 GLN B 127 -23.190 -41.104 7.025 1.00 21.13 N
ATOM 3063 N ALA B 128 -24.012 -44.971 3.160 1.00 22.98 N
ATOM 3064 CA ALA B 128 -23.823 -44.325 1.864 1.00 24.25 C
ATOM 3065 C ALA B 128 -25.031 -44.528 0.952 1.00 28.12 C
ATOM 3066 O ALA B 128 -25.445 -43.600 0.244 1.00 26.78 O
ATOM 3067 CB ALA B 128 -22.544 -44.832 1.197 1.00 26.29 C
ATOM 3068 N ALA B 129 -25.599 -45.737 0.929 1.00 26.09 N
ATOM 3069 CA ALA B 129 -26.818 -45.934 0.150 1.00 28.64 C
ATOM 3070 C ALA B 129 -27.937 -45.042 0.672 1.00 25.10 C
ATOM 3071 O ALA B 129 -28.687 -44.448 -0.107 1.00 25.68 O
ATOM 3072 CB ALA B 129 -27.244 -47.402 0.175 1.00 28.17 C
ATOM 3073 N TYR B 130 -28.069 -44.939 1.992 1.00 23.65 N
ATOM 3074 CA TYR B 130 -29.111 -44.084 2.550 1.00 23.91 C
ATOM 3075 C TYR B 130 -28.861 -42.602 2.260 1.00 25.70 C
ATOM 3076 O TYR B 130 -29.820 -41.832 2.121 1.00 25.24 O
ATOM 3077 CB TYR B 130 -29.253 -44.349 4.050 1.00 21.90 C
ATOM 3078 CG TYR B 130 -30.309 -45.406 4.305 1.00 24.14 C
ATOM 3079 CD1 TYR B 130 -31.648 -45.064 4.372 1.00 24.89 C
ATOM 3080 CD2 TYR B 130 -29.971 -46.744 4.420 1.00 21.36 C
ATOM 3081 CE1 TYR B 130 -32.626 -46.018 4.569 1.00 27.69 C
ATOM 3082 CE2 TYR B 130 -30.945 -47.711 4.616 1.00 25.33 C
ATOM 3083 CZ TYR B 130 -32.269 -47.342 4.683 1.00 28.62 C
ATOM 3084 OH TYR B 130 -33.251 -48.286 4.878 1.00 24.94 O
ATOM 3085 N GLN B 131 -27.598 -42.172 2.175 1.00 23.51 N
ATOM 3086 CA GLN B 131 -27.339 -40.772 1.831 1.00 26.16 C
ATOM 3087 C GLN B 131 -27.793 -40.457 0.410 1.00 21.68 C
ATOM 3088 O GLN B 131 -28.282 -39.354 0.141 1.00 24.55 O
ATOM 3089 CB GLN B 131 -25.861 -40.440 2.020 1.00 21.76 C
ATOM 3090 CG GLN B 131 -25.390 -40.647 3.446 1.00 22.45 C
ATOM 3091 CD GLN B 131 -25.844 -39.561 4.387 1.00 21.53 C
ATOM 3092 OE1 GLN B 131 -25.601 -39.644 5.584 1.00 25.02 O
ATOM 3093 NE2 GLN B 131 -26.490 -38.521 3.852 1.00 20.80 N
ATOM 3094 N LYS B 132 -27.649 -41.415 -0.513 1.00 24.94 N
ATOM 3095 CA LYS B 132 -28.179 -41.236 -1.863 1.00 25.93 C
ATOM 3096 C LYS B 132 -29.691 -41.074 -1.848 1.00 25.52 C
ATOM 3097 O LYS B 132 -30.249 -40.284 -2.619 1.00 23.64 O
ATOM 3098 CB LYS B 132 -27.805 -42.428 -2.747 1.00 28.12 C
ATOM 3099 CG LYS B 132 -26.384 -42.446 -3.245 1.00 28.20 C
ATOM 3100 CD LYS B 132 -26.050 -43.850 -3.723 1.00 34.21 C
ATOM 3101 CE LYS B 132 -24.795 -43.880 -4.557 1.00 29.63 C
ATOM 3102 NZ LYS B 132 -24.685 -45.167 -5.315 1.00 44.96 N
ATOM 3103 N VAL B 133 -30.374 -41.869 -1.024 1.00 25.86 N
ATOM 3104 CA VAL B 133 -31.832 -41.801 -0.947 1.00 23.92 C
ATOM 3105 C VAL B 133 -32.276 -40.457 -0.384 1.00 21.35 C
ATOM 3106 O VAL B 133 -33.149 -39.793 -0.954 1.00 23.81 O
ATOM 3107 CB VAL B 133 -32.385 -42.976 -0.118 1.00 24.55 C
ATOM 3108 CG1 VAL B 133 -33.887 -42.876 -0.014 1.00 24.12 C
ATOM 3109 CG2 VAL B 133 -32.008 -44.299 -0.776 1.00 20.50 C
ATOM 3110 N VAL B 134 -31.717 -40.047 0.760 1.00 21.21 N
