HEADER TRANSCRIPTION ACTIVATOR/INHIBITOR 12-AUG-02 1H2M
TITLE FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA
TITLE 2 FRAGMENT PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FACTOR INHIBITING HIF1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FIH1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA;
COMPND 8 CHAIN: S;
COMPND 9 FRAGMENT: C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES
COMPND 10 775-826;
COMPND 11 SYNONYM: HIF-1 ALPHA, ARNT INTERACTING PROTEIN, MEMBER OF PAS
COMPND 12 PROTEIN 1, MOP1, HIF1 ALPHA, HIF1A.;
COMPND 13 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(+);
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;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PGEX-GP-1
KEYWDS TRANSCRIPTION ACTIVATOR-INHIBITOR COMPLEX, FIH, HIF, DSBH,
KEYWDS 2 OXYGENASE, TRANSCRIPTION, HYPOXIA, 2- OXOGLUTARATE, ASPARAGINYL
KEYWDS 3 HYDROXYLASE, HYDROXYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,I.SCHLEMMINGER,J.F.SEIBEL,
AUTHOR 2 C.J.SCHOFIELD
REVDAT 5 13-JUL-11 1H2M 1 VERSN
REVDAT 4 21-JUL-09 1H2M 1 HETNAM
REVDAT 3 24-FEB-09 1H2M 1 VERSN
REVDAT 2 30-JAN-03 1H2M 1 JRNL
REVDAT 1 28-NOV-02 1H2M 0
JRNL AUTH J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,
JRNL AUTH 2 I.SCHLEMMINGER,C.PUGH,P.RATCLIFFE,C.J.SCHOFIELD
JRNL TITL STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR
JRNL TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF
JRNL TITL 3 HIF-1ALPHA
JRNL REF J.BIOL.CHEM. V. 278 1802 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12446723
JRNL DOI 10.1074/JBC.C200644200
REMARK 2
REMARK 2 RESOLUTION. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 18404
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 + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1516
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1267
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2859
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 99
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.68000
REMARK 3 B22 (A**2) : -0.68000
REMARK 3 B33 (A**2) : 1.35000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.334
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.233
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.825
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2957 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2546 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4022 ; 1.612 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5944 ; 0.832 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 350 ; 4.024 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 512 ;18.015 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 413 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3315 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 602 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 731 ; 0.232 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2492 ; 0.214 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 193 ; 0.173 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 6 ; 0.126 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.054 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 15 ; 0.194 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 54 ; 0.255 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.244 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.053 ; 0.500
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1767 ; 0.761 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2846 ; 1.421 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1190 ; 2.220 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1176 ; 3.678 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 15 A 349
REMARK 3 RESIDUE RANGE : S 795 S 822
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5990 26.9200 28.6340
REMARK 3 T TENSOR
REMARK 3 T11: 0.1903 T22: 0.0302
REMARK 3 T33: 0.0452 T12: -0.0025
REMARK 3 T13: -0.0536 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 0.7638 L22: 2.2674
REMARK 3 L33: 1.0629 L12: 0.7977
REMARK 3 L13: 0.4200 L23: 1.0769
REMARK 3 S TENSOR
REMARK 3 S11: 0.0306 S12: -0.1225 S13: -0.0490
REMARK 3 S21: 0.1656 S22: 0.0303 S23: 0.0478
REMARK 3 S31: 0.2046 S32: 0.0231 S33: -0.0609
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1H2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-02.
