HEADER OXIDOREDUCTASE 02-FEB-09 2WA3
TITLE FACTOR INHIBITING HIF-1 ALPHA WITH 2-(3-HYDROXYPHENYL)-2-OXOACETIC
TITLE 2 ACID
CAVEAT 2WA3 GLU A 307 C-ALPHA IS PLANAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1-ALPHA INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FACTOR INHIBITING HIF1, HYPOXIA-INDUCIBLE FACTOR ASPARAGINE
COMPND 5 HYDROXYLASE, FACTOR 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 2WA3 1 REMARK LINK
REVDAT 5 21-FEB-18 2WA3 1 AUTHOR JRNL
REVDAT 4 05-JUL-17 2WA3 1 REMARK
REVDAT 3 29-SEP-10 2WA3 1 JRNL
REVDAT 2 22-SEP-10 2WA3 1 CAVEAT KEYWDS JRNL REMARK
REVDAT 1 21-APR-10 2WA3 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.ELKINS,K.S.HEWITSON,L.MCNEILL,J.SEIBEL,I.SCHLEMMINGER,
REMARK 1 AUTH 2 C.PUGH,P.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
REMARK 1 TITL 3 HIF-1ALPHA
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. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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) : 74.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19325
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1043
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) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1414
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.4320
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.4170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2765
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.10000
REMARK 3 B22 (A**2) : 1.10000
REMARK 3 B33 (A**2) : -2.21000
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): 0.314
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.242
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.182
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.119
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2879 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1988 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3913 ; 1.872 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4816 ; 1.376 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 338 ; 7.987 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;38.609 ;24.557
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 475 ;18.478 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;21.983 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 390 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3232 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 598 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 630 ; 0.233 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2026 ; 0.208 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1374 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1503 ; 0.096 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 108 ; 0.167 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.016 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.074 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 11 ; 0.330 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 33 ; 0.263 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.133 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
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): 2140 ; 1.182 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 671 ; 0.187 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2724 ; 1.456 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1444 ; 2.355 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1187 ; 3.461 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 15 A 44
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5460 31.5680 15.5700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: -0.1871
REMARK 3 T33: 0.6203 T12: -0.0038
REMARK 3 T13: -0.2374 T23: -0.0699
REMARK 3 L TENSOR
REMARK 3 L11: 0.7211 L22: 1.7867
REMARK 3 L33: 3.3026 L12: 1.0131
REMARK 3 L13: 0.5975 L23: -0.1705
REMARK 3 S TENSOR
REMARK 3 S11: -0.2245 S12: 0.1155 S13: 0.4093
REMARK 3 S21: -0.4946 S22: -0.0873 S23: 0.7395
REMARK 3 S31: 0.0922 S32: -0.2830 S33: 0.3117
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 45 A 77
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2090 20.8580 13.0030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1364 T22: -0.2255
REMARK 3 T33: 0.3408 T12: -0.0193
REMARK 3 T13: -0.1158 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 2.5865 L22: 3.2102
REMARK 3 L33: 4.0577 L12: 1.4074
REMARK 3 L13: 0.1612 L23: 0.8866
REMARK 3 S TENSOR
REMARK 3 S11: -0.1956 S12: 0.4520 S13: -0.2063
REMARK 3 S21: -0.3359 S22: 0.3871 S23: 0.0522
REMARK 3 S31: 0.1600 S32: 0.0997 S33: -0.1915
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 78 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6080 19.0460 38.5260
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.1099
REMARK 3 T33: 0.2854 T12: -0.0498
REMARK 3 T13: 0.0372 T23: 0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 1.6176 L22: 0.7607
REMARK 3 L33: 3.5288 L12: 1.0397
REMARK 3 L13: 1.1410 L23: 0.2315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0322 S12: -0.3616 S13: -0.0375
REMARK 3 S21: 1.0624 S22: -0.1231 S23: 0.1846
REMARK 3 S31: 0.5967 S32: -0.3386 S33: 0.0910
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 163 A 224
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0510 23.6000 23.3080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0954 T22: -0.1953
REMARK 3 T33: 0.3929 T12: -0.0347
REMARK 3 T13: -0.1153 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.5261 L22: 2.8133
REMARK 3 L33: 1.3712 L12: 0.2047
REMARK 3 L13: 0.1987 L23: 1.6810
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.1356 S13: -0.0329
REMARK 3 S21: 0.0672 S22: 0.1906 S23: -0.0973
REMARK 3 S31: 0.1601 S32: 0.0192 S33: -0.1915
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 225 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7010 43.3290 32.3680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: -0.2171
REMARK 3 T33: 0.4143 T12: -0.0149
REMARK 3 T13: -0.0712 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 2.0146 L22: 4.5959
REMARK 3 L33: 4.1919 L12: -0.0187
REMARK 3 L13: 1.4547 L23: -0.5068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0431 S12: -0.1370 S13: 0.1224
REMARK 3 S21: -0.0489 S22: -0.0737 S23: 0.3753
REMARK 3 S31: -0.1840 S32: -0.0872 S33: 0.0306
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 262 A 349
