Header list of 1qbh.pdb file
Complete list - r 2 2 Bytes
HEADER APOPTOSIS 20-APR-99 1QBH
TITLE SOLUTION STRUCTURE OF A BACULOVIRAL INHIBITOR OF APOPTOSIS (IAP)
TITLE 2 REPEAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INHIBITOR OF APOPTOSIS PROTEIN (2MIHB/C-IAP-1);
COMPND 3 CHAIN: A;
COMPND 4 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
KEYWDS INHIBITOR OF APOPTOSIS (IAP), BACULOVIRAL IAP REPEAT (BIR), ZINC
KEYWDS 2 BINDING DOMAIN, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.G.HINDS,R.S.NORTON,D.L.VAUX,C.L.DAY
REVDAT 3 02-MAR-22 1QBH 1 REMARK LINK
REVDAT 2 24-FEB-09 1QBH 1 VERSN
REVDAT 1 20-OCT-99 1QBH 0
JRNL AUTH M.G.HINDS,R.S.NORTON,D.L.VAUX,C.L.DAY
JRNL TITL SOLUTION STRUCTURE OF A BACULOVIRAL INHIBITOR OF APOPTOSIS
JRNL TITL 2 (IAP) REPEAT.
JRNL REF NAT.STRUCT.BIOL. V. 6 648 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10404221
JRNL DOI 10.1038/10701
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER AG (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QBH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000009047.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 35
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : ROOM
REMARK 210 SAMPLE CONTENTS : 1MM BIR3 U-15N, 13C; 20 MM
REMARK 210 SODIUM PHOSPHATE PH 6.7, 75 MM
REMARK 210 SODIUM CHLORIDE AND 0.04% SODIUM
REMARK 210 AZIDE; 1MM BIR3 U-15N; 20 MM
REMARK 210 SODIUM PHOSPHATE PH 6.7, 75 MM
REMARK 210 SODIUM CHLORIDE AND 0.04% SODIUM
REMARK 210 AZIDE; 1MM BIR3; 20 MM SODIUM
REMARK 210 PHOSPHATE PH 6.7, 75 MM SODIUM
REMARK 210 CHLORIDE AND 0.04% SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS DISTANCE
REMARK 210 GEOMETRY SIMULATED ANNEALING
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON- BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: 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 1 PHE A 276 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 PHE A 276 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 TYR A 296 CB - CG - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 1 TYR A 296 CB - CG - CD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 1 TYR A 297 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TYR A 297 CB - CG - CD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 CYS A 306 CB - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 CYS A 309 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 ARG A 314 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 HIS A 326 CB - CG - CD2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 1 HIS A 326 CB - CG - ND1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 1 PHE A 330 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 1 PHE A 330 CB - CG - CD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 1 CYS A 333 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 1 PHE A 335 CB - CG - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 PHE A 335 CB - CG - CD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 PHE A 344 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 PHE A 344 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 TYR A 352 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 TYR A 352 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 PHE A 276 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 PHE A 276 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 2 TRP A 279 CA - CB - CG ANGL. DEV. = 11.4 DEGREES
REMARK 500 2 VAL A 283 CA - CB - CG1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 2 TYR A 296 CB - CG - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 2 TYR A 296 CB - CG - CD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 2 TYR A 297 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TYR A 297 CB - CG - CD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 2 CYS A 306 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 2 CYS A 309 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 HIS A 326 CB - CG - CD2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 2 HIS A 326 CB - CG - ND1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 2 ALA A 327 CB - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 2 PHE A 330 CB - CG - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 2 PHE A 330 CB - CG - CD1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 2 PHE A 335 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 2 PHE A 335 CB - CG - CD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 2 PHE A 344 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 2 PHE A 344 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 TYR A 352 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 TYR A 352 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 THR A 362 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 3 PHE A 276 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 GLN A 286 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 3 TYR A 296 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 3 TYR A 296 CB - CG - CD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 3 TYR A 297 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 3 TYR A 297 CB - CG - CD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 CYS A 306 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 3 CYS A 309 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 346 ANGLE DEVIATIONS.
