HEADER OXIDOREDUCTASE 13-SEP-12 4H3E
TITLE CRYSTAL STRUCTURE OF A PUTATIVE IRON SUPEROXIDE DISMUTASE FROM
TITLE 2 TRYPANOSOMA CRUZI BOUND TO IRON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FESOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 353153;
SOURCE 4 STRAIN: CL BRENER;
SOURCE 5 GENE: TC00.1047053509775.40;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAVA0421
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 3 INFECTIOUS DISEASE, SSGCID, RADICAL OXYGEN SPECIES, TRYPANOSOMIASIS,
KEYWDS 4 PARASITIC EUGLENOID TRYPANOSOME, CHAGAS DISEASE, RADICAL SCAVENGER,
KEYWDS 5 HYDROGEN PEROXIDE, ANTIOXIDANT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 26-SEP-12 4H3E 0
JRNL AUTH T.E.EDWARDS,M.C.CLIFTON,
JRNL AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 3 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE IRON SUPEROXIDE DISMUTASE
JRNL TITL 2 FROM TRYPANOSOMA CRUZI BOUND TO IRON
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 44.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 19189
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1038
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) : 1368
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3350
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 348
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : 0.35000
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): 0.364
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.698
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3456 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3150 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4712 ; 1.407 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7242 ; 1.008 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 428 ; 6.073 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 161 ;38.245 ;24.534
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 517 ;12.935 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;11.965 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 499 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3993 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 841 ; 0.004 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 20 233 B 20 233 12529
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 20 A 233
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2983 1.0483 6.1511
REMARK 3 T TENSOR
REMARK 3 T11: 0.0531 T22: 0.0108
REMARK 3 T33: 0.0024 T12: 0.0000
REMARK 3 T13: -0.0076 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.6030 L22: 0.2751
REMARK 3 L33: 0.1527 L12: -0.0847
REMARK 3 L13: 0.0463 L23: -0.0099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: 0.0231 S13: -0.0274
REMARK 3 S21: -0.0343 S22: -0.0256 S23: 0.0054
REMARK 3 S31: -0.0137 S32: -0.0050 S33: -0.0031
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 20 B 233
REMARK 3 RESIDUE RANGE : B 301 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5696 11.2692 31.6990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0306 T22: 0.0120
REMARK 3 T33: 0.0273 T12: 0.0022
REMARK 3 T13: -0.0133 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.4817 L22: 0.2454
REMARK 3 L33: 0.2134 L12: -0.1651