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3400 35.3040 29.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0313 T22: -0.1427
REMARK 3 T33: 0.3850 T12: 0.0117
REMARK 3 T13: -0.0705 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.6296 L22: 2.7128
REMARK 3 L33: 1.8086 L12: 1.7494
REMARK 3 L13: 1.5076 L23: 1.5943
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: -0.0393 S13: -0.0361
REMARK 3 S21: -0.1454 S22: 0.0521 S23: -0.0621
REMARK 3 S31: 0.2172 S32: 0.1983 S33: -0.0819
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 : 1.20
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 RIDING
REMARK 3 POSITIONS. ANISOTROPIC U FACTORS CALCULATED FROM TLS MODEL. ATOM
REMARK 3 RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD
REMARK 3 CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2WA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1290038014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-04
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 : PX10.1
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 : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20426
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 37.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.19000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: PDB ENTRY 1H2N
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 100MM HEPES PH
REMARK 280 7.5, 3% PEG400, 1MM FESO4, 28MG/ML PROTEIN, 10MM 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 74.21000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.46900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.46900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.10500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.46900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.46900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.31500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.46900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.46900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.10500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.46900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.46900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.31500
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 74.21000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.8 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 86.93800
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 86.93800
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 74.21000
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 181 CD GLN A 181 OE1 0.142
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 177 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 248 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 248 CB - CG - OD2 ANGL. DEV. = -6.0 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 ALA A 22 16.37 57.48
REMARK 500 LEU A 23 10.47 -65.42
REMARK 500 ASP A 66 36.23 -140.73
REMARK 500 ASN A 110 -89.45 -27.90
REMARK 500 ASN A 113 53.42 -55.49
REMARK 500 SER A 118 75.99 -171.26
REMARK 500 ARG A 138 35.78 -147.94
REMARK 500 ASN A 151 -115.98 -147.30
REMARK 500 ILE A 210 -53.29 -125.08
REMARK 500 ASP A 237 131.03 -39.02
REMARK 500 ARG A 238 -0.33 79.70
REMARK 500 TYR A 276 -3.61 74.55
REMARK 500 ARG A 305 83.61 -48.27
REMARK 500 ASN A 332 118.48 -160.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 2-(3-HYDROXYPHENYL)-2-OXOACETIC ACID (A29): PUBCHEM CID
REMARK 600 13548097
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 A 350 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199 NE2
REMARK 620 2 ASP A 201 OD2 117.0
REMARK 620 3 HIS A 279 NE2 84.9 77.0
REMARK 620 4 A29 A 400 O2 157.2 75.8 79.7
REMARK 620 5 A29 A 400 O7 84.2 157.7 99.4 81.9
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 FE2 A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A29 A 400
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: 2W0X RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA WITH PYRIDINE 2,4 DICARBOXYLIC ACID
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: 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: 2CGO RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA WITH FUMARATE
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: 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 2WA3 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 A 350 1
HET A29 A 400 12
HETNAM FE2 FE (II) ION
HETNAM A29 2-(3-HYDROXYPHENYL)-2-OXO-ETHANOIC ACID
FORMUL 2 FE2 FE 2+
FORMUL 3 A29 C8 H6 O4
FORMUL 4 HOH *84(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 ALA A 109 5 6
HELIX 6 6 LYS A 124 GLN A 137 1 14
HELIX 7 7 GLY A 155 GLY A 164 1 10
HELIX 8 8 ASN A 166 GLY A 178 1 13
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 LEU A 330 1 20
HELIX 13 13 ASN A 332 GLN A 334 5 3
HELIX 14 14 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 9 ARG A 44 LEU A 45 0
SHEET 2 AB 9 VAL A 62 LEU A 64 1 O VAL A 63 N LEU A 45
SHEET 3 AB 9 VAL A 270 ILE A 273 -1 O VAL A 270 N LEU A 64
SHEET 4 AB 9 GLN A 204 LYS A 211 -1 O ASN A 205 N ILE A 273
SHEET 5 AB 9 THR A 290 TYR A 297 -1 O ILE A 291 N ILE A 210
SHEET 6 AB 9 LEU A 186 GLY A 190 -1 O LEU A 186 N ASN A 294
SHEET 7 AB 9 ARG A 143 THR A 149 -1 O LEU A 146 N ILE A 189
SHEET 8 AB 9 PHE A 90 ALA A 95 -1 O SER A 91 N GLN A 147
SHEET 9 AB 9 ARG A 120 MET A 123 -1 O GLU A 121 N VAL A 92
SHEET 1 AC 6 ARG A 44 LEU A 45 0
SHEET 2 AC 6 VAL A 62 LEU A 64 1 O VAL A 63 N LEU A 45
SHEET 3 AC 6 VAL A 270 ILE A 273 -1 O VAL A 270 N LEU A 64
SHEET 4 AC 6 GLN A 204 LYS A 211 -1 O ASN A 205 N ILE A 273
SHEET 5 AC 6 THR A 290 TYR A 297 -1 O ILE A 291 N ILE A 210
SHEET 6 AC 6 LEU A 182 SER A 184 -1 N THR A 183 O TRP A 296
LINK NE2 HIS A 199 FE FE2 A 350 1555 1555 2.32
LINK OD2 ASP A 201 FE FE2 A 350 1555 1555 2.12
LINK NE2 HIS A 279 FE FE2 A 350 1555 1555 2.30
LINK FE FE2 A 350 O2 A29 A 400 1555 1555 1.89
LINK FE FE2 A 350 O7 A29 A 400 1555 1555 2.26
CISPEP 1 TYR A 308 PRO A 309 0 7.03
SITE 1 AC1 4 HIS A 199 ASP A 201 HIS A 279 A29 A 400
SITE 1 AC2 12 TYR A 145 LEU A 188 THR A 196 HIS A 199
SITE 2 AC2 12 ASP A 201 ASN A 205 PHE A 207 HIS A 279
SITE 3 AC2 12 ILE A 281 ASN A 294 TRP A 296 FE2 A 350
CRYST1 86.938 86.938 148.420 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 0.011502 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011502 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006738 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