REMARK 100 THE PDBE ID CODE IS EBI-11173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20058
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 87.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULPHATE,
REMARK 280 4% PEG400, 0.1M HEPES PH7.5, 11MG/ML PROTEIN WITH
REMARK 280 1MM ZN(II), 2.5MM NOG AND 2.5MM PEPTIDE
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 74.13000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.12450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.12450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.06500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.12450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.12450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.19500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.12450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.12450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.06500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.12450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.12450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.19500
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 74.13000
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 300
REMARK 300 DETAILS:THE PROTEIN IS A DIMERIC FORMED BY CHAIN
REMARK 300 A.A HETERODIMERIC ASSOCIATION OF CHAIN A WITH
REMARK 300 CHAIN SPRODUCES A TETRAMER.THE BURIED SURFACE AREA
REMARK 300 SHOWN BELOW IS AN AVERAGECALCULATED FOR THE
REMARK 300 HETEROTETRAMER AND DOES NOTCORRESPOND TO THE BURIED
REMARK 300 SURFACE AREA FOR THEHOMODIMER OF CHAIN A
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S
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 86.24900
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 86.24900
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 74.13000
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 465 ALA A 8
REMARK 465 VAL A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 GLY A 12
REMARK 465 SER A 13
REMARK 465 GLY A 14
REMARK 465 LYS A 304
REMARK 465 ARG A 305
REMARK 465 ILE A 306
REMARK 465 PRO S 775
REMARK 465 SER S 776
REMARK 465 ASP S 777
REMARK 465 LEU S 778
REMARK 465 ALA S 779
REMARK 465 CYS S 780
REMARK 465 ARG S 781
REMARK 465 LEU S 782
REMARK 465 LEU S 783
REMARK 465 GLY S 784
REMARK 465 GLN S 785
REMARK 465 SER S 786
REMARK 465 MET S 787
REMARK 465 ASP S 788
REMARK 465 GLU S 789
REMARK 465 SER S 790
REMARK 465 GLY S 791
REMARK 465 LEU S 792
REMARK 465 PRO S 793
REMARK 465 GLN S 794
REMARK 465 GLN S 807
REMARK 465 GLY S 808
REMARK 465 SER S 809
REMARK 465 ARG S 810
REMARK 465 ASN S 811
REMARK 465 LEU S 812
REMARK 465 ASP S 823
REMARK 465 GLN S 824
REMARK 465 VAL S 825
REMARK 465 ASN S 826
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 GLU A 15 CG CD OE1 OE2
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 ASN A 87 CG OD1 ND2
REMARK 470 LYS A 106 CD CE NZ
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 ARG A 117 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 133 CG CD OE1 NE2
REMARK 470 GLN A 136 CG CD OE1 NE2
REMARK 470 GLN A 137 CG CD OE1 NE2
REMARK 470 ARG A 156 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 157 CD CE NZ
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O ALA A 300 OH TYR S 798 2.09
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 ARG A 347 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 347 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
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 ILE A 210 -50.75 -121.45
REMARK 500 ASP A 237 126.92 -37.49
REMARK 500 ARG A 238 -11.04 86.83
REMARK 500 ASN A 246 71.86 -152.50
REMARK 500 TYR A 276 -8.35 80.15
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 A1350 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199 NE2