ATOM 3111 CA VAL B 134 -32.196 -38.799 1.358 1.00 24.69 C
ATOM 3112 C VAL B 134 -31.792 -37.601 0.503 1.00 24.33 C
ATOM 3113 O VAL B 134 -32.460 -36.560 0.530 1.00 28.28 O
ATOM 3114 CB VAL B 134 -31.727 -38.632 2.820 1.00 22.41 C
ATOM 3115 CG1 VAL B 134 -32.313 -39.729 3.712 1.00 27.87 C
ATOM 3116 CG2 VAL B 134 -30.213 -38.580 2.941 1.00 22.50 C
ATOM 3117 N ALA B 135 -30.693 -37.708 -0.252 1.00 22.75 N
ATOM 3118 CA ALA B 135 -30.348 -36.635 -1.176 1.00 23.92 C
ATOM 3119 C ALA B 135 -31.335 -36.584 -2.333 1.00 26.85 C
ATOM 3120 O ALA B 135 -31.755 -35.497 -2.751 1.00 24.02 O
ATOM 3121 CB ALA B 135 -28.919 -36.810 -1.689 1.00 27.09 C
ATOM 3122 N GLY B 136 -31.746 -37.748 -2.843 1.00 26.31 N
ATOM 3123 CA GLY B 136 -32.764 -37.758 -3.882 1.00 26.19 C
ATOM 3124 C GLY B 136 -34.072 -37.156 -3.404 1.00 25.91 C
ATOM 3125 O GLY B 136 -34.712 -36.384 -4.123 1.00 28.32 O
ATOM 3126 N VAL B 137 -34.472 -37.484 -2.176 1.00 23.65 N
ATOM 3127 CA VAL B 137 -35.720 -36.962 -1.621 1.00 28.48 C
ATOM 3128 C VAL B 137 -35.634 -35.450 -1.441 1.00 25.40 C
ATOM 3129 O VAL B 137 -36.553 -34.715 -1.813 1.00 25.70 O
ATOM 3130 CB VAL B 137 -36.063 -37.677 -0.298 1.00 28.87 C
ATOM 3131 CG1 VAL B 137 -37.202 -36.967 0.417 1.00 26.16 C
ATOM 3132 CG2 VAL B 137 -36.424 -39.133 -0.555 1.00 23.09 C
ATOM 3133 N ALA B 138 -34.544 -34.962 -0.845 1.00 25.02 N
ATOM 3134 CA ALA B 138 -34.393 -33.518 -0.681 1.00 24.54 C
ATOM 3135 C ALA B 138 -34.414 -32.801 -2.027 1.00 25.51 C
ATOM 3136 O ALA B 138 -35.004 -31.719 -2.156 1.00 25.10 O
ATOM 3137 CB ALA B 138 -33.106 -33.203 0.087 1.00 23.78 C
ATOM 3138 N ASN B 139 -33.762 -33.378 -3.039 1.00 26.53 N
ATOM 3139 CA ASN B 139 -33.754 -32.763 -4.363 1.00 29.95 C
ATOM 3140 C ASN B 139 -35.149 -32.767 -4.977 1.00 30.14 C
ATOM 3141 O ASN B 139 -35.569 -31.780 -5.592 1.00 29.28 O
ATOM 3142 CB ASN B 139 -32.759 -33.484 -5.272 1.00 30.24 C
ATOM 3143 CG ASN B 139 -32.720 -32.898 -6.664 1.00 45.66 C
ATOM 3144 OD1 ASN B 139 -32.163 -31.819 -6.875 1.00 45.97 O
ATOM 3145 ND2 ASN B 139 -33.314 -33.605 -7.628 1.00 43.20 N
ATOM 3146 N ALA B 140 -35.875 -33.874 -4.839 1.00 24.86 N
ATOM 3147 CA ALA B 140 -37.237 -33.922 -5.355 1.00 27.26 C
ATOM 3148 C ALA B 140 -38.130 -32.927 -4.625 1.00 27.06 C
ATOM 3149 O ALA B 140 -39.017 -32.316 -5.231 1.00 30.24 O
ATOM 3150 CB ALA B 140 -37.796 -35.339 -5.225 1.00 28.33 C
ATOM 3151 N LEU B 141 -37.918 -32.758 -3.316 1.00 27.08 N
ATOM 3152 CA LEU B 141 -38.699 -31.783 -2.563 1.00 25.42 C
ATOM 3153 C LEU B 141 -38.393 -30.349 -2.980 1.00 27.59 C
ATOM 3154 O LEU B 141 -39.289 -29.498 -2.962 1.00 26.59 O
ATOM 3155 CB LEU B 141 -38.444 -31.950 -1.072 1.00 27.06 C
ATOM 3156 CG LEU B 141 -39.511 -32.728 -0.313 1.00 29.96 C
ATOM 3157 CD1 LEU B 141 -39.127 -32.783 1.146 1.00 29.67 C
ATOM 3158 CD2 LEU B 141 -40.856 -32.052 -0.486 1.00 29.03 C
ATOM 3159 N ALA B 142 -37.148 -30.056 -3.347 1.00 25.66 N
