HEADER OXIDOREDUCTASE 14-JUN-06 2HBT
TITLE CRYSTAL STRUCTURE OF HIF PROLYL HYDROXYLASE EGLN-1 IN COMPLEX WITH A
TITLE 2 BIOLOGICALLY ACTIVE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EGL NINE HOMOLOG 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: HYPOXIA-INDUCIBLE FACTOR PROLYL HYDROXYLASE 2, HIF-PROLYL
COMPND 6 HYDROXYLASE 2, HIF-PH2, HPH-2, PROLYL HYDROXYLASE DOMAIN-CONTAINING
COMPND 7 PROTEIN 2, PHD2, SM-20;
COMPND 8 EC: 1.14.11.-;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EGLN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)*;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET45-DEST
KEYWDS PROLYL HYDROXYLASE, HYPOXIA INDUCIBLE FACTOR, HIF, EGLN, 2-
KEYWDS 2 OXOGLUTARATE, OXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.G.EVDOKIMOV,R.L.WALTER,M.MEKEL,M.E.POKROSS,R.KAWAMOTO,A.BOYER
REVDAT 3 18-OCT-17 2HBT 1 REMARK
REVDAT 2 24-FEB-09 2HBT 1 VERSN
REVDAT 1 27-JUN-06 2HBT 0
JRNL AUTH A.G.EVDOKIMOV,R.L.WALTER,M.MEKEL,M.E.POKROSS,R.KAWAMOTO,
JRNL AUTH 2 A.BOYER
JRNL TITL CRYSTAL STRUCTURE OF HIF PROLYL HYDROXYLASE IN COMPLEX WITH
JRNL TITL 2 A BIOLOGICALLY ACTIVE INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 36503
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1814
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2581
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 119
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.22000
REMARK 3 B12 (A**2) : -0.07000
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): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.292
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1916 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1749 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2601 ; 1.470 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4090 ; 0.695 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ;11.270 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 89 ;34.553 ;23.371
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 351 ;20.582 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.558 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 275 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2147 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 406 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 428 ; 0.267 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1867 ; 0.248 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 904 ; 0.197 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1104 ; 0.095 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 119 ; 0.213 ; 0.200
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): 25 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 77 ; 0.329 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.442 ; 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): 1493 ; 2.937 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 476 ; 1.079 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1852 ; 3.228 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 918 ; 4.638 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 736 ; 5.770 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 2HBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038171.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARGUI
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36629
