HEADER OXIDOREDUCTASE 05-MAR-12 3VPN
TITLE CRYSTAL STRUCTURE OF HUMAN RIBONUCLEOTIDE REDUCTASE SUBUNIT M2 (HRRM2)
TITLE 2 MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 66-350;
COMPND 5 SYNONYM: RIBONUCLEOTIDE REDUCTASE SMALL CHAIN, RIBONUCLEOTIDE
COMPND 6 REDUCTASE SMALL SUBUNIT;
COMPND 7 EC: 1.17.4.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: RR2, RRM2;
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
KEYWDS METAL-BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.CHEN,Z.XU,H.LIU,L.ZHANG,B.CHEN,L.ZHU,C.YANG,W.ZHU,J.SHAO
REVDAT 3 08-NOV-23 3VPN 1 REMARK SEQADV LINK
REVDAT 2 22-NOV-17 3VPN 1 REMARK
REVDAT 1 06-MAR-13 3VPN 0
JRNL AUTH X.CHEN,Z.XU,H.LIU,L.ZHANG,B.CHEN,L.ZHU,C.YANG,W.ZHU,J.SHAO
JRNL TITL ESSENTIAL ROLE OF E106 IN THE PROTON-COUPLED ELECTRON
JRNL TITL 2 TRANSFER IN HUMAN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 48252
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.212
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 : 2577
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3510
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4732
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.11000
REMARK 3 B22 (A**2) : 1.11000
REMARK 3 B33 (A**2) : -2.22000
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): 0.203
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.932
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
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): 4870 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6572 ; 1.137 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 574 ; 4.755 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;35.986 ;23.680
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 873 ;14.410 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;15.534 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 694 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3723 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2862 ; 0.671 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4630 ; 1.310 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2008 ; 1.951 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1940 ; 3.226 ; 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 : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3VPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000095343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-11
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51165
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : 0.69200
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 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 3OLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL, 0.1MM KCL, PH 7.5,
REMARK 280 TEMPERATURE 293K, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 88.26150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.54100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.54100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 132.39225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.54100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.54100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.13075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.54100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.54100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 132.39225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.54100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.54100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.13075
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 88.26150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 OE2 GLU B 232 FE FE B 1001 1.62
