HEADER OXIDOREDUCTASE 12-MAY-16 5JWL
TITLE FACTOR INHIBITING HIF D201E IN COMPLEX WITH ZN, AND ALPHA-
TITLE 2 KETOGLUTARATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1-ALPHA INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FACTOR INHIBITING HIF-1,FIH-1,HYPOXIA-INDUCIBLE FACTOR
COMPND 5 ASPARAGINE HYDROXYLASE;
COMPND 6 EC: 1.14.11.30,1.14.11.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HIF1AN, FIH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYPOXIA INDUCIBLE FACTOR, FACTOR INHIBITING HIF, OXYGENASE, OXYGEN
KEYWDS 2 SENSING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Y.TAABAZUING,S.C.GARMAN,S.ERON,M.J.KNAPP
REVDAT 4 27-SEP-23 5JWL 1 REMARK
REVDAT 3 25-DEC-19 5JWL 1 REMARK
REVDAT 2 27-SEP-17 5JWL 1 SEQRES
REVDAT 1 17-MAY-17 5JWL 0
JRNL AUTH J.A.HANGASKY,C.Y.TAABAZUING,C.MARTIN,S.ERON,S.C.GARMAN,
JRNL AUTH 2 M.J.KNAPP
JRNL TITL FACTOR INHIBITING HIF D201E IN COMPLEX WITH ZN, AND
JRNL TITL 2 ALPHA-KETOGLUTARATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 18715
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1592
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1213
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2798
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : 2.06000
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): 0.300
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.157
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.043
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2903 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2662 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3937 ; 1.755 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6133 ; 0.889 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 340 ; 7.254 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;40.475 ;24.551
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 477 ;17.130 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;19.017 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 395 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3332 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 709 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1363 ; 4.251 ; 4.891
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1362 ; 4.251 ; 4.891
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1702 ; 6.334 ; 7.315
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : NULL
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 1 A (A**2): 5447 ; 0.000 ; 0.500
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 9 A 349
REMARK 3 RESIDUE RANGE : A 401 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3779 21.5591 -9.3437
REMARK 3 T TENSOR
REMARK 3 T11: 0.0574 T22: 0.3366
REMARK 3 T33: 0.0583 T12: 0.0109
REMARK 3 T13: -0.0007 T23: 0.1181
REMARK 3 L TENSOR
REMARK 3 L11: 1.3686 L22: 0.3074
REMARK 3 L33: 0.7104 L12: -0.4849
REMARK 3 L13: 0.9324 L23: -0.2399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: -0.0469 S13: 0.1022
REMARK 3 S21: 0.0811 S22: -0.0297 S23: -0.0605
REMARK 3 S31: 0.0554 S32: -0.1283 S33: 0.0235
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5JWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-13
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 : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT
REMARK 200 OPTICS : FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22314
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 0.98900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3D8C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.6MM AMMONIUM SULFATE, 3%
REMARK 280 PEG 400, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 74.60650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.06550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.06550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.30325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.06550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.06550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.90975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.06550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.06550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.30325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.06550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.06550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.90975
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 74.60650
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 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 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 614 LIES ON A SPECIAL POSITION.