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.01900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.26100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200-300 MM (NH4)2SO4, 100 MM NAOAC PH
REMARK 280 4.8-5.4, 22-25% PEG-4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K, PH 5.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 20.11450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 20.11450
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 20.11450
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: MONOMERIC
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 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 180
REMARK 465 ALA A 181
REMARK 465 HIS A 182
REMARK 465 HIS A 183
REMARK 465 HIS A 184
REMARK 465 HIS A 185
REMARK 465 HIS A 186
REMARK 465 HIS A 187
REMARK 465 THR A 405
REMARK 465 GLY A 406
REMARK 465 GLU A 407
REMARK 465 ASN A 415
REMARK 465 LYS A 416
REMARK 465 PRO A 417
REMARK 465 SER A 418
REMARK 465 ASP A 419
REMARK 465 SER A 420
REMARK 465 VAL A 421
REMARK 465 GLY A 422
REMARK 465 LYS A 423
REMARK 465 ASP A 424
REMARK 465 VAL A 425
REMARK 465 PHE A 426
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 TYR A 403 O HOH A 1040 1.90
REMARK 500 OE1 GLN A 220 O HOH A 956 1.99
REMARK 500 O HOH A 936 O HOH A 1010 2.05
REMARK 500 O HOH A 1009 O HOH A 1033 2.08
REMARK 500 O HOH A 991 O HOH A 1011 2.08
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 O HOH A 1027 O HOH A 1029 2455 1.46
REMARK 500 O HOH A 989 O HOH A 1029 2455 2.12
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 TYR A 197 -60.80 -129.02
REMARK 500 GLU A 348 133.68 -38.03
REMARK 500 ALA A 351 88.71 -67.16
REMARK 500 GLN A 352 166.20 170.36
REMARK 500 TYR A 403 -88.09 -77.81
REMARK 500 VAL A 410 -7.01 61.33
REMARK 500 GLU A 413 -153.89 73.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 245 ASP A 246 135.20
REMARK 500 LYS A 350 ALA A 351 145.48
REMARK 500 ALA A 351 GLN A 352 145.13
REMARK 500 LYS A 408 GLY A 409 -130.28
REMARK 500 GLY A 409 VAL A 410 -132.22
REMARK 500 VAL A 412 GLU A 413 137.52
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 FE2 A 900 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 313 NE2
REMARK 620 2 ASP A 315 OD2 93.4
REMARK 620 3 HIS A 374 NE2 89.2 91.1
REMARK 620 4 UN9 A 1 O13 94.5 171.7 86.5
REMARK 620 5 UN9 A 1 N8 87.4 105.8 162.9 77.1
REMARK 620 6 HOH A1002 O 175.2 87.3 95.5 85.0 87.8
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 FE2 A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UN9 A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HBU RELATED DB: PDB
REMARK 900 SAME COMPLEX, REDUCED S-S BOND
DBREF 2HBT A 188 426 UNP Q9GZT9 EGLN1_HUMAN 188 426
SEQADV 2HBT MET A 180 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT ALA A 181 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT HIS A 182 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT HIS A 183 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT HIS A 184 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT HIS A 185 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT HIS A 186 UNP Q9GZT9 CLONING ARTIFACT
SEQADV 2HBT HIS A 187 UNP Q9GZT9 CLONING ARTIFACT
SEQRES 1 A 247 MET ALA HIS HIS HIS HIS HIS HIS LEU PRO ALA LEU LYS
SEQRES 2 A 247 LEU ALA LEU GLU TYR ILE VAL PRO CYS MET ASN LYS HIS