ATOM 3160 CA ALA B 142 -36.763 -28.716 -3.775 1.00 30.00 C
ATOM 3161 C ALA B 142 -37.018 -28.460 -5.257 1.00 37.66 C
ATOM 3162 O ALA B 142 -36.687 -27.372 -5.748 1.00 36.82 O
ATOM 3163 CB ALA B 142 -35.281 -28.472 -3.455 1.00 31.38 C
ATOM 3164 N HIS B 143 -37.624 -29.418 -5.969 1.00 32.71 N
ATOM 3165 CA HIS B 143 -37.712 -29.338 -7.426 1.00 36.48 C
ATOM 3166 C HIS B 143 -38.419 -28.072 -7.898 1.00 41.60 C
ATOM 3167 O HIS B 143 -38.032 -27.491 -8.919 1.00 40.21 O
ATOM 3168 CB HIS B 143 -38.425 -30.570 -7.983 1.00 39.75 C
ATOM 3169 CG HIS B 143 -38.165 -30.807 -9.439 1.00 48.33 C
ATOM 3170 ND1 HIS B 143 -36.898 -30.779 -9.983 1.00 52.15 N
ATOM 3171 CD2 HIS B 143 -39.010 -31.065 -10.466 1.00 44.79 C
ATOM 3172 CE1 HIS B 143 -36.972 -31.021 -11.280 1.00 49.74 C
ATOM 3173 NE2 HIS B 143 -38.242 -31.197 -11.598 1.00 50.70 N
ATOM 3174 N LYS B 144 -39.472 -27.634 -7.196 1.00 37.65 N
ATOM 3175 CA LYS B 144 -40.133 -26.404 -7.630 1.00 37.29 C
ATOM 3176 C LYS B 144 -39.258 -25.167 -7.445 1.00 44.43 C
ATOM 3177 O LYS B 144 -39.644 -24.084 -7.899 1.00 41.67 O
ATOM 3178 CB LYS B 144 -41.464 -26.221 -6.899 1.00 37.15 C
ATOM 3179 CG LYS B 144 -42.577 -27.167 -7.360 1.00 35.53 C
ATOM 3180 CD LYS B 144 -42.746 -27.188 -8.884 1.00 42.31 C
ATOM 3181 CE LYS B 144 -43.189 -25.838 -9.450 1.00 33.39 C
ATOM 3182 NZ LYS B 144 -44.461 -25.323 -8.843 1.00 38.48 N
ATOM 3183 N TYR B 145 -38.091 -25.309 -6.806 1.00 44.80 N
ATOM 3184 CA TYR B 145 -37.092 -24.248 -6.720 1.00 44.54 C
ATOM 3185 C TYR B 145 -36.134 -24.253 -7.899 1.00 47.24 C
ATOM 3186 O TYR B 145 -35.596 -23.199 -8.257 1.00 48.54 O
ATOM 3187 CB TYR B 145 -36.240 -24.403 -5.456 1.00 43.41 C
ATOM 3188 CG TYR B 145 -36.866 -23.991 -4.144 1.00 38.89 C
ATOM 3189 CD1 TYR B 145 -37.607 -22.818 -4.027 1.00 40.91 C
ATOM 3190 CD2 TYR B 145 -36.680 -24.768 -3.006 1.00 31.81 C
ATOM 3191 CE1 TYR B 145 -38.160 -22.442 -2.815 1.00 38.01 C
ATOM 3192 CE2 TYR B 145 -37.229 -24.405 -1.794 1.00 36.81 C
ATOM 3193 CZ TYR B 145 -37.967 -23.244 -1.702 1.00 35.17 C
ATOM 3194 OH TYR B 145 -38.504 -22.892 -0.490 1.00 28.87 O
ATOM 3195 N HIS B 146 -35.882 -25.418 -8.486 1.00 50.14 N
ATOM 3196 CA HIS B 146 -34.857 -25.548 -9.512 1.00 56.71 C
ATOM 3197 C HIS B 146 -35.265 -26.508 -10.623 1.00 63.29 C
ATOM 3198 O HIS B 146 -36.019 -26.127 -11.524 1.00 68.40 O
ATOM 3199 CB HIS B 146 -33.520 -25.980 -8.881 1.00 60.00 C
ATOM 3200 CG HIS B 146 -33.579 -27.251 -8.086 1.00 52.71 C
ATOM 3201 ND1 HIS B 146 -34.168 -28.406 -8.558 1.00 53.29 N
ATOM 3202 CD2 HIS B 146 -33.088 -27.554 -6.860 1.00 45.39 C
ATOM 3203 CE1 HIS B 146 -34.045 -29.361 -7.652 1.00 47.33 C
ATOM 3204 NE2 HIS B 146 -33.390 -28.871 -6.616 1.00 44.20 N
ATOM 3205 OXT HIS B 146 -34.827 -27.662 -10.664 1.00 65.42 O
TER 3206 HIS B 146
TER 4330 HIS D 146
TER 5273 GLY F 129
TER 6230 GLY E 129
HETATM 6354 CHA HEM B 201 -46.113 -30.983 5.623 1.00 22.99 C
