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HEADER VIRAL PROTEIN 15-JUL-08 3DTJ
TITLE HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (E187A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 CAPSID PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 278-363;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11698;
SOURCE 5 STRAIN: NL4-3;
SOURCE 6 GENE: GAG;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS-RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS HIV, CAPSID, MUTANT, INHIBITOR, ASSEMBLY, POLYPROTEIN, COMPLEX(VIRAL
KEYWDS 2 PROTEIN-PEPTIDE), MAINLY ALPHA, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.IGONET,M.C.VANEY,F.A.REY
REVDAT 7 25-OCT-17 3DTJ 1 REMARK
REVDAT 6 12-FEB-14 3DTJ 1 REMARK
REVDAT 5 24-FEB-09 3DTJ 1 VERSN
REVDAT 4 25-NOV-08 3DTJ 1 JRNL
REVDAT 3 16-SEP-08 3DTJ 1 REMARK
REVDAT 2 09-SEP-08 3DTJ 1 JRNL
REVDAT 1 02-SEP-08 3DTJ 0
JRNL AUTH V.BARTONOVA,S.IGONET,J.STICHT,B.GLASS,A.HABERMANN,M.C.VANEY,
JRNL AUTH 2 P.SEHR,J.LEWIS,F.A.REY,H.G.KRAUSSLICH
JRNL TITL RESIDUES IN THE HIV-1 CAPSID ASSEMBLY INHIBITOR BINDING SITE
JRNL TITL 2 ARE ESSENTIAL FOR MAINTAINING THE ASSEMBLY-COMPETENT
JRNL TITL 3 QUATERNARY STRUCTURE OF THE CAPSID PROTEIN.
JRNL REF J.BIOL.CHEM. V. 283 32024 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18772135
JRNL DOI 10.1074/JBC.M804230200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.TERNOIS,J.STICHT,S.DUQUERROY,H.-G.KRAUSSLICH,F.A.REY
REMARK 1 TITL THE HIV-1 CAPSID PROTEIN C-TERMINAL DOMAIN IN COMPLEX WITH A
REMARK 1 TITL 2 VIRUS ASSEMBLY INHIBITOR
REMARK 1 REF NAT.STRUCT.MOL.BIOL. V. 12 678 2005
REMARK 1 REFN ISSN 1545-9993
REMARK 1 PMID 16041386
REMARK 1 DOI 10.1038/NSMB967
REMARK 2
REMARK 2 RESOLUTION. 4.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NO REFINEMENT
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NO REFINEMENT WAS UNDERTAKEN BECAUSE OF
REMARK 3 THE LOW RESOLUTION DATA. ONLY MOLECULAR REPLACEMENT WITH THE 3D
REMARK 3 MODEL 3DS5 (HIV-1 C-TERMINAL DOMAIN CAPSID MUTANT (N183A)) GAVE
REMARK 3 A SOLUTION WITH THE SAME PACKING OF THE MOLECULES.
REMARK 4
REMARK 4 3DTJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.044
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 2160
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 62.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3DS5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4,000, 100 MM AMMONIUM ACETATE
REMARK 280 PH 5.0 AND 10 MM MGCL2., EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SER A 146
REMARK 465 PRO A 147
REMARK 465 THR A 148
REMARK 465 GLY A 222
REMARK 465 GLY A 223
REMARK 465 PRO A 224
REMARK 465 GLY A 225
REMARK 465 HIS A 226
REMARK 465 LYS A 227
REMARK 465 ALA A 228
REMARK 465 ARG A 229
REMARK 465 VAL A 230
REMARK 465 LEU A 231
REMARK 465 SER B 146
REMARK 465 PRO B 147
REMARK 465 THR B 148
REMARK 465 GLY B 222
REMARK 465 GLY B 223
REMARK 465 PRO B 224
REMARK 465 GLY B 225
REMARK 465 HIS B 226
REMARK 465 LYS B 227
REMARK 465 ALA B 228
REMARK 465 ARG B 229
REMARK 465 VAL B 230
REMARK 465 LEU B 231
REMARK 465 SER C 146
REMARK 465 PRO C 147
REMARK 465 THR C 148
REMARK 465 GLY C 222
REMARK 465 GLY C 223
REMARK 465 PRO C 224
REMARK 465 GLY C 225
REMARK 465 HIS C 226
REMARK 465 LYS C 227
REMARK 465 ALA C 228
REMARK 465 ARG C 229
REMARK 465 VAL C 230
REMARK 465 LEU C 231
REMARK 465 SER D 146
REMARK 465 PRO D 147
REMARK 465 THR D 148
REMARK 465 GLY D 222
REMARK 465 GLY D 223
REMARK 465 PRO D 224
REMARK 465 GLY D 225
REMARK 465 HIS D 226
REMARK 465 LYS D 227
REMARK 465 ALA D 228
REMARK 465 ARG D 229
REMARK 465 VAL D 230
REMARK 465 LEU D 231
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 THR A 188 -80.29 -113.39
REMARK 500 THR B 188 -81.15 -115.55
REMARK 500 THR C 188 -82.51 -116.05
REMARK 500 THR D 188 -80.29 -117.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DS4 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (L211S) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DS2 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (Y169A)
REMARK 900 RELATED ID: 3DS3 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (Y169A) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DS1 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (E187A) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DS5 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (N183A)
REMARK 900 RELATED ID: 3DS0 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (N183A) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DPH RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (L211S)
DBREF 3DTJ A 146 231 UNP Q72497 Q72497_9HIV1 278 363
DBREF 3DTJ B 146 231 UNP Q72497 Q72497_9HIV1 278 363
DBREF 3DTJ C 146 231 UNP Q72497 Q72497_9HIV1 278 363
DBREF 3DTJ D 146 231 UNP Q72497 Q72497_9HIV1 278 363
SEQADV 3DTJ ALA A 187 UNP Q72497 GLU 319 ENGINEERED
SEQADV 3DTJ ALA B 187 UNP Q72497 GLU 319 ENGINEERED
SEQADV 3DTJ ALA C 187 UNP Q72497 GLU 319 ENGINEERED
SEQADV 3DTJ ALA D 187 UNP Q72497 GLU 319 ENGINEERED
SEQRES 1 A 86 SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY PRO LYS