REMARK 3 L13: -0.1367 L23: -0.0257
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0289 S13: 0.0100
REMARK 3 S21: 0.0047 S22: 0.0275 S23: -0.0346
REMARK 3 S31: -0.0024 S32: -0.0133 S33: -0.0162
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:
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4H3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074968.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20226
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
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) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.990
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: PDB ENTRY 4F2N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRCRA.00198.B.B1 PS01521 AT 23.05 MG/
REMARK 280 ML AGAINST JCSG+ SCREEN CONDITION G1: 0.1 M HEPES, PH 7.0, 30%
REMARK 280 JEFFAMINE ED-2001, CRYSTAL TRACKING ID 235439G1, UNIQUE PUCK ID
REMARK 280 GVR7-6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 23.82500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.84000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.82500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.84000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 ARG A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
REMARK 465 VAL A 6
REMARK 465 ASN A 7
REMARK 465 ILE A 8
REMARK 465 SER A 9
REMARK 465 ILE A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 GLY A 13
REMARK 465 ARG A 14
REMARK 465 MET A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 MET A 18
REMARK 465 SER A 19
REMARK 465 MET B -7
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ARG B 3
REMARK 465 ARG B 4
REMARK 465 ALA B 5
REMARK 465 VAL B 6
REMARK 465 ASN B 7
REMARK 465 ILE B 8
REMARK 465 SER B 9
REMARK 465 ILE B 10
REMARK 465 ALA B 11
REMARK 465 ARG B 12
REMARK 465 GLY B 13
REMARK 465 ARG B 14
REMARK 465 MET B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 MET B 18
REMARK 465 SER B 19
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 LYS A 38 CG CD CE NZ
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 LYS B 97 CG CD CE NZ
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 GLN B 148 CG CD OE1 NE2
REMARK 470 GLN B 170 CG CD OE1 NE2
REMARK 470 LYS B 226 CG CD CE NZ
REMARK 470 GLN B 230 CG CD OE1 NE2
REMARK 470 LYS B 233 CG CD CE NZ
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 207 NE - CZ - NH1 ANGL. DEV. = 3.0 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 LYS A 62 -63.95 -107.86
REMARK 500 ASN A 178 -112.52 62.88
REMARK 500 GLU A 205 -130.73 51.71
REMARK 500 LYS B 62 -63.21 -109.52
REMARK 500 ASN B 178 -111.63 59.51
REMARK 500 GLU B 205 -131.12 50.69
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 B 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 194 OD2
REMARK 620 2 HIS B 110 NE2 118.1
REMARK 620 3 HIS B 198 NE2 122.0 119.8
REMARK 620 4 HOH B 402 O 90.3 89.8 87.4
REMARK 620 5 HIS B 59 NE2 81.1 95.9 95.6 171.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 194 OD2
REMARK 620 2 HIS A 198 NE2 123.0
REMARK 620 3 HIS A 110 NE2 116.0 120.3
REMARK 620 4 HIS A 59 NE2 79.9 99.4 98.6
REMARK 620 5 HOH A 402 O 86.3 86.3 89.5 166.0
REMARK 620 N 1 2 3 4