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 ARG A 148 -73.84 -119.64
REMARK 500 ASN A 195 31.58 -94.06
REMARK 500 MET A 252 71.68 57.60
REMARK 500 GLU A 306 -54.96 -124.59
REMARK 500 ARG B 148 -73.44 -122.03
REMARK 500 MET B 252 86.98 44.42
REMARK 500 GLU B 306 -57.98 -132.77
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 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 78 O
REMARK 620 2 VAL A 81 O 84.5
REMARK 620 3 THR A 156 OG1 84.7 96.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A1001 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 169 OE2
REMARK 620 2 GLU A 232 OE2 114.8
REMARK 620 3 GLU A 266 OE1 136.3 80.6
REMARK 620 4 GLU A 266 OE2 97.9 141.0 60.8
REMARK 620 5 HIS A 269 ND1 91.4 111.4 122.2 87.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 78 O
REMARK 620 2 VAL B 81 O 71.1
REMARK 620 3 THR B 156 OG1 79.4 81.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B1001 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 169 OE2
REMARK 620 2 GLU B 266 OE2 105.0
REMARK 620 3 GLU B 266 OE1 141.6 58.4
REMARK 620 4 HIS B 269 ND1 88.1 86.7 121.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OLJ RELATED DB: PDB
REMARK 900 RELATED ID: 3VPM RELATED DB: PDB
REMARK 900 RELATED ID: 3VPO RELATED DB: PDB
DBREF 3VPN A 66 350 UNP P31350 RIR2_HUMAN 66 350
DBREF 3VPN B 66 350 UNP P31350 RIR2_HUMAN 66 350
SEQADV 3VPN MET A 65 UNP P31350 EXPRESSION TAG
SEQADV 3VPN ASP A 106 UNP P31350 GLU 106 ENGINEERED MUTATION
SEQADV 3VPN MET B 65 UNP P31350 EXPRESSION TAG
SEQADV 3VPN ASP B 106 UNP P31350 GLU 106 ENGINEERED MUTATION
SEQRES 1 A 286 MET GLY VAL GLU ASP GLU PRO LEU LEU ARG GLU ASN PRO
SEQRES 2 A 286 ARG ARG PHE VAL ILE PHE PRO ILE GLU TYR HIS ASP ILE
SEQRES 3 A 286 TRP GLN MET TYR LYS LYS ALA GLU ALA SER PHE TRP THR
SEQRES 4 A 286 ALA GLU ASP VAL ASP LEU SER LYS ASP ILE GLN HIS TRP
SEQRES 5 A 286 GLU SER LEU LYS PRO GLU GLU ARG TYR PHE ILE SER HIS
SEQRES 6 A 286 VAL LEU ALA PHE PHE ALA ALA SER ASP GLY ILE VAL ASN
SEQRES 7 A 286 GLU ASN LEU VAL GLU ARG PHE SER GLN GLU VAL GLN ILE
SEQRES 8 A 286 THR GLU ALA ARG CYS PHE TYR GLY PHE GLN ILE ALA MET
SEQRES 9 A 286 GLU ASN ILE HIS SER GLU MET TYR SER LEU LEU ILE ASP
SEQRES 10 A 286 THR TYR ILE LYS ASP PRO LYS GLU ARG GLU PHE LEU PHE
SEQRES 11 A 286 ASN ALA ILE GLU THR MET PRO CYS VAL LYS LYS LYS ALA
SEQRES 12 A 286 ASP TRP ALA LEU ARG TRP ILE GLY ASP LYS GLU ALA THR
SEQRES 13 A 286 TYR GLY GLU ARG VAL VAL ALA PHE ALA ALA VAL GLU GLY
SEQRES 14 A 286 ILE PHE PHE SER GLY SER PHE ALA SER ILE PHE TRP LEU
SEQRES 15 A 286 LYS LYS ARG GLY LEU MET PRO GLY LEU THR PHE SER ASN
SEQRES 16 A 286 GLU LEU ILE SER ARG ASP GLU GLY LEU HIS CYS ASP PHE
SEQRES 17 A 286 ALA CYS LEU MET PHE LYS HIS LEU VAL HIS LYS PRO SER
SEQRES 18 A 286 GLU GLU ARG VAL ARG GLU ILE ILE ILE ASN ALA VAL ARG
SEQRES 19 A 286 ILE GLU GLN GLU PHE LEU THR GLU ALA LEU PRO VAL LYS
SEQRES 20 A 286 LEU ILE GLY MET ASN CYS THR LEU MET LYS GLN TYR ILE
SEQRES 21 A 286 GLU PHE VAL ALA ASP ARG LEU MET LEU GLU LEU GLY PHE
SEQRES 22 A 286 SER LYS VAL PHE ARG VAL GLU ASN PRO PHE ASP PHE MET
SEQRES 1 B 286 MET GLY VAL GLU ASP GLU PRO LEU LEU ARG GLU ASN PRO
SEQRES 2 B 286 ARG ARG PHE VAL ILE PHE PRO ILE GLU TYR HIS ASP ILE
SEQRES 3 B 286 TRP GLN MET TYR LYS LYS ALA GLU ALA SER PHE TRP THR
SEQRES 4 B 286 ALA GLU ASP VAL ASP LEU SER LYS ASP ILE GLN HIS TRP
SEQRES 5 B 286 GLU SER LEU LYS PRO GLU GLU ARG TYR PHE ILE SER HIS
SEQRES 6 B 286 VAL LEU ALA PHE PHE ALA ALA SER ASP GLY ILE VAL ASN
SEQRES 7 B 286 GLU ASN LEU VAL GLU ARG PHE SER GLN GLU VAL GLN ILE