SEQRES 2 A 86 GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR LYS THR
SEQRES 3 A 86 LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS ASN TRP
SEQRES 4 A 86 MET THR ALA THR LEU LEU VAL GLN ASN ALA ASN PRO ASP
SEQRES 5 A 86 CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY ALA THR
SEQRES 6 A 86 LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL GLY GLY
SEQRES 7 A 86 PRO GLY HIS LYS ALA ARG VAL LEU
SEQRES 1 B 86 SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY PRO LYS
SEQRES 2 B 86 GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR LYS THR
SEQRES 3 B 86 LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS ASN TRP
SEQRES 4 B 86 MET THR ALA THR LEU LEU VAL GLN ASN ALA ASN PRO ASP
SEQRES 5 B 86 CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY ALA THR
SEQRES 6 B 86 LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL GLY GLY
SEQRES 7 B 86 PRO GLY HIS LYS ALA ARG VAL LEU
SEQRES 1 C 86 SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY PRO LYS
SEQRES 2 C 86 GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR LYS THR
SEQRES 3 C 86 LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS ASN TRP
SEQRES 4 C 86 MET THR ALA THR LEU LEU VAL GLN ASN ALA ASN PRO ASP
SEQRES 5 C 86 CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY ALA THR
SEQRES 6 C 86 LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL GLY GLY
SEQRES 7 C 86 PRO GLY HIS LYS ALA ARG VAL LEU
SEQRES 1 D 86 SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY PRO LYS
SEQRES 2 D 86 GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR LYS THR
SEQRES 3 D 86 LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS ASN TRP
SEQRES 4 D 86 MET THR ALA THR LEU LEU VAL GLN ASN ALA ASN PRO ASP
SEQRES 5 D 86 CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY ALA THR
SEQRES 6 D 86 LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL GLY GLY
SEQRES 7 D 86 PRO GLY HIS LYS ALA ARG VAL LEU
HELIX 1 1 SER A 149 ILE A 153 5 5
HELIX 2 2 PRO A 160 GLU A 175 1 16
HELIX 3 3 SER A 178 THR A 188 1 11
HELIX 4 4 THR A 188 ASN A 193 1 6
HELIX 5 5 ASN A 195 GLY A 206 1 12
HELIX 6 6 THR A 210 GLN A 219 1 10
HELIX 7 7 SER B 149 ILE B 153 5 5
HELIX 8 8 PRO B 160 GLU B 175 1 16
HELIX 9 9 SER B 178 THR B 188 1 11
HELIX 10 10 THR B 188 ASN B 193 1 6
HELIX 11 11 ASN B 195 GLY B 206 1 12
HELIX 12 12 THR B 210 GLN B 219 1 10
HELIX 13 13 SER C 149 ILE C 153 5 5
HELIX 14 14 PRO C 160 GLU C 175 1 16
HELIX 15 15 SER C 178 THR C 188 1 11
HELIX 16 16 THR C 188 ASN C 193 1 6
HELIX 17 17 ASN C 195 GLY C 206 1 12
HELIX 18 18 THR C 210 GLN C 219 1 10
HELIX 19 19 SER D 149 ILE D 153 5 5
HELIX 20 20 PRO D 160 GLU D 175 1 16
HELIX 21 21 SER D 178 THR D 188 1 11
HELIX 22 22 THR D 188 ASN D 193 1 6
HELIX 23 23 ASN D 195 GLY D 206 1 12
HELIX 24 24 THR D 210 CYS D 218 1 9
CRYST1 51.603 51.675 51.797 109.94 108.48 110.02 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019379 0.007061 0.011626 0.00000
SCALE2 0.000000 0.020596 0.012034 0.00000
SCALE3 0.000000 0.000000 0.023576 0.00000
ATOM 1 N SER A 149 7.341 -1.725 -8.821 1.00 69.43 N
ATOM 2 CA SER A 149 6.944 -1.112 -7.568 1.00 69.07 C
ATOM 3 C SER A 149 5.921 -1.944 -6.841 1.00 68.63 C
ATOM 4 O SER A 149 5.805 -1.862 -5.638 1.00 68.79 O
ATOM 5 CB SER A 149 6.395 0.279 -7.788 1.00 68.94 C
ATOM 6 OG SER A 149 6.100 0.879 -6.547 1.00 69.34 O
ATOM 7 N ILE A 150 5.183 -2.749 -7.582 1.00 67.94 N
ATOM 8 CA ILE A 150 4.286 -3.696 -6.972 1.00 67.34 C
ATOM 9 C ILE A 150 5.122 -4.872 -6.572 1.00 67.07 C
ATOM 10 O ILE A 150 4.677 -5.750 -5.888 1.00 66.76 O
ATOM 11 CB ILE A 150 3.232 -4.156 -7.935 1.00 67.21 C
ATOM 12 CG1 ILE A 150 2.282 -5.114 -7.243 1.00 65.49 C
ATOM 13 CG2 ILE A 150 3.872 -4.836 -9.073 1.00 68.32 C
ATOM 14 CD1 ILE A 150 1.056 -4.484 -6.787 1.00 61.86 C
ATOM 15 N LEU A 151 6.355 -4.860 -7.025 1.00 67.10 N
ATOM 16 CA LEU A 151 7.335 -5.846 -6.666 1.00 66.77 C
ATOM 17 C LEU A 151 7.692 -5.666 -5.232 1.00 66.97 C
ATOM 18 O LEU A 151 8.246 -6.546 -4.614 1.00 67.34 O
ATOM 19 CB LEU A 151 8.582 -5.606 -7.479 1.00 66.49 C
ATOM 20 CG LEU A 151 9.334 -6.814 -7.971 1.00 66.13 C
ATOM 21 CD1 LEU A 151 8.373 -7.785 -8.490 1.00 62.28 C
ATOM 22 CD2 LEU A 151 10.260 -6.404 -9.033 1.00 64.42 C
ATOM 23 N ASP A 152 7.396 -4.499 -4.705 1.00 67.44 N
ATOM 24 CA ASP A 152 7.828 -4.154 -3.375 1.00 67.82 C
ATOM 25 C ASP A 152 6.681 -4.250 -2.401 1.00 67.21 C
ATOM 26 O ASP A 152 6.827 -3.937 -1.244 1.00 67.30 O
ATOM 27 CB ASP A 152 8.464 -2.755 -3.346 1.00 68.70 C
ATOM 28 CG ASP A 152 9.838 -2.702 -4.015 1.00 69.84 C
ATOM 29 OD1 ASP A 152 10.613 -3.658 -3.903 1.00 71.28 O
ATOM 30 OD2 ASP A 152 10.149 -1.693 -4.654 1.00 72.15 O
ATOM 31 N ILE A 153 5.529 -4.689 -2.874 1.00 66.76 N
ATOM 32 CA ILE A 153 4.416 -5.054 -1.975 1.00 65.79 C
ATOM 33 C ILE A 153 4.531 -6.537 -1.684 1.00 65.88 C
ATOM 34 O ILE A 153 4.154 -7.390 -2.510 1.00 65.82 O
ATOM 35 CB ILE A 153 3.021 -4.743 -2.529 1.00 65.61 C
ATOM 36 CG1 ILE A 153 2.903 -3.260 -2.918 1.00 66.71 C
ATOM 37 CG2 ILE A 153 1.942 -5.159 -1.528 1.00 64.67 C
