HEADER OXIDOREDUCTASE 25-AUG-11 3TJT
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE SUPEROXIDE DISMUTASE FROM
TITLE 2 CLOSTRIDIUM DIFFICILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 27-234;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM DIFFICILE;
SOURCE 3 ORGANISM_TAXID: 272563;
SOURCE 4 STRAIN: 630;
SOURCE 5 GENE: CD630_16310, SODA, YP_001088132.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSSETA(DE3)PLYS S;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X
KEYWDS SUPEROXIDE DISMUTASE, METAL ION BINDING, ROSSMANN FOLD,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.LI,C.LEI,T.L.YING,H.F.WANG,X.S.TAN
REVDAT 1 29-AUG-12 3TJT 0
JRNL AUTH W.LI,C.LEI,T.L.YING,H.F.WANG,X.S.TAN
JRNL TITL CRYSTAL STRUCTURE OF THE SUPEROXIDE DISMUTASE FROM
JRNL TITL 2 CLOSTRIDIUM DIFFICILE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 40736
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.570
REMARK 3 FREE R VALUE TEST SET COUNT : 1946
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.7978 - 4.3387 0.78 2685 128 0.1856 0.1951
REMARK 3 2 4.3387 - 3.4443 0.78 2517 121 0.1629 0.1836
REMARK 3 3 3.4443 - 3.0091 0.96 3032 144 0.1780 0.1986
REMARK 3 4 3.0091 - 2.7341 0.99 3083 146 0.1815 0.1954
REMARK 3 5 2.7341 - 2.5381 0.98 3049 145 0.1843 0.2095
REMARK 3 6 2.5381 - 2.3885 0.98 3035 146 0.1792 0.1968
REMARK 3 7 2.3885 - 2.2689 0.98 3025 144 0.1780 0.2037
REMARK 3 8 2.2689 - 2.1701 0.97 2965 140 0.1678 0.2186
REMARK 3 9 2.1701 - 2.0866 0.97 2969 145 0.1706 0.1919
REMARK 3 10 2.0866 - 2.0146 0.97 2950 140 0.1735 0.2289
REMARK 3 11 2.0146 - 1.9516 0.96 2923 142 0.1828 0.1991
REMARK 3 12 1.9516 - 1.8958 0.94 2870 138 0.1922 0.2079
REMARK 3 13 1.8958 - 1.8459 0.93 2801 136 0.1936 0.2369
REMARK 3 14 1.8459 - 1.8009 0.91 2767 131 0.1947 0.2248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 38.25
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26460
REMARK 3 B22 (A**2) : -0.26460
REMARK 3 B33 (A**2) : 0.52920
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1717
REMARK 3 ANGLE : 0.979 2330
REMARK 3 CHIRALITY : 0.074 241
REMARK 3 PLANARITY : 0.005 300
REMARK 3 DIHEDRAL : 17.172 616
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST SQUARES
REMARK 3 PROCEDURE
REMARK 4
REMARK 4 3TJT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB067565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
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 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42617
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 20.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : 0.38600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 2RCV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CITRATE DIHYDROGEN, 20%
REMARK 280 PEG 3350, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 167.75400
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 83.87700
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 125.81550
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 41.93850
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 209.69250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 167.75400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 83.87700
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 41.93850
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 125.81550
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 209.69250
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: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 BIOMT1 2 0.500000 0.866025 0.000000 40.19950
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -69.62758
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -41.93850
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 2 LIES ON A SPECIAL POSITION.
