Header list of 1xox.pdb file
Complete list - 2 20 Bytes
HEADER APOPTOSIS 07-OCT-04 1XOX
TITLE SOLUTION STRUCTURE OF HUMAN SURVIVIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS INHIBITOR SURVIVIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-117;
COMPND 5 SYNONYM: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 5; APOPTOSIS
COMPND 6 INHIBITOR 4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BIRC5, API4, IAP4;
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: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BIR DOMAIN; APOPTOSIS, APOPTOSIS
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR C.SUN,D.NETTESHEIM,Z.LIU,E.T.OLEJNICZAK
REVDAT 3 02-MAR-22 1XOX 1 REMARK LINK
REVDAT 2 24-FEB-09 1XOX 1 VERSN
REVDAT 1 18-JAN-05 1XOX 0
JRNL AUTH C.SUN,D.NETTESHEIM,Z.LIU,E.T.OLEJNICZAK
JRNL TITL SOLUTION STRUCTURE OF HUMAN SURVIVIN AND ITS BINDING
JRNL TITL 2 INTERFACE WITH SMAC/DIABLO
JRNL REF BIOCHEMISTRY V. 44 11 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15628841
JRNL DOI 10.1021/BI0485171
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES WERE CALCULATED USING 1394 INTRA-MONOMER NOE
REMARK 3 CONSTRAINTS,
REMARK 3 THIRTY HYDROGEN BOND RESTRAINTS DERIVED FROM AN ANALYSIS OF AMIDE
REMARK 3 EXCHANGE RATES AND FIFTY-SIX TORSIONAL RESTRAINTS FROM AN ANALYSIS
REMARK 3 OF
REMARK 3 THE BACKBONE CHEMICAL SHIFTS. DIMER STRUCTURES WERE CALCULATED
REMARK 3 USING
REMARK 3 ADDITIONAL INTER-MONOMER NOE CONSTRAINTS.
REMARK 4
REMARK 4 1XOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030595.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D 12C
REMARK 210 FILTERED 13C-SEP NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D NMR
REMARK 210 TECHNIQUES
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: DIMERIC
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 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 PRO A 4 177.26 -51.11
REMARK 500 ALA A 9 -81.52 -44.22
REMARK 500 TRP A 10 60.23 -107.84
REMARK 500 ASN A 24 -73.98 -122.53
REMARK 500 TRP A 25 101.85 56.17
REMARK 500 PHE A 27 83.47 -68.28
REMARK 500 LEU A 28 -79.01 -115.53
REMARK 500 CYS A 46 60.46 -162.59
REMARK 500 ASP A 53 47.51 -92.32
REMARK 500 CYS A 60 -39.08 -179.28
REMARK 500 PHE A 61 116.60 70.66
REMARK 500 LYS A 62 97.81 -174.50
REMARK 500 PRO A 69 55.81 -68.75
REMARK 500 ASP A 70 41.78 168.69
REMARK 500 SER A 81 144.06 -177.16
REMARK 500 SER A 82 37.92 -96.75
REMARK 500 GLN A 92 158.80 -48.06
REMARK 500 PRO B 4 177.28 -51.11
REMARK 500 ALA B 9 -81.48 -44.29
REMARK 500 TRP B 10 60.15 -107.83
REMARK 500 ASN B 24 -73.98 -122.51
REMARK 500 TRP B 25 101.84 56.19
REMARK 500 PHE B 27 83.52 -68.33
REMARK 500 LEU B 28 -79.00 -115.56
REMARK 500 CYS B 46 60.42 -162.62
REMARK 500 ASP B 53 47.44 -92.26
REMARK 500 CYS B 60 -39.12 -179.30
REMARK 500 PHE B 61 116.56 70.69
REMARK 500 LYS B 62 97.69 -174.45
REMARK 500 PRO B 69 55.83 -68.75
REMARK 500 ASP B 70 41.79 168.73
REMARK 500 SER B 81 144.00 -177.20