ATOM 38 CD1 ILE A 153 3.281 -2.252 -1.813 1.00 66.65 C
ATOM 39 N ARG A 154 5.119 -6.829 -0.521 1.00 65.42 N
ATOM 40 CA ARG A 154 5.243 -8.180 -0.034 1.00 64.86 C
ATOM 41 C ARG A 154 4.403 -8.207 1.210 1.00 64.32 C
ATOM 42 O ARG A 154 4.190 -7.165 1.830 1.00 64.72 O
ATOM 43 CB ARG A 154 6.702 -8.519 0.248 1.00 65.22 C
ATOM 44 CG ARG A 154 7.608 -8.379 -0.968 1.00 66.02 C
ATOM 45 CD ARG A 154 8.823 -9.275 -0.871 1.00 69.52 C
ATOM 46 NE ARG A 154 8.447 -10.681 -0.714 1.00 71.61 N
ATOM 47 CZ ARG A 154 8.210 -11.524 -1.721 1.00 72.89 C
ATOM 48 NH1 ARG A 154 8.315 -11.110 -2.982 1.00 73.27 N
ATOM 49 NH2 ARG A 154 7.862 -12.786 -1.467 1.00 70.97 N
ATOM 50 N GLN A 155 3.864 -9.376 1.534 1.00 63.91 N
ATOM 51 CA GLN A 155 2.983 -9.550 2.698 1.00 62.86 C
ATOM 52 C GLN A 155 3.794 -9.742 3.984 1.00 63.74 C
ATOM 53 O GLN A 155 4.710 -10.563 4.018 1.00 63.09 O
ATOM 54 CB GLN A 155 2.089 -10.769 2.494 1.00 62.06 C
ATOM 55 CG GLN A 155 1.009 -10.930 3.540 1.00 58.92 C
ATOM 56 CD GLN A 155 0.336 -12.282 3.465 1.00 56.13 C
ATOM 57 OE1 GLN A 155 0.693 -13.119 2.630 1.00 53.31 O
ATOM 58 NE2 GLN A 155 -0.646 -12.505 4.336 1.00 50.61 N
ATOM 59 N GLY A 156 3.417 -9.020 5.034 1.00 64.98 N
ATOM 60 CA GLY A 156 4.063 -9.141 6.327 1.00 66.51 C
ATOM 61 C GLY A 156 3.883 -10.521 6.928 1.00 67.59 C
ATOM 62 O GLY A 156 2.875 -11.180 6.700 1.00 67.67 O
ATOM 63 N PRO A 157 4.867 -10.954 7.704 1.00 68.68 N
ATOM 64 CA PRO A 157 4.862 -12.294 8.299 1.00 69.24 C
ATOM 65 C PRO A 157 3.602 -12.618 9.090 1.00 69.33 C
ATOM 66 O PRO A 157 3.233 -13.785 9.171 1.00 69.38 O
ATOM 67 CB PRO A 157 6.073 -12.264 9.237 1.00 68.87 C
ATOM 68 CG PRO A 157 6.913 -11.140 8.753 1.00 68.81 C
ATOM 69 CD PRO A 157 5.953 -10.124 8.244 1.00 68.97 C
ATOM 70 N LYS A 158 2.957 -11.611 9.667 1.00 70.16 N
ATOM 71 CA LYS A 158 1.759 -11.844 10.464 1.00 71.00 C
ATOM 72 C LYS A 158 0.570 -11.032 9.972 1.00 70.68 C
ATOM 73 O LYS A 158 -0.518 -11.104 10.534 1.00 71.28 O
ATOM 74 CB LYS A 158 2.030 -11.537 11.939 1.00 71.68 C
ATOM 75 CG LYS A 158 2.322 -12.768 12.786 1.00 74.05 C
ATOM 76 CD LYS A 158 1.106 -13.190 13.597 1.00 76.88 C
ATOM 77 CE LYS A 158 1.490 -13.561 15.021 1.00 79.49 C
ATOM 78 NZ LYS A 158 1.659 -15.029 15.194 1.00 79.73 N
ATOM 79 N GLU A 159 0.786 -10.259 8.916 1.00 69.58 N
ATOM 80 CA GLU A 159 -0.270 -9.447 8.332 1.00 68.29 C
ATOM 81 C GLU A 159 -1.339 -10.347 7.725 1.00 67.70 C
ATOM 82 O GLU A 159 -1.022 -11.291 7.011 1.00 67.38 O
ATOM 83 CB GLU A 159 0.323 -8.534 7.256 1.00 68.46 C
ATOM 84 CG GLU A 159 -0.696 -7.799 6.407 1.00 66.71 C
ATOM 85 CD GLU A 159 -0.050 -7.005 5.291 1.00 67.08 C
ATOM 86 OE1 GLU A 159 0.950 -7.484 4.724 1.00 68.70 O
ATOM 87 OE2 GLU A 159 -0.537 -5.903 4.981 1.00 64.06 O
ATOM 88 N PRO A 160 -2.606 -10.065 8.008 1.00 67.12 N
ATOM 89 CA PRO A 160 -3.672 -10.863 7.428 1.00 66.39 C
ATOM 90 C PRO A 160 -3.681 -10.719 5.903 1.00 65.51 C
ATOM 91 O PRO A 160 -3.637 -9.590 5.371 1.00 64.87 O
ATOM 92 CB PRO A 160 -4.944 -10.271 8.066 1.00 66.71 C
ATOM 93 CG PRO A 160 -4.458 -9.560 9.320 1.00 66.96 C
ATOM 94 CD PRO A 160 -3.131 -9.003 8.894 1.00 67.37 C
ATOM 95 N PHE A 161 -3.706 -11.861 5.214 1.00 63.83 N
ATOM 96 CA PHE A 161 -3.848 -11.888 3.763 1.00 62.49 C
ATOM 97 C PHE A 161 -4.735 -10.779 3.213 1.00 62.97 C
ATOM 98 O PHE A 161 -4.409 -10.160 2.203 1.00 63.72 O
ATOM 99 CB PHE A 161 -4.380 -13.236 3.294 1.00 60.72 C
ATOM 100 CG PHE A 161 -4.361 -13.399 1.801 1.00 58.39 C
ATOM 101 CD1 PHE A 161 -3.145 -13.467 1.107 1.00 54.74 C
ATOM 102 CD2 PHE A 161 -5.552 -13.474 1.084 1.00 53.26 C
ATOM 103 CE1 PHE A 161 -3.128 -13.634 -0.271 1.00 54.21 C
ATOM 104 CE2 PHE A 161 -5.537 -13.639 -0.265 1.00 52.67 C
ATOM 105 CZ PHE A 161 -4.322 -13.713 -0.961 1.00 53.35 C
ATOM 106 N ARG A 162 -5.847 -10.516 3.884 1.00 63.63 N
ATOM 107 CA ARG A 162 -6.804 -9.523 3.418 1.00 64.52 C
ATOM 108 C ARG A 162 -6.269 -8.099 3.390 1.00 64.49 C
ATOM 109 O ARG A 162 -6.679 -7.306 2.546 1.00 65.37 O
ATOM 110 CB ARG A 162 -8.062 -9.566 4.262 1.00 65.20 C
ATOM 111 CG ARG A 162 -9.170 -8.773 3.644 1.00 66.54 C
ATOM 112 CD ARG A 162 -10.440 -8.875 4.428 1.00 68.20 C
ATOM 113 NE ARG A 162 -10.251 -8.408 5.778 1.00 69.57 N
ATOM 114 CZ ARG A 162 -10.555 -9.120 6.852 1.00 73.05 C
ATOM 115 NH1 ARG A 162 -11.107 -10.331 6.726 1.00 72.59 N
ATOM 116 NH2 ARG A 162 -10.324 -8.601 8.052 1.00 74.18 N
ATOM 117 N ASP A 163 -5.379 -7.771 4.328 1.00 64.08 N
ATOM 118 CA ASP A 163 -4.752 -6.462 4.388 1.00 62.75 C
ATOM 119 C ASP A 163 -3.659 -6.346 3.359 1.00 61.78 C
ATOM 120 O ASP A 163 -3.417 -5.266 2.828 1.00 62.50 O
ATOM 121 CB ASP A 163 -4.161 -6.243 5.772 1.00 63.65 C
ATOM 122 CG ASP A 163 -5.212 -6.017 6.815 1.00 63.73 C
ATOM 123 OD1 ASP A 163 -6.262 -5.422 6.490 1.00 66.00 O
ATOM 124 OD2 ASP A 163 -4.974 -6.419 7.964 1.00 65.53 O
ATOM 125 N TYR A 164 -2.969 -7.456 3.111 1.00 60.56 N
ATOM 126 CA TYR A 164 -2.003 -7.548 2.014 1.00 59.30 C
ATOM 127 C TYR A 164 -2.674 -7.336 0.627 1.00 60.06 C
ATOM 128 O TYR A 164 -2.060 -6.754 -0.281 1.00 60.36 O
ATOM 129 CB TYR A 164 -1.291 -8.884 2.086 1.00 57.65 C
ATOM 130 CG TYR A 164 -0.584 -9.311 0.822 1.00 55.29 C