HETATM 6355 CHB HEM B 201 -43.183 -34.460 3.988 1.00 24.74 C
HETATM 6356 CHC HEM B 201 -39.293 -31.788 5.127 1.00 23.60 C
HETATM 6357 CHD HEM B 201 -42.232 -28.414 6.993 1.00 23.35 C
HETATM 6358 C1A HEM B 201 -45.660 -32.184 5.136 1.00 25.28 C
HETATM 6359 C2A HEM B 201 -46.472 -33.340 4.822 1.00 28.60 C
HETATM 6360 C3A HEM B 201 -45.657 -34.296 4.371 1.00 28.05 C
HETATM 6361 C4A HEM B 201 -44.304 -33.776 4.383 1.00 21.76 C
HETATM 6362 CMA HEM B 201 -46.064 -35.715 3.918 1.00 23.66 C
HETATM 6363 CAA HEM B 201 -48.003 -33.440 4.998 1.00 29.53 C
HETATM 6364 CBA HEM B 201 -48.726 -32.594 3.960 1.00 40.89 C
HETATM 6365 CGA HEM B 201 -50.189 -32.978 3.884 1.00 48.78 C
HETATM 6366 O1A HEM B 201 -50.886 -32.442 2.982 1.00 45.84 O
HETATM 6367 O2A HEM B 201 -50.663 -33.805 4.716 1.00 52.76 O
HETATM 6368 C1B HEM B 201 -41.885 -34.030 4.117 1.00 24.27 C
HETATM 6369 C2B HEM B 201 -40.719 -34.749 3.656 1.00 24.16 C
HETATM 6370 C3B HEM B 201 -39.643 -34.021 3.955 1.00 22.54 C
HETATM 6371 C4B HEM B 201 -40.084 -32.807 4.628 1.00 21.27 C
HETATM 6372 CMB HEM B 201 -40.706 -36.113 2.915 1.00 25.04 C
HETATM 6373 CAB HEM B 201 -38.200 -34.470 3.613 1.00 28.34 C
HETATM 6374 CBB HEM B 201 -37.169 -33.622 3.657 1.00 30.33 C
HETATM 6375 C1C HEM B 201 -39.740 -30.652 5.776 1.00 22.60 C
HETATM 6376 C2C HEM B 201 -38.919 -29.631 6.406 1.00 21.44 C
HETATM 6377 C3C HEM B 201 -39.739 -28.709 6.932 1.00 24.35 C
HETATM 6378 C4C HEM B 201 -41.100 -29.101 6.629 1.00 21.48 C
HETATM 6379 CMC HEM B 201 -37.378 -29.650 6.476 1.00 18.29 C
HETATM 6380 CAC HEM B 201 -39.364 -27.420 7.703 1.00 25.53 C
HETATM 6381 CBC HEM B 201 -38.190 -27.296 8.332 1.00 27.02 C
HETATM 6382 C1D HEM B 201 -43.528 -28.827 6.791 1.00 26.34 C
HETATM 6383 C2D HEM B 201 -44.709 -28.121 7.229 1.00 26.37 C
HETATM 6384 C3D HEM B 201 -45.774 -28.822 6.849 1.00 27.90 C
HETATM 6385 C4D HEM B 201 -45.312 -30.004 6.160 1.00 26.81 C
HETATM 6386 CMD HEM B 201 -44.734 -26.786 8.005 1.00 28.77 C
HETATM 6387 CAD HEM B 201 -47.243 -28.433 7.121 1.00 23.40 C
HETATM 6388 CBD HEM B 201 -47.596 -29.063 8.466 1.00 24.65 C
HETATM 6389 CGD HEM B 201 -48.952 -28.587 8.929 1.00 35.88 C
HETATM 6390 O1D HEM B 201 -49.931 -29.373 8.850 1.00 32.31 O
HETATM 6391 O2D HEM B 201 -49.050 -27.418 9.386 1.00 37.50 O
HETATM 6392 NA HEM B 201 -44.343 -32.485 4.854 1.00 23.07 N
HETATM 6393 NB HEM B 201 -41.464 -32.848 4.705 1.00 21.80 N
HETATM 6394 NC HEM B 201 -41.064 -30.288 5.939 1.00 21.46 N
HETATM 6395 ND HEM B 201 -43.930 -29.977 6.141 1.00 22.57 N
HETATM 6396 FE HEM B 201 -42.685 -31.327 5.404 1.00 25.12 FE
HETATM 6612 O HOH B 301 -50.008 -31.635 -6.874 1.00 34.84 O
HETATM 6613 O HOH B 302 -47.788 -36.653 24.125 1.00 36.56 O
HETATM 6614 O HOH B 303 -30.602 -56.486 12.779 1.00 34.29 O
HETATM 6615 O HOH B 304 -49.025 -28.302 -2.902 1.00 36.26 O
