HEADER TRANSFERASE 26-JAN-04 1S6P
TITLE CRYSTAL STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE
TITLE 2 TRANSCRIPTASE (RT) IN COMPLEX WITH JANSSEN-R100943
CAVEAT 1S6P THERE IS A CHIRALITY ERROR IN A ILE 31.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POL POLYPROTEIN [CONTAINS: REVERSE TRANSCRIPTASE];
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P66 SUBUNIT;
COMPND 5 SYNONYM: HIV-1 RT;
COMPND 6 EC: 2.7.7.49;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: POL POLYPROTEIN [CONTAINS: REVERSE TRANSCRIPTASE];
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: P51 SUBUNIT;
COMPND 13 SYNONYM: HIV-1 RT;
COMPND 14 EC: 2.7.7.49;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: POL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BH10 ISOLATE;
SOURCE 8 OTHER_DETAILS: HIV-1 CLONE 12;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 11 ORGANISM_TAXID: 11676;
SOURCE 12 GENE: POL;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BH10 ISOLATE;
SOURCE 16 OTHER_DETAILS: HIV-1 CLONE 12
KEYWDS REVERSE TRANSCRIPTASE, NNRTI, NONNUCLEOSIDE INHIBITOR, PROTEIN-
KEYWDS 2 INHIBITOR COMPLEX, AIDS, DRUG DESIGN, DRUG RESISTANCE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.DAS,E.ARNOLD
REVDAT 5 14-FEB-24 1S6P 1 REMARK
REVDAT 4 27-OCT-21 1S6P 1 REMARK SEQADV LINK
REVDAT 3 13-OCT-10 1S6P 1 REMARK
REVDAT 2 24-FEB-09 1S6P 1 VERSN
REVDAT 1 11-MAY-04 1S6P 0
JRNL AUTH K.DAS,A.D.CLARK JR.,P.LEWI,J.HEERES,M.DEJONGE,L.KOYMANS,
JRNL AUTH 2 H.VINKERS,F.DAEYAERT,D.W.LUDOVICI,M.J.KUKLA,B.DECORTE,
JRNL AUTH 3 R.W.KAVASH,C.Y.HO,H.YE,M.LICHTENSTEIN,K.ANDRIES,R.PAUWLES,
JRNL AUTH 4 M.-P.DEBETHUNE,P.L.BOYER,P.CLARK,S.H.HUGHES,P.A.JANSSEN,
JRNL AUTH 5 E.ARNOLD
JRNL TITL ROLES OF CONFORMATIONAL AND POSITIONAL ADAPTABILITY IN
JRNL TITL 2 STRUCTURE-BASED DESIGN OF TMC125-R165335 (ETRAVIRINE) AND
JRNL TITL 3 RELATED NON-NUCLEOSIDE REVERSE TRANSCRIPTASE INHIBITORS THAT
JRNL TITL 4 ARE HIGHLY POTENT AND EFFECTIVE AGAINST WILD-TYPE AND
JRNL TITL 5 DRUG-RESISTANT HIV-1 VARIANTS
JRNL REF J.MED.CHEM. V. 47 2550 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 15115397
JRNL DOI 10.1021/JM030558S
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.DING,K.DAS,H.MOEREELS,L.KOYMANS,K.ANDRIES,P.A.J.JANSSEN,
REMARK 1 AUTH 2 S.H.HUGHES,E.ARNOLD
REMARK 1 TITL STRUCTURE OF HIV-1 RT/TIBO R 86183 COMPLEX REVEALS
REMARK 1 TITL 2 SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE
REMARK 1 TITL 3 INHIBITORS.
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 407 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.DING,K.DAS,C.TANTILLO,W.ZHANG,A.D.CLARK JR.,S.JESSEN,X.LU,
REMARK 1 AUTH 2 Y.HSIOU,A.JACOBO-MOLINA,K.ANDRIES,R.PAUWELS,H.MOEREELS,
REMARK 1 AUTH 3 L.KOYMANS,P.A.J.JANSSEN,R.H.SMITH JR.,M.KROEGER KOEPKE,
REMARK 1 AUTH 4 C.J.MICHEJDA,S.H.HUGHES,E.ARNOLD
REMARK 1 TITL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN A COMPLEX WITH
REMARK 1 TITL 2 THE NON-NUCLEOSIDE INHIBITOR ALPHA-APA R 95845 AT 2.8 A
REMARK 1 TITL 3 RESOLUTION.