ATOM 131 CD1 TYR A 164 0.495 -8.588 0.320 1.00 53.21 C
ATOM 132 CD2 TYR A 164 -0.990 -10.453 0.140 1.00 53.81 C
ATOM 133 CE1 TYR A 164 1.142 -8.977 -0.840 1.00 52.81 C
ATOM 134 CE2 TYR A 164 -0.369 -10.850 -1.021 1.00 52.55 C
ATOM 135 CZ TYR A 164 0.691 -10.112 -1.507 1.00 54.38 C
ATOM 136 OH TYR A 164 1.313 -10.519 -2.648 1.00 55.40 O
ATOM 137 N VAL A 165 -3.921 -7.814 0.493 1.00 59.87 N
ATOM 138 CA VAL A 165 -4.709 -7.723 -0.742 1.00 59.73 C
ATOM 139 C VAL A 165 -5.097 -6.247 -1.002 1.00 60.39 C
ATOM 140 O VAL A 165 -4.927 -5.765 -2.129 1.00 59.98 O
ATOM 141 CB VAL A 165 -5.980 -8.689 -0.700 1.00 59.87 C
ATOM 142 CG1 VAL A 165 -7.006 -8.382 -1.813 1.00 59.32 C
ATOM 143 CG2 VAL A 165 -5.574 -10.190 -0.720 1.00 57.85 C
ATOM 144 N ASP A 166 -5.583 -5.527 0.026 1.00 60.42 N
ATOM 145 CA ASP A 166 -5.827 -4.074 -0.129 1.00 60.79 C
ATOM 146 C ASP A 166 -4.596 -3.281 -0.581 1.00 59.98 C
ATOM 147 O ASP A 166 -4.735 -2.398 -1.412 1.00 60.10 O
ATOM 148 CB ASP A 166 -6.427 -3.399 1.110 1.00 61.08 C
ATOM 149 CG ASP A 166 -7.588 -4.169 1.717 1.00 63.87 C
ATOM 150 OD1 ASP A 166 -8.323 -4.879 0.996 1.00 64.79 O
ATOM 151 OD2 ASP A 166 -7.778 -4.047 2.951 1.00 67.65 O
ATOM 152 N ARG A 167 -3.406 -3.585 -0.048 1.00 59.49 N
ATOM 153 CA ARG A 167 -2.188 -2.842 -0.424 1.00 58.78 C
ATOM 154 C ARG A 167 -1.808 -3.170 -1.855 1.00 58.71 C
ATOM 155 O ARG A 167 -1.500 -2.273 -2.660 1.00 59.24 O
ATOM 156 CB ARG A 167 -0.997 -3.125 0.524 1.00 59.27 C
ATOM 157 CG ARG A 167 -1.229 -2.774 2.015 1.00 59.43 C
ATOM 158 CD ARG A 167 0.070 -2.782 2.854 1.00 57.46 C
ATOM 159 NE ARG A 167 0.510 -4.142 3.125 1.00 53.69 N
ATOM 160 CZ ARG A 167 1.686 -4.651 2.761 1.00 54.72 C
ATOM 161 NH1 ARG A 167 2.616 -3.903 2.152 1.00 51.97 N
ATOM 162 NH2 ARG A 167 1.956 -5.923 3.047 1.00 54.67 N
ATOM 163 N PHE A 168 -1.856 -4.462 -2.175 1.00 58.21 N
ATOM 164 CA PHE A 168 -1.513 -4.946 -3.523 1.00 57.18 C
ATOM 165 C PHE A 168 -2.336 -4.224 -4.595 1.00 57.76 C
ATOM 166 O PHE A 168 -1.766 -3.640 -5.511 1.00 58.01 O
ATOM 167 CB PHE A 168 -1.728 -6.467 -3.602 1.00 56.04 C
ATOM 168 CG PHE A 168 -1.096 -7.113 -4.800 1.00 53.19 C
ATOM 169 CD1 PHE A 168 -1.834 -7.334 -5.954 1.00 51.69 C
ATOM 170 CD2 PHE A 168 0.234 -7.513 -4.769 1.00 50.14 C
ATOM 171 CE1 PHE A 168 -1.256 -7.942 -7.068 1.00 51.57 C
ATOM 172 CE2 PHE A 168 0.829 -8.113 -5.866 1.00 50.58 C
ATOM 173 CZ PHE A 168 0.083 -8.338 -7.022 1.00 52.67 C
ATOM 174 N TYR A 169 -3.669 -4.272 -4.463 1.00 58.17 N
ATOM 175 CA TYR A 169 -4.601 -3.658 -5.424 1.00 59.13 C
ATOM 176 C TYR A 169 -4.599 -2.136 -5.393 1.00 60.10 C
ATOM 177 O TYR A 169 -4.697 -1.506 -6.439 1.00 60.72 O
ATOM 178 CB TYR A 169 -6.030 -4.240 -5.288 1.00 58.31 C
ATOM 179 CG TYR A 169 -6.081 -5.664 -5.750 1.00 57.05 C
ATOM 180 CD1 TYR A 169 -6.119 -6.710 -4.832 1.00 56.29 C
ATOM 181 CD2 TYR A 169 -6.022 -5.981 -7.115 1.00 55.40 C
ATOM 182 CE1 TYR A 169 -6.113 -8.027 -5.249 1.00 56.00 C
ATOM 183 CE2 TYR A 169 -6.019 -7.288 -7.538 1.00 54.55 C
ATOM 184 CZ TYR A 169 -6.061 -8.314 -6.601 1.00 56.95 C
ATOM 185 OH TYR A 169 -6.077 -9.636 -7.005 1.00 57.08 O
ATOM 186 N LYS A 170 -4.459 -1.572 -4.193 1.00 61.72 N
ATOM 187 CA LYS A 170 -4.241 -0.139 -3.968 1.00 63.38 C
ATOM 188 C LYS A 170 -3.067 0.366 -4.792 1.00 64.08 C
ATOM 189 O LYS A 170 -3.188 1.373 -5.475 1.00 64.45 O
ATOM 190 CB LYS A 170 -3.952 0.093 -2.492 1.00 64.03 C
ATOM 191 CG LYS A 170 -4.141 1.521 -2.000 1.00 66.61 C
ATOM 192 CD LYS A 170 -4.279 1.550 -0.463 1.00 68.40 C
ATOM 193 CE LYS A 170 -4.822 2.897 0.030 1.00 70.58 C
ATOM 194 NZ LYS A 170 -4.094 4.017 -0.624 1.00 70.38 N
ATOM 195 N THR A 171 -1.946 -0.361 -4.727 1.00 64.66 N
ATOM 196 CA THR A 171 -0.736 -0.058 -5.492 1.00 64.92 C
ATOM 197 C THR A 171 -0.976 -0.222 -6.983 1.00 65.41 C
ATOM 198 O THR A 171 -0.521 0.589 -7.797 1.00 66.44 O
ATOM 199 CB THR A 171 0.441 -0.966 -5.058 1.00 64.82 C
ATOM 200 OG1 THR A 171 0.555 -0.961 -3.625 1.00 66.65 O
ATOM 201 CG2 THR A 171 1.757 -0.501 -5.650 1.00 64.07 C
ATOM 202 N LEU A 172 -1.692 -1.275 -7.351 1.00 65.52 N
ATOM 203 CA LEU A 172 -2.053 -1.491 -8.746 1.00 65.25 C
ATOM 204 C LEU A 172 -2.936 -0.363 -9.323 1.00 65.93 C
ATOM 205 O LEU A 172 -2.728 0.056 -10.469 1.00 65.85 O
ATOM 206 CB LEU A 172 -2.712 -2.863 -8.912 1.00 64.90 C
ATOM 207 CG LEU A 172 -2.035 -4.054 -9.614 1.00 64.40 C
ATOM 208 CD1 LEU A 172 -0.502 -4.004 -9.705 1.00 62.55 C
ATOM 209 CD2 LEU A 172 -2.523 -5.366 -8.995 1.00 64.15 C
ATOM 210 N ARG A 173 -3.912 0.114 -8.537 1.00 66.39 N
ATOM 211 CA ARG A 173 -4.748 1.263 -8.938 1.00 66.90 C
ATOM 212 C ARG A 173 -3.911 2.515 -9.204 1.00 67.48 C
ATOM 213 O ARG A 173 -4.046 3.139 -10.262 1.00 67.71 O
ATOM 214 CB ARG A 173 -5.872 1.566 -7.928 1.00 66.66 C
ATOM 215 CG ARG A 173 -7.095 0.666 -8.084 1.00 66.53 C
ATOM 216 CD ARG A 173 -8.396 1.210 -7.443 1.00 66.60 C
ATOM 217 NE ARG A 173 -8.283 1.476 -5.996 1.00 67.19 N
ATOM 218 CZ ARG A 173 -8.272 0.550 -5.023 1.00 64.78 C
ATOM 219 NH1 ARG A 173 -8.358 -0.755 -5.312 1.00 62.30 N
ATOM 220 NH2 ARG A 173 -8.155 0.941 -3.749 1.00 60.69 N
