HEADER OXIDOREDUCTASE 03-DEC-04 1Y67
TITLE CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE DISMUTASE FROM
TITLE 2 DEINOCOCCUS RADIODURANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MNSOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: SODA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS SUPEROXIDE DISMUTASE, MANGANESE ENZYME, METALLOPROTEIN,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CHAN,S.TANAKA,M.R.SAWAYA,L.J.PERRY
REVDAT 2 24-FEB-09 1Y67 1 VERSN
REVDAT 1 21-DEC-04 1Y67 0
JRNL AUTH S.CHAN,S.TANAKA,M.R.SAWAYA,L.J.PERRY
JRNL TITL CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE
JRNL TITL 2 DISMUTASE FROM DEINOCOCCUS RADIODURANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.N.MURSHUDOV
REMARK 1 TITL REFINEMENT OF MACROMOLECULAR STRUCTURES BY THE
REMARK 1 TITL 2 MAXIMUM-LIKELIHOOD METHOD
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 53 240 1997
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 119.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 74526
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.961
REMARK 3 FREE R VALUE TEST SET COUNT : 3697
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5071
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 266
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6565
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.90300
REMARK 3 B22 (A**2) : -0.95900
REMARK 3 B33 (A**2) : -1.01600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.79700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6743 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9172 ; 1.093 ; 1.918
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 825 ; 5.212 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 352 ;35.443 ;24.830
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1029 ;12.946 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;12.197 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 953 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5333 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2992 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4663 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 420 ; 0.106 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.025 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 36 ; 0.141 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.117 ; 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): 4241 ; 0.540 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6570 ; 0.862 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2933 ; 1.446 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2602 ; 2.279 ; 4.500
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 : 4
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 1 A 93
REMARK 3 RESIDUE RANGE : A 97 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9494 16.4962 14.2350
REMARK 3 T TENSOR
REMARK 3 T11: -0.1359 T22: -0.1242
REMARK 3 T33: -0.1349 T12: -0.0249
REMARK 3 T13: 0.0135 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.6603 L22: 2.4764
REMARK 3 L33: 1.5235 L12: 0.3411
REMARK 3 L13: 0.5030 L23: 0.3781
REMARK 3 S TENSOR
REMARK 3 S11: -0.0502 S12: -0.0190 S13: 0.0351
REMARK 3 S21: -0.3158 S22: 0.0077 S23: 0.0475
REMARK 3 S31: -0.0491 S32: 0.0661 S33: 0.0424
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 1 B 90
REMARK 3 RESIDUE RANGE : B 98 B 211
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3050 27.9594 39.7315
REMARK 3 T TENSOR
REMARK 3 T11: -0.1419 T22: -0.1051
REMARK 3 T33: -0.1491 T12: -0.0441
REMARK 3 T13: -0.0023 T23: -0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 1.4630 L22: 1.9144
REMARK 3 L33: 2.5240 L12: 0.2652
REMARK 3 L13: 1.1158 L23: 0.1777
REMARK 3 S TENSOR
REMARK 3 S11: -0.1047 S12: -0.0825 S13: 0.1760
REMARK 3 S21: 0.1919 S22: -0.0810 S23: -0.0461
REMARK 3 S31: -0.2949 S32: 0.0107 S33: 0.1857
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 89
REMARK 3 RESIDUE RANGE : C 98 C 213
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3888 26.4932 72.5899
REMARK 3 T TENSOR
REMARK 3 T11: -0.1447 T22: -0.0939
REMARK 3 T33: -0.1608 T12: -0.0044
REMARK 3 T13: -0.0157 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.2965 L22: 2.0345
REMARK 3 L33: 2.3783 L12: 0.3248
REMARK 3 L13: 0.4772 L23: 1.1512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0355 S12: 0.2108 S13: -0.0167
REMARK 3 S21: -0.1621 S22: 0.1460 S23: -0.0671
REMARK 3 S31: 0.0003 S32: 0.0197 S33: -0.1815
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 215
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9661 18.7900 100.5325
REMARK 3 T TENSOR
REMARK 3 T11: 0.0373 T22: -0.2063
REMARK 3 T33: -0.1173 T12: -0.0063
REMARK 3 T13: -0.1017 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.2085 L22: 1.3554
REMARK 3 L33: 1.7743 L12: 0.1924
REMARK 3 L13: 0.5607 L23: 0.3588
REMARK 3 S TENSOR
REMARK 3 S11: 0.1723 S12: 0.0062 S13: -0.1939
REMARK 3 S21: 0.3459 S22: 0.0118 S23: -0.1297
REMARK 3 S31: 0.3405 S32: -0.0201 S33: -0.1841
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1Y67 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-04.