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 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 HOH A 588 O HOH A 593 1.98
REMARK 500 O HOH A 590 O HOH A 604 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 40 CG ARG A 156 6554 1.86
REMARK 500 NH1 ARG A 40 O ARG A 156 6554 2.13
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 PRO A 303 C - N - CD ANGL. DEV. = -25.2 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 10 56.04 -99.82
REMARK 500 ASN A 113 74.78 -66.16
REMARK 500 PHE A 114 103.84 -161.13
REMARK 500 ILE A 210 -54.27 -121.89
REMARK 500 ARG A 238 -0.84 80.39
REMARK 500 MET A 275 123.92 -36.89
REMARK 500 TYR A 276 -2.95 76.59
REMARK 500 ARG A 305 -169.79 -113.58
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 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199 NE2
REMARK 620 2 GLU A 201 OE1 103.6
REMARK 620 3 HIS A 279 NE2 83.7 80.0
REMARK 620 4 AKG A 401 O2 174.4 81.8 98.8
REMARK 620 5 AKG A 401 O5 89.4 165.9 107.1 85.1
REMARK 620 6 HOH A 503 O 81.3 97.4 163.6 96.8 79.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AKG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JWK RELATED DB: PDB
REMARK 900 RELATED ID: 5JWP RELATED DB: PDB
DBREF 5JWL A 1 349 UNP Q9NWT6 HIF1N_HUMAN 1 349
SEQADV 5JWL GLY A -2 UNP Q9NWT6 EXPRESSION TAG
SEQADV 5JWL SER A -1 UNP Q9NWT6 EXPRESSION TAG
SEQADV 5JWL HIS A 0 UNP Q9NWT6 EXPRESSION TAG
SEQADV 5JWL GLU A 201 UNP Q9NWT6 ASP 201 ENGINEERED MUTATION
SEQRES 1 A 352 GLY SER HIS MET ALA ALA THR ALA ALA GLU ALA VAL ALA
SEQRES 2 A 352 SER GLY SER GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU
SEQRES 3 A 352 GLY PRO ALA TRP ASP GLU SER GLN LEU ARG SER TYR SER
SEQRES 4 A 352 PHE PRO THR ARG PRO ILE PRO ARG LEU SER GLN SER ASP
SEQRES 5 A 352 PRO ARG ALA GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL
SEQRES 6 A 352 VAL LEU THR ASP THR ASN LEU VAL TYR PRO ALA LEU LYS
SEQRES 7 A 352 TRP ASP LEU GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY
SEQRES 8 A 352 ASP PHE SER VAL TYR SER ALA SER THR HIS LYS PHE LEU
SEQRES 9 A 352 TYR TYR ASP GLU LYS LYS MET ALA ASN PHE GLN ASN PHE
SEQRES 10 A 352 LYS PRO ARG SER ASN ARG GLU GLU MET LYS PHE HIS GLU
SEQRES 11 A 352 PHE VAL GLU LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY
SEQRES 12 A 352 GLU GLU ARG LEU TYR LEU GLN GLN THR LEU ASN ASP THR
SEQRES 13 A 352 VAL GLY ARG LYS ILE VAL MET ASP PHE LEU GLY PHE ASN
SEQRES 14 A 352 TRP ASN TRP ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP
SEQRES 15 A 352 GLY GLN LEU THR SER ASN LEU LEU LEU ILE GLY MET GLU
SEQRES 16 A 352 GLY ASN VAL THR PRO ALA HIS TYR GLU GLU GLN GLN ASN
SEQRES 17 A 352 PHE PHE ALA GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU
SEQRES 18 A 352 PHE PRO PRO ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO
SEQRES 19 A 352 VAL HIS HIS PRO CYS ASP ARG GLN SER GLN VAL ASP PHE
SEQRES 20 A 352 ASP ASN PRO ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN
SEQRES 21 A 352 VAL VAL GLY TYR GLU THR VAL VAL GLY PRO GLY ASP VAL
SEQRES 22 A 352 LEU TYR ILE PRO MET TYR TRP TRP HIS HIS ILE GLU SER
SEQRES 23 A 352 LEU LEU ASN GLY GLY ILE THR ILE THR VAL ASN PHE TRP