ATOM 221 N ALA A 174 -3.035 2.868 -8.264 1.00 67.96 N
ATOM 222 CA ALA A 174 -2.174 4.047 -8.417 1.00 68.40 C
ATOM 223 C ALA A 174 -1.420 4.035 -9.744 1.00 68.80 C
ATOM 224 O ALA A 174 -1.196 5.087 -10.350 1.00 69.79 O
ATOM 225 CB ALA A 174 -1.196 4.166 -7.241 1.00 68.16 C
ATOM 226 N GLU A 175 -1.045 2.847 -10.208 1.00 68.89 N
ATOM 227 CA GLU A 175 -0.274 2.700 -11.444 1.00 68.67 C
ATOM 228 C GLU A 175 -1.182 2.450 -12.634 1.00 68.75 C
ATOM 229 O GLU A 175 -0.713 2.053 -13.714 1.00 68.44 O
ATOM 230 CB GLU A 175 0.712 1.547 -11.297 1.00 68.98 C
ATOM 231 CG GLU A 175 1.658 1.673 -10.113 1.00 68.61 C
ATOM 232 CD GLU A 175 2.643 0.516 -10.041 1.00 70.18 C
ATOM 233 OE1 GLU A 175 3.867 0.774 -9.950 1.00 73.30 O
ATOM 234 OE2 GLU A 175 2.205 -0.652 -10.079 1.00 70.90 O
ATOM 235 N GLN A 176 -2.483 2.665 -12.415 1.00 68.86 N
ATOM 236 CA GLN A 176 -3.533 2.505 -13.431 1.00 69.53 C
ATOM 237 C GLN A 176 -3.498 1.176 -14.167 1.00 69.04 C
ATOM 238 O GLN A 176 -3.686 1.134 -15.390 1.00 69.13 O
ATOM 239 CB GLN A 176 -3.520 3.647 -14.450 1.00 70.09 C
ATOM 240 CG GLN A 176 -4.143 4.925 -13.961 1.00 73.08 C
ATOM 241 CD GLN A 176 -3.104 5.888 -13.494 1.00 76.78 C
ATOM 242 OE1 GLN A 176 -2.038 6.007 -14.116 1.00 79.15 O
ATOM 243 NE2 GLN A 176 -3.388 6.594 -12.392 1.00 76.91 N
ATOM 244 N ALA A 177 -3.253 0.096 -13.431 1.00 68.35 N
ATOM 245 CA ALA A 177 -3.243 -1.229 -14.022 1.00 67.29 C
ATOM 246 C ALA A 177 -4.583 -1.487 -14.706 1.00 66.87 C
ATOM 247 O ALA A 177 -5.645 -1.287 -14.110 1.00 67.10 O
ATOM 248 CB ALA A 177 -2.971 -2.271 -12.965 1.00 67.04 C
ATOM 249 N SER A 178 -4.530 -1.930 -15.957 1.00 66.42 N
ATOM 250 CA SER A 178 -5.737 -2.350 -16.659 1.00 65.60 C
ATOM 251 C SER A 178 -6.374 -3.583 -16.016 1.00 65.77 C
ATOM 252 O SER A 178 -5.800 -4.220 -15.120 1.00 66.07 O
ATOM 253 CB SER A 178 -5.465 -2.587 -18.142 1.00 65.64 C
ATOM 254 OG SER A 178 -4.694 -3.751 -18.362 1.00 63.27 O
ATOM 255 N GLN A 179 -7.573 -3.914 -16.480 1.00 65.14 N
ATOM 256 CA GLN A 179 -8.334 -5.005 -15.929 1.00 64.54 C
ATOM 257 C GLN A 179 -7.658 -6.323 -16.231 1.00 62.92 C
ATOM 258 O GLN A 179 -7.655 -7.235 -15.396 1.00 61.78 O
ATOM 259 CB GLN A 179 -9.758 -5.027 -16.506 1.00 65.25 C
ATOM 260 CG GLN A 179 -10.822 -5.289 -15.418 1.00 68.65 C
ATOM 261 CD GLN A 179 -10.699 -4.276 -14.264 1.00 70.98 C
ATOM 262 OE1 GLN A 179 -10.280 -3.136 -14.479 1.00 71.63 O
ATOM 263 NE2 GLN A 179 -11.031 -4.704 -13.041 1.00 69.93 N
ATOM 264 N GLU A 180 -7.123 -6.412 -17.444 1.00 61.24 N
ATOM 265 CA GLU A 180 -6.448 -7.599 -17.906 1.00 60.81 C
ATOM 266 C GLU A 180 -5.149 -7.795 -17.092 1.00 59.65 C
ATOM 267 O GLU A 180 -4.779 -8.930 -16.760 1.00 59.21 O
ATOM 268 CB GLU A 180 -6.150 -7.497 -19.401 1.00 60.74 C
ATOM 269 CG GLU A 180 -5.756 -8.827 -20.045 1.00 63.76 C
ATOM 270 CD GLU A 180 -4.869 -8.656 -21.305 1.00 68.75 C
ATOM 271 OE1 GLU A 180 -4.604 -7.479 -21.725 1.00 68.80 O
ATOM 272 OE2 GLU A 180 -4.438 -9.718 -21.870 1.00 69.97 O
ATOM 273 N VAL A 181 -4.486 -6.674 -16.779 1.00 57.45 N
ATOM 274 CA VAL A 181 -3.316 -6.669 -15.919 1.00 56.07 C
ATOM 275 C VAL A 181 -3.619 -7.100 -14.455 1.00 54.90 C
ATOM 276 O VAL A 181 -2.846 -7.851 -13.867 1.00 54.07 O
ATOM 277 CB VAL A 181 -2.587 -5.313 -15.977 1.00 55.68 C
ATOM 278 CG1 VAL A 181 -1.696 -5.129 -14.757 1.00 55.41 C
ATOM 279 CG2 VAL A 181 -1.815 -5.180 -17.284 1.00 53.68 C
ATOM 280 N LYS A 182 -4.736 -6.644 -13.895 1.00 54.08 N
ATOM 281 CA LYS A 182 -5.120 -7.032 -12.530 1.00 53.97 C
ATOM 282 C LYS A 182 -5.354 -8.523 -12.389 1.00 53.28 C
ATOM 283 O LYS A 182 -4.953 -9.091 -11.369 1.00 52.80 O
ATOM 284 CB LYS A 182 -6.319 -6.244 -11.989 1.00 53.84 C
ATOM 285 CG LYS A 182 -6.121 -4.747 -12.085 1.00 56.99 C
ATOM 286 CD LYS A 182 -6.817 -3.944 -10.962 1.00 62.22 C
ATOM 287 CE LYS A 182 -8.313 -3.719 -11.190 1.00 62.91 C
ATOM 288 NZ LYS A 182 -9.091 -4.934 -10.804 1.00 64.83 N
ATOM 289 N ASN A 183 -5.971 -9.148 -13.420 1.00 20.00 N
ATOM 290 CA ASN A 183 -6.266 -10.571 -13.533 1.00 20.00 C
ATOM 291 C ASN A 183 -4.999 -11.420 -13.580 1.00 20.00 C
ATOM 292 O ASN A 183 -4.913 -12.469 -12.908 1.00 51.28 O
ATOM 293 CB ASN A 183 -7.128 -10.844 -14.766 1.00 20.00 C
ATOM 294 CG ASN A 183 -8.547 -10.335 -14.610 1.00 20.00 C
ATOM 295 OD1 ASN A 183 -9.038 -10.162 -13.494 1.00 20.00 O
ATOM 296 ND2 ASN A 183 -9.216 -10.092 -15.731 1.00 20.00 N
ATOM 297 N TRP A 184 -4.041 -11.013 -14.405 1.00 51.69 N
ATOM 298 CA TRP A 184 -2.727 -11.660 -14.468 1.00 51.80 C
ATOM 299 C TRP A 184 -1.927 -11.458 -13.150 1.00 52.19 C
ATOM 300 O TRP A 184 -1.219 -12.362 -12.699 1.00 52.28 O
ATOM 301 CB TRP A 184 -1.938 -11.110 -15.654 1.00 51.41 C
ATOM 302 CG TRP A 184 -2.267 -11.773 -16.980 1.00 51.30 C
ATOM 303 CD1 TRP A 184 -3.280 -11.449 -17.828 1.00 50.28 C
ATOM 304 CD2 TRP A 184 -1.540 -12.844 -17.614 1.00 51.56 C
ATOM 305 NE1 TRP A 184 -3.239 -12.255 -18.948 1.00 49.98 N
ATOM 306 CE2 TRP A 184 -2.192 -13.125 -18.835 1.00 50.35 C
ATOM 307 CE3 TRP A 184 -0.423 -13.621 -17.240 1.00 52.00 C
ATOM 308 CZ2 TRP A 184 -1.774 -14.141 -19.692 1.00 51.21 C
ATOM 309 CZ3 TRP A 184 -0.009 -14.633 -18.084 1.00 52.03 C
