HEADER GENE REGULATION 09-MAY-02 1LQB
TITLE CRYSTAL STRUCTURE OF A HYDROXYLATED HIF-1 ALPHA PEPTIDE BOUND TO THE
TITLE 2 PVHL/ELONGIN-C/ELONGIN-B COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGIN B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSCRIPTION ELONGATION FACTOR B, POLYPEPTIDE 2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ELONGIN C;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 17-112;
COMPND 10 SYNONYM: TRANSCRIPTION ELONGATION FACTOR B (SIII), POLYPEPTIDE 1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPRESSOR;
COMPND 14 CHAIN: C;
COMPND 15 FRAGMENT: RESIDUES 52-213;
COMPND 16 SYNONYM: PVHL, G7 PROTEIN;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA;
COMPND 20 CHAIN: D;
COMPND 21 FRAGMENT: RESIDUES 549-582;
COMPND 22 SYNONYM: HIF-1 ALPHA;
COMPND 23 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX-4T3;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PBB75;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 23 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 24 EXPRESSION_SYSTEM_VECTOR: PGEX-4T3;
SOURCE 25 MOL_ID: 4;
SOURCE 26 SYNTHETIC: YES;
SOURCE 27 OTHER_DETAILS: THE PEPTIDE WAS SYNTHESIZED WITH A BIOTIN TAG AT THE
SOURCE 28 N-TERMINUS AND WITH P564 AS A 4(R)HYDROXYPROLINE. THE SEQUENCE OF
SOURCE 29 THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS PROTEIN-PEPTIDE COMPLEX, TUMOR SUPPRESSOR, CANCER, PROTEOSOMAL
KEYWDS 2 DEGRADATION, UBIQUITIN, PROLYL HYDROXYLATION, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR W.C.HON,M.I.WILSON,K.HARLOS,T.D.CLARIDGE,C.J.SCHOFIELD,C.W.PUGH,
AUTHOR 2 P.H.MAXWELL,P.J.RATCLIFFE,D.I.STUART,E.Y.JONES
REVDAT 3 16-AUG-23 1LQB 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1LQB 1 VERSN
REVDAT 1 03-JUL-02 1LQB 0
JRNL AUTH W.C.HON,M.I.WILSON,K.HARLOS,T.D.CLARIDGE,C.J.SCHOFIELD,
JRNL AUTH 2 C.W.PUGH,P.H.MAXWELL,P.J.RATCLIFFE,D.I.STUART,E.Y.JONES
JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF HYDROXYPROLINE IN
JRNL TITL 2 HIF-1 ALPHA BY PVHL.
JRNL REF NATURE V. 417 975 2002
JRNL REFN ISSN 0028-0836
JRNL PMID 12050673
JRNL DOI 10.1038/NATURE00767
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 76.2
REMARK 3 NUMBER OF REFLECTIONS : 23019
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1108
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 42.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1978
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 102
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.035
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2905
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.910
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 38.51
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_HYP.PAR
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : WATER.TOP
REMARK 3 TOPOLOGY FILE 2 : PROTEIN_HYP.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LQB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016181.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : DIAMOND [111] AND GE CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24245
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.0
REMARK 200 DATA REDUNDANCY : 18.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 30.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: 1VCB.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, PEG2000 MONOMETHYLESTER,