REMARK 100 THE RCSB ID CODE IS RCSB031166.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74526
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 119.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1VEW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM ACETATE (PH 7.1) 20%
REMARK 280 (W/V) PEG3350, 0.3M NACL, 0.3M IMIDAZOLE, 20MM TRIS (PH 8.0),
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.96100
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER FORMED FROM EITHER
REMARK 300 CHAINS A AND B OR CHAINS C AND D.
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, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 0
REMARK 465 GLN A 94
REMARK 465 ASN A 95
REMARK 465 GLY A 96
REMARK 465 PRO A 214
REMARK 465 ARG A 215
REMARK 465 GLY A 216
REMARK 465 SER A 217
REMARK 465 ALA A 218
REMARK 465 ALA A 219
REMARK 465 ALA A 220
REMARK 465 LEU A 221
REMARK 465 GLU A 222
REMARK 465 HIS A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
REMARK 465 HIS A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 MET B 0
REMARK 465 GLY B 91
REMARK 465 GLN B 92
REMARK 465 GLY B 93
REMARK 465 GLN B 94
REMARK 465 ASN B 95
REMARK 465 GLY B 96
REMARK 465 ALA B 97
REMARK 465 LEU B 212
REMARK 465 VAL B 213
REMARK 465 PRO B 214
REMARK 465 ARG B 215
REMARK 465 GLY B 216
REMARK 465 SER B 217
REMARK 465 ALA B 218
REMARK 465 ALA B 219
REMARK 465 ALA B 220
REMARK 465 LEU B 221
REMARK 465 GLU B 222
REMARK 465 HIS B 223
REMARK 465 HIS B 224
REMARK 465 HIS B 225
REMARK 465 HIS B 226
REMARK 465 HIS B 227
REMARK 465 HIS B 228
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 GLN C 90
REMARK 465 GLY C 91
REMARK 465 GLN C 92
REMARK 465 GLY C 93
REMARK 465 GLN C 94
REMARK 465 ASN C 95
REMARK 465 GLY C 96
REMARK 465 ALA C 97
REMARK 465 PRO C 214
REMARK 465 ARG C 215
REMARK 465 GLY C 216
REMARK 465 SER C 217
REMARK 465 ALA C 218
REMARK 465 ALA C 219
REMARK 465 ALA C 220
REMARK 465 LEU C 221
REMARK 465 GLU C 222
REMARK 465 HIS C 223
REMARK 465 HIS C 224
REMARK 465 HIS C 225
REMARK 465 HIS C 226
REMARK 465 HIS C 227
REMARK 465 HIS C 228
REMARK 465 MET D 0
REMARK 465 ALA D 1
REMARK 465 GLY D 216
REMARK 465 SER D 217
REMARK 465 ALA D 218
REMARK 465 ALA D 219
REMARK 465 ALA D 220
REMARK 465 LEU D 221
REMARK 465 GLU D 222
REMARK 465 HIS D 223
REMARK 465 HIS D 224
REMARK 465 HIS D 225
REMARK 465 HIS D 226
REMARK 465 HIS D 227
REMARK 465 HIS D 228
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 151 -119.84 54.84
REMARK 500 TYR A 179 -10.57 -141.12
REMARK 500 GLN A 184 -126.64 48.94
REMARK 500 ASN B 151 -120.87 50.86
REMARK 500 TYR B 179 -8.17 -142.01
REMARK 500 GLN B 184 -127.30 48.36
REMARK 500 LYS C 30 -60.36 -109.56
REMARK 500 ASN C 151 -120.94 53.93
REMARK 500 TYR C 179 -8.92 -140.51
REMARK 500 GLN C 184 -129.18 50.96
REMARK 500 PRO D 9 1.74 -69.78
REMARK 500 LYS D 30 -65.23 -104.87
REMARK 500 ASN D 95 69.27 20.71
REMARK 500 ASN D 151 -119.02 54.00
REMARK 500 TYR D 179 -6.98 -141.54
REMARK 500 GLN D 184 -127.64 48.43
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 229 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 27 NE2
REMARK 620 2 HIS A 81 NE2 88.3
REMARK 620 3 ASP A 173 OD2 88.0 108.7
REMARK 620 4 HIS A 177 NE2 97.8 134.8 116.2
REMARK 620 5 HOH A 233 O 170.8 89.4 84.2 90.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 229 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 27 NE2
REMARK 620 2 HIS B 81 NE2 85.0
REMARK 620 3 ASP B 173 OD2 84.4 109.1
REMARK 620 4 HIS B 177 NE2 99.0 136.3 114.6
REMARK 620 5 HOH B 230 O 168.2 93.8 85.0 90.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 229 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 27 NE2
REMARK 620 2 HIS C 81 NE2 86.5
REMARK 620 3 ASP C 173 OD2 89.9 106.6
REMARK 620 4 HIS C 177 NE2 95.5 134.4 118.9
REMARK 620 5 HOH C 230 O 171.9 91.7 83.1 91.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 229 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 27 NE2
REMARK 620 2 HIS D 81 NE2 84.8
REMARK 620 3 ASP D 173 OD2 85.7 109.0
REMARK 620 4 HIS D 177 NE2 94.1 135.8 115.0
REMARK 620 5 HOH D 234 O 169.9 94.6 84.9 93.3
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 FE A 229
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 229
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 229
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 229
DBREF 1Y67 A 2 211 UNP Q9RUV2 SODM_DEIRA 1 210
DBREF 1Y67 B 2 211 UNP Q9RUV2 SODM_DEIRA 1 210
DBREF 1Y67 C 2 211 UNP Q9RUV2 SODM_DEIRA 1 210
DBREF 1Y67 D 2 211 UNP Q9RUV2 SODM_DEIRA 1 210
