HEADER OXIDOREDUCTASE 16-NOV-18 6N43
TITLE CRYSTAL STRUCTURE OF CYSTEINE, NITRIC OXIDE-BOUND FERROUS FORM OF THE
TITLE 2 CROSSLINKED HUMAN CYSTEINE DIOXYGENASE IN THE ANAEROBIC CONDITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I,CDO-I;
COMPND 5 EC: 1.13.11.20;
COMPND 6 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: CDO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYSTEINE, CYS-TYR COFACTOR, IRON, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LIU,J.LI
REVDAT 5 11-OCT-23 6N43 1 REMARK
REVDAT 4 27-NOV-19 6N43 1 REMARK
REVDAT 3 15-MAY-19 6N43 1 JRNL
REVDAT 2 01-MAY-19 6N43 1 JRNL
REVDAT 1 17-APR-19 6N43 0
JRNL AUTH J.LI,T.KOTO,I.DAVIS,A.LIU
JRNL TITL PROBING THE CYS-TYR COFACTOR BIOGENESIS IN CYSTEINE
JRNL TITL 2 DIOXYGENASE BY THE GENETIC INCORPORATION OF FLUOROTYROSINE.
JRNL REF BIOCHEMISTRY V. 58 2218 2019
JRNL REFN ISSN 0006-2960
JRNL PMID 30946568
JRNL DOI 10.1021/ACS.BIOCHEM.9B00006
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 15427
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) : 0.177
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1542
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 32.7310 - 5.0854 1.00 1341 148 0.1763 0.2197
REMARK 3 2 5.0854 - 4.0388 1.00 1301 141 0.1388 0.1501
REMARK 3 3 4.0388 - 3.5290 1.00 1263 147 0.1477 0.2129
REMARK 3 4 3.5290 - 3.2066 1.00 1267 137 0.1697 0.1709
REMARK 3 5 3.2066 - 2.9769 1.00 1276 142 0.1998 0.2379
REMARK 3 6 2.9769 - 2.8015 1.00 1258 134 0.2050 0.2539
REMARK 3 7 2.8015 - 2.6613 1.00 1251 140 0.1990 0.2690
REMARK 3 8 2.6613 - 2.5455 1.00 1272 141 0.2078 0.2370
REMARK 3 9 2.5455 - 2.4475 1.00 1237 139 0.2179 0.2670
REMARK 3 10 2.4475 - 2.3631 0.99 1262 140 0.2429 0.2810
REMARK 3 11 2.3631 - 2.2892 0.94 1157 133 0.2448 0.3087
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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: NULL
REMARK 4
REMARK 4 6N43 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000236364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16139
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.5000
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) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.45400
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
REMARK 200 STARTING MODEL: PDB ENTRY 2IC1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 2 M AMMONIUM SULFATE, 2%
REMARK 280 PEG400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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
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 22.78467
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 11.39233
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 17.08850
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 5.69617
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 28.48083
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 TOTAL BURIED SURFACE AREA: 500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 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 SER A 1
REMARK 465 GLU A 2
REMARK 465 GLN A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 ASN A 191
REMARK 465 ALA A 192
REMARK 465 THR A 193
REMARK 465 SER A 194
REMARK 465 GLY A 195
REMARK 465 SER A 196
REMARK 465 LEU A 197
REMARK 465 GLU A 198
REMARK 465 ASN A 199
REMARK 465 ASN A 200
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 O HOH A 478 O HOH A 492 2.17
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 ASN A 115 -174.04 -174.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 498 DISTANCE = 6.85 ANGSTROMS
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 302 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 NE2
REMARK 620 2 HIS A 88 NE2 98.7
REMARK 620 3 HIS A 140 NE2 91.8 91.9
REMARK 620 4 CYS A 301 N 87.8 93.7 174.4