REMARK 500 SER B 82 37.97 -96.73
REMARK 500 GLN B 92 158.78 -48.12
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 ZN A 999 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 57 SG
REMARK 620 2 CYS A 60 SG 108.5
REMARK 620 3 HIS A 77 ND1 108.5 110.6
REMARK 620 4 CYS A 84 SG 110.0 109.6 109.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 998 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 57 SG
REMARK 620 2 CYS B 60 SG 108.5
REMARK 620 3 HIS B 77 ND1 108.5 110.6
REMARK 620 4 CYS B 84 SG 110.0 109.6 109.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999
DBREF 1XOX A 1 117 UNP O15392 BIRC5_HUMAN 1 117
DBREF 1XOX B 1 117 UNP O15392 BIRC5_HUMAN 1 117
SEQRES 1 A 117 MET GLY ALA PRO THR LEU PRO PRO ALA TRP GLN PRO PHE
SEQRES 2 A 117 LEU LYS ASP HIS ARG ILE SER THR PHE LYS ASN TRP PRO
SEQRES 3 A 117 PHE LEU GLU GLY CYS ALA CYS THR PRO GLU ARG MET ALA
SEQRES 4 A 117 GLU ALA GLY PHE ILE HIS CYS PRO THR GLU ASN GLU PRO
SEQRES 5 A 117 ASP LEU ALA GLN CYS PHE PHE CYS PHE LYS GLU LEU GLU
SEQRES 6 A 117 GLY TRP GLU PRO ASP ASP ASP PRO ILE GLU GLU HIS LYS
SEQRES 7 A 117 LYS HIS SER SER GLY CYS ALA PHE LEU SER VAL LYS LYS
SEQRES 8 A 117 GLN PHE GLU GLU LEU THR LEU GLY GLU PHE LEU LYS LEU
SEQRES 9 A 117 ASP ARG GLU ARG ALA LYS ASN LYS ILE ALA LYS GLU THR
SEQRES 1 B 117 MET GLY ALA PRO THR LEU PRO PRO ALA TRP GLN PRO PHE
SEQRES 2 B 117 LEU LYS ASP HIS ARG ILE SER THR PHE LYS ASN TRP PRO
SEQRES 3 B 117 PHE LEU GLU GLY CYS ALA CYS THR PRO GLU ARG MET ALA
SEQRES 4 B 117 GLU ALA GLY PHE ILE HIS CYS PRO THR GLU ASN GLU PRO
SEQRES 5 B 117 ASP LEU ALA GLN CYS PHE PHE CYS PHE LYS GLU LEU GLU
SEQRES 6 B 117 GLY TRP GLU PRO ASP ASP ASP PRO ILE GLU GLU HIS LYS
SEQRES 7 B 117 LYS HIS SER SER GLY CYS ALA PHE LEU SER VAL LYS LYS
SEQRES 8 B 117 GLN PHE GLU GLU LEU THR LEU GLY GLU PHE LEU LYS LEU
SEQRES 9 B 117 ASP ARG GLU ARG ALA LYS ASN LYS ILE ALA LYS GLU THR
HET ZN A 999 1
HET ZN B 998 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 LEU A 14 THR A 21 1 8
HELIX 2 2 THR A 34 GLU A 40 1 7
HELIX 3 3 ASP A 72 SER A 81 1 10
HELIX 4 4 THR A 97 THR A 117 1 21
HELIX 5 5 LEU B 14 THR B 21 1 8
HELIX 6 6 THR B 34 GLU B 40 1 7
HELIX 7 7 ASP B 72 SER B 81 1 10
HELIX 8 8 THR B 97 THR B 117 1 21
SHEET 1 A 2 PHE A 43 HIS A 45 0
SHEET 2 A 2 ALA A 55 CYS A 57 -1 O GLN A 56 N ILE A 44
SHEET 1 B 2 PHE B 43 HIS B 45 0
SHEET 2 B 2 ALA B 55 CYS B 57 -1 O GLN B 56 N ILE B 44
LINK SG CYS A 57 ZN ZN A 999 1555 1555 2.10
LINK SG CYS A 60 ZN ZN A 999 1555 1555 2.10
LINK ND1 HIS A 77 ZN ZN A 999 1555 1555 2.20
LINK SG CYS A 84 ZN ZN A 999 1555 1555 2.10
LINK SG CYS B 57 ZN ZN B 998 1555 1555 2.10
LINK SG CYS B 60 ZN ZN B 998 1555 1555 2.10
LINK ND1 HIS B 77 ZN ZN B 998 1555 1555 2.20
LINK SG CYS B 84 ZN ZN B 998 1555 1555 2.10
SITE 1 AC1 5 CYS B 57 PHE B 58 CYS B 60 HIS B 77
SITE 2 AC1 5 CYS B 84
SITE 1 AC2 5 CYS A 57 PHE A 58 CYS A 60 HIS A 77
SITE 2 AC2 5 CYS A 84
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
Complete list - 2 20 Bytes