HEADER OXIDOREDUCTASE 10-OCT-08 2W0X
TITLE FACTOR INHIBITING HIF-1 ALPHA WITH PYRIDINE 2,4 DICARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYPOXIA-INDUCIBLE FACTOR ASPARAGINE HYDROXYLASE, FACTOR
COMPND 5 INHIBITING HIF-1, FIH-1;
COMPND 6 EC: 1.14.11.16;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYDROXYLASE, DIOXYGENASE, TRANSCRIPTION, OXIDOREDUCTASE,
KEYWDS 2 TRANSCRIPTION ACTIVATOR/INHIBITOR, HYPOXIA
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CONEJO-GARCIA,B.M.R.LIENARD,I.J.CLIFTON,M.A.MCDONOUGH,C.J.SCHOFIELD
REVDAT 6 13-DEC-23 2W0X 1 REMARK LINK
REVDAT 5 21-FEB-18 2W0X 1 AUTHOR JRNL
REVDAT 4 05-JUL-17 2W0X 1 REMARK
REVDAT 3 29-SEP-10 2W0X 1 JRNL
REVDAT 2 22-SEP-10 2W0X 1 KEYWDS JRNL REMARK
REVDAT 1 24-NOV-09 2W0X 0
JRNL AUTH A.CONEJO-GARCIA,M.A.MCDONOUGH,C.LOENARZ,L.A.MCNEILL,
JRNL AUTH 2 K.S.HEWITSON,W.GE,B.M.LIENARD,C.J.SCHOFIELD,I.J.CLIFTON
JRNL TITL STRUCTURAL BASIS FOR BINDING OF CYCLIC 2-OXOGLUTARATE
JRNL TITL 2 ANALOGUES TO FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR.
JRNL REF BIOORG. MED. CHEM. LETT. V. 20 6125 2010
JRNL REFN ESSN 1464-3405
JRNL PMID 20822901
JRNL DOI 10.1016/J.BMCL.2010.08.032
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,
REMARK 1 AUTH 2 I.SCHLEMMINGER,C.W.PUGH,P.J.RATCLIFFE,C.J.SCHOFIELD
REMARK 1 TITL STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR
REMARK 1 TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF HIF-1
REMARK 1 TITL 3 ALPHA.
REMARK 1 REF J.BIOL.CHEM. V. 278 1802 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12446723
REMARK 1 DOI 10.1074/JBC.C200644200
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 30050
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.6776 - 4.7234 0.99 2989 149 0.1832 0.2261
REMARK 3 2 4.7234 - 3.7501 0.99 2800 168 0.1643 0.2336
REMARK 3 3 3.7501 - 3.2764 0.99 2757 143 0.2025 0.2377
REMARK 3 4 3.2764 - 2.9769 0.97 2727 127 0.2299 0.2496
REMARK 3 5 2.9769 - 2.7636 0.95 2647 129 0.2370 0.2709
REMARK 3 6 2.7636 - 2.6007 0.94 2604 124 0.2338 0.3043
REMARK 3 7 2.6007 - 2.4705 0.93 2530 148 0.2437 0.3075
REMARK 3 8 2.4705 - 2.3630 0.93 2537 147 0.2356 0.3424
REMARK 3 9 2.3630 - 2.2720 0.88 2387 132 0.2424 0.2785
REMARK 3 10 2.2720 - 2.1936 0.87 2364 137 0.2649 0.3152
REMARK 3 11 2.1936 - 2.1250 0.80 2192 112 0.3138 0.3763
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 52.63
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.89360
REMARK 3 B22 (A**2) : -3.89360
REMARK 3 B33 (A**2) : 7.78710
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.000 2919
REMARK 3 ANGLE : 1.000 3965
REMARK 3 CHIRALITY : 0.070 395
REMARK 3 PLANARITY : 0.000 525
REMARK 3 DIHEDRAL : 19.000 1076
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2W0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1290037161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4880
REMARK 200 MONOCHROMATOR : SI (1 1 1)
REMARK 200 OPTICS : RH COATED MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32255
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 61.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1H2N
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 0.1M HEPES PH
REMARK 280 7.5, 5% PEG400, 1MM FESO4, 2MM SUBSTRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 73.61850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.23550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.23550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.80925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.23550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.23550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.42775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.23550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.23550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.80925
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.23550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.23550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 110.42775
