HEADER ZN-BINDING PROTEIN 11-JUN-98 1WJF
TITLE SOLUTION STRUCTURE OF H12C MUTANT OF THE N-TERMINAL ZN BINDING DOMAIN
TITLE 2 OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM, NMR, 40 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 CELL_LINE: BL21;
SOURCE 5 GENE: POTENTIAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: T7 RNA POLYMERASE;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-15B;
SOURCE 12 EXPRESSION_SYSTEM_GENE: T7
KEYWDS ZN-BINDING PROTEIN, AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR M.CAI,A.M.GRONENBORN,G.M.CLORE
REVDAT 3 14-MAR-18 1WJF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WJF 1 VERSN
REVDAT 1 16-DEC-98 1WJF 0
JRNL AUTH M.CAI,Y.HUANG,M.CAFFREY,R.ZHENG,R.CRAIGIE,G.M.CLORE,
JRNL AUTH 2 A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE OF THE HIS12 --> CYS MUTANT OF THE
JRNL TITL 2 N-TERMINAL ZINC BINDING DOMAIN OF HIV-1 INTEGRASE COMPLEXED
JRNL TITL 3 TO CADMIUM.
JRNL REF PROTEIN SCI. V. 7 2669 1998
JRNL REFN ISSN 0961-8368
JRNL PMID 9865962
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.CAI,R.ZHENG,M.CAFFREY,R.CRAIGIE,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL SOLUTION STRUCTURE OF THE N-TERMINAL ZINC BINDING DOMAIN OF
REMARK 1 TITL 2 HIV-1 INTEGRASE
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 567 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.CAI,R.ZHENG,M.CAFFREY,R.CRAIGIE,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL ERRATUM. SOLUTION STRUCTURE OF THE N-TERMINAL ZINC BINDING
REMARK 1 TITL 2 DOMAIN OF HIV-1 INTEGRASE
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 839 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177211.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 HIS A 16 -134.68 58.08
REMARK 500 1 GLU A 48 -102.95 -86.62
REMARK 500 1 ALA A 49 -135.00 -168.29
REMARK 500 1 HIS B 16 -134.57 58.12
REMARK 500 1 GLU B 48 -102.79 -86.63
REMARK 500 1 ALA B 49 -135.04 -168.33
REMARK 500 2 HIS A 16 -139.48 58.93
REMARK 500 2 GLN A 44 -70.07 -78.04
REMARK 500 2 ALA A 49 -143.15 47.78
REMARK 500 2 MET A 50 -88.56 40.00
REMARK 500 2 HIS B 16 -139.57 58.96
REMARK 500 2 GLN B 44 -70.02 -77.99
REMARK 500 2 ALA B 49 -143.10 47.84
REMARK 500 2 MET B 50 -89.18 39.93
REMARK 500 3 HIS A 16 -126.58 58.04
REMARK 500 3 GLN A 44 -70.08 -78.90
REMARK 500 3 GLU A 48 -77.93 -89.20
REMARK 500 3 ALA A 49 -50.09 -165.75
REMARK 500 3 HIS B 16 -126.67 57.96
REMARK 500 3 GLU B 48 -78.11 -89.28
REMARK 500 3 ALA B 49 -50.03 -165.62
REMARK 500 4 HIS A 16 -138.27 58.22
REMARK 500 4 PRO A 30 -20.71 -38.94
REMARK 500 4 LYS A 46 20.20 -75.90
REMARK 500 4 HIS B 16 -138.69 58.24
REMARK 500 4 PRO B 30 -20.55 -39.04
REMARK 500 5 HIS A 16 -127.01 56.71
REMARK 500 5 GLN A 53 -76.65 -152.34
REMARK 500 5 HIS B 16 -126.86 56.73
REMARK 500 5 GLN B 53 -76.58 -152.44
REMARK 500 6 HIS A 16 -119.14 56.51
REMARK 500 6 PRO A 30 -25.81 -39.06
REMARK 500 6 GLN A 44 -70.10 -78.86
REMARK 500 6 ALA A 49 78.71 -166.95
REMARK 500 6 MET A 50 102.02 -160.45
REMARK 500 6 GLN A 53 -18.45 -156.15
REMARK 500 6 VAL A 54 -73.40 -90.10
REMARK 500 6 HIS B 16 -119.25 56.50
REMARK 500 6 PRO B 30 -25.96 -38.99
REMARK 500 6 ALA B 49 78.79 -167.02
REMARK 500 6 MET B 50 101.09 -160.63
REMARK 500 6 GLN B 53 -18.47 -156.16
REMARK 500 6 VAL B 54 -73.36 -90.05
REMARK 500 7 HIS A 16 -133.03 57.64
REMARK 500 7 PRO A 30 -22.43 -38.03
REMARK 500 7 ALA A 49 -110.43 -78.29
REMARK 500 7 MET A 50 157.74 55.96
REMARK 500 7 HIS B 16 -133.05 57.45
REMARK 500 7 PRO B 30 -22.32 -38.24
REMARK 500 7 ALA B 49 -110.35 -78.25
REMARK 500
REMARK 500 THIS ENTRY HAS 244 RAMACHANDRAN OUTLIERS.