SEQRES 3 A 247 GLY ILE CYS VAL VAL ASP ASP PHE LEU GLY LYS GLU THR
SEQRES 4 A 247 GLY GLN GLN ILE GLY ASP GLU VAL ARG ALA LEU HIS ASP
SEQRES 5 A 247 THR GLY LYS PHE THR ASP GLY GLN LEU VAL SER GLN LYS
SEQRES 6 A 247 SER ASP SER SER LYS ASP ILE ARG GLY ASP LYS ILE THR
SEQRES 7 A 247 TRP ILE GLU GLY LYS GLU PRO GLY CYS GLU THR ILE GLY
SEQRES 8 A 247 LEU LEU MET SER SER MET ASP ASP LEU ILE ARG HIS CYS
SEQRES 9 A 247 ASN GLY LYS LEU GLY SER TYR LYS ILE ASN GLY ARG THR
SEQRES 10 A 247 LYS ALA MET VAL ALA CYS TYR PRO GLY ASN GLY THR GLY
SEQRES 11 A 247 TYR VAL ARG HIS VAL ASP ASN PRO ASN GLY ASP GLY ARG
SEQRES 12 A 247 CYS VAL THR CYS ILE TYR TYR LEU ASN LYS ASP TRP ASP
SEQRES 13 A 247 ALA LYS VAL SER GLY GLY ILE LEU ARG ILE PHE PRO GLU
SEQRES 14 A 247 GLY LYS ALA GLN PHE ALA ASP ILE GLU PRO LYS PHE ASP
SEQRES 15 A 247 ARG LEU LEU PHE PHE TRP SER ASP ARG ARG ASN PRO HIS
SEQRES 16 A 247 GLU VAL GLN PRO ALA TYR ALA THR ARG TYR ALA ILE THR
SEQRES 17 A 247 VAL TRP TYR PHE ASP ALA ASP GLU ARG ALA ARG ALA LYS
SEQRES 18 A 247 VAL LYS TYR LEU THR GLY GLU LYS GLY VAL ARG VAL GLU
SEQRES 19 A 247 LEU ASN LYS PRO SER ASP SER VAL GLY LYS ASP VAL PHE
HET FE2 A 900 1
HET UN9 A 1 19
HETNAM FE2 FE (II) ION
HETNAM UN9 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
FORMUL 2 FE2 FE 2+
FORMUL 3 UN9 C12 H9 CL N2 O4
FORMUL 4 HOH *140(H2 O)
HELIX 1 1 PRO A 189 TYR A 197 1 9
HELIX 2 2 TYR A 197 HIS A 205 1 9
HELIX 3 3 GLY A 215 THR A 232 1 18
HELIX 4 4 CYS A 266 CYS A 283 1 18
HELIX 5 5 ASP A 335 GLY A 340 1 6
HELIX 6 6 ALA A 393 TYR A 403 1 11
SHEET 1 A 6 ILE A 207 VAL A 210 0
SHEET 2 A 6 ARG A 362 TRP A 367 -1 O PHE A 365 N CYS A 208
SHEET 3 A 6 ARG A 322 TYR A 329 -1 N THR A 325 O PHE A 366
SHEET 4 A 6 ARG A 383 ASP A 392 -1 O TYR A 390 N VAL A 324
SHEET 5 A 6 ALA A 298 TYR A 303 -1 N MET A 299 O THR A 387
SHEET 6 A 6 LYS A 255 ILE A 259 -1 N ILE A 259 O ALA A 298
SHEET 1 B 5 ILE A 207 VAL A 210 0
SHEET 2 B 5 ARG A 362 TRP A 367 -1 O PHE A 365 N CYS A 208
SHEET 3 B 5 ARG A 322 TYR A 329 -1 N THR A 325 O PHE A 366
SHEET 4 B 5 ARG A 383 ASP A 392 -1 O TYR A 390 N VAL A 324
SHEET 5 B 5 ILE A 292 ARG A 295 -1 N GLY A 294 O PHE A 391
SHEET 1 C 2 LEU A 240 SER A 242 0
SHEET 2 C 2 ILE A 251 ARG A 252 -1 O ILE A 251 N VAL A 241
SHEET 1 D 4 TYR A 310 HIS A 313 0
SHEET 2 D 4 HIS A 374 VAL A 376 -1 O HIS A 374 N HIS A 313
SHEET 3 D 4 LEU A 343 ILE A 345 -1 N ARG A 344 O GLU A 375
SHEET 4 D 4 ALA A 354 ILE A 356 -1 O ALA A 354 N ILE A 345
SSBOND 1 CYS A 201 CYS A 208 1555 1555 2.07
LINK NE2 HIS A 313 FE FE2 A 900 1555 1555 2.13
LINK OD2 ASP A 315 FE FE2 A 900 1555 1555 2.15
LINK NE2 HIS A 374 FE FE2 A 900 1555 1555 2.11
LINK O13 UN9 A 1 FE FE2 A 900 1555 1555 2.05
LINK N8 UN9 A 1 FE FE2 A 900 1555 1555 2.25
LINK O HOH A1002 FE FE2 A 900 1555 1555 2.13
SITE 1 AC1 5 UN9 A 1 HIS A 313 ASP A 315 HIS A 374
SITE 2 AC1 5 HOH A1002
SITE 1 AC2 15 ASP A 254 MET A 299 TYR A 303 TYR A 310
SITE 2 AC2 15 HIS A 313 ASP A 315 TYR A 329 HIS A 374
SITE 3 AC2 15 VAL A 376 ARG A 383 ARG A 398 FE2 A 900
SITE 4 AC2 15 HOH A 921 HOH A 924 HOH A1002
CRYST1 111.166 111.166 40.229 90.00 90.00 120.00 P 63 6
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 0.008996 0.005194 0.000000 0.00000
SCALE2 0.000000 0.010387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024858 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