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 MET A 266 26.14 -140.80
REMARK 500 1 HIS A 269 -45.58 61.37
REMARK 500 1 ALA A 270 -24.08 178.25
REMARK 500 1 MET A 277 -114.28 -64.92
REMARK 500 1 PRO A 280 -88.60 -92.58
REMARK 500 1 SER A 282 151.82 166.83
REMARK 500 1 VAL A 285 -122.35 -86.98
REMARK 500 1 TYR A 296 99.99 52.89
REMARK 500 1 TYR A 297 -43.14 72.80
REMARK 500 1 ASN A 301 -102.90 68.52
REMARK 500 1 VAL A 304 90.14 -22.77
REMARK 500 1 CYS A 306 -179.88 86.51
REMARK 500 1 CYS A 315 3.04 -156.23
REMARK 500 1 TRP A 316 103.48 1.80
REMARK 500 1 GLU A 317 -104.90 -81.94
REMARK 500 1 HIS A 326 57.45 -91.33
REMARK 500 1 ALA A 327 14.04 -168.21
REMARK 500 1 CYS A 333 89.30 -161.19
REMARK 500 1 ARG A 338 -81.84 -83.03
REMARK 500 1 GLU A 343 -50.56 -142.06
REMARK 500 1 PHE A 344 -71.63 -50.65
REMARK 500 1 GLN A 358 -97.57 -93.69
REMARK 500 1 LEU A 360 -84.09 -162.68
REMARK 500 2 HIS A 265 71.85 54.37
REMARK 500 2 HIS A 269 -46.67 61.49
REMARK 500 2 ALA A 270 -25.71 174.84
REMARK 500 2 MET A 277 -107.48 -60.60
REMARK 500 2 TRP A 279 -50.80 -123.13
REMARK 500 2 SER A 281 8.83 -157.66
REMARK 500 2 SER A 282 157.14 169.81
REMARK 500 2 PRO A 284 31.18 -81.72
REMARK 500 2 VAL A 285 -129.66 -89.91
REMARK 500 2 TYR A 296 106.36 57.07
REMARK 500 2 TYR A 297 -42.18 70.71
REMARK 500 2 ARG A 300 -138.73 -169.42
REMARK 500 2 ASN A 301 -100.69 -81.70
REMARK 500 2 VAL A 304 98.89 -40.60
REMARK 500 2 LYS A 305 -67.14 -94.97
REMARK 500 2 CYS A 306 179.96 161.70
REMARK 500 2 PHE A 307 -71.73 -93.36
REMARK 500 2 CYS A 309 115.56 -34.58
REMARK 500 2 GLU A 317 -121.83 -78.41
REMARK 500 2 ASP A 320 -156.92 -67.21
REMARK 500 2 ALA A 327 -46.65 -150.99
REMARK 500 2 ARG A 338 -76.95 -86.81
REMARK 500 2 GLU A 343 -44.97 -141.21
REMARK 500 2 PHE A 344 -72.51 -56.14
REMARK 500 2 HIS A 354 57.73 -141.30
REMARK 500 2 LEU A 360 -173.34 -171.98
REMARK 500 3 HIS A 265 89.85 65.75
REMARK 500
REMARK 500 THIS ENTRY HAS 545 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 1 ARG A 272 0.09 SIDE CHAIN
REMARK 500 1 ARG A 300 0.10 SIDE CHAIN
REMARK 500 1 ARG A 314 0.11 SIDE CHAIN
REMARK 500 1 ARG A 332 0.08 SIDE CHAIN
REMARK 500 2 ARG A 274 0.08 SIDE CHAIN
REMARK 500 2 ARG A 300 0.08 SIDE CHAIN
REMARK 500 2 ARG A 332 0.11 SIDE CHAIN
REMARK 500 2 ARG A 351 0.10 SIDE CHAIN
REMARK 500 3 ARG A 272 0.14 SIDE CHAIN
REMARK 500 4 ARG A 272 0.09 SIDE CHAIN
REMARK 500 4 ARG A 300 0.08 SIDE CHAIN
REMARK 500 5 ARG A 274 0.10 SIDE CHAIN
REMARK 500 5 ARG A 338 0.09 SIDE CHAIN
REMARK 500 6 ARG A 300 0.10 SIDE CHAIN
REMARK 500 6 ARG A 332 0.14 SIDE CHAIN
REMARK 500 7 ARG A 272 0.10 SIDE CHAIN
REMARK 500 7 ARG A 300 0.14 SIDE CHAIN
REMARK 500 8 ARG A 272 0.12 SIDE CHAIN
REMARK 500 8 ARG A 300 0.12 SIDE CHAIN