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 PRO A 27
REMARK 465 GLU A 28
REMARK 465 LYS A 231
REMARK 465 SER A 232
REMARK 465 GLN A 233
REMARK 465 ASP A 234
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 GLU A 127 -142.36 54.03
REMARK 500 ASN A 177 -123.90 55.21
REMARK 500 TYR A 199 -6.26 -143.35
REMARK 500 GLN A 204 -127.54 47.96
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 1 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 193 OD2
REMARK 620 2 HIS A 56 NE2 85.0
REMARK 620 3 HIS A 197 NE2 121.5 101.5
REMARK 620 4 HOH A 4 O 83.9 168.1 87.8
REMARK 620 5 HIS A 111 NE2 111.8 88.7 126.3 91.6
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 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RCV RELATED DB: PDB
REMARK 900 HOMOLOGUE
DBREF 3TJT A 27 234 UNP Q186I6 Q186I6_CLOD6 27 234
SEQRES 1 A 208 PRO GLU ASN ASN LYS PHE LYS VAL LYS PRO LEU PRO TYR
SEQRES 2 A 208 ALA TYR ASP ALA LEU GLU PRO TYR ILE ASP LYS GLU THR
SEQRES 3 A 208 MET LYS LEU HIS HIS ASP LYS HIS TYR GLN ALA TYR VAL
SEQRES 4 A 208 ASP LYS LEU ASN ALA ALA LEU GLU LYS TYR PRO GLU LEU
SEQRES 5 A 208 TYR ASN TYR SER LEU CYS GLU LEU LEU GLN ASN LEU ASP
SEQRES 6 A 208 SER LEU PRO LYS ASP ILE ALA THR THR VAL ARG ASN ASN
SEQRES 7 A 208 ALA GLY GLY ALA TYR ASN HIS LYS PHE PHE PHE ASP ILE
SEQRES 8 A 208 MET THR PRO GLU LYS THR ILE PRO SER GLU SER LEU LYS
SEQRES 9 A 208 GLU ALA ILE ASP ARG ASP PHE GLY SER PHE GLU LYS PHE
SEQRES 10 A 208 LYS GLN GLU PHE GLN LYS SER ALA LEU ASP VAL PHE GLY
SEQRES 11 A 208 SER GLY TRP ALA TRP LEU VAL ALA THR LYS ASP GLY LYS
SEQRES 12 A 208 LEU SER ILE MET THR THR PRO ASN GLN ASP SER PRO VAL
SEQRES 13 A 208 SER LYS ASN LEU THR PRO ILE ILE GLY LEU ASP VAL TRP
SEQRES 14 A 208 GLU HIS ALA TYR TYR LEU LYS TYR GLN ASN ARG ARG ASN
SEQRES 15 A 208 GLU TYR ILE ASP ASN TRP PHE ASN VAL VAL ASN TRP ASN
SEQRES 16 A 208 GLY ALA LEU GLU ASN TYR LYS ASN LEU LYS SER GLN ASP
HET FE A 1 1
HETNAM FE FE (III) ION
FORMUL 2 FE FE 3+
FORMUL 3 HOH *361(H2 O)
HELIX 1 1 ASP A 49 LYS A 59 1 11
HELIX 2 2 LYS A 59 GLU A 73 1 15
HELIX 3 3 LYS A 74 TYR A 81 5 8
HELIX 4 4 SER A 82 ASN A 89 1 8
HELIX 5 5 LEU A 90 LEU A 93 5 4
HELIX 6 6 PRO A 94 ASP A 96 5 3
HELIX 7 7 ILE A 97 ILE A 117 1 21
HELIX 8 8 SER A 126 GLY A 138 1 13
HELIX 9 9 SER A 139 VAL A 154 1 16
HELIX 10 10 SER A 180 ASN A 185 5 6
HELIX 11 11 TRP A 195 ALA A 198 5 4
HELIX 12 12 TYR A 199 GLN A 204 1 6
HELIX 13 13 ARG A 206 PHE A 215 1 10
HELIX 14 14 ASN A 219 ASN A 229 1 11
SHEET 1 A 3 LEU A 170 PRO A 176 0
SHEET 2 A 3 GLY A 158 ALA A 164 -1 N TRP A 161 O MET A 173
SHEET 3 A 3 THR A 187 ASP A 193 -1 O ILE A 189 N LEU A 162
LINK OD2 ASP A 193 FE FE A 1 1555 1555 1.92
LINK NE2 HIS A 56 FE FE A 1 1555 1555 2.16
LINK NE2 HIS A 197 FE FE A 1 1555 1555 2.19
LINK FE FE A 1 O HOH A 4 1555 1555 2.23
LINK NE2 HIS A 111 FE FE A 1 1555 1555 2.23
CISPEP 1 GLU A 45 PRO A 46 0 4.40
SITE 1 AC1 5 HOH A 4 HIS A 56 HIS A 111 ASP A 193
SITE 2 AC1 5 HIS A 197
CRYST1 80.399 80.399 251.631 90.00 90.00 120.00 P 65 2 2 12
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 0.012438 0.007181 0.000000 0.00000
SCALE2 0.000000 0.014362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003974 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