REMARK 1 REF STRUCTURE V. 3 365 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.DAS,J.DING,Y.HSIOU,A.D.CLARK JR.,H.MOEREELS,L.KOYMANS,
REMARK 1 AUTH 2 K.ANDRIES,R.PAUWELS,P.A.JANSSEN,P.L.BOYER,P.CLARK,
REMARK 1 AUTH 3 R.H.SMITH JR.,M.B.KROEGER SMITH,C.J.MICHEJDA,S.H.HUGHES,
REMARK 1 AUTH 4 E.ARNOLD
REMARK 1 TITL CRYSTAL STRUCTURES OF 8-CL AND 9-CL TIBO COMPLEXED WITH
REMARK 1 TITL 2 WILD-TYPE HIV-1 RT AND 8-CL TIBO COMPLEXED WITH THE
REMARK 1 TITL 3 TYR181CYS HIV-1 RT DRUG-RESISTANT MUTANT.
REMARK 1 REF J.MOL.BIOL. V. 264 1085 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1996.0698
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.DING,K.DAS,Y.HSIOU,S.G.SARAFIANOS,A.D.CLARK JR.,
REMARK 1 AUTH 2 A.JACOBO-MOLINA,C.TANTILLO,S.H.HUGHES,E.ARNOLD
REMARK 1 TITL STRUCTURE AND FUNCTIONAL IMPLICATIONS OF THE POLYMERASE
REMARK 1 TITL 2 ACTIVE SITE REGION IN A COMPLEX OF HIV-1 RT WITH A
REMARK 1 TITL 3 DOUBLE-STRANDED DNA TEMPLATE-PRIMER AND AN ANTIBODY FAB
REMARK 1 TITL 4 FRAGMENT AT 2.8 A RESOLUTION.
REMARK 1 REF J.MOL.BIOL. V. 284 1095 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2208
REMARK 1 REFERENCE 5
REMARK 1 AUTH D.W.LUDOVICI,M.J.KUKLA,P.G.GROUS,S.KRISHNAN,K.ANDRIES,
REMARK 1 AUTH 2 M.DE BETHUNE,H.AZIJN,R.PAUWELS,E.DE CLERCQ,E.ARNOLD,
REMARK 1 AUTH 3 P.A.JANSSEN
REMARK 1 TITL EVOLUTION OF ANTI-HIV DRUG CANDIDATES. PART 1: FROM
REMARK 1 TITL 2 ALPHA-ANILINOPHENYLACETAMIDE (ALPHA-APA) TO IMIDOYL THIOUREA
REMARK 1 TITL 3 (ITU).
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 11 2225 2001
REMARK 1 REFN ISSN 0960-894X
REMARK 1 DOI 10.1016/S0960-894X(01)00410-3
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : CNS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 30206
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1542
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4310
REMARK 3 BIN FREE R VALUE : 0.4520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 194
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8027
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 151
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.250
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1S6P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31923
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.5
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.80
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 113.35000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 113.35000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.70000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 553
REMARK 465 ALA A 554
REMARK 465 GLY A 555
REMARK 465 ILE A 556
REMARK 465 ARG A 557
REMARK 465 LYS A 558
REMARK 465 ILE A 559
REMARK 465 LEU A 560
REMARK 465 GLN B 428
REMARK 465 LEU B 429
REMARK 465 GLU B 430
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ILE A 31 CD1
REMARK 480 LYS A 219 CG CD CE NZ
REMARK 480 LYS A 220 CG CD CE NZ
REMARK 480 HIS A 221 CG ND1 CD2 CE1 NE2
REMARK 480 LYS A 287 CG CD CE NZ
REMARK 480 TRP B 229 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 480 TRP B 229 CZ3 CH2
REMARK 480 MET B 230 CG SD CE
REMARK 480 ILE B 270 CG1 CG2 CD1
REMARK 480 THR B 362 OG1 CG2
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 LYS A 64 N LYS A 66 2.06
REMARK 500 O GLU B 298 N GLU B 302 2.11
REMARK 500 OH TYR B 115 O MET B 184 2.16
REMARK 500 O GLU A 224 O PRO A 226 2.17
REMARK 500 OD1 ASP B 76 NE ARG B 78 2.17
REMARK 500 O PRO B 150 OG SER B 156 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE A 31 CG1 ILE A 31 CD1 1.607
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 ILE A 31 CB - CG1 - CD1 ANGL. DEV. = -58.5 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 HIS A 221 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG A 284 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LYS A 287 O - C - N ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO A 345 C - N - CA ANGL. DEV. = 11.7 DEGREES