REMARK 500 9 ARG A 272 0.08 SIDE CHAIN
REMARK 500 9 ARG A 314 0.09 SIDE CHAIN
REMARK 500 10 ARG A 274 0.14 SIDE CHAIN
REMARK 500 10 ARG A 300 0.09 SIDE CHAIN
REMARK 500 11 ARG A 300 0.16 SIDE CHAIN
REMARK 500 12 ARG A 272 0.16 SIDE CHAIN
REMARK 500 13 ARG A 272 0.08 SIDE CHAIN
REMARK 500 13 ARG A 300 0.11 SIDE CHAIN
REMARK 500 13 ARG A 332 0.08 SIDE CHAIN
REMARK 500 13 ARG A 351 0.14 SIDE CHAIN
REMARK 500 15 ARG A 274 0.10 SIDE CHAIN
REMARK 500 15 ARG A 300 0.18 SIDE CHAIN
REMARK 500 16 ARG A 300 0.20 SIDE CHAIN
REMARK 500 16 ARG A 314 0.12 SIDE CHAIN
REMARK 500 16 ARG A 351 0.10 SIDE CHAIN
REMARK 500 17 ARG A 314 0.11 SIDE CHAIN
REMARK 500 19 ARG A 274 0.07 SIDE CHAIN
REMARK 500 19 ARG A 300 0.11 SIDE CHAIN
REMARK 500 19 ARG A 314 0.10 SIDE CHAIN
REMARK 500 19 ARG A 332 0.09 SIDE CHAIN
REMARK 500 20 ARG A 314 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 TRP A 279 10.16
REMARK 500 3 TRP A 279 10.27
REMARK 500 5 TRP A 279 10.17
REMARK 500 8 TRP A 279 10.55
REMARK 500 10 TRP A 279 11.08
REMARK 500 11 TRP A 279 11.11
REMARK 500 12 TRP A 279 10.81
REMARK 500 13 TRP A 279 11.34
REMARK 500 15 TRP A 279 11.58
REMARK 500 17 TRP A 279 10.27
REMARK 500 19 TRP A 279 10.32
REMARK 500 20 TRP A 279 10.56
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 364 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 306 SG
REMARK 620 2 CYS A 309 SG 111.5
REMARK 620 3 HIS A 326 NE2 113.5 109.7
REMARK 620 4 CYS A 333 SG 106.9 105.1 109.7
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 364
DBREF 1QBH A 266 363 UNP Q13490 BIRC2_HUMAN 266 363
SEQADV 1QBH GLY A 263 UNP Q13490 SEE REMARK 999
SEQADV 1QBH SER A 264 UNP Q13490 SEE REMARK 999
SEQADV 1QBH HIS A 265 UNP Q13490 SEE REMARK 999
SEQRES 1 A 101 GLY SER HIS MET GLN THR HIS ALA ALA ARG MET ARG THR
SEQRES 2 A 101 PHE MET TYR TRP PRO SER SER VAL PRO VAL GLN PRO GLU
SEQRES 3 A 101 GLN LEU ALA SER ALA GLY PHE TYR TYR VAL GLY ARG ASN
SEQRES 4 A 101 ASP ASP VAL LYS CYS PHE CYS CYS ASP GLY GLY LEU ARG
SEQRES 5 A 101 CYS TRP GLU SER GLY ASP ASP PRO TRP VAL GLU HIS ALA
SEQRES 6 A 101 LYS TRP PHE PRO ARG CYS GLU PHE LEU ILE ARG MET LYS
SEQRES 7 A 101 GLY GLN GLU PHE VAL ASP GLU ILE GLN GLY ARG TYR PRO
SEQRES 8 A 101 HIS LEU LEU GLU GLN LEU LEU SER THR SER
HET ZN A 364 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ALA A 270 THR A 275 1 6
HELIX 2 2 GLN A 286 GLY A 294 1 9
HELIX 3 3 ASP A 321 HIS A 326 1 6
HELIX 4 4 GLU A 343 TYR A 352 1 10
LINK SG CYS A 306 ZN ZN A 364 1555 1555 2.29
LINK SG CYS A 309 ZN ZN A 364 1555 1555 2.29
LINK NE2 HIS A 326 ZN ZN A 364 1555 1555 2.11
LINK SG CYS A 333 ZN ZN A 364 1555 1555 2.28
SITE 1 AC1 4 CYS A 306 CYS A 309 HIS A 326 CYS A 333
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
Complete list - r 2 2 Bytes