REMARK 280 AMMONIUM SULFATE, PH 7.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 121.69000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 29.47000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.47000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 182.53500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.47000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.47000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 60.84500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.47000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.47000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 182.53500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.47000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.47000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 60.84500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 121.69000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 117.88000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 117.88000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 121.69000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 105
REMARK 465 GLN A 106
REMARK 465 ASP A 107
REMARK 465 SER A 108
REMARK 465 GLY A 109
REMARK 465 SER A 110
REMARK 465 SER A 111
REMARK 465 ALA A 112
REMARK 465 ASN A 113
REMARK 465 GLU A 114
REMARK 465 GLN A 115
REMARK 465 ALA A 116
REMARK 465 VAL A 117
REMARK 465 GLN A 118
REMARK 465 GLY B 50
REMARK 465 GLN B 51
REMARK 465 PHE B 52
REMARK 465 ALA B 53
REMARK 465 GLU B 54
REMARK 465 ASN B 55
REMARK 465 GLU B 56
REMARK 465 THR B 57
REMARK 465 GLY C 52
REMARK 465 SER C 53
REMARK 465 MET C 54
REMARK 465 GLU C 55
REMARK 465 ALA C 56
REMARK 465 GLY C 57
REMARK 465 ARG C 58
REMARK 465 PRO C 59
REMARK 465 ARG C 60
REMARK 465 MET C 211
REMARK 465 GLY C 212
REMARK 465 ASP C 213
REMARK 465 PRO D 549
REMARK 465 PHE D 550
REMARK 465 SER D 551
REMARK 465 THR D 552
REMARK 465 GLN D 553
REMARK 465 ASP D 554
REMARK 465 THR D 555
REMARK 465 ASP D 556
REMARK 465 LEU D 557
REMARK 465 ASP D 558
REMARK 465 LEU D 559
REMARK 465 ASP D 578
REMARK 465 GLN D 579
REMARK 465 LEU D 580
REMARK 465 SER D 581
REMARK 465 PRO D 582
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 HIS A 10 -118.21 54.44
REMARK 500 ASP A 47 -119.11 66.30
REMARK 500 ASP A 83 18.17 -141.20
REMARK 500 ARG C 79 46.76 -97.03
REMARK 500 ASN C 90 -164.15 -69.36
REMARK 500 SER C 111 -162.81 -115.72
REMARK 500 ARG C 176 1.53 -69.95
REMARK 500 GLN C 209 2.63 -178.23
REMARK 500 MET D 568 66.98 73.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801
DBREF 1LQB A 1 118 UNP Q15370 ELOB_HUMAN 1 118
DBREF 1LQB B 17 112 UNP Q15369 ELOC_HUMAN 17 112
DBREF 1LQB C 52 213 UNP P40337 VHL_HUMAN 52 213
DBREF 1LQB D 549 582 UNP Q16665 HIF1A_HUMAN 549 582
SEQADV 1LQB HYP D 564 UNP Q16665 PRO 564 MODIFIED RESIDUE
SEQRES 1 A 118 MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR
SEQRES 2 A 118 ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU
SEQRES 3 A 118 LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO
SEQRES 4 A 118 ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP
SEQRES 5 A 118 ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN
SEQRES 6 A 118 THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA
SEQRES 7 A 118 PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU
SEQRES 8 A 118 PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS
SEQRES 9 A 118 PRO GLN ASP SER GLY SER SER ALA ASN GLU GLN ALA VAL
SEQRES 10 A 118 GLN
SEQRES 1 B 96 MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU PHE
