HEADER OXIDOREDUCTASE 23-MAY-14 4QGN
TITLE HUMAN ACIREDUCTONE DIOXYGENASE WITH IRON ION AND L-METHIONINE IN
TITLE 2 ACTIVE CENTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,2-DIHYDROXY-3-KETO-5-METHYLTHIOPENTENE DIOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACIREDUCTONE DIOXYGENASE (FE(2+)-REQUIRING), ARD, FE-ARD,
COMPND 5 MEMBRANE-TYPE 1 MATRIX METALLOPROTEINASE CYTOPLASMIC TAIL-BINDING
COMPND 6 PROTEIN 1, MTCBP-1, SUBMERGENCE-INDUCED PROTEIN-LIKE FACTOR, SIP-L;
COMPND 7 EC: 1.13.11.54;
COMPND 8 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: ADI1, HMFT1638, MTCBP1, NP_060739;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODONPLUS DE3 RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS RMLC-LIKE CUPIN, OXIDOREDUCTASE, IRON BINDING, 1, 2-DIHYDROXY-5-
KEYWDS 2 (METHYLTHIO)PENT-1-EN-3-ONE DIOXYGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.MILACZEWSKA,M.CHRUSZCZ,J.J.PETKOWSKI,E.NIEDZIALKOWSKA,W.MINOR,
AUTHOR 2 T.BOROWSKI
REVDAT 6 06-DEC-23 4QGN 1 REMARK
REVDAT 5 20-SEP-23 4QGN 1 REMARK
REVDAT 4 09-AUG-23 4QGN 1 JRNL
REVDAT 3 13-APR-22 4QGN 1 AUTHOR JRNL REMARK SEQADV
REVDAT 3 2 1 LINK
REVDAT 2 22-NOV-17 4QGN 1 REMARK
REVDAT 1 27-MAY-15 4QGN 0
JRNL AUTH A.MILACZEWSKA,E.KOT,J.A.AMAYA,T.M.MAKRIS,M.ZAJAC,J.KORECKI,
JRNL AUTH 2 A.CHUMAKOV,B.TRZEWIK,S.KEDRACKA-KROK,W.MINOR,M.CHRUSZCZ,
JRNL AUTH 3 T.BOROWSKI
JRNL TITL ON THE STRUCTURE AND REACTION MECHANISM OF HUMAN
JRNL TITL 2 ACIREDUCTONE DIOXYGENASE.
JRNL REF CHEMISTRY V. 24 5225 2018
JRNL REFN ISSN 0947-6539
JRNL PMID 29193386
JRNL DOI 10.1002/CHEM.201704617
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 4829
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 232
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) : 3.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 333
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 16
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1487
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 26
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.22000
REMARK 3 B22 (A**2) : -3.22000
REMARK 3 B33 (A**2) : 4.84000
REMARK 3 B12 (A**2) : -1.61000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.401
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.287
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.496
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1570 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1090 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2120 ; 1.276 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2617 ; 0.836 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 177 ; 6.629 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 85 ;30.544 ;23.059
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 253 ;16.611 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;14.445 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 212 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1726 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 352 ; 0.002 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8444 -27.0129 -0.4558
REMARK 3 T TENSOR
REMARK 3 T11: 0.0486 T22: 0.0071
REMARK 3 T33: 0.0329 T12: 0.0039
REMARK 3 T13: -0.0077 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.5779 L22: 1.5831
REMARK 3 L33: 0.5637 L12: 0.3508
REMARK 3 L13: -0.1791 L23: 0.0794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: -0.0172 S13: 0.0348
REMARK 3 S21: -0.1248 S22: -0.0603 S23: 0.0809
REMARK 3 S31: -0.0217 S32: -0.0513 S33: 0.0409
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000086030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97912
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR.