SEQADV 1Y67 MET A 0 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA A 1 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU A 212 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 VAL A 213 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 PRO A 214 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ARG A 215 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLY A 216 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 SER A 217 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA A 218 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA A 219 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA A 220 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU A 221 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLU A 222 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS A 223 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS A 224 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS A 225 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS A 226 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS A 227 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS A 228 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 MET B 0 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA B 1 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU B 212 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 VAL B 213 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 PRO B 214 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ARG B 215 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLY B 216 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 SER B 217 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA B 218 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA B 219 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA B 220 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU B 221 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLU B 222 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS B 223 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS B 224 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS B 225 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS B 226 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS B 227 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS B 228 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 MET C 0 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA C 1 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU C 212 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 VAL C 213 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 PRO C 214 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ARG C 215 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLY C 216 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 SER C 217 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA C 218 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA C 219 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA C 220 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU C 221 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLU C 222 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS C 223 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS C 224 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS C 225 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS C 226 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS C 227 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS C 228 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 MET D 0 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA D 1 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU D 212 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 VAL D 213 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 PRO D 214 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ARG D 215 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLY D 216 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 SER D 217 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA D 218 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA D 219 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 ALA D 220 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 LEU D 221 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 GLU D 222 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS D 223 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS D 224 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS D 225 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS D 226 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS D 227 UNP Q9RUV2 EXPRESSION TAG
SEQADV 1Y67 HIS D 228 UNP Q9RUV2 EXPRESSION TAG