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F2N RELATED DB: PDB
REMARK 900 FESOD FROM L. MAJOR
REMARK 900 RELATED ID: SSGCID-TRCRA.00198.B RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 L128F IS A NATURAL VARIANT.
DBREF 4H3E A 1 233 UNP Q4DCQ3 Q4DCQ3_TRYCC 1 233
DBREF 4H3E B 1 233 UNP Q4DCQ3 Q4DCQ3_TRYCC 1 233
SEQADV 4H3E MET A -7 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E ALA A -6 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS A -5 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS A -4 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS A -3 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS A -2 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS A -1 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS A 0 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E PHE A 128 UNP Q4DCQ3 LEU 128 SEE REMARK 999
SEQADV 4H3E MET B -7 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E ALA B -6 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS B -5 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS B -4 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS B -3 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS B -2 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS B -1 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E HIS B 0 UNP Q4DCQ3 EXPRESSION TAG
SEQADV 4H3E PHE B 128 UNP Q4DCQ3 LEU 128 SEE REMARK 999
SEQRES 1 A 241 MET ALA HIS HIS HIS HIS HIS HIS MET LEU ARG ARG ALA
SEQRES 2 A 241 VAL ASN ILE SER ILE ALA ARG GLY ARG MET ALA LEU MET
SEQRES 3 A 241 SER TYR ALA THR LEU PRO ASP LEU LEU LYS PRO SER GLY
SEQRES 4 A 241 ALA PRO ALA GLU LEU PRO LYS LEU GLY PHE ASN TRP LYS
SEQRES 5 A 241 ASP GLY CYS ALA PRO VAL PHE SER PRO ARG GLN MET GLU
SEQRES 6 A 241 LEU HIS TYR THR LYS HIS HIS LYS ALA TYR VAL ASP LYS
SEQRES 7 A 241 LEU ASN ALA LEU ALA GLY THR THR TYR ASP GLY LYS SER
SEQRES 8 A 241 ILE GLU GLU ILE ILE LEU ALA VAL ALA ASN ASP ALA GLU
SEQRES 9 A 241 LYS LYS GLY LEU PHE ASN GLN ALA ALA GLN HIS PHE ASN
SEQRES 10 A 241 HIS THR PHE TYR PHE ARG CYS ILE THR PRO ASN GLY LYS
SEQRES 11 A 241 ALA MET PRO LYS SER PHE GLU SER ALA VAL THR ALA GLN
SEQRES 12 A 241 PHE GLY SER VAL GLU GLN PHE LYS ASP ALA PHE VAL GLN
SEQRES 13 A 241 ALA GLY VAL ASN ASN PHE GLY SER GLY TRP THR TRP LEU
SEQRES 14 A 241 CYS VAL ASP PRO SER ASN LYS ASN GLN LEU VAL ILE ASP
SEQRES 15 A 241 ASN THR SER ASN ALA GLY CYS PRO LEU THR LYS GLY LEU
SEQRES 16 A 241 ARG PRO VAL LEU ALA VAL ASP VAL TRP GLU HIS ALA TYR
SEQRES 17 A 241 TYR LYS ASP PHE GLU ASN ARG ARG PRO ASP TYR LEU LYS
SEQRES 18 A 241 GLU ILE TRP SER VAL ILE ASP TRP GLU PHE VAL ALA LYS
SEQRES 19 A 241 MET HIS ALA GLN ALA ILE LYS
SEQRES 1 B 241 MET ALA HIS HIS HIS HIS HIS HIS MET LEU ARG ARG ALA
SEQRES 2 B 241 VAL ASN ILE SER ILE ALA ARG GLY ARG MET ALA LEU MET
SEQRES 3 B 241 SER TYR ALA THR LEU PRO ASP LEU LEU LYS PRO SER GLY
SEQRES 4 B 241 ALA PRO ALA GLU LEU PRO LYS LEU GLY PHE ASN TRP LYS
SEQRES 5 B 241 ASP GLY CYS ALA PRO VAL PHE SER PRO ARG GLN MET GLU
SEQRES 6 B 241 LEU HIS TYR THR LYS HIS HIS LYS ALA TYR VAL ASP LYS
SEQRES 7 B 241 LEU ASN ALA LEU ALA GLY THR THR TYR ASP GLY LYS SER
SEQRES 8 B 241 ILE GLU GLU ILE ILE LEU ALA VAL ALA ASN ASP ALA GLU