HETATM 6616 O HOH B 305 -25.911 -30.045 11.200 1.00 34.68 O
HETATM 6617 O HOH B 306 -39.644 -19.824 9.180 1.00 31.14 O
HETATM 6618 O HOH B 307 -42.487 -33.685 -10.628 1.00 46.65 O
HETATM 6619 O HOH B 308 -35.493 -56.636 6.609 1.00 29.18 O
HETATM 6620 O HOH B 309 -17.603 -50.855 14.034 1.00 41.93 O
HETATM 6621 O HOH B 310 -41.385 -48.222 0.968 1.00 43.79 O
HETATM 6622 O HOH B 311 -47.178 -39.428 4.116 1.00 29.48 O
HETATM 6623 O HOH B 312 -43.800 -38.656 24.635 1.00 40.75 O
HETATM 6624 O HOH B 313 -45.887 -29.926 -8.467 1.00 33.92 O
HETATM 6625 O HOH B 314 -30.953 -31.350 -4.656 1.00 39.64 O
HETATM 6626 O HOH B 315 -45.066 -31.901 24.753 1.00 30.42 O
HETATM 6627 O HOH B 316 -49.400 -32.736 9.464 1.00 33.76 O
HETATM 6628 O HOH B 317 -40.686 -50.534 7.309 1.00 35.47 O
HETATM 6629 O HOH B 318 -26.878 -25.936 7.501 1.00 46.37 O
HETATM 6630 O HOH B 319 -43.240 -35.752 19.915 1.00 25.77 O
HETATM 6631 O HOH B 320 -31.293 -24.705 7.234 1.00 26.78 O
HETATM 6632 O HOH B 321 -28.266 -53.609 14.433 1.00 27.93 O
HETATM 6633 O HOH B 322 -47.586 -25.975 11.001 1.00 38.29 O
HETATM 6634 O HOH B 323 -26.752 -55.326 0.457 1.00 50.28 O
HETATM 6635 O HOH B 324 -30.101 -55.148 7.458 1.00 36.13 O
HETATM 6636 O HOH B 325 -44.603 -40.851 15.183 1.00 35.69 O
HETATM 6637 O HOH B 326 -46.338 -27.174 -8.706 1.00 31.27 O
HETATM 6638 O HOH B 327 -26.995 -37.452 1.450 1.00 23.75 O
HETATM 6639 O HOH B 328 -29.038 -39.024 -4.628 1.00 32.96 O
HETATM 6640 O HOH B 329 -20.634 -50.239 11.364 1.00 28.88 O
HETATM 6641 O HOH B 330 -45.840 -43.587 8.342 1.00 34.14 O
HETATM 6642 O HOH B 331 -30.646 -26.826 19.764 1.00 33.78 O
HETATM 6643 O HOH B 332 -48.803 -42.091 -1.178 1.00 38.88 O
HETATM 6644 O HOH B 333 -49.551 -30.495 20.604 1.00 26.72 O
HETATM 6645 O HOH B 334 -40.549 -35.977 26.242 1.00 35.58 O
HETATM 6646 O HOH B 335 -33.513 -27.378 21.264 1.00 37.92 O
HETATM 6647 O HOH B 336 -42.510 -32.255 7.554 1.00 26.74 O
HETATM 6648 O HOH B 337 -49.774 -24.033 18.908 1.00 41.67 O
HETATM 6649 O HOH B 338 -41.508 -41.962 18.216 1.00 36.60 O
HETATM 6650 O HOH B 339 -50.184 -39.466 11.680 1.00 33.51 O
HETATM 6651 O HOH B 340 -22.783 -48.229 -0.530 1.00 33.48 O
HETATM 6652 O HOH B 341 -40.850 -32.391 -7.330 1.00 36.24 O
HETATM 6653 O HOH B 342 -46.579 -39.182 -3.101 1.00 31.22 O
HETATM 6654 O HOH B 343 -30.150 -33.235 -2.423 1.00 34.37 O
HETATM 6655 O HOH B 344 -22.545 -53.587 4.843 1.00 35.63 O
HETATM 6656 O HOH B 345 -38.354 -52.901 3.154 1.00 35.37 O
HETATM 6657 O HOH B 346 -33.183 -56.975 0.967 1.00 35.18 O
HETATM 6658 O HOH B 347 -29.639 -35.271 3.694 1.00 28.94 O
HETATM 6659 O HOH B 348 -34.042 -35.690 2.699 1.00 31.67 O
HETATM 6660 O HOH B 349 -34.653 -36.302 -6.948 1.00 28.11 O
HETATM 6661 O HOH B 350 -25.365 -54.143 7.361 1.00 33.08 O
HETATM 6662 O HOH B 351 -31.475 -21.121 -0.505 1.00 55.65 O
HETATM 6663 O HOH B 352 -49.876 -33.226 13.627 1.00 28.16 O