ATOM 310 CH2 TRP A 184 -0.678 -14.880 -19.308 1.00 51.60 C
ATOM 311 N MET A 185 -2.058 -10.279 -12.544 1.00 51.71 N
ATOM 312 CA MET A 185 -1.345 -9.968 -11.303 1.00 51.96 C
ATOM 313 C MET A 185 -1.851 -10.783 -10.136 1.00 51.94 C
ATOM 314 O MET A 185 -1.045 -11.232 -9.289 1.00 52.51 O
ATOM 315 CB MET A 185 -1.367 -8.461 -10.985 1.00 51.46 C
ATOM 316 CG MET A 185 -0.434 -7.652 -11.885 1.00 51.08 C
ATOM 317 SD MET A 185 1.322 -7.974 -11.569 1.00 56.25 S
ATOM 318 CE MET A 185 1.864 -8.347 -13.196 1.00 49.56 C
ATOM 319 N THR A 186 -3.168 -11.000 -10.132 1.00 51.61 N
ATOM 320 CA THR A 186 -3.892 -11.797 -9.142 1.00 51.45 C
ATOM 321 C THR A 186 -3.347 -13.223 -9.057 1.00 52.31 C
ATOM 322 O THR A 186 -3.260 -13.792 -7.967 1.00 52.96 O
ATOM 323 CB THR A 186 -5.412 -11.799 -9.502 1.00 51.68 C
ATOM 324 OG1 THR A 186 -5.893 -10.445 -9.488 1.00 50.76 O
ATOM 325 CG2 THR A 186 -6.261 -12.665 -8.540 1.00 48.83 C
ATOM 326 N ALA A 187 -2.960 -13.781 -10.201 1.00 20.00 N
ATOM 327 CA ALA A 187 -2.542 -15.176 -10.280 1.00 20.00 C
ATOM 328 C ALA A 187 -1.024 -15.301 -10.198 1.00 20.00 C
ATOM 329 O ALA A 187 -0.543 -16.444 -10.036 1.00 52.58 O
ATOM 330 CB ALA A 187 -3.060 -15.813 -11.560 1.00 20.00 C
ATOM 331 N THR A 188 -0.314 -14.243 -10.348 1.00 51.72 N
ATOM 332 CA THR A 188 1.134 -14.316 -10.369 1.00 51.33 C
ATOM 333 C THR A 188 1.772 -13.631 -9.172 1.00 51.76 C
ATOM 334 O THR A 188 2.158 -14.286 -8.213 1.00 51.47 O
ATOM 335 CB THR A 188 1.691 -13.716 -11.665 1.00 51.46 C
ATOM 336 OG1 THR A 188 1.155 -12.403 -11.849 1.00 50.09 O
ATOM 337 CG2 THR A 188 1.300 -14.576 -12.849 1.00 51.58 C
ATOM 338 N LEU A 189 1.880 -12.313 -9.236 1.00 52.18 N
ATOM 339 CA LEU A 189 2.516 -11.551 -8.168 1.00 52.14 C
ATOM 340 C LEU A 189 1.823 -11.682 -6.813 1.00 51.37 C
ATOM 341 O LEU A 189 2.487 -11.858 -5.799 1.00 51.54 O
ATOM 342 CB LEU A 189 2.665 -10.083 -8.563 1.00 53.06 C
ATOM 343 CG LEU A 189 4.079 -9.534 -8.391 1.00 55.14 C
ATOM 344 CD1 LEU A 189 5.045 -10.254 -9.308 1.00 57.88 C
ATOM 345 CD2 LEU A 189 4.116 -8.041 -8.634 1.00 56.27 C
ATOM 346 N LEU A 190 0.498 -11.598 -6.787 1.00 50.03 N
ATOM 347 CA LEU A 190 -0.222 -11.744 -5.529 1.00 49.07 C
ATOM 348 C LEU A 190 0.227 -13.006 -4.807 1.00 49.56 C
ATOM 349 O LEU A 190 0.458 -12.996 -3.606 1.00 49.43 O
ATOM 350 CB LEU A 190 -1.729 -11.773 -5.760 1.00 48.93 C
ATOM 351 CG LEU A 190 -2.588 -11.797 -4.496 1.00 48.63 C
ATOM 352 CD1 LEU A 190 -2.399 -10.530 -3.690 1.00 46.85 C
ATOM 353 CD2 LEU A 190 -4.046 -11.995 -4.840 1.00 46.65 C
ATOM 354 N VAL A 191 0.351 -14.095 -5.554 1.00 49.71 N
ATOM 355 CA VAL A 191 0.834 -15.357 -5.006 1.00 49.53 C
ATOM 356 C VAL A 191 2.327 -15.262 -4.554 1.00 50.99 C
ATOM 357 O VAL A 191 2.619 -15.526 -3.372 1.00 51.24 O
ATOM 358 CB VAL A 191 0.531 -16.554 -5.959 1.00 49.30 C
ATOM 359 CG1 VAL A 191 1.194 -17.822 -5.479 1.00 46.33 C
ATOM 360 CG2 VAL A 191 -0.992 -16.759 -6.097 1.00 46.04 C
ATOM 361 N GLN A 192 3.245 -14.868 -5.450 1.00 51.20 N
ATOM 362 CA GLN A 192 4.671 -14.877 -5.121 1.00 52.82 C
ATOM 363 C GLN A 192 5.085 -13.902 -4.002 1.00 52.46 C
ATOM 364 O GLN A 192 6.116 -14.127 -3.367 1.00 53.35 O
ATOM 365 CB GLN A 192 5.575 -14.630 -6.339 1.00 52.77 C
ATOM 366 CG GLN A 192 5.373 -15.605 -7.471 1.00 58.29 C
ATOM 367 CD GLN A 192 6.290 -16.825 -7.421 1.00 62.14 C
ATOM 368 OE1 GLN A 192 7.302 -16.881 -8.143 1.00 64.09 O
ATOM 369 NE2 GLN A 192 5.935 -17.814 -6.595 1.00 59.24 N
ATOM 370 N ASN A 193 4.302 -12.852 -3.779 1.00 51.56 N
ATOM 371 CA ASN A 193 4.614 -11.807 -2.806 1.00 51.50 C
ATOM 372 C ASN A 193 3.860 -12.035 -1.491 1.00 51.50 C
ATOM 373 O ASN A 193 3.879 -11.197 -0.603 1.00 50.80 O
ATOM 374 CB ASN A 193 4.257 -10.411 -3.369 1.00 51.31 C
ATOM 375 CG ASN A 193 5.333 -9.833 -4.308 1.00 51.50 C
ATOM 376 OD1 ASN A 193 6.274 -10.514 -4.727 1.00 50.42 O
ATOM 377 ND2 ASN A 193 5.187 -8.563 -4.626 1.00 51.54 N
ATOM 378 N ALA A 194 3.162 -13.157 -1.404 1.00 51.89 N
ATOM 379 CA ALA A 194 2.502 -13.581 -0.166 1.00 52.91 C
ATOM 380 C ALA A 194 3.535 -14.185 0.798 1.00 53.25 C
ATOM 381 O ALA A 194 4.630 -14.581 0.382 1.00 52.49 O
ATOM 382 CB ALA A 194 1.373 -14.593 -0.455 1.00 52.08 C
ATOM 383 N ASN A 195 3.183 -14.238 2.085 1.00 54.31 N
ATOM 384 CA ASN A 195 4.090 -14.731 3.107 1.00 55.50 C
ATOM 385 C ASN A 195 4.196 -16.248 2.979 1.00 57.08 C
ATOM 386 O ASN A 195 3.411 -16.851 2.243 1.00 58.11 O
ATOM 387 CB ASN A 195 3.659 -14.251 4.501 1.00 54.51 C
ATOM 388 CG ASN A 195 2.382 -14.887 4.975 1.00 54.40 C
ATOM 389 OD1 ASN A 195 2.049 -16.006 4.572 1.00 54.25 O
ATOM 390 ND2 ASN A 195 1.650 -14.184 5.855 1.00 51.74 N
ATOM 391 N PRO A 196 5.190 -16.879 3.642 1.00 58.13 N
ATOM 392 CA PRO A 196 5.413 -18.316 3.415 1.00 57.83 C
ATOM 393 C PRO A 196 4.195 -19.211 3.602 1.00 57.62 C
ATOM 394 O PRO A 196 4.065 -20.257 2.942 1.00 58.22 O
ATOM 395 CB PRO A 196 6.487 -18.651 4.453 1.00 57.65 C
ATOM 396 CG PRO A 196 7.278 -17.362 4.579 1.00 57.19 C
ATOM 397 CD PRO A 196 6.204 -16.312 4.568 1.00 58.32 C
ATOM 398 N ASP A 197 3.310 -18.841 4.498 1.00 57.60 N
ATOM 399 CA ASP A 197 2.159 -19.714 4.756 1.00 58.50 C