REMARK 620 5 CYS A 301 SG 92.7 167.2 93.5 81.0
REMARK 620 6 NO A 303 N 171.3 87.4 94.2 85.6 80.7
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 CYS A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306
DBREF 6N43 A 2 200 UNP Q16878 CDO1_HUMAN 2 200
SEQADV 6N43 SER A 1 UNP Q16878 EXPRESSION TAG
SEQADV 6N43 VAL A 137 UNP Q16878 ILE 137 CONFLICT
SEQRES 1 A 200 SER GLU GLN THR GLU VAL LEU LYS PRO ARG THR LEU ALA
SEQRES 2 A 200 ASP LEU ILE ARG ILE LEU HIS GLN LEU PHE ALA GLY ASP
SEQRES 3 A 200 GLU VAL ASN VAL GLU GLU VAL GLN ALA ILE MET GLU ALA
SEQRES 4 A 200 TYR GLU SER ASP PRO THR GLU TRP ALA MET TYR ALA LYS
SEQRES 5 A 200 PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN
SEQRES 6 A 200 GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY
SEQRES 7 A 200 GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASN SER
SEQRES 8 A 200 HIS CYS PHE LEU LYS MET LEU GLN GLY ASN LEU LYS GLU
SEQRES 9 A 200 THR LEU PHE ALA TRP PRO ASP LYS LYS SER ASN GLU MET
SEQRES 10 A 200 VAL LYS LYS SER GLU ARG VAL LEU ARG GLU ASN GLN CYS
SEQRES 11 A 200 ALA TYR ILE ASN ASP SER VAL GLY LEU HIS ARG VAL GLU
SEQRES 12 A 200 ASN ILE SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU
SEQRES 13 A 200 TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN
SEQRES 14 A 200 ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS
SEQRES 15 A 200 SER LYS PHE GLY ILE ARG THR PRO ASN ALA THR SER GLY
SEQRES 16 A 200 SER LEU GLU ASN ASN
HET CYS A 301 7
HET FE A 302 1
HET NO A 303 2
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HETNAM CYS CYSTEINE
HETNAM FE FE (III) ION
HETNAM NO NITRIC OXIDE
HETNAM SO4 SULFATE ION
HETSYN NO NITROGEN MONOXIDE
FORMUL 2 CYS C3 H7 N O2 S
FORMUL 3 FE FE 3+
FORMUL 4 NO N O
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 8 HOH *98(H2 O)
HELIX 1 AA1 THR A 11 PHE A 23 1 13
HELIX 2 AA2 ASN A 29 TYR A 40 1 12
HELIX 3 AA3 ASP A 43 ALA A 48 1 6
HELIX 4 AA4 MET A 49 ALA A 51 5 3
HELIX 5 AA5 GLN A 65 LYS A 69 5 5
SHEET 1 AA1 7 CYS A 130 ILE A 133 0
SHEET 2 AA1 7 HIS A 92 GLN A 99 -1 N LEU A 95 O ALA A 131
SHEET 3 AA1 7 ALA A 151 SER A 158 -1 O LEU A 154 N LYS A 96
SHEET 4 AA1 7 ASN A 71 TRP A 77 -1 N MET A 73 O HIS A 155
SHEET 5 AA1 7 THR A 59 ASP A 64 -1 N VAL A 63 O LEU A 72
SHEET 6 AA1 7 SER A 183 LYS A 184 1 O SER A 183 N LEU A 62
SHEET 7 AA1 7 ILE A 187 ARG A 188 -1 O ILE A 187 N LYS A 184
SHEET 1 AA2 3 ILE A 85 HIS A 86 0
SHEET 2 AA2 3 THR A 163 PHE A 167 -1 O PHE A 167 N ILE A 85
SHEET 3 AA2 3 LYS A 174 THR A 178 -1 O VAL A 177 N CYS A 164
SHEET 1 AA3 3 LYS A 119 VAL A 124 0
SHEET 2 AA3 3 LEU A 102 PHE A 107 -1 N LEU A 106 O LYS A 120
SHEET 3 AA3 3 LEU A 139 ASN A 144 -1 O LEU A 139 N PHE A 107
LINK SG CYS A 93 CE1 TYR A 157 1555 1555 1.90
LINK NE2 HIS A 86 FE FE A 302 1555 1555 2.02
LINK NE2 HIS A 88 FE FE A 302 1555 1555 2.15
LINK NE2 HIS A 140 FE FE A 302 1555 1555 2.13
LINK N CYS A 301 FE FE A 302 1555 1555 2.36
LINK SG CYS A 301 FE FE A 302 1555 1555 2.37
LINK FE FE A 302 N NO A 303 1555 1555 1.93
CISPEP 1 SER A 158 PRO A 159 0 -5.93
SITE 1 AC1 10 TYR A 58 ARG A 60 LEU A 75 HIS A 86
SITE 2 AC1 10 HIS A 88 HIS A 140 TYR A 157 MET A 179
SITE 3 AC1 10 FE A 302 NO A 303
SITE 1 AC2 5 HIS A 86 HIS A 88 HIS A 140 CYS A 301
SITE 2 AC2 5 NO A 303
SITE 1 AC3 7 HIS A 88 CYS A 93 HIS A 140 HIS A 155
SITE 2 AC3 7 TYR A 157 CYS A 301 FE A 302
SITE 1 AC4 5 GLN A 34 ARG A 123 ALA A 131 TYR A 132
SITE 2 AC4 5 HOH A 403
SITE 1 AC5 6 TYR A 56 HIS A 173 LYS A 174 HOH A 406
SITE 2 AC5 6 HOH A 411 HOH A 469
SITE 1 AC6 3 LYS A 119 ARG A 141 GLN A 169
CRYST1 131.161 131.161 34.177 90.00 90.00 120.00 P 65 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 0.007624 0.004402 0.000000 0.00000
SCALE2 0.000000 0.008804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029259 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