REMARK 620 2 ASP A 201 OD2 103.4
REMARK 620 3 HIS A 279 NE2 84.2 88.5
REMARK 620 4 OGA A1351 O2 169.0 87.2 99.0
REMARK 620 5 OGA A1351 O2' 86.3 169.1 97.3 82.8
REMARK 620 N 1 2 3 4
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 ZN A1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA A1351
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D7G RELATED DB: PDB
REMARK 900 A MODEL FOR THE COMPLEX BETWEEN THE
REMARK 900 HYPOXIA-INDUCIBLE FACTOR-1 (HIF-1) AND ITS
REMARK 900 CONSENSUS DEOXYRIBONUCLEIC ACID SEQUENCE
REMARK 900 RELATED ID: 1H2K RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX
REMARK 900 WITH HIF-1 ALPHA FRAGMENT PEPTIDE
REMARK 900 RELATED ID: 1H2L RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX
REMARK 900 WITH HIF-1 ALPHA FRAGMENT PEPTIDE
REMARK 900 RELATED ID: 1H2N RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX
REMARK 900 WITH HIF-1 ALPHA FRAGMENT PEPTIDE
REMARK 900 RELATED ID: 1L8C RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR HIF-1ALPHA/CBP
REMARK 900 RECOGNITION IN THECELLULAR HYPOXIC RESPONSE
REMARK 900 RELATED ID: 1LM8 RELATED DB: PDB
REMARK 900 STRUCTURE OF A HIF-1A-PVHL-ELONGINB-
REMARK 900 ELONGINC COMPLEX
REMARK 900 RELATED ID: 1LQB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HYDROXYLATED HIF-1
REMARK 900 ALPHA PEPTIDEBOUND TO THE PVHL/ELONGIN-C/
REMARK 900 ELONGIN-B COMPLEX
DBREF 1H2M A 1 349 UNP Q969Q7 Q969Q7 1 349
DBREF 1H2M S 775 826 UNP Q16665 HIFA_HUMAN 775 826
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
SEQRES 1 S 52 PRO SER ASP LEU ALA CYS ARG LEU LEU GLY GLN SER MET
SEQRES 2 S 52 ASP GLU SER GLY LEU PRO GLN LEU THR SER TYR ASP CYS
SEQRES 3 S 52 GLU VAL ASN ALA PRO ILE GLN GLY SER ARG ASN LEU LEU
SEQRES 4 S 52 GLN GLY GLU GLU LEU LEU ARG ALA LEU ASP GLN VAL ASN
HET ZN A1350 1
HET SO4 A1352 5
HET SO4 A1353 5
HET OGA A1351 10
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM OGA N-OXALYLGLYCINE
FORMUL 3 ZN ZN 2+
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 OGA C4 H5 N O5
FORMUL 7 HOH *99(H2 O)
HELIX 1 1 ASP A 28 LEU A 32 5 5
HELIX 2 2 ASP A 49 ASN A 58 1 10
HELIX 3 3 VAL A 70 TRP A 76 5 7
HELIX 4 4 ASP A 77 ILE A 85 1 9
HELIX 5 5 ASP A 104 GLN A 112 5 9
HELIX 6 6 LYS A 124 ARG A 138 1 15
HELIX 7 7 GLY A 155 GLY A 164 1 10
HELIX 8 8 ASN A 166 ARG A 177 1 12
HELIX 9 9 PRO A 220 ASP A 222 5 3
HELIX 10 10 GLN A 223 TYR A 228 1 6
HELIX 11 11 PHE A 252 VAL A 258 5 7
HELIX 12 12 LYS A 311 GLY A 331 1 21
HELIX 13 13 ASN A 332 GLN A 334 5 3
HELIX 14 14 GLU A 335 LYS A 345 1 11
HELIX 15 15 GLN S 814 LEU S 822 1 9
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 203 LYS A 211 -1 O ASN A 205 N ILE A 273
SHEET 5 AB 6 THR A 290 LYS A 298 -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 203 LYS A 211 -1 O ASN A 205 N ILE A 273
SHEET 5 AC 9 THR A 290 LYS A 298 -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 SER A 118 MET A 123 -1 O ASN A 119 N SER A 94
LINK ZN ZN A1350 NE2 HIS A 199 1555 1555 2.04
LINK ZN ZN A1350 OD2 ASP A 201 1555 1555 2.05
LINK ZN ZN A1350 NE2 HIS A 279 1555 1555 1.99
LINK ZN ZN A1350 O2 OGA A1351 1555 1555 2.03
LINK ZN ZN A1350 O2' OGA A1351 1555 1555 2.09
CISPEP 1 TYR A 308 PRO A 309 0 1.05
SITE 1 AC1 4 HIS A 199 ASP A 201 HIS A 279 OGA A1351
SITE 1 AC2 4 ARG A 138 GLY A 140 GLU A 141 GLU A 142
SITE 1 AC3 5 ARG A 143 GLU A 192 GLY A 193 LEU A 285
SITE 2 AC3 5 ASN A 286
SITE 1 AC4 14 TYR A 145 LEU A 188 THR A 196 HIS A 199
SITE 2 AC4 14 ASP A 201 ASN A 205 PHE A 207 LYS A 214
SITE 3 AC4 14 HIS A 279 ILE A 281 ASN A 294 TRP A 296
SITE 4 AC4 14 ZN A1350 HOH A2047
CRYST1 86.249 86.249 148.260 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 0.011594 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