REMARK 200 LN2 COOLED FIRST CRYSTAL,
REMARK 200 SAGITTAL FOCUSING 2ND CRYSTAL
REMARK 200 OPTICS : ROSENBAUM-ROCK VERTICAL FOCUSING
REMARK 200 MIRROR, WITH PT, GLASS, PD LANES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO 3000: MOLREP, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK 3000: MOLREP, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5073
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.18200
REMARK 200 R SYM (I) : 0.18200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0370
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.72600
REMARK 200 R SYM FOR SHELL (I) : 0.72600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.118
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: 1VR3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 20 MG/ML IN 50 MM TRIS-HCL PH
REMARK 280 7.8, 150MM NACL, 2.5MM L-SELENOMETHIONINE, CRYSTALLIZATION
REMARK 280 CONDITION: 0.1M SODIUM ACETATE, AMMONIUM SULFATE PH 4.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 13.60733
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 27.21467
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 0.00000
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 13.60733
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 27.21467
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLY A -3
REMARK 465 ALA A -2
REMARK 465 ALA A -1
REMARK 465 ALA A 0
REMARK 465 ALA A 179
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 MET A 1 CG SD CE
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 LYS A 80 CE NZ
REMARK 470 LYS A 82 CD CE NZ
REMARK 470 GLN A 170 CD OE1 NE2
REMARK 470 LYS A 173 CE NZ
REMARK 470 GLN A 177 CG CD OE1 NE2
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 ASN A 48 70.59 -150.23
REMARK 500 ALA A 162 52.70 -148.18
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 FE A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 88 NE2
REMARK 620 2 HIS A 90 NE2 97.6
REMARK 620 3 GLU A 94 OE1 164.8 85.9
REMARK 620 4 HIS A 133 NE2 85.4 96.5 79.5
REMARK 620 5 MSE A 204 O 88.4 160.4 93.1 102.7
REMARK 620 6 MSE A 204 N 135.4 88.7 59.1 137.9 74.2
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 FE A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 209
DBREF 4QGN A 1 179 UNP Q9BV57 MTND_HUMAN 1 179
SEQADV 4QGN GLY A -3 UNP Q9BV57 EXPRESSION TAG
SEQADV 4QGN ALA A -2 UNP Q9BV57 EXPRESSION TAG
SEQADV 4QGN ALA A -1 UNP Q9BV57 EXPRESSION TAG
SEQADV 4QGN ALA A 0 UNP Q9BV57 EXPRESSION TAG
SEQRES 1 A 183 GLY ALA ALA ALA MET VAL GLN ALA TRP TYR MET ASP ASP
SEQRES 2 A 183 ALA PRO GLY ASP PRO ARG GLN PRO HIS ARG PRO ASP PRO
SEQRES 3 A 183 GLY ARG PRO VAL GLY LEU GLU GLN LEU ARG ARG LEU GLY
SEQRES 4 A 183 VAL LEU TYR TRP LYS LEU ASP ALA ASP LYS TYR GLU ASN
SEQRES 5 A 183 ASP PRO GLU LEU GLU LYS ILE ARG ARG GLU ARG ASN TYR