ATOM 400 C ASP A 197 1.083 -19.559 3.691 1.00 57.62 C
ATOM 401 O ASP A 197 0.561 -20.559 3.183 1.00 56.89 O
ATOM 402 CB ASP A 197 1.563 -19.445 6.143 1.00 59.27 C
ATOM 403 CG ASP A 197 2.434 -19.962 7.255 1.00 60.83 C
ATOM 404 OD1 ASP A 197 2.829 -21.157 7.207 1.00 60.53 O
ATOM 405 OD2 ASP A 197 2.724 -19.152 8.163 1.00 62.75 O
ATOM 406 N CYS A 198 0.778 -18.299 3.363 1.00 57.31 N
ATOM 407 CA CYS A 198 -0.211 -17.976 2.324 1.00 57.00 C
ATOM 408 C CYS A 198 0.285 -18.417 0.963 1.00 57.16 C
ATOM 409 O CYS A 198 -0.423 -19.125 0.217 1.00 57.32 O
ATOM 410 CB CYS A 198 -0.554 -16.508 2.354 1.00 56.77 C
ATOM 411 SG CYS A 198 -1.478 -16.116 3.833 1.00 56.79 S
ATOM 412 N LYS A 199 1.528 -18.070 0.668 1.00 56.77 N
ATOM 413 CA LYS A 199 2.182 -18.560 -0.542 1.00 56.65 C
ATOM 414 C LYS A 199 1.954 -20.054 -0.800 1.00 56.28 C
ATOM 415 O LYS A 199 1.556 -20.444 -1.904 1.00 57.45 O
ATOM 416 CB LYS A 199 3.669 -18.247 -0.494 1.00 56.36 C
ATOM 417 CG LYS A 199 4.345 -18.535 -1.783 1.00 56.44 C
ATOM 418 CD LYS A 199 5.531 -17.642 -1.955 1.00 54.97 C
ATOM 419 CE LYS A 199 6.261 -18.124 -3.158 1.00 55.04 C
ATOM 420 NZ LYS A 199 7.314 -17.157 -3.478 1.00 55.93 N
ATOM 421 N THR A 200 2.193 -20.881 0.214 1.00 54.95 N
ATOM 422 CA THR A 200 2.034 -22.332 0.082 1.00 53.81 C
ATOM 423 C THR A 200 0.578 -22.728 -0.217 1.00 53.15 C
ATOM 424 O THR A 200 0.319 -23.609 -1.032 1.00 52.88 O
ATOM 425 CB THR A 200 2.537 -23.050 1.365 1.00 54.14 C
ATOM 426 OG1 THR A 200 3.965 -22.958 1.442 1.00 53.32 O
ATOM 427 CG2 THR A 200 2.104 -24.518 1.398 1.00 53.39 C
ATOM 428 N ILE A 201 -0.354 -22.074 0.475 1.00 52.61 N
ATOM 429 CA ILE A 201 -1.789 -22.284 0.301 1.00 51.91 C
ATOM 430 C ILE A 201 -2.263 -21.895 -1.119 1.00 51.74 C
ATOM 431 O ILE A 201 -2.871 -22.718 -1.828 1.00 51.70 O
ATOM 432 CB ILE A 201 -2.582 -21.554 1.379 1.00 51.60 C
ATOM 433 CG1 ILE A 201 -2.274 -22.142 2.769 1.00 49.46 C
ATOM 434 CG2 ILE A 201 -4.069 -21.671 1.075 1.00 52.09 C
ATOM 435 CD1 ILE A 201 -2.706 -21.234 3.926 1.00 48.11 C
ATOM 436 N LEU A 202 -1.909 -20.680 -1.544 1.00 51.06 N
ATOM 437 CA LEU A 202 -2.195 -20.192 -2.898 1.00 51.15 C
ATOM 438 C LEU A 202 -1.595 -21.054 -4.001 1.00 51.57 C
ATOM 439 O LEU A 202 -2.277 -21.328 -4.977 1.00 52.08 O
ATOM 440 CB LEU A 202 -1.793 -18.719 -3.059 1.00 50.99 C
ATOM 441 CG LEU A 202 -2.456 -17.834 -1.994 1.00 51.69 C
ATOM 442 CD1 LEU A 202 -1.825 -16.470 -1.919 1.00 50.56 C
ATOM 443 CD2 LEU A 202 -3.986 -17.762 -2.168 1.00 50.44 C
ATOM 444 N LYS A 203 -0.353 -21.516 -3.853 1.00 51.97 N
ATOM 445 CA LYS A 203 0.215 -22.428 -4.832 1.00 53.38 C
ATOM 446 C LYS A 203 -0.542 -23.738 -4.823 1.00 53.24 C
ATOM 447 O LYS A 203 -0.828 -24.307 -5.887 1.00 53.77 O
ATOM 448 CB LYS A 203 1.716 -22.671 -4.614 1.00 53.56 C
ATOM 449 CG LYS A 203 2.565 -21.377 -4.460 1.00 56.12 C
ATOM 450 CD LYS A 203 4.071 -21.640 -4.475 1.00 56.71 C
ATOM 451 CE LYS A 203 4.625 -21.651 -5.918 1.00 62.21 C
ATOM 452 NZ LYS A 203 5.972 -20.960 -6.022 1.00 61.80 N
ATOM 453 N ALA A 204 -0.921 -24.211 -3.637 1.00 53.38 N
ATOM 454 CA ALA A 204 -1.690 -25.454 -3.557 1.00 53.16 C
ATOM 455 C ALA A 204 -3.087 -25.307 -4.231 1.00 53.02 C
ATOM 456 O ALA A 204 -3.516 -26.191 -4.940 1.00 53.08 O
ATOM 457 CB ALA A 204 -1.783 -25.919 -2.141 1.00 52.25 C
ATOM 458 N LEU A 205 -3.780 -24.187 -4.011 1.00 53.32 N
ATOM 459 CA LEU A 205 -5.048 -23.884 -4.707 1.00 53.63 C
ATOM 460 C LEU A 205 -4.860 -23.848 -6.218 1.00 53.98 C
ATOM 461 O LEU A 205 -5.675 -24.394 -6.963 1.00 54.22 O
ATOM 462 CB LEU A 205 -5.563 -22.517 -4.303 1.00 53.85 C
ATOM 463 CG LEU A 205 -6.635 -22.326 -3.273 1.00 54.08 C
ATOM 464 CD1 LEU A 205 -7.135 -20.910 -3.502 1.00 53.50 C
ATOM 465 CD2 LEU A 205 -7.747 -23.352 -3.485 1.00 54.40 C
ATOM 466 N GLY A 206 -3.807 -23.187 -6.673 1.00 53.71 N
ATOM 467 CA GLY A 206 -3.442 -23.291 -8.078 1.00 55.08 C
ATOM 468 C GLY A 206 -3.947 -22.126 -8.912 1.00 56.49 C
ATOM 469 O GLY A 206 -4.784 -21.317 -8.449 1.00 55.97 O
ATOM 470 N PRO A 207 -3.461 -22.041 -10.157 1.00 57.46 N
ATOM 471 CA PRO A 207 -3.868 -21.021 -11.112 1.00 58.14 C
ATOM 472 C PRO A 207 -5.378 -21.003 -11.364 1.00 58.48 C
ATOM 473 O PRO A 207 -6.061 -22.028 -11.297 1.00 58.11 O
ATOM 474 CB PRO A 207 -3.113 -21.414 -12.393 1.00 58.74 C
ATOM 475 CG PRO A 207 -2.777 -22.928 -12.187 1.00 58.99 C
ATOM 476 CD PRO A 207 -2.471 -22.976 -10.733 1.00 58.32 C
ATOM 477 N GLY A 208 -5.894 -19.817 -11.636 1.00 58.29 N
ATOM 478 CA GLY A 208 -7.282 -19.712 -11.975 1.00 58.31 C
ATOM 479 C GLY A 208 -8.187 -19.721 -10.783 1.00 58.02 C
ATOM 480 O GLY A 208 -9.397 -19.799 -10.935 1.00 58.98 O
ATOM 481 N ALA A 209 -7.626 -19.609 -9.586 1.00 57.79 N
ATOM 482 CA ALA A 209 -8.481 -19.390 -8.413 1.00 56.56 C
ATOM 483 C ALA A 209 -8.936 -17.945 -8.462 1.00 56.29 C
ATOM 484 O ALA A 209 -8.208 -17.046 -8.903 1.00 56.69 O
ATOM 485 CB ALA A 209 -7.744 -19.673 -7.124 1.00 55.78 C
ATOM 486 N THR A 210 -10.148 -17.720 -8.020 1.00 56.35 N
ATOM 487 CA THR A 210 -10.612 -16.370 -7.854 1.00 56.83 C
ATOM 488 C THR A 210 -10.073 -15.811 -6.542 1.00 56.92 C