SEQRES 24 A 352 TYR LYS GLY ALA PRO THR PRO LYS ARG ILE GLU TYR PRO
SEQRES 25 A 352 LEU LYS ALA HIS GLN LYS VAL ALA ILE MET ARG ASN ILE
SEQRES 26 A 352 GLU LYS MET LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU
SEQRES 27 A 352 VAL GLY PRO LEU LEU ASN THR MET ILE LYS GLY ARG TYR
SEQRES 28 A 352 ASN
HET AKG A 401 10
HET PEG A 402 7
HET ZN A 403 1
HET SO4 A 404 5
HET SO4 A 405 5
HETNAM AKG 2-OXOGLUTARIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 2 AKG C5 H6 O5
FORMUL 3 PEG C4 H10 O3
FORMUL 4 ZN ZN 2+
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *114(H2 O)
HELIX 1 AA1 ASP A 28 LEU A 32 5 5
HELIX 2 AA2 ASP A 49 ASN A 58 1 10
HELIX 3 AA3 VAL A 70 TRP A 76 5 7
HELIX 4 AA4 ASP A 77 ILE A 85 1 9
HELIX 5 AA5 GLU A 105 PHE A 111 5 7
HELIX 6 AA6 LYS A 124 ARG A 138 1 15
HELIX 7 AA7 GLY A 155 GLY A 164 1 10
HELIX 8 AA8 ASN A 166 ARG A 177 1 12
HELIX 9 AA9 PRO A 220 ASP A 222 5 3
HELIX 10 AB1 GLN A 223 TYR A 228 1 6
HELIX 11 AB2 PHE A 252 VAL A 258 5 7
HELIX 12 AB3 LYS A 311 GLY A 331 1 21
HELIX 13 AB4 ASN A 332 GLN A 334 5 3
HELIX 14 AB5 GLU A 335 LYS A 345 1 11
SHEET 1 AA1 5 THR A 39 PRO A 41 0
SHEET 2 AA1 5 GLY A 260 VAL A 265 1 O GLU A 262 N ARG A 40
SHEET 3 AA1 5 LYS A 214 PHE A 219 -1 N LEU A 218 O TYR A 261
SHEET 4 AA1 5 TRP A 278 SER A 283 -1 O GLU A 282 N ARG A 215
SHEET 5 AA1 5 VAL A 195 HIS A 199 -1 N HIS A 199 O HIS A 279
SHEET 1 AA2 9 ARG A 44 LEU A 45 0
SHEET 2 AA2 9 VAL A 62 LEU A 64 1 O VAL A 63 N LEU A 45
SHEET 3 AA2 9 VAL A 270 ILE A 273 -1 O VAL A 270 N LEU A 64
SHEET 4 AA2 9 GLN A 204 LYS A 211 -1 N ASN A 205 O ILE A 273
SHEET 5 AA2 9 THR A 290 TYR A 297 -1 O ILE A 291 N LYS A 211
SHEET 6 AA2 9 LEU A 186 GLY A 190 -1 N LEU A 188 O THR A 292
SHEET 7 AA2 9 ARG A 143 THR A 149 -1 N LEU A 146 O ILE A 189
SHEET 8 AA2 9 PHE A 90 ALA A 95 -1 N TYR A 93 O TYR A 145
SHEET 9 AA2 9 ARG A 120 MET A 123 -1 O MET A 123 N PHE A 90
SHEET 1 AA3 6 ARG A 44 LEU A 45 0
SHEET 2 AA3 6 VAL A 62 LEU A 64 1 O VAL A 63 N LEU A 45
SHEET 3 AA3 6 VAL A 270 ILE A 273 -1 O VAL A 270 N LEU A 64
SHEET 4 AA3 6 GLN A 204 LYS A 211 -1 N ASN A 205 O ILE A 273
SHEET 5 AA3 6 THR A 290 TYR A 297 -1 O ILE A 291 N LYS A 211
SHEET 6 AA3 6 LEU A 182 SER A 184 -1 N SER A 184 O TRP A 296
LINK NE2 HIS A 199 ZN ZN A 403 1555 1555 2.21
LINK OE1 GLU A 201 ZN ZN A 403 1555 1555 2.02
LINK NE2 HIS A 279 ZN ZN A 403 1555 1555 2.29
LINK O2 AKG A 401 ZN ZN A 403 1555 1555 1.92
LINK O5 AKG A 401 ZN ZN A 403 1555 1555 2.05
LINK ZN ZN A 403 O HOH A 503 1555 1555 2.33
CISPEP 1 LYS A 304 ARG A 305 0 -19.03
CISPEP 2 TYR A 308 PRO A 309 0 8.56
SITE 1 AC1 14 TYR A 145 LEU A 188 THR A 196 HIS A 199
SITE 2 AC1 14 GLU A 201 ASN A 205 PHE A 207 LYS A 214
SITE 3 AC1 14 HIS A 279 ILE A 281 ASN A 294 TRP A 296
SITE 4 AC1 14 ZN A 403 HOH A 503
SITE 1 AC2 4 TYR A 102 GLN A 147 HIS A 199 HOH A 503
SITE 1 AC3 5 HIS A 199 GLU A 201 HIS A 279 AKG A 401
SITE 2 AC3 5 HOH A 503
SITE 1 AC4 3 LYS A 311 ALA A 312 HOH A 578
SITE 1 AC5 4 ARG A 138 GLY A 140 GLU A 141 GLU A 142
CRYST1 86.131 86.131 149.213 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 0.011610 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