SEQRES 6 A 183 SER TRP MET ASP ILE ILE THR ILE CYS LYS ASP LYS LEU
SEQRES 7 A 183 PRO ASN TYR GLU GLU LYS ILE LYS MET PHE TYR GLU GLU
SEQRES 8 A 183 HIS LEU HIS LEU ASP ASP GLU ILE ARG TYR ILE LEU ASP
SEQRES 9 A 183 GLY SER GLY TYR PHE ASP VAL ARG ASP LYS GLU ASP GLN
SEQRES 10 A 183 TRP ILE ARG ILE PHE MET GLU LYS GLY ASP MET VAL THR
SEQRES 11 A 183 LEU PRO ALA GLY ILE TYR HIS ARG PHE THR VAL ASP GLU
SEQRES 12 A 183 LYS ASN TYR THR LYS ALA MET ARG LEU PHE VAL GLY GLU
SEQRES 13 A 183 PRO VAL TRP THR ALA TYR ASN ARG PRO ALA ASP HIS PHE
SEQRES 14 A 183 GLU ALA ARG GLY GLN TYR VAL LYS PHE LEU ALA GLN THR
SEQRES 15 A 183 ALA
HET FE A 201 1
HET CL A 202 1
HET CL A 203 1
HET MSE A 204 14
HET SO4 A 205 5
HET SO4 A 206 5
HET SO4 A 207 5
HET SO4 A 208 5
HET ACT A 209 4
HETNAM FE FE (III) ION
HETNAM CL CHLORIDE ION
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
FORMUL 2 FE FE 3+
FORMUL 3 CL 2(CL 1-)
FORMUL 5 MSE C5 H11 N O2 SE
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 10 ACT C2 H3 O2 1-
FORMUL 11 HOH *26(H2 O)
HELIX 1 1 GLY A 27 ARG A 33 1 7
HELIX 2 2 LYS A 45 ASN A 48 5 4
HELIX 3 3 ASP A 49 ARG A 59 1 11
HELIX 4 4 ASN A 76 GLU A 86 1 11
HELIX 5 5 PHE A 165 GLN A 177 1 13
SHEET 1 A 4 ALA A 4 TYR A 6 0
SHEET 2 A 4 TRP A 114 MET A 119 -1 O ARG A 116 N TRP A 5
SHEET 3 A 4 GLY A 103 ARG A 108 -1 N VAL A 107 O ILE A 115
SHEET 4 A 4 HIS A 133 VAL A 137 -1 O THR A 136 N TYR A 104
SHEET 1 B 5 LEU A 37 LYS A 40 0
SHEET 2 B 5 ASP A 123 LEU A 127 -1 O MET A 124 N TRP A 39
SHEET 3 B 5 GLU A 94 GLY A 101 -1 N GLU A 94 O LEU A 127
SHEET 4 B 5 THR A 143 PHE A 149 -1 O LYS A 144 N ASP A 100
SHEET 5 B 5 TRP A 63 ILE A 69 -1 N ILE A 69 O THR A 143
SHEET 1 C 2 HIS A 88 LEU A 89 0
SHEET 2 C 2 TYR A 158 ASN A 159 -1 O TYR A 158 N LEU A 89
LINK NE2 HIS A 88 FE FE A 201 1555 1555 2.23
LINK NE2 HIS A 90 FE FE A 201 1555 1555 2.19
LINK OE1 GLU A 94 FE FE A 201 1555 1555 2.28
LINK NE2 HIS A 133 FE FE A 201 1555 1555 2.19
LINK FE FE A 201 O MSE A 204 1555 1555 2.16
LINK FE FE A 201 N MSE A 204 1555 1555 2.22
CISPEP 1 ASP A 21 PRO A 22 0 4.98
CISPEP 2 ARG A 160 PRO A 161 0 -6.85
SITE 1 AC1 5 HIS A 88 HIS A 90 GLU A 94 HIS A 133
SITE 2 AC1 5 MSE A 204
SITE 1 AC2 2 ARG A 96 MSE A 204
SITE 1 AC3 2 ASN A 76 TYR A 77
SITE 1 AC4 5 TRP A 5 ARG A 19 GLY A 23 ARG A 24
SITE 2 AC4 5 PRO A 25
SITE 1 AC5 5 ARG A 24 ARG A 56 SER A 62 MET A 64
SITE 2 AC5 5 HOH A 315
SITE 1 AC6 4 GLY A 12 ASP A 13 GLU A 53 ARG A 57
SITE 1 AC7 2 ARG A 108 TRP A 114
SITE 1 AC8 5 ASP A 93 GLU A 94 ARG A 96 PHE A 149
SITE 2 AC8 5 MSE A 204
CRYST1 105.195 105.195 40.822 90.00 90.00 120.00 P 64 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 0.009506 0.005488 0.000000 0.00000
SCALE2 0.000000 0.010977 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024497 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