SEQRES 2 B 96 ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR ILE
SEQRES 3 B 96 LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU ASN
SEQRES 4 B 96 GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER HIS
SEQRES 5 B 96 VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS VAL
SEQRES 6 B 96 ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE PRO
SEQRES 7 B 96 ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA ALA
SEQRES 8 B 96 ASN PHE LEU ASP CYS
SEQRES 1 C 162 GLY SER MET GLU ALA GLY ARG PRO ARG PRO VAL LEU ARG
SEQRES 2 C 162 SER VAL ASN SER ARG GLU PRO SER GLN VAL ILE PHE CYS
SEQRES 3 C 162 ASN ARG SER PRO ARG VAL VAL LEU PRO VAL TRP LEU ASN
SEQRES 4 C 162 PHE ASP GLY GLU PRO GLN PRO TYR PRO THR LEU PRO PRO
SEQRES 5 C 162 GLY THR GLY ARG ARG ILE HIS SER TYR ARG GLY HIS LEU
SEQRES 6 C 162 TRP LEU PHE ARG ASP ALA GLY THR HIS ASP GLY LEU LEU
SEQRES 7 C 162 VAL ASN GLN THR GLU LEU PHE VAL PRO SER LEU ASN VAL
SEQRES 8 C 162 ASP GLY GLN PRO ILE PHE ALA ASN ILE THR LEU PRO VAL
SEQRES 9 C 162 TYR THR LEU LYS GLU ARG CYS LEU GLN VAL VAL ARG SER
SEQRES 10 C 162 LEU VAL LYS PRO GLU ASN TYR ARG ARG LEU ASP ILE VAL
SEQRES 11 C 162 ARG SER LEU TYR GLU ASP LEU GLU ASP HIS PRO ASN VAL
SEQRES 12 C 162 GLN LYS ASP LEU GLU ARG LEU THR GLN GLU ARG ILE ALA
SEQRES 13 C 162 HIS GLN ARG MET GLY ASP
SEQRES 1 D 34 PRO PHE SER THR GLN ASP THR ASP LEU ASP LEU GLU MET
SEQRES 2 D 34 LEU ALA HYP TYR ILE PRO MET ASP ASP ASP PHE GLN LEU
SEQRES 3 D 34 ARG SER PHE ASP GLN LEU SER PRO
MODRES 1LQB HYP D 564 PRO 4-HYDROXYPROLINE
HET HYP D 564 8
HET SO4 A 801 5
HETNAM HYP 4-HYDROXYPROLINE
HETNAM SO4 SULFATE ION
HETSYN HYP HYDROXYPROLINE
FORMUL 4 HYP C5 H9 N O3
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *84(H2 O)
HELIX 1 1 THR A 23 LYS A 36 1 14
HELIX 2 2 PRO A 38 ASP A 40 5 3
HELIX 3 3 PRO A 100 LYS A 104 5 5
HELIX 4 4 ARG B 33 LEU B 37 1 5
HELIX 5 5 SER B 39 LEU B 46 1 8
HELIX 6 6 PRO B 66 THR B 84 1 19
HELIX 7 7 ALA B 96 GLU B 98 5 3
HELIX 8 8 ILE B 99 ASP B 111 1 13
HELIX 9 9 THR C 157 VAL C 170 1 14
HELIX 10 10 LYS C 171 LEU C 178 5 8
HELIX 11 11 ARG C 182 ASP C 190 1 9
HELIX 12 12 ASN C 193 HIS C 208 1 16
SHEET 1 A 8 GLN A 49 LEU A 50 0
SHEET 2 A 8 GLN A 42 LYS A 46 -1 N LYS A 46 O GLN A 49
SHEET 3 A 8 ALA A 73 PHE A 79 -1 O GLY A 76 N TYR A 45
SHEET 4 A 8 ASP A 2 ARG A 9 1 N MET A 6 O VAL A 75
SHEET 5 A 8 THR A 12 LYS A 19 -1 O ILE A 14 N ILE A 7
SHEET 6 A 8 GLU B 28 LYS B 32 1 O ILE B 30 N THR A 13
SHEET 7 A 8 TYR B 18 ILE B 22 -1 N LEU B 21 O PHE B 29
SHEET 8 A 8 GLU B 59 ASN B 61 1 O VAL B 60 N LYS B 20
SHEET 1 B 5 LEU C 129 VAL C 130 0
SHEET 2 B 5 ILE C 147 THR C 152 -1 O THR C 152 N LEU C 129
SHEET 3 B 5 PRO C 71 ASN C 78 1 N CYS C 77 O ALA C 149
SHEET 4 B 5 THR C 105 TYR C 112 -1 O ILE C 109 N VAL C 74
SHEET 5 B 5 PHE D 572 GLN D 573 -1 O PHE D 572 N GLY C 106
SHEET 1 C 3 PRO C 95 PRO C 97 0
SHEET 2 C 3 VAL C 84 LEU C 89 -1 N TRP C 88 O GLN C 96
SHEET 3 C 3 LEU C 116 ASP C 121 -1 O LEU C 118 N VAL C 87
LINK C ALA D 563 N HYP D 564 1555 1555 1.34
LINK C HYP D 564 N TYR D 565 1555 1555 1.33
CISPEP 1 GLY B 48 PRO B 49 0 -0.13
SITE 1 AC1 2 ALA A 73 THR A 74
CRYST1 58.940 58.940 243.380 90.00 90.00 90.00 P 43 21 2 8
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 0.016966 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016966 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004109 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