SEQRES 8 B 286 THR GLU ALA ARG CYS PHE TYR GLY PHE GLN ILE ALA MET
SEQRES 9 B 286 GLU ASN ILE HIS SER GLU MET TYR SER LEU LEU ILE ASP
SEQRES 10 B 286 THR TYR ILE LYS ASP PRO LYS GLU ARG GLU PHE LEU PHE
SEQRES 11 B 286 ASN ALA ILE GLU THR MET PRO CYS VAL LYS LYS LYS ALA
SEQRES 12 B 286 ASP TRP ALA LEU ARG TRP ILE GLY ASP LYS GLU ALA THR
SEQRES 13 B 286 TYR GLY GLU ARG VAL VAL ALA PHE ALA ALA VAL GLU GLY
SEQRES 14 B 286 ILE PHE PHE SER GLY SER PHE ALA SER ILE PHE TRP LEU
SEQRES 15 B 286 LYS LYS ARG GLY LEU MET PRO GLY LEU THR PHE SER ASN
SEQRES 16 B 286 GLU LEU ILE SER ARG ASP GLU GLY LEU HIS CYS ASP PHE
SEQRES 17 B 286 ALA CYS LEU MET PHE LYS HIS LEU VAL HIS LYS PRO SER
SEQRES 18 B 286 GLU GLU ARG VAL ARG GLU ILE ILE ILE ASN ALA VAL ARG
SEQRES 19 B 286 ILE GLU GLN GLU PHE LEU THR GLU ALA LEU PRO VAL LYS
SEQRES 20 B 286 LEU ILE GLY MET ASN CYS THR LEU MET LYS GLN TYR ILE
SEQRES 21 B 286 GLU PHE VAL ALA ASP ARG LEU MET LEU GLU LEU GLY PHE
SEQRES 22 B 286 SER LYS VAL PHE ARG VAL GLU ASN PRO PHE ASP PHE MET
HET FE A1001 1
HET MG A1002 1
HET FE B1001 1
HET MG B1002 1
HETNAM FE FE (III) ION
HETNAM MG MAGNESIUM ION
FORMUL 3 FE 2(FE 3+)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *210(H2 O)
HELIX 1 1 TYR A 87 SER A 100 1 14
HELIX 2 2 THR A 103 VAL A 107 5 5
HELIX 3 3 ASP A 112 LEU A 119 1 8
HELIX 4 4 LYS A 120 ARG A 148 1 29
HELIX 5 5 ARG A 148 VAL A 153 1 6
HELIX 6 6 ILE A 155 ILE A 184 1 30
HELIX 7 7 ASP A 186 ASN A 195 1 10
HELIX 8 8 ASN A 195 MET A 200 1 6
HELIX 9 9 MET A 200 ASP A 216 1 17
HELIX 10 10 THR A 220 ILE A 234 1 15
HELIX 11 11 PHE A 236 ARG A 249 1 14
HELIX 12 12 MET A 252 HIS A 279 1 28
HELIX 13 13 SER A 285 GLU A 306 1 22
HELIX 14 14 PRO A 309 GLY A 314 5 6
HELIX 15 15 ASN A 316 LEU A 335 1 20
HELIX 16 16 TYR B 87 SER B 100 1 14
HELIX 17 17 THR B 103 VAL B 107 5 5
HELIX 18 18 LYS B 111 SER B 118 1 8
HELIX 19 19 LYS B 120 ARG B 148 1 29
HELIX 20 20 ARG B 148 VAL B 153 1 6
HELIX 21 21 ILE B 155 ILE B 184 1 30
HELIX 22 22 ASP B 186 ASN B 195 1 10
HELIX 23 23 ASN B 195 MET B 200 1 6
HELIX 24 24 MET B 200 ASP B 216 1 17
HELIX 25 25 THR B 220 ILE B 234 1 15
HELIX 26 26 PHE B 236 ARG B 249 1 14
HELIX 27 27 MET B 252 HIS B 279 1 28
HELIX 28 28 SER B 285 GLU B 306 1 22
HELIX 29 29 PRO B 309 GLY B 314 5 6
HELIX 30 30 ASN B 316 LEU B 335 1 20
LINK O ARG A 78 MG MG A1002 1555 1555 2.40
LINK O VAL A 81 MG MG A1002 1555 1555 2.22
LINK OG1 THR A 156 MG MG A1002 1555 1555 2.47
LINK OE2 GLU A 169 FE FE A1001 1555 1555 2.17
LINK OE2 GLU A 232 FE FE A1001 1555 1555 1.70
LINK OE1 GLU A 266 FE FE A1001 1555 1555 2.07
LINK OE2 GLU A 266 FE FE A1001 1555 1555 2.20
LINK ND1 HIS A 269 FE FE A1001 1555 1555 2.39
LINK O ARG B 78 MG MG B1002 1555 1555 2.60
LINK O VAL B 81 MG MG B1002 1555 1555 2.44
LINK OG1 THR B 156 MG MG B1002 1555 1555 2.62
LINK OE2 GLU B 169 FE FE B1001 1555 1555 2.15
LINK OE2 GLU B 266 FE FE B1001 1555 1555 2.12
LINK OE1 GLU B 266 FE FE B1001 1555 1555 2.35
LINK ND1 HIS B 269 FE FE B1001 1555 1555 2.36
CISPEP 1 MET A 65 GLY A 66 0 8.04
CISPEP 2 PHE A 83 PRO A 84 0 -2.25
CISPEP 3 MET B 65 GLY B 66 0 0.79
CISPEP 4 PHE B 83 PRO B 84 0 -5.15
SITE 1 AC1 5 GLN A 165 GLU A 169 GLU A 232 GLU A 266
SITE 2 AC1 5 HIS A 269
SITE 1 AC2 3 ARG A 78 VAL A 81 THR A 156
SITE 1 AC3 5 GLN B 165 GLU B 169 GLU B 232 GLU B 266
SITE 2 AC3 5 HIS B 269
SITE 1 AC4 3 ARG B 78 VAL B 81 THR B 156
CRYST1 109.082 109.082 176.523 90.00 90.00 90.00 P 43 21 2 16
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 0.009167 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009167 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005665 0.00000
(ATOM LINES ARE NOT SHOWN.)
END