ATOM 489 O THR A 210 -9.651 -16.565 -5.646 1.00 57.43 O
ATOM 490 CB THR A 210 -12.115 -16.321 -7.844 1.00 56.79 C
ATOM 491 OG1 THR A 210 -12.566 -16.969 -6.661 1.00 54.73 O
ATOM 492 CG2 THR A 210 -12.672 -17.037 -9.100 1.00 56.82 C
ATOM 493 N LEU A 211 -10.101 -14.493 -6.440 1.00 56.48 N
ATOM 494 CA LEU A 211 -9.651 -13.797 -5.264 1.00 55.96 C
ATOM 495 C LEU A 211 -10.411 -14.244 -4.025 1.00 56.31 C
ATOM 496 O LEU A 211 -9.812 -14.352 -2.947 1.00 57.01 O
ATOM 497 CB LEU A 211 -9.823 -12.302 -5.468 1.00 55.39 C
ATOM 498 CG LEU A 211 -9.364 -11.355 -4.364 1.00 54.40 C
ATOM 499 CD1 LEU A 211 -7.863 -11.465 -4.124 1.00 50.98 C
ATOM 500 CD2 LEU A 211 -9.765 -9.965 -4.783 1.00 50.96 C
ATOM 501 N GLU A 212 -11.714 -14.486 -4.165 1.00 55.99 N
ATOM 502 CA GLU A 212 -12.534 -14.868 -3.026 1.00 56.55 C
ATOM 503 C GLU A 212 -12.066 -16.224 -2.511 1.00 56.25 C
ATOM 504 O GLU A 212 -12.005 -16.443 -1.299 1.00 56.22 O
ATOM 505 CB GLU A 212 -14.026 -14.911 -3.404 1.00 57.31 C
ATOM 506 CG GLU A 212 -14.960 -15.577 -2.379 1.00 58.89 C
ATOM 507 CD GLU A 212 -15.039 -17.093 -2.567 1.00 65.50 C
ATOM 508 OE1 GLU A 212 -14.788 -17.575 -3.713 1.00 67.86 O
ATOM 509 OE2 GLU A 212 -15.352 -17.808 -1.580 1.00 67.02 O
ATOM 510 N GLU A 213 -11.756 -17.122 -3.442 1.00 55.49 N
ATOM 511 CA GLU A 213 -11.235 -18.424 -3.128 1.00 55.83 C
ATOM 512 C GLU A 213 -9.867 -18.323 -2.447 1.00 56.30 C
ATOM 513 O GLU A 213 -9.642 -18.944 -1.394 1.00 56.44 O
ATOM 514 CB GLU A 213 -11.173 -19.283 -4.379 1.00 55.70 C
ATOM 515 CG GLU A 213 -12.495 -19.887 -4.721 1.00 55.36 C
ATOM 516 CD GLU A 213 -12.485 -20.505 -6.088 1.00 59.36 C
ATOM 517 OE1 GLU A 213 -11.520 -20.256 -6.839 1.00 59.76 O
ATOM 518 OE2 GLU A 213 -13.443 -21.238 -6.423 1.00 61.34 O
ATOM 519 N MET A 214 -8.991 -17.505 -3.022 1.00 55.81 N
ATOM 520 CA MET A 214 -7.717 -17.158 -2.406 1.00 55.68 C
ATOM 521 C MET A 214 -7.842 -16.671 -0.952 1.00 56.91 C
ATOM 522 O MET A 214 -7.042 -17.060 -0.074 1.00 56.05 O
ATOM 523 CB MET A 214 -6.997 -16.119 -3.256 1.00 54.87 C
ATOM 524 CG MET A 214 -6.531 -16.639 -4.590 1.00 52.76 C
ATOM 525 SD MET A 214 -5.607 -15.351 -5.416 1.00 55.34 S
ATOM 526 CE MET A 214 -4.901 -16.258 -6.813 1.00 55.29 C
ATOM 527 N MET A 215 -8.854 -15.837 -0.700 1.00 57.77 N
ATOM 528 CA MET A 215 -9.077 -15.287 0.649 1.00 59.15 C
ATOM 529 C MET A 215 -9.669 -16.290 1.649 1.00 59.32 C
ATOM 530 O MET A 215 -9.254 -16.339 2.792 1.00 60.21 O
ATOM 531 CB MET A 215 -9.929 -14.040 0.584 1.00 58.55 C
ATOM 532 CG MET A 215 -9.196 -12.856 0.014 1.00 60.12 C
ATOM 533 SD MET A 215 -10.305 -11.507 -0.378 1.00 60.82 S
ATOM 534 CE MET A 215 -11.253 -11.391 1.137 1.00 59.35 C
ATOM 535 N THR A 216 -10.643 -17.074 1.214 1.00 59.66 N
ATOM 536 CA THR A 216 -11.208 -18.145 2.023 1.00 59.59 C
ATOM 537 C THR A 216 -10.107 -19.118 2.516 1.00 59.44 C
ATOM 538 O THR A 216 -10.065 -19.460 3.692 1.00 59.94 O
ATOM 539 CB THR A 216 -12.213 -18.871 1.164 1.00 59.41 C
ATOM 540 OG1 THR A 216 -13.123 -17.900 0.661 1.00 60.42 O
ATOM 541 CG2 THR A 216 -12.946 -19.969 1.903 1.00 58.24 C
ATOM 542 N ALA A 217 -9.233 -19.534 1.603 1.00 59.18 N
ATOM 543 CA ALA A 217 -8.119 -20.452 1.865 1.00 58.83 C
ATOM 544 C ALA A 217 -7.068 -19.873 2.817 1.00 59.40 C
ATOM 545 O ALA A 217 -6.400 -20.630 3.505 1.00 59.64 O
ATOM 546 CB ALA A 217 -7.485 -20.873 0.558 1.00 57.52 C
ATOM 547 N CYS A 218 -6.952 -18.537 2.864 1.00 60.35 N
ATOM 548 CA CYS A 218 -5.954 -17.816 3.676 1.00 60.86 C
ATOM 549 C CYS A 218 -6.505 -17.078 4.898 1.00 62.70 C
ATOM 550 O CYS A 218 -5.769 -16.351 5.569 1.00 62.42 O
ATOM 551 CB CYS A 218 -5.197 -16.820 2.814 1.00 59.63 C
ATOM 552 SG CYS A 218 -4.135 -17.584 1.608 1.00 59.34 S
ATOM 553 N GLN A 219 -7.770 -17.250 5.199 1.00 65.49 N
ATOM 554 CA GLN A 219 -8.275 -16.701 6.426 1.00 68.97 C
ATOM 555 C GLN A 219 -7.737 -17.545 7.558 1.00 70.14 C
ATOM 556 O GLN A 219 -7.679 -18.752 7.461 1.00 70.52 O
ATOM 557 CB GLN A 219 -9.789 -16.691 6.440 1.00 69.23 C
ATOM 558 CG GLN A 219 -10.371 -15.302 6.313 1.00 73.58 C
ATOM 559 CD GLN A 219 -11.015 -14.790 7.585 1.00 78.06 C
ATOM 560 OE1 GLN A 219 -11.640 -15.538 8.322 1.00 80.15 O
ATOM 561 NE2 GLN A 219 -10.867 -13.504 7.840 1.00 78.25 N
ATOM 562 N GLY A 220 -7.313 -16.907 8.626 1.00 71.84 N
ATOM 563 CA GLY A 220 -6.772 -17.639 9.741 1.00 74.32 C
ATOM 564 C GLY A 220 -5.262 -17.674 9.822 1.00 76.00 C
ATOM 565 O GLY A 220 -4.702 -17.534 10.891 1.00 77.09 O
ATOM 566 N VAL A 221 -4.589 -17.876 8.707 1.00 77.26 N
ATOM 567 CA VAL A 221 -3.145 -17.931 8.738 1.00 78.44 C
ATOM 568 C VAL A 221 -2.570 -17.552 7.400 1.00 78.79 C
ATOM 569 O VAL A 221 -2.410 -18.387 6.540 1.00 79.63 O
ATOM 570 CB VAL A 221 -2.638 -19.323 9.174 1.00 78.78 C
ATOM 571 CG1 VAL A 221 -2.096 -20.123 8.005 1.00 78.96 C
ATOM 572 CG2 VAL A 221 -1.606 -19.207 10.281 1.00 78.37 C
TER 573 VAL A 221
ATOM 574 N SER B 149 1.095 -20.571 -13.795 1.00 69.31 N
ATOM 575 CA SER B 149 1.821 -21.367 -14.853 1.00 69.04 C
ATOM 576 C SER B 149 3.096 -20.689 -15.383 1.00 68.59 C
ATOM 577 O SER B 149 4.138 -21.347 -15.509 1.00 68.56 O
ATOM 578 CB SER B 149 0.899 -21.748 -16.011 1.00 68.87 C