HETATM 6664 O HOH B 353 -51.803 -27.999 13.925 1.00 39.70 O
HETATM 6665 O HOH B 354 -29.161 -53.543 5.540 1.00 34.72 O
HETATM 6666 O HOH B 355 -50.419 -34.228 11.140 1.00 48.19 O
HETATM 6667 O HOH B 356 -39.527 -29.606 30.005 1.00 46.46 O
HETATM 6668 O HOH B 357 -45.763 -23.088 8.311 1.00 34.88 O
HETATM 6669 O HOH B 358 -46.592 -36.426 -10.643 1.00 39.40 O
HETATM 6670 O HOH B 359 -37.840 -47.784 -6.072 1.00 38.14 O
HETATM 6671 O HOH B 360 -53.103 -35.223 5.486 1.00 46.12 O
HETATM 6672 O HOH B 361 -35.125 -20.250 0.455 1.00 44.54 O
HETATM 6673 O HOH B 362 -33.035 -41.975 17.963 1.00 30.76 O
HETATM 6674 O HOH B 363 -25.844 -33.792 3.087 1.00 35.90 O
HETATM 6675 O HOH B 364 -44.187 -20.803 6.231 1.00 38.08 O
HETATM 6676 O HOH B 365 -42.636 -18.467 6.709 1.00 39.83 O
HETATM 6677 O HOH B 366 -47.666 -23.847 11.905 1.00 40.97 O
HETATM 6678 O HOH B 367 -35.610 -39.969 -8.952 1.00 39.59 O
HETATM 6679 O HOH B 368 -50.873 -29.463 -5.642 1.00 36.54 O
HETATM 6680 O HOH B 369 -39.083 -45.626 -10.394 1.00 50.52 O
HETATM 6681 O HOH B 370 -36.935 -38.358 -10.377 1.00 51.52 O
HETATM 6682 O HOH B 371 -36.225 -27.461 22.390 1.00 36.91 O
HETATM 6683 O HOH B 372 -26.318 -53.821 16.259 1.00 46.95 O
HETATM 6684 O HOH B 373 -49.750 -43.423 10.716 1.00 56.79 O
HETATM 6685 O HOH B 374 -43.698 -14.591 12.401 1.00 34.87 O
HETATM 6686 O HOH B 375 -35.320 -39.239 -12.198 1.00 47.37 O
HETATM 6687 O HOH B 376 -45.782 -39.153 -0.831 1.00 38.05 O
HETATM 6688 O HOH B 377 -36.360 -19.539 2.725 1.00 39.08 O
HETATM 6689 O HOH B 378 -44.941 -30.568 27.130 1.00 30.42 O
HETATM 6690 O HOH B 379 -51.988 -34.780 17.143 1.00 38.56 O
HETATM 6691 O HOH B 380 -45.990 -37.961 25.852 1.00 39.50 O
HETATM 6692 O HOH B 381 -39.608 -43.118 20.165 1.00 55.90 O
HETATM 6693 O HOH B 382 -25.925 -27.717 9.457 1.00 36.78 O
HETATM 6694 O HOH B 383 -40.454 -52.368 4.485 1.00 35.37 O
HETATM 6695 O HOH B 384 -27.924 -34.891 1.997 1.00 34.05 O
HETATM 6696 O HOH B 385 -30.267 -57.595 6.584 1.00 44.04 O
HETATM 6697 O HOH B 386 -22.802 -50.503 -1.365 1.00 38.63 O
HETATM 6698 O HOH B 387 -36.866 -57.133 4.373 1.00 54.70 O
HETATM 6699 O HOH B 388 -48.409 -30.887 -8.927 1.00 33.67 O
HETATM 6700 O HOH B 389 -47.792 -44.027 4.583 1.00 48.32 O
HETATM 6701 O HOH B 390 -53.790 -32.024 13.976 1.00 37.21 O
HETATM 6702 O HOH B 391 -50.659 -29.446 -0.942 1.00 34.43 O
HETATM 6703 O HOH B 392 -51.474 -30.760 13.074 1.00 35.42 O
HETATM 6704 O HOH B 393 -47.257 -50.550 15.888 1.00 41.71 O
HETATM 6705 O HOH B 394 -33.704 -38.369 -8.212 1.00 41.45 O
HETATM 6706 O HOH B 395 -20.260 -47.672 -0.282 1.00 39.19 O
HETATM 6707 O HOH B 396 -47.581 -31.359 24.438 1.00 23.86 O
HETATM 6708 O HOH B 397 -35.635 -57.695 2.326 1.00 43.00 O
HETATM 6709 O HOH B 398 -35.680 -36.905 24.811 1.00 33.59 O
HETATM 6710 O HOH B 399 -28.633 -24.310 8.077 1.00 35.06 O
HETATM 6711 O HOH B 400 -47.885 -41.202 -3.788 1.00 33.70 O