SEQRES 1 A 229 MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR
SEQRES 2 A 229 ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU
SEQRES 3 A 229 ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN
SEQRES 4 A 229 ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU
SEQRES 5 A 229 PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO
SEQRES 6 A 229 ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY
SEQRES 7 A 229 HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN
SEQRES 8 A 229 GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU
SEQRES 9 A 229 LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP
SEQRES 10 A 229 ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG
SEQRES 11 A 229 PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY
SEQRES 12 A 229 LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO
SEQRES 13 A 229 LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO
SEQRES 14 A 229 ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU
SEQRES 15 A 229 ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE
SEQRES 16 A 229 TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR
SEQRES 17 A 229 ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA
SEQRES 18 A 229 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 229 MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR
SEQRES 2 B 229 ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU
SEQRES 3 B 229 ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN
SEQRES 4 B 229 ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU
SEQRES 5 B 229 PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO
SEQRES 6 B 229 ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY
SEQRES 7 B 229 HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN
SEQRES 8 B 229 GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU
SEQRES 9 B 229 LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP
SEQRES 10 B 229 ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG
SEQRES 11 B 229 PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY
SEQRES 12 B 229 LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO
SEQRES 13 B 229 LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO
SEQRES 14 B 229 ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU
SEQRES 15 B 229 ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE
SEQRES 16 B 229 TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR
SEQRES 17 B 229 ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA
SEQRES 18 B 229 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 229 MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR
SEQRES 2 C 229 ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU
SEQRES 3 C 229 ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN
SEQRES 4 C 229 ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU
SEQRES 5 C 229 PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO
SEQRES 6 C 229 ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY
SEQRES 7 C 229 HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN
SEQRES 8 C 229 GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU
SEQRES 9 C 229 LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP
SEQRES 10 C 229 ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG
SEQRES 11 C 229 PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY
SEQRES 12 C 229 LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO
SEQRES 13 C 229 LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO
SEQRES 14 C 229 ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU
SEQRES 15 C 229 ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE
SEQRES 16 C 229 TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR
SEQRES 17 C 229 ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA
SEQRES 18 C 229 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 229 MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR
SEQRES 2 D 229 ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU
SEQRES 3 D 229 ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN
SEQRES 4 D 229 ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU
SEQRES 5 D 229 PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO
SEQRES 6 D 229 ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY
SEQRES 7 D 229 HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN
SEQRES 8 D 229 GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU
SEQRES 9 D 229 LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP
SEQRES 10 D 229 ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG
SEQRES 11 D 229 PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY