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 CD A 56 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 40 SG 112.5
REMARK 620 3 CYS A 43 SG 112.0 105.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 56 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 12 SG
REMARK 620 2 CYS B 40 SG 112.5
REMARK 620 3 CYS B 43 SG 112.1 105.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 56
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WJE RELATED DB: PDB
DBREF 1WJF A 1 55 UNP P04587 POL_HV1B5 728 782
DBREF 1WJF B 1 55 UNP P04587 POL_HV1B5 728 782
SEQADV 1WJF CYS A 12 UNP P04587 HIS 739 ENGINEERED MUTATION
SEQADV 1WJF CYS B 12 UNP P04587 HIS 739 ENGINEERED MUTATION
SEQRES 1 A 55 PHE LEU ASP GLY ILE ASP LYS ALA GLN GLU GLU CYS GLU
SEQRES 2 A 55 LYS TYR HIS SER ASN TRP ARG ALA MET ALA SER ASP PHE
SEQRES 3 A 55 ASN LEU PRO PRO VAL VAL ALA LYS GLU ILE VAL ALA SER
SEQRES 4 A 55 CYS ASP LYS CYS GLN LEU LYS GLY GLU ALA MET HIS GLY
SEQRES 5 A 55 GLN VAL ASP
SEQRES 1 B 55 PHE LEU ASP GLY ILE ASP LYS ALA GLN GLU GLU CYS GLU
SEQRES 2 B 55 LYS TYR HIS SER ASN TRP ARG ALA MET ALA SER ASP PHE
SEQRES 3 B 55 ASN LEU PRO PRO VAL VAL ALA LYS GLU ILE VAL ALA SER
SEQRES 4 B 55 CYS ASP LYS CYS GLN LEU LYS GLY GLU ALA MET HIS GLY
SEQRES 5 B 55 GLN VAL ASP
HET CD A 56 1
HET CD B 56 1
HETNAM CD CADMIUM ION
FORMUL 3 CD 2(CD 2+)
HELIX 1 1 ASP A 3 TYR A 15 5 13
HELIX 2 2 TRP A 19 PHE A 26 1 8
HELIX 3 3 PRO A 30 SER A 39 1 10
HELIX 4 4 ASP B 3 TYR B 15 5 13
HELIX 5 5 TRP B 19 PHE B 26 1 8
HELIX 6 6 PRO B 30 SER B 39 1 10
LINK CD CD A 56 SG CYS A 12 1555 1555 2.61
LINK CD CD A 56 SG CYS A 40 1555 1555 2.59
LINK CD CD A 56 SG CYS A 43 1555 1555 2.61
LINK CD CD B 56 SG CYS B 12 1555 1555 2.61
LINK CD CD B 56 SG CYS B 40 1555 1555 2.59
LINK CD CD B 56 SG CYS B 43 1555 1555 2.61
SITE 1 AC1 3 CYS A 12 CYS A 40 CYS A 43
SITE 1 AC2 3 CYS B 12 CYS B 40 CYS B 43
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