SEQRES 9 B 241 LYS LYS GLY LEU PHE ASN GLN ALA ALA GLN HIS PHE ASN
SEQRES 10 B 241 HIS THR PHE TYR PHE ARG CYS ILE THR PRO ASN GLY LYS
SEQRES 11 B 241 ALA MET PRO LYS SER PHE GLU SER ALA VAL THR ALA GLN
SEQRES 12 B 241 PHE GLY SER VAL GLU GLN PHE LYS ASP ALA PHE VAL GLN
SEQRES 13 B 241 ALA GLY VAL ASN ASN PHE GLY SER GLY TRP THR TRP LEU
SEQRES 14 B 241 CYS VAL ASP PRO SER ASN LYS ASN GLN LEU VAL ILE ASP
SEQRES 15 B 241 ASN THR SER ASN ALA GLY CYS PRO LEU THR LYS GLY LEU
SEQRES 16 B 241 ARG PRO VAL LEU ALA VAL ASP VAL TRP GLU HIS ALA TYR
SEQRES 17 B 241 TYR LYS ASP PHE GLU ASN ARG ARG PRO ASP TYR LEU LYS
SEQRES 18 B 241 GLU ILE TRP SER VAL ILE ASP TRP GLU PHE VAL ALA LYS
SEQRES 19 B 241 MET HIS ALA GLN ALA ILE LYS
HET FE2 A 301 1
HET FE2 B 301 1
HETNAM FE2 FE (II) ION
FORMUL 3 FE2 2(FE 2+)
FORMUL 5 HOH *348(H2 O)
HELIX 1 1 ASN A 42 GLY A 46 5 5
HELIX 2 2 SER A 52 LYS A 62 1 11
HELIX 3 3 LYS A 62 GLY A 76 1 15
HELIX 4 4 SER A 83 ALA A 92 1 10
HELIX 5 5 ASP A 94 GLU A 96 5 3
HELIX 6 6 LYS A 97 CYS A 116 1 20
HELIX 7 7 PRO A 125 GLY A 137 1 13
HELIX 8 8 SER A 138 ASN A 152 1 15
HELIX 9 9 PRO A 165 LYS A 168 5 4
HELIX 10 10 CYS A 181 GLY A 186 5 6
HELIX 11 11 TRP A 196 ALA A 199 5 4
HELIX 12 12 TYR A 200 GLU A 205 1 6
HELIX 13 13 ARG A 207 ILE A 215 1 9
HELIX 14 14 TRP A 216 ILE A 219 5 4
HELIX 15 15 ASP A 220 LYS A 233 1 14
HELIX 16 16 ASN B 42 GLY B 46 5 5
HELIX 17 17 SER B 52 LYS B 62 1 11
HELIX 18 18 LYS B 62 GLY B 76 1 15
HELIX 19 19 SER B 83 ALA B 92 1 10
HELIX 20 20 ASP B 94 GLU B 96 5 3
HELIX 21 21 LYS B 97 CYS B 116 1 20
HELIX 22 22 PRO B 125 GLY B 137 1 13
HELIX 23 23 SER B 138 ASN B 152 1 15
HELIX 24 24 PRO B 165 LYS B 168 5 4
HELIX 25 25 CYS B 181 GLY B 186 5 6
HELIX 26 26 TRP B 196 ALA B 199 5 4
HELIX 27 27 TYR B 200 GLU B 205 1 6
HELIX 28 28 ARG B 207 ILE B 215 1 9
HELIX 29 29 TRP B 216 ILE B 219 5 4
HELIX 30 30 ASP B 220 LYS B 233 1 14
SHEET 1 A 3 LEU A 171 SER A 177 0
SHEET 2 A 3 GLY A 157 VAL A 163 -1 N CYS A 162 O VAL A 172
SHEET 3 A 3 ARG A 188 ASP A 194 -1 O VAL A 190 N LEU A 161
SHEET 1 B 3 LEU B 171 SER B 177 0
SHEET 2 B 3 GLY B 157 VAL B 163 -1 N CYS B 162 O VAL B 172
SHEET 3 B 3 ARG B 188 ASP B 194 -1 O VAL B 190 N LEU B 161
LINK OD2 ASP B 194 FE FE2 B 301 1555 1555 1.94
LINK OD2 ASP A 194 FE FE2 A 301 1555 1555 2.01
LINK NE2 HIS B 110 FE FE2 B 301 1555 1555 2.14
LINK NE2 HIS B 198 FE FE2 B 301 1555 1555 2.15
LINK NE2 HIS A 198 FE FE2 A 301 1555 1555 2.15
LINK NE2 HIS A 110 FE FE2 A 301 1555 1555 2.16
LINK NE2 HIS A 59 FE FE2 A 301 1555 1555 2.26
LINK FE FE2 B 301 O HOH B 402 1555 1555 2.30
LINK FE FE2 A 301 O HOH A 402 1555 1555 2.32
LINK NE2 HIS B 59 FE FE2 B 301 1555 1555 2.33
CISPEP 1 ALA A 48 PRO A 49 0 4.54
CISPEP 2 ALA B 48 PRO B 49 0 2.10
SITE 1 AC1 5 HIS A 59 HIS A 110 ASP A 194 HIS A 198
SITE 2 AC1 5 HOH A 402
SITE 1 AC2 5 HIS B 59 HIS B 110 ASP B 194 HIS B 198
SITE 2 AC2 5 HOH B 402
CRYST1 47.650 75.680 117.450 90.00 90.00 90.00 P 21 21 21 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 0.020986 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013214 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008514 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
