Header list of 1c9q.pdb file
Complete list - 3 20 Bytes
HEADER APOPTOSIS 03-AUG-99 1C9Q
TITLE AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2 DOMAIN OF XIAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS INHIBITOR IAP HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BIR-2 DOMAIN (RESIDUES 124-240) OF HUMAN XIAP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ZINC FINGER, APOPTOSIS, INHIBITOR
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR R.P.MEADOWS,S.W.FESIK
REVDAT 4 03-NOV-21 1C9Q 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1C9Q 1 VERSN
REVDAT 2 01-APR-03 1C9Q 1 JRNL
REVDAT 1 09-AUG-00 1C9Q 0
JRNL AUTH C.SUN,M.CAI,A.H.GUNASEKERA,R.P.MEADOWS,H.WANG,J.CHEN,
JRNL AUTH 2 H.ZHANG,W.WU,N.XU,S.C.NG,S.W.FESIK
JRNL TITL NMR STRUCTURE AND MUTAGENESIS OF THE INHIBITOR-OF-APOPTOSIS
JRNL TITL 2 PROTEIN XIAP.
JRNL REF NATURE V. 401 818 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10548111
JRNL DOI 10.1038/44617
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DREAMWALKER 2.0, X-PLOR 3.8X
REMARK 3 AUTHORS : OLEJNICZAK, E., MEADOWS, R. (DREAMWALKER),
REMARK 3 BRUNGER, A. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009467.
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 : 0.0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.6 MM XIAP U-15N,13C; 50 MM
REMARK 210 TRIS, 300MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; RESIDUAL
REMARK 210 DIPOLAR COUPLING IN PHAGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.8X
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NONE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NONE
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: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 2 76.81 -67.27
REMARK 500 LEU A 6 -38.76 -176.08
REMARK 500 ASP A 7 55.94 75.45
REMARK 500 ARG A 8 55.88 33.72
REMARK 500 GLU A 11 123.57 70.43
REMARK 500 THR A 12 -46.17 -131.47
REMARK 500 THR A 20 -54.34 -133.40
REMARK 500 GLN A 22 124.50 72.63
REMARK 500 VAL A 24 107.99 -53.22
REMARK 500 ASP A 25 -78.94 -54.16
REMARK 500 ASP A 28 30.06 -163.50
REMARK 500 THR A 29 -170.78 48.17
REMARK 500 ILE A 30 18.05 -178.21
REMARK 500 ASN A 34 71.21 -173.12
REMARK 500 PHE A 47 34.04 -89.85
REMARK 500 ASN A 49 50.70 74.52
REMARK 500 PRO A 51 177.91 -56.25
REMARK 500 HIS A 55 -38.97 168.03
REMARK 500 ALA A 79 -71.19 -78.94
REMARK 500 ASN A 86 32.09 74.11
REMARK 500 PHE A 101 73.48 -150.66
REMARK 500 LEU A 108 -84.80 -50.76
REMARK 500 ARG A 110 -59.34 69.32
REMARK 500 ASN A 111 166.92 89.89
REMARK 500 LEU A 112 174.29 77.17
REMARK 500 ASN A 113 -90.78 -46.16
REMARK 500 ILE A 114 38.32 32.20
REMARK 500 ARG A 115 -76.93 -56.73
REMARK 500 SER A 116 -64.79 75.67
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 77 SG
REMARK 620 2 CYS A 80 SG 109.0
REMARK 620 3 HIS A 97 NE2 109.5 109.7
REMARK 620 4 CYS A 104 SG 108.5 109.2 110.8
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 A 999
DBREF 1C9Q A 1 117 UNP P98170 BIRC4_HUMAN 124 240
SEQADV 1C9Q ALA A 79 UNP P98170 CYS 202 ENGINEERED MUTATION
SEQADV 1C9Q GLY A 90 UNP P98170 CYS 213 ENGINEERED MUTATION
SEQRES 1 A 117 ARG ASP HIS PHE ALA LEU ASP ARG PRO SER GLU THR HIS
SEQRES 2 A 117 ALA ASP TYR LEU LEU ARG THR GLY GLN VAL VAL ASP ILE
SEQRES 3 A 117 SER ASP THR ILE TYR PRO ARG ASN PRO ALA MET TYR SER
SEQRES 4 A 117 GLU GLU ALA ARG LEU LYS SER PHE GLN ASN TRP PRO ASP
SEQRES 5 A 117 TYR ALA HIS LEU THR PRO ARG GLU LEU ALA SER ALA GLY
SEQRES 6 A 117 LEU TYR TYR THR GLY ILE GLY ASP GLN VAL GLN CYS PHE
SEQRES 7 A 117 ALA CYS GLY GLY LYS LEU LYS ASN TRP GLU PRO GLY ASP
SEQRES 8 A 117 ARG ALA TRP SER GLU HIS ARG ARG HIS PHE PRO ASN CYS
SEQRES 9 A 117 PHE PHE VAL LEU GLY ARG ASN LEU ASN ILE ARG SER GLU
HET ZN A 999 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ASP A 2 LEU A 6 5 5
HELIX 2 2 HIS A 13 LEU A 18 1 6
HELIX 3 3 ASN A 34 TYR A 38 5 5
HELIX 4 4 SER A 39 PHE A 47 1 9
HELIX 5 5 THR A 57 ALA A 64 1 8
HELIX 6 6 TRP A 94 PHE A 101 1 8
HELIX 7 7 CYS A 104 ARG A 110 1 7
SHEET 1 A 3 LEU A 66 ILE A 71 0
SHEET 2 A 3 GLN A 74 CYS A 77 -1 N GLN A 74 O ILE A 71
SHEET 3 A 3 GLY A 82 LEU A 84 -1 O GLY A 82 N CYS A 77
LINK SG CYS A 77 ZN ZN A 999 1555 1555 2.10
LINK SG CYS A 80 ZN ZN A 999 1555 1555 2.10
LINK NE2 HIS A 97 ZN ZN A 999 1555 1555 2.21
LINK SG CYS A 104 ZN ZN A 999 1555 1555 2.10
SITE 1 AC1 4 CYS A 77 CYS A 80 HIS A 97 CYS A 104
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 - 3 20 Bytes