REMARK 500 ARG B 83 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO B 225 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 PRO B 225 CB - CA - C ANGL. DEV. = -14.9 DEGREES
REMARK 500 PRO B 225 O - C - N ANGL. DEV. = -11.6 DEGREES
REMARK 500 VAL B 241 N - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 GLN B 242 N - CA - C ANGL. DEV. = 19.2 DEGREES
REMARK 500 PRO B 412 C - N - CA ANGL. DEV. = -10.0 DEGREES
REMARK 500 PRO B 420 C - N - CA ANGL. DEV. = -12.5 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 ILE A 2 178.14 -51.64
REMARK 500 ILE A 5 142.06 -24.08
REMARK 500 PRO A 14 125.53 -26.21
REMARK 500 MET A 16 131.60 -36.74
REMARK 500 PRO A 25 85.99 -15.49
REMARK 500 THR A 27 104.30 -40.07
REMARK 500 GLU A 28 -5.35 -56.59
REMARK 500 GLU A 44 -3.99 -59.25
REMARK 500 PRO A 52 9.25 -44.76
REMARK 500 GLU A 53 -72.17 -48.37
REMARK 500 TYR A 56 -149.00 -112.22
REMARK 500 ASN A 57 146.58 -170.95
REMARK 500 LYS A 64 40.43 -172.56
REMARK 500 LYS A 65 -38.18 -15.07
REMARK 500 LYS A 66 176.81 -51.90
REMARK 500 SER A 68 -160.08 -128.95
REMARK 500 ARG A 78 -68.72 -20.74
REMARK 500 GLN A 85 158.67 -49.13
REMARK 500 GLU A 89 105.39 -59.98
REMARK 500 ALA A 98 5.43 -56.96
REMARK 500 LYS A 102 146.78 -33.41
REMARK 500 LYS A 104 -83.50 -68.63
REMARK 500 ASP A 113 41.16 -105.66
REMARK 500 PRO A 119 173.09 -52.59
REMARK 500 ASP A 121 117.64 -38.53
REMARK 500 GLU A 122 16.44 -60.67
REMARK 500 PRO A 133 -162.72 -73.80
REMARK 500 ASN A 136 108.36 -174.24
REMARK 500 VAL A 148 -153.55 -132.57
REMARK 500 TRP A 153 143.17 -25.38
REMARK 500 SER A 156 -62.24 -137.92
REMARK 500 ALA A 158 -85.25 -67.97
REMARK 500 ILE A 159 -34.76 -35.13
REMARK 500 SER A 162 -95.79 -65.45
REMARK 500 SER A 163 -55.99 -13.51
REMARK 500 MET A 164 -79.25 -48.84
REMARK 500 THR A 165 -50.02 -28.07
REMARK 500 ASN A 175 37.07 -146.25
REMARK 500 PRO A 176 -4.54 -47.52
REMARK 500 TYR A 183 84.84 -158.88
REMARK 500 MET A 184 -71.11 61.79
REMARK 500 GLU A 194 132.24 -27.75
REMARK 500 ILE A 195 -40.35 -26.55
REMARK 500 LYS A 220 68.93 28.39
REMARK 500 HIS A 221 -99.32 -109.39
REMARK 500 GLN A 222 -56.98 -170.80
REMARK 500 LYS A 223 98.35 -11.77
REMARK 500 GLU A 224 41.36 -143.59
REMARK 500 MET A 230 11.52 45.31
REMARK 500 PRO A 236 1.85 -54.66
REMARK 500
REMARK 500 THIS ENTRY HAS 166 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE B 130 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 443 OD2
REMARK 620 2 ASP A 443 OD1 54.3
REMARK 620 3 ASP A 498 OD2 131.3 85.5
REMARK 620 4 ASP A 549 OD1 72.5 96.1 146.1
REMARK 620 5 HOH A1001 O 133.6 139.8 94.5 63.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IET A 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SV5 RELATED DB: PDB
REMARK 900 1SV5 IS THE STRUCTURE OF K103N MUTANT HIV-1 REVERSE TRANSCRIPTASE
REMARK 900 IN COMPLEX WITH JANSSEN-R165335
REMARK 900 RELATED ID: 1S9G RELATED DB: PDB
REMARK 900 1S9G IS THE STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX
REMARK 900 WITH JANSSEN-R120394
REMARK 900 RELATED ID: 1SUQ RELATED DB: PDB
REMARK 900 ISUQ IS THE STRUCTURE OF K103N MUTANT HIV-1 REVERSE TRANSCRIPTASE
REMARK 900 IN COMPLEX WITH JANSSEN-R165335
REMARK 900 RELATED ID: 1S9E RELATED DB: PDB
REMARK 900 1S9E IS THE STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX
REMARK 900 WITH JANSSEN-R129385
REMARK 900 RELATED ID: 1S6Q RELATED DB: PDB
REMARK 900 IS6Q IS THE STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX
REMARK 900 WITH JANSSEN-R147681
REMARK 900 RELATED ID: 1HNV RELATED DB: PDB
REMARK 900 1HNV IS THE STRUCTURE OF HIV-1 RT/TIBO R 86183 COMPLEX
REMARK 900 RELATED ID: 1HNI RELATED DB: PDB
REMARK 900 1HNI IS THE STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN A COMPLEX
REMARK 900 WITH THE NON-NUCLEOSIDE INHIBITOR ALPHA-APA R 95845
REMARK 900 RELATED ID: 2HMI RELATED DB: PDB
REMARK 900 2HMI IS HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH A DOUBLE -
REMARK 900 STRANDED DNA AND FAB28
REMARK 900 RELATED ID: 1DLO RELATED DB: PDB
DBREF 1S6P A 1 560 UNP P03366 POL_HV1B1 168 727
DBREF 1S6P B 1 430 UNP P03366 POL_HV1B1 168 597