HETATM 6712 O HOH B 401 -51.222 -40.556 14.417 1.00 53.53 O
HETATM 6713 O HOH B 402 -41.556 -45.119 -10.328 1.00 51.07 O
HETATM 6714 O HOH B 403 -28.875 -32.956 -0.473 1.00 34.68 O
HETATM 6715 O HOH B 404 -46.526 -45.586 6.922 1.00 41.29 O
HETATM 6716 O HOH B 405 -53.243 -29.330 -6.429 1.00 37.43 O
HETATM 6717 O HOH B 406 -52.221 -34.138 14.882 1.00 35.21 O
HETATM 6718 O HOH B 407 -50.237 -32.367 24.615 1.00 21.62 O
HETATM 6719 O HOH B 408 -18.417 -49.655 -0.073 1.00 38.37 O
CONECT 650 6273
CONECT 1681 6353
CONECT 2783 6396
CONECT 3907 6439
CONECT 4474 5045
CONECT 5045 4474
CONECT 5431 6002
CONECT 6002 5431
CONECT 6231 6235 6262 6303
CONECT 6232 6238 6245 6274
CONECT 6233 6248 6252 6275
CONECT 6234 6255 6259 6276
CONECT 6235 6231 6236 6269
CONECT 6236 6235 6237 6240
CONECT 6237 6236 6238 6239
CONECT 6238 6232 6237 6269
CONECT 6239 6237 6277 6278 6279
CONECT 6240 6236 6241 6280 6281
CONECT 6241 6240 6242 6282 6283
CONECT 6242 6241 6243 6244
CONECT 6243 6242
CONECT 6244 6242
CONECT 6245 6232 6246 6270
CONECT 6246 6245 6247 6249
CONECT 6247 6246 6248 6250
CONECT 6248 6233 6247 6270
CONECT 6249 6246 6284 6285 6286
CONECT 6250 6247 6251 6287
CONECT 6251 6250 6288 6289
CONECT 6252 6233 6253 6271
CONECT 6253 6252 6254 6256
CONECT 6254 6253 6255 6257
CONECT 6255 6234 6254 6271
CONECT 6256 6253 6290 6291 6292
CONECT 6257 6254 6258 6293
CONECT 6258 6257 6294 6295
CONECT 6259 6234 6260 6272
CONECT 6260 6259 6261 6263
CONECT 6261 6260 6262 6264
CONECT 6262 6231 6261 6272
CONECT 6263 6260 6296 6297 6298
CONECT 6264 6261 6265 6299 6300
CONECT 6265 6264 6266 6301 6302
CONECT 6266 6265 6267 6268
CONECT 6267 6266
CONECT 6268 6266
CONECT 6269 6235 6238 6273
CONECT 6270 6245 6248 6273
CONECT 6271 6252 6255 6273
CONECT 6272 6259 6262 6273
CONECT 6273 650 6269 6270 6271
CONECT 6273 6272 6446
CONECT 6274 6232
CONECT 6275 6233
CONECT 6276 6234
CONECT 6277 6239
CONECT 6278 6239
CONECT 6279 6239
CONECT 6280 6240
CONECT 6281 6240
CONECT 6282 6241
CONECT 6283 6241
CONECT 6284 6249
CONECT 6285 6249
CONECT 6286 6249
CONECT 6287 6250
CONECT 6288 6251
CONECT 6289 6251
CONECT 6290 6256
CONECT 6291 6256
CONECT 6292 6256
CONECT 6293 6257
CONECT 6294 6258
CONECT 6295 6258
CONECT 6296 6263
CONECT 6297 6263
CONECT 6298 6263
CONECT 6299 6264
CONECT 6300 6264
CONECT 6301 6265
CONECT 6302 6265
CONECT 6303 6231
CONECT 6304 6305 6306 6307
CONECT 6305 6304
CONECT 6306 6304 6308 6309 6310
CONECT 6307 6304
CONECT 6308 6306
CONECT 6309 6306
CONECT 6310 6306
CONECT 6311 6315 6342
CONECT 6312 6318 6325
CONECT 6313 6328 6332
CONECT 6314 6335 6339
CONECT 6315 6311 6316 6349
CONECT 6316 6315 6317 6320
CONECT 6317 6316 6318 6319
CONECT 6318 6312 6317 6349
CONECT 6319 6317
CONECT 6320 6316 6321
CONECT 6321 6320 6322
CONECT 6322 6321 6323 6324
CONECT 6323 6322
CONECT 6324 6322
CONECT 6325 6312 6326 6350
CONECT 6326 6325 6327 6329
