Header list of 1f9x.pdb file
Complete list - 23 20 Bytes
HEADER APOPTOSIS INHIBITOR 11-JUL-00 1F9X
TITLE AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-3 DOMAIN OF XIAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INHIBITOR OF APOPTOSIS PROTEIN XIAP;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 241-356;
COMPND 5 SYNONYM: APOPTOSIS INHIBITOR 3;
COMPND 6 ENGINEERED: 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: PET28B
KEYWDS BIR3 DOMAIN, INHIBITOR OF APOPTOSIS PROTEIN XIAP, ZINC FINGER,
KEYWDS 2 CASPASE-9 INHIBITION, APOPTOSIS INHIBITOR
EXPDTA SOLUTION NMR
AUTHOR C.SUN,M.CAI,R.P.MEADOWS,S.W.FESIK
REVDAT 4 23-FEB-22 1F9X 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1F9X 1 VERSN
REVDAT 2 01-APR-03 1F9X 1 JRNL
REVDAT 1 11-JUL-01 1F9X 0
JRNL AUTH C.SUN,M.CAI,R.P.MEADOWS,N.XU,A.H.GUNASEKERA,J.HERRMANN,
JRNL AUTH 2 J.C.WU,S.W.FESIK
JRNL TITL NMR STRUCTURE AND MUTAGENESIS OF THE THIRD BIR DOMAIN OF THE
JRNL TITL 2 INHIBITOR OF APOPTOSIS PROTEIN XIAP.
JRNL REF J.BIOL.CHEM. V. 275 33777 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10934209
JRNL DOI 10.1074/JBC.M006226200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX, CNX
REMARK 3 AUTHORS : MSI INC. (CNX), MSI INC. (CNX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011424.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 300 MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.7 MM XIAP(RESIDUES 241-356)U
REMARK 210 -15N; 1.7 MM XIAP(RESIDUES 241-
REMARK 210 356)U-15N, 13C;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCANH; CBCACONH; CCH-COSY;
REMARK 210 HNCO; 3D_13C-SEPARATED_NOESY; 3D_
REMARK 210 15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ; 600 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 : 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 237
REMARK 465 SER A 238
REMARK 465 HIS A 239
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 SER A 241 -165.17 73.35
REMARK 500 ASP A 242 70.18 -69.27
REMARK 500 ALA A 243 106.29 57.98
REMARK 500 ASP A 247 -86.58 -139.13
REMARK 500 ARG A 248 34.98 176.19
REMARK 500 ASN A 249 26.12 46.71
REMARK 500 PHE A 250 157.62 169.15
REMARK 500 ASN A 252 86.48 49.50
REMARK 500 THR A 254 98.08 -68.30
REMARK 500 PRO A 257 -150.75 -80.07
REMARK 500 ASP A 264 -173.84 -50.43
REMARK 500 ARG A 268 -70.28 -59.89
REMARK 500 TRP A 275 -44.08 -133.79
REMARK 500 ILE A 276 -172.38 -62.25
REMARK 500 TYR A 277 -176.96 -57.13
REMARK 500 LYS A 281 -74.80 -48.57
REMARK 500 ASP A 296 -6.84 88.96
REMARK 500 TRP A 310 28.49 -155.79
REMARK 500 PRO A 312 170.56 -43.66
REMARK 500 SER A 313 -39.28 -32.33
REMARK 500 GLU A 314 100.31 17.15
REMARK 500 TYR A 324 124.16 172.40
REMARK 500 LYS A 328 -88.66 -32.91
REMARK 500 LEU A 344 -93.76 -64.21
REMARK 500 THR A 345 -176.05 166.72
REMARK 500 SER A 347 -33.44 170.70
REMARK 500 LEU A 348 -82.58 -46.89
REMARK 500 CYS A 351 87.08 66.04
REMARK 500 LEU A 352 -45.96 85.95
REMARK 500 VAL A 353 -52.14 166.42
REMARK 500 ARG A 354 -86.26 55.17
REMARK 500 THR A 355 50.61 -147.19
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 300 SG
REMARK 620 2 CYS A 303 SG 109.3
REMARK 620 3 HIS A 320 NE2 103.3 116.6
REMARK 620 4 CYS A 327 SG 115.6 108.5 103.7
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 1F9X A 241 356 UNP P98170 BIRC4_HUMAN 241 356
SEQADV 1F9X GLY A 237 UNP P98170 CLONING ARTIFACT
SEQADV 1F9X SER A 238 UNP P98170 CLONING ARTIFACT
SEQADV 1F9X HIS A 239 UNP P98170 CLONING ARTIFACT
SEQADV 1F9X MET A 240 UNP P98170 CLONING ARTIFACT
SEQRES 1 A 120 GLY SER HIS MET SER ASP ALA VAL SER SER ASP ARG ASN
SEQRES 2 A 120 PHE PRO ASN SER THR ASN LEU PRO ARG ASN PRO SER MET
SEQRES 3 A 120 ALA ASP TYR GLU ALA ARG ILE PHE THR PHE GLY THR TRP
SEQRES 4 A 120 ILE TYR SER VAL ASN LYS GLU GLN LEU ALA ARG ALA GLY
SEQRES 5 A 120 PHE TYR ALA LEU GLY GLU GLY ASP LYS VAL LYS CYS PHE
SEQRES 6 A 120 HIS CYS GLY GLY GLY LEU THR ASP TRP LYS PRO SER GLU
SEQRES 7 A 120 ASP PRO TRP GLU GLN HIS ALA LYS TRP TYR PRO GLY CYS
SEQRES 8 A 120 LYS TYR LEU LEU GLU GLN LYS GLY GLN GLU TYR ILE ASN
SEQRES 9 A 120 ASN ILE HIS LEU THR HIS SER LEU GLU GLU CYS LEU VAL
SEQRES 10 A 120 ARG THR THR
HET ZN A 999 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ALA A 243 ASP A 247 5 5
HELIX 2 2 ASP A 264 GLY A 273 1 10
HELIX 3 3 VAL A 279 GLY A 288 1 10
HELIX 4 4 ASP A 315 TYR A 324 1 10
HELIX 5 5 CYS A 327 GLY A 335 1 9
HELIX 6 6 LYS A 334 LEU A 344 1 11
SHEET 1 A 3 PHE A 289 TYR A 290 0
SHEET 2 A 3 LYS A 299 CYS A 300 -1 O LYS A 299 N TYR A 290
SHEET 3 A 3 GLY A 305 GLY A 306 -1 O GLY A 305 N CYS A 300
LINK SG CYS A 300 ZN ZN A 999 1555 1555 2.11
LINK SG CYS A 303 ZN ZN A 999 1555 1555 2.11
LINK NE2 HIS A 320 ZN ZN A 999 1555 1555 2.20
LINK SG CYS A 327 ZN ZN A 999 1555 1555 2.11
SITE 1 AC1 4 CYS A 300 CYS A 303 HIS A 320 CYS A 327
CRYST1 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 - 23 20 Bytes