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 73.61850
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.9 KCAL/MOL
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 86.47100
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 86.47100
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 73.61850
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 96 OG
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 PHE A 100 74.56 -109.57
REMARK 500 ASN A 151 -154.57 -110.76
REMARK 500 GLU A 202 41.92 -89.91
REMARK 500 ILE A 210 -58.90 -126.46
REMARK 500 ASP A 237 134.93 -38.95
REMARK 500 ARG A 238 -12.60 78.20
REMARK 500 TYR A 276 -13.64 79.82
REMARK 500 PRO A 303 160.94 -49.90
REMARK 500 LYS A 304 -88.43 -9.05
REMARK 500 ASN A 332 119.82 -160.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PYRIDINE-2,4-DICARBOXYLIC ACID(PD2): PUBCHEM CID 10365
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 FE2 A1350 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199 NE2
REMARK 620 2 ASP A 201 OD2 105.1
REMARK 620 3 HIS A 279 NE2 84.0 83.3
REMARK 620 4 PD2 A1351 N1 89.9 164.3 103.1
REMARK 620 5 PD2 A1351 O21 173.2 81.0 93.9 84.2
REMARK 620 6 GOL A1355 O3 82.3 86.7 160.4 90.9 101.2
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PD2 A 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1355
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WA4 RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA WITH N,3- DIHYDROXYBENZAMIDE
REMARK 900 RELATED ID: 1MZE RELATED DB: PDB
REMARK 900 HUMAN FACTOR INHIBITING HIF (FIH1)
REMARK 900 RELATED ID: 2CGN RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA WITH SUCCINATE
REMARK 900 RELATED ID: 1MZF RELATED DB: PDB
REMARK 900 HUMAN FACTOR INHIBITING HIF (FIH1) IN COMPLEX WITH 2-OXOGLUTARATE
REMARK 900 RELATED ID: 2WA3 RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA WITH 2-(3- HYDROXYPHENYL)-2-OXOACETIC
REMARK 900 ACID
REMARK 900 RELATED ID: 1H2N RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 1YCI RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH N-(CARBOXYCARBONYL)-D-
REMARK 900 PHENYLALANINE
REMARK 900 RELATED ID: 1H2K RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 2CGO RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA WITH FUMARATE
REMARK 900 RELATED ID: 1IZ3 RELATED DB: PDB
REMARK 900 DIMERIC STRUCTURE OF FIH (FACTOR INHIBITING HIF)
REMARK 900 RELATED ID: 1H2L RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 1H2M RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT
REMARK 900 PEPTIDE
DBREF 2W0X A 1 349 UNP Q9NWT6 HIF1N_HUMAN 1 349
SEQRES 1 A 349 MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER GLY SER
SEQRES 2 A 349 GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA
SEQRES 3 A 349 TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR
SEQRES 4 A 349 ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA
SEQRES 5 A 349 GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR
SEQRES 6 A 349 ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU
SEQRES 7 A 349 GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER
SEQRES 8 A 349 VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP
SEQRES 9 A 349 GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS PRO ARG
SEQRES 10 A 349 SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE VAL GLU
SEQRES 11 A 349 LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG
SEQRES 12 A 349 LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY ARG
SEQRES 13 A 349 LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP ASN TRP
SEQRES 14 A 349 ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU
SEQRES 15 A 349 THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY ASN VAL
SEQRES 16 A 349 THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA
SEQRES 17 A 349 GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO
SEQRES 18 A 349 ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS
SEQRES 19 A 349 PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO
SEQRES 20 A 349 ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY
SEQRES 21 A 349 TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE
SEQRES 22 A 349 PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN
SEQRES 23 A 349 GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY
SEQRES 24 A 349 ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA
SEQRES 25 A 349 HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU LYS MET
SEQRES 26 A 349 LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO
SEQRES 27 A 349 LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN
HET FE2 A1350 1
HET PD2 A1351 12
HET SO4 A1352 5
HET SO4 A1353 5
HET SO4 A1354 5
HET GOL A1355 6
HETNAM FE2 FE (II) ION
HETNAM PD2 PYRIDINE-2,4-DICARBOXYLIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 FE2 FE 2+
FORMUL 3 PD2 C7 H5 N O4
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *200(H2 O)
HELIX 1 1 GLU A 19 LEU A 23 5 5
HELIX 2 2 ASP A 28 LEU A 32 5 5
HELIX 3 3 ASP A 49 ASN A 58 1 10
HELIX 4 4 VAL A 70 TRP A 76 5 7
HELIX 5 5 ASP A 77 ILE A 85 1 9
HELIX 6 6 ASP A 104 PHE A 111 5 8
HELIX 7 7 LYS A 124 ARG A 138 1 15
HELIX 8 8 GLY A 155 GLY A 164 1 10
HELIX 9 9 ASN A 166 ARG A 177 1 12
HELIX 10 10 PRO A 220 ASP A 222 5 3
HELIX 11 11 GLN A 223 TYR A 228 1 6
HELIX 12 12 PHE A 252 VAL A 258 5 7
HELIX 13 13 LYS A 311 GLY A 331 1 21
HELIX 14 14 ASN A 332 GLN A 334 5 3
HELIX 15 15 GLU A 335 LYS A 345 1 11
SHEET 1 AA 5 THR A 39 PRO A 41 0
SHEET 2 AA 5 GLY A 260 VAL A 265 1 O GLY A 260 N ARG A 40
SHEET 3 AA 5 LYS A 214 PHE A 219 -1 O LYS A 214 N VAL A 265
SHEET 4 AA 5 TRP A 278 SER A 283 -1 O TRP A 278 N PHE A 219
SHEET 5 AA 5 VAL A 195 HIS A 199 -1 O THR A 196 N ILE A 281
SHEET 1 AB 6 ARG A 44 LEU A 45 0
SHEET 2 AB 6 VAL A 62 LEU A 64 1 O VAL A 63 N LEU A 45
SHEET 3 AB 6 VAL A 270 ILE A 273 -1 O VAL A 270 N LEU A 64
SHEET 4 AB 6 GLN A 204 LYS A 211 -1 O ASN A 205 N ILE A 273
SHEET 5 AB 6 THR A 290 TYR A 297 -1 O ILE A 291 N ILE A 210
SHEET 6 AB 6 LEU A 182 SER A 184 -1 N THR A 183 O TRP A 296
SHEET 1 AC 9 ARG A 44 LEU A 45 0
SHEET 2 AC 9 VAL A 62 LEU A 64 1 O VAL A 63 N LEU A 45
SHEET 3 AC 9 VAL A 270 ILE A 273 -1 O VAL A 270 N LEU A 64
SHEET 4 AC 9 GLN A 204 LYS A 211 -1 O ASN A 205 N ILE A 273
SHEET 5 AC 9 THR A 290 TYR A 297 -1 O ILE A 291 N ILE A 210
SHEET 6 AC 9 LEU A 186 GLY A 190 -1 O LEU A 186 N ASN A 294
SHEET 7 AC 9 ARG A 143 THR A 149 -1 O LEU A 146 N ILE A 189
SHEET 8 AC 9 PHE A 90 ALA A 95 -1 O SER A 91 N GLN A 147
SHEET 9 AC 9 ASN A 119 MET A 123 -1 O ASN A 119 N SER A 94
LINK NE2 HIS A 199 FE FE2 A1350 1555 1555 2.28
LINK OD2 ASP A 201 FE FE2 A1350 1555 1555 2.12
LINK NE2 HIS A 279 FE FE2 A1350 1555 1555 2.35
LINK FE FE2 A1350 N1 PD2 A1351 1555 1555 2.11
LINK FE FE2 A1350 O21 PD2 A1351 1555 1555 2.18
LINK FE FE2 A1350 O3 GOL A1355 1555 1555 2.33
CISPEP 1 TYR A 308 PRO A 309 0 3.50
SITE 1 AC1 5 HIS A 199 ASP A 201 HIS A 279 PD2 A1351
SITE 2 AC1 5 GOL A1355
SITE 1 AC2 14 TYR A 145 THR A 196 HIS A 199 ASP A 201
SITE 2 AC2 14 ASN A 205 PHE A 207 LYS A 214 HIS A 279
SITE 3 AC2 14 ILE A 281 ASN A 294 TRP A 296 FE2 A1350
SITE 4 AC2 14 GOL A1355 HOH A2111
SITE 1 AC3 4 ARG A 138 GLY A 140 GLU A 141 GLU A 142
SITE 1 AC4 5 ARG A 143 GLU A 192 GLY A 193 LEU A 285
SITE 2 AC4 5 ASN A 286
SITE 1 AC5 5 LYS A 107 GLU A 202 ARG A 320 HOH A2068
SITE 2 AC5 5 HOH A2199
SITE 1 AC6 8 TYR A 102 LEU A 186 HIS A 199 ASP A 201
SITE 2 AC6 8 TRP A 296 FE2 A1350 PD2 A1351 HOH A2200
CRYST1 86.471 86.471 147.237 90.00 90.00 90.00 P 41 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 0.011565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011565 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006792 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