CONECT 6327 6326 6328 6330
CONECT 6328 6313 6327 6350
CONECT 6329 6326
CONECT 6330 6327 6331
CONECT 6331 6330
CONECT 6332 6313 6333 6351
CONECT 6333 6332 6334 6336
CONECT 6334 6333 6335 6337
CONECT 6335 6314 6334 6351
CONECT 6336 6333
CONECT 6337 6334 6338
CONECT 6338 6337
CONECT 6339 6314 6340 6352
CONECT 6340 6339 6341 6343
CONECT 6341 6340 6342 6344
CONECT 6342 6311 6341 6352
CONECT 6343 6340
CONECT 6344 6341 6345
CONECT 6345 6344 6346
CONECT 6346 6345 6347 6348
CONECT 6347 6346
CONECT 6348 6346
CONECT 6349 6315 6318 6353
CONECT 6350 6325 6328 6353
CONECT 6351 6332 6335 6353
CONECT 6352 6339 6342 6353
CONECT 6353 1681 6349 6350 6351
CONECT 6353 6352 6544
CONECT 6354 6358 6385
CONECT 6355 6361 6368
CONECT 6356 6371 6375
CONECT 6357 6378 6382
CONECT 6358 6354 6359 6392
CONECT 6359 6358 6360 6363
CONECT 6360 6359 6361 6362
CONECT 6361 6355 6360 6392
CONECT 6362 6360
CONECT 6363 6359 6364
CONECT 6364 6363 6365
CONECT 6365 6364 6366 6367
CONECT 6366 6365
CONECT 6367 6365
CONECT 6368 6355 6369 6393
CONECT 6369 6368 6370 6372
CONECT 6370 6369 6371 6373
CONECT 6371 6356 6370 6393
CONECT 6372 6369
CONECT 6373 6370 6374
CONECT 6374 6373
CONECT 6375 6356 6376 6394
CONECT 6376 6375 6377 6379
CONECT 6377 6376 6378 6380
CONECT 6378 6357 6377 6394
CONECT 6379 6376
CONECT 6380 6377 6381
CONECT 6381 6380
CONECT 6382 6357 6383 6395
CONECT 6383 6382 6384 6386
CONECT 6384 6383 6385 6387
CONECT 6385 6354 6384 6395
CONECT 6386 6383
CONECT 6387 6384 6388
CONECT 6388 6387 6389
CONECT 6389 6388 6390 6391
CONECT 6390 6389
CONECT 6391 6389
CONECT 6392 6358 6361 6396
CONECT 6393 6368 6371 6396
CONECT 6394 6375 6378 6396
CONECT 6395 6382 6385 6396
CONECT 6396 2783 6392 6393 6394
CONECT 6396 6395 6647
CONECT 6397 6401 6428
CONECT 6398 6404 6411
CONECT 6399 6414 6418
CONECT 6400 6421 6425
CONECT 6401 6397 6402 6435
CONECT 6402 6401 6403 6406
CONECT 6403 6402 6404 6405
CONECT 6404 6398 6403 6435
CONECT 6405 6403
CONECT 6406 6402 6407
CONECT 6407 6406 6408
CONECT 6408 6407 6409 6410
CONECT 6409 6408
CONECT 6410 6408
CONECT 6411 6398 6412 6436
CONECT 6412 6411 6413 6415
CONECT 6413 6412 6414 6416
CONECT 6414 6399 6413 6436
CONECT 6415 6412
CONECT 6416 6413 6417
CONECT 6417 6416
CONECT 6418 6399 6419 6437
CONECT 6419 6418 6420 6422
CONECT 6420 6419 6421 6423
CONECT 6421 6400 6420 6437
CONECT 6422 6419
CONECT 6423 6420 6424
CONECT 6424 6423
CONECT 6425 6400 6426 6438
CONECT 6426 6425 6427 6429
CONECT 6427 6426 6428 6430
CONECT 6428 6397 6427 6438
CONECT 6429 6426
CONECT 6430 6427 6431
CONECT 6431 6430 6432
CONECT 6432 6431 6433 6434
CONECT 6433 6432
CONECT 6434 6432
CONECT 6435 6401 6404 6439
CONECT 6436 6411 6414 6439
CONECT 6437 6418 6421 6439
CONECT 6438 6425 6428 6439
CONECT 6439 3907 6435 6436 6437
CONECT 6439 6438 6743
CONECT 6446 6273
CONECT 6544 6353
CONECT 6647 6396
CONECT 6743 6439
MASTER 403 0 5 48 28 0 0 6 6839 6 225 68
END