SEQADV 1S6P SER A 280 UNP P03366 CYS 447 ENGINEERED MUTATION
SEQADV 1S6P SER B 280 UNP P03366 CYS 447 ENGINEERED MUTATION
SEQRES 1 A 560 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 560 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 560 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 560 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 560 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 560 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 560 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 560 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 A 560 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 560 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 560 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 560 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 560 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 560 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 A 560 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 560 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 560 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 560 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 560 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 560 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 A 560 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 560 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 A 560 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 560 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 560 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 560 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 560 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 560 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 560 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 560 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 560 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 560 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 560 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 560 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 560 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 560 GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL VAL PRO
SEQRES 37 A 560 LEU THR ASN THR THR ASN GLN LYS THR GLU LEU GLN ALA
SEQRES 38 A 560 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 560 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 560 ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 560 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 560 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 A 560 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS ILE
SEQRES 44 A 560 LEU
SEQRES 1 B 430 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 B 430 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 B 430 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 B 430 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 B 430 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 B 430 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 B 430 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 B 430 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 B 430 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 B 430 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 B 430 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 B 430 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 B 430 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 B 430 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 B 430 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 B 430 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 B 430 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 B 430 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 B 430 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 B 430 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 B 430 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 B 430 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 B 430 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 B 430 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 B 430 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 B 430 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 B 430 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 B 430 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 B 430 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 B 430 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 B 430 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 B 430 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 B 430 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 B 430 GLU
HET MG A 601 1
HET IET A 701 23
HETNAM MG MAGNESIUM ION
HETNAM IET 1-(4-CYANO-PHENYL)-3-[2-(2,6-DICHLORO-PHENYL)-1-IMINO-
HETNAM 2 IET ETHYL]-THIOUREA
FORMUL 3 MG MG 2+
FORMUL 4 IET C16 H12 CL2 N4 S
FORMUL 5 HOH *151(H2 O)
HELIX 1 1 THR A 27 GLU A 44 1 18
HELIX 2 2 PHE A 77 ARG A 83 1 7
HELIX 3 3 HIS A 96 LEU A 100 5 5
HELIX 4 4 ALA A 114 VAL A 118 5 5
HELIX 5 5 ARG A 125 ALA A 129 5 5
HELIX 6 6 SER A 156 GLN A 174 1 19
HELIX 7 7 GLU A 194 ARG A 211 1 18
HELIX 8 8 THR A 253 ILE A 270 1 18
HELIX 9 9 VAL A 276 LYS A 281 1 6
HELIX 10 10 THR A 296 GLU A 312 1 17
HELIX 11 11 ASN A 363 GLY A 384 1 22
HELIX 12 12 GLN A 394 TYR A 405 1 12
HELIX 13 13 THR A 473 ASP A 488 1 16
HELIX 14 14 SER A 499 ALA A 508 1 10
HELIX 15 15 GLU A 516 LYS A 527 1 12
HELIX 16 16 GLY A 544 VAL A 552 1 9
HELIX 17 17 THR B 27 GLU B 44 1 18
HELIX 18 18 PHE B 77 ARG B 83 1 7
HELIX 19 19 GLY B 99 LYS B 103 5 5
HELIX 20 20 GLY B 112 PHE B 116 5 5
HELIX 21 21 PHE B 124 ALA B 129 5 6
HELIX 22 22 SER B 134 GLU B 138 5 5
HELIX 23 23 GLY B 155 GLN B 174 1 20
HELIX 24 24 GLU B 194 GLY B 213 1 20
HELIX 25 25 THR B 253 ALA B 267 1 15
HELIX 26 26 VAL B 276 LYS B 281 1 6
HELIX 27 27 THR B 296 LYS B 311 1 16
HELIX 28 28 ASN B 363 GLY B 384 1 22
HELIX 29 29 GLN B 394 TRP B 402 1 9
SHEET 1 A 3 ILE A 47 ILE A 50 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1
SHEET 3 A 3 THR A 128 ILE A 132 -1
SHEET 1 B 2 VAL A 60 ILE A 63 0
SHEET 2 B 2 ARG A 72 ASP A 76 -1
SHEET 1 C 3 SER A 105 ASP A 110 0
SHEET 2 C 3 ASP A 186 SER A 191 -1
SHEET 3 C 3 VAL A 179 TYR A 183 -1
SHEET 1 D 3 PHE A 227 TRP A 229 0
SHEET 2 D 3 TYR A 232 LEU A 234 -1
SHEET 3 D 3 LYS A 238 THR A 240 -1
SHEET 1 E 5 LYS A 347 ALA A 355 0
SHEET 2 E 5 GLN A 336 TYR A 342 -1
SHEET 3 E 5 LEU A 325 GLN A 332 -1
SHEET 4 E 5 LYS A 388 LEU A 391 1
SHEET 5 E 5 GLU A 413 THR A 419 1
SHEET 1 F 2 HIS A 361 THR A 362 0
SHEET 2 F 2 LYS A 512 SER A 513 -1
SHEET 1 G 5 ARG A 463 THR A 470 0
SHEET 2 G 5 LEU A 452 THR A 459 -1
SHEET 3 G 5 GLU A 438 ASN A 447 -1
SHEET 4 G 5 GLU A 492 THR A 497 1
SHEET 5 G 5 LYS A 530 VAL A 536 1
SHEET 1 H 3 ILE B 47 ILE B 50 0
SHEET 2 H 3 ILE B 142 TYR B 146 -1
SHEET 3 H 3 ALA B 129 ILE B 132 -1
SHEET 1 I 2 VAL B 60 ILE B 63 0
SHEET 2 I 2 ARG B 72 ASP B 76 -1
SHEET 1 J 4 VAL B 179 TYR B 183 0
SHEET 2 J 4 ASP B 186 SER B 191 -1
SHEET 3 J 4 SER B 105 ASP B 110 0
SHEET 4 J 4 GLU B 233 LEU B 234 -1
SHEET 1 K 4 GLN B 336 TYR B 342 0
SHEET 2 K 4 ILE B 326 LYS B 331 -1
SHEET 3 K 4 LYS B 388 LEU B 391 1
SHEET 4 K 4 GLU B 413 VAL B 417 1
LINK OD2 ASP A 443 MG MG A 601 1555 1555 2.40
LINK OD1 ASP A 443 MG MG A 601 1555 1555 2.49
LINK OD2 ASP A 498 MG MG A 601 1555 1555 1.95
LINK OD1 ASP A 549 MG MG A 601 1555 1555 2.49
LINK MG MG A 601 O HOH A1001 1555 1555 2.30
CISPEP 1 PRO A 225 PRO A 226 0 0.27
CISPEP 2 PRO A 420 PRO A 421 0 -2.50
SITE 1 AC1 4 ASP A 443 ASP A 498 ASP A 549 HOH A1001
SITE 1 AC2 11 LEU A 100 LYS A 101 LYS A 103 VAL A 106
SITE 2 AC2 11 VAL A 179 TYR A 181 TYR A 188 PHE A 227
SITE 3 AC2 11 LEU A 234 HIS A 235 TYR A 318
CRYST1 226.700 67.400 104.300 90.00 107.00 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004411 0.000000 0.001348 0.00000
SCALE2 0.000000 0.014837 -0.000001 0.00000
SCALE3 0.000000 0.000000 0.010026 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