SEQRES 12 D 229 LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO
SEQRES 13 D 229 LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO
SEQRES 14 D 229 ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU
SEQRES 15 D 229 ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE
SEQRES 16 D 229 TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR
SEQRES 17 D 229 ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA
SEQRES 18 D 229 LEU GLU HIS HIS HIS HIS HIS HIS
HET FE A 229 1
HET FE B 229 1
HET FE C 229 1
HET FE D 229 1
HETNAM FE FE (III) ION
FORMUL 5 FE 4(FE 3+)
FORMUL 9 HOH *396(H2 O)
HELIX 1 1 ASP A 20 LYS A 30 1 11
HELIX 2 2 LYS A 30 GLU A 44 1 15
HELIX 3 3 PRO A 52 ILE A 57 1 6
HELIX 4 4 PRO A 64 ILE A 87 1 24
HELIX 5 5 SER A 101 GLY A 113 1 13
HELIX 6 6 SER A 114 ARG A 129 1 16
HELIX 7 7 ASN A 154 MET A 157 5 4
HELIX 8 8 GLY A 158 GLY A 163 1 6
HELIX 9 9 TRP A 175 ALA A 178 5 4
HELIX 10 10 TYR A 179 GLN A 184 1 6
HELIX 11 11 ARG A 186 TRP A 195 1 10
HELIX 12 12 ASN A 199 LEU A 212 1 14
HELIX 13 13 ASP B 20 LYS B 30 1 11
HELIX 14 14 LYS B 30 GLU B 44 1 15
HELIX 15 15 PRO B 52 ILE B 57 1 6
HELIX 16 16 LYS B 67 ILE B 87 1 21
HELIX 17 17 SER B 101 GLY B 113 1 13
HELIX 18 18 SER B 114 THR B 128 1 15
HELIX 19 19 ASN B 154 MET B 157 5 4
HELIX 20 20 GLY B 158 GLY B 163 1 6
HELIX 21 21 TRP B 175 ALA B 178 5 4
HELIX 22 22 TYR B 179 GLN B 184 1 6
HELIX 23 23 ARG B 186 TRP B 195 1 10
HELIX 24 24 ASN B 199 LYS B 211 1 13
HELIX 25 25 ASP C 20 LYS C 30 1 11
HELIX 26 26 LYS C 30 GLU C 44 1 15
HELIX 27 27 PRO C 52 ILE C 57 1 6
HELIX 28 28 PRO C 64 ILE C 87 1 24
HELIX 29 29 SER C 101 GLY C 113 1 13
HELIX 30 30 SER C 114 ARG C 129 1 16
HELIX 31 31 ASN C 154 MET C 157 5 4
HELIX 32 32 GLY C 158 GLY C 163 1 6
HELIX 33 33 TRP C 175 ALA C 178 5 4
HELIX 34 34 TYR C 179 GLN C 184 1 6
HELIX 35 35 ARG C 186 TRP C 195 1 10
HELIX 36 36 ASN C 199 LEU C 212 1 14
HELIX 37 37 ASP D 20 LYS D 30 1 11
HELIX 38 38 LYS D 30 GLU D 44 1 15
HELIX 39 39 PRO D 52 ILE D 57 1 6
HELIX 40 40 PRO D 64 ASP D 66 5 3
HELIX 41 41 LYS D 67 ILE D 87 1 21
HELIX 42 42 SER D 101 GLY D 113 1 13
HELIX 43 43 SER D 114 ARG D 129 1 16
HELIX 44 44 ASN D 154 MET D 157 5 4
HELIX 45 45 GLY D 158 GLY D 163 1 6
HELIX 46 46 TRP D 175 ALA D 178 5 4
HELIX 47 47 TYR D 179 GLN D 184 1 6
HELIX 48 48 ARG D 186 TRP D 195 1 10
HELIX 49 49 ASN D 196 VAL D 198 5 3
HELIX 50 50 ASN D 199 LYS D 211 1 13
SHEET 1 A 3 LYS A 143 ALA A 150 0
SHEET 2 A 3 GLY A 133 LYS A 140 -1 N LYS A 140 O LYS A 143
SHEET 3 A 3 THR A 167 ASP A 173 -1 O ILE A 169 N LEU A 137
SHEET 1 B 3 LYS A 143 ALA A 150 0
SHEET 2 B 3 GLY A 133 LYS A 140 -1 N TRP A 136 O VAL A 147
SHEET 3 B 3 THR A 167 ASP A 173 -1 O THR A 167 N VAL A 139
SHEET 1 C 3 LYS A 143 ALA A 150 0
SHEET 2 C 3 GLY A 133 LYS A 140 -1 N LYS A 140 O LYS A 143
SHEET 3 C 3 THR A 167 ASP A 173 -1 O ILE A 169 N LEU A 137
SHEET 1 D 3 LYS A 143 ALA A 150 0
SHEET 2 D 3 GLY A 133 LYS A 140 -1 N TRP A 136 O VAL A 147
SHEET 3 D 3 THR A 167 ASP A 173 -1 O LEU A 170 N LEU A 137
LINK NE2 HIS A 27 FE FE A 229 1555 1555 2.12
LINK NE2 HIS A 81 FE FE A 229 1555 1555 2.19
LINK OD2 ASP A 173 FE FE A 229 1555 1555 1.93
LINK NE2 HIS A 177 FE FE A 229 1555 1555 2.20
LINK NE2 HIS B 27 FE FE B 229 1555 1555 2.18
LINK NE2 HIS B 81 FE FE B 229 1555 1555 2.24
LINK OD2 ASP B 173 FE FE B 229 1555 1555 1.98
LINK NE2 HIS B 177 FE FE B 229 1555 1555 2.16
LINK NE2 HIS C 27 FE FE C 229 1555 1555 2.17
LINK NE2 HIS C 81 FE FE C 229 1555 1555 2.22
LINK OD2 ASP C 173 FE FE C 229 1555 1555 1.98
LINK NE2 HIS C 177 FE FE C 229 1555 1555 2.11
LINK NE2 HIS D 27 FE FE D 229 1555 1555 2.20
LINK NE2 HIS D 81 FE FE D 229 1555 1555 2.20
LINK OD2 ASP D 173 FE FE D 229 1555 1555 1.99
LINK NE2 HIS D 177 FE FE D 229 1555 1555 2.15
LINK FE FE A 229 O HOH A 233 1555 1555 2.27
LINK FE FE B 229 O HOH B 230 1555 1555 2.19
LINK FE FE C 229 O HOH C 230 1555 1555 2.15
LINK FE FE D 229 O HOH D 234 1555 1555 1.97
CISPEP 1 GLU A 16 PRO A 17 0 -2.64
CISPEP 2 GLU B 16 PRO B 17 0 0.75
CISPEP 3 GLU C 16 PRO C 17 0 -3.23
CISPEP 4 GLU D 16 PRO D 17 0 -2.23
SITE 1 AC1 5 HIS A 27 HIS A 81 ASP A 173 HIS A 177
SITE 2 AC1 5 HOH A 233
SITE 1 AC2 5 HIS B 27 HIS B 81 ASP B 173 HIS B 177
SITE 2 AC2 5 HOH B 230
SITE 1 AC3 5 HIS C 27 HIS C 81 ASP C 173 HIS C 177
SITE 2 AC3 5 HOH C 230
SITE 1 AC4 5 HIS D 27 HIS D 81 ASP D 173 HIS D 177
SITE 2 AC4 5 HOH D 234
CRYST1 43.801 87.922 116.198 90.00 91.14 90.00 P 1 21 1 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 0.022831 0.000000 0.000454 0.00000
SCALE2 0.000000 0.011374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008608 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
