HEADER OXIDOREDUCTASE 08-APR-15 4Z82
TITLE CYSTEINE BOUND RAT CYSTEINE DIOXYGENASE C164S VARIANT AT PH 8.1
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;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CDO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-32A(+)
KEYWDS THIOETHER BOND, POST-TRANSLATIONAL MODIFICATION, POST TRANSLATIONAL,
KEYWDS 2 POSTTRANSLATIONAL, SUBSTRATE BOUND, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,E.P.TCHESNOKOV,E.SIAKKOU,M.T.RUTLEDGE,M.KANITZ,
AUTHOR 2 G.N.L.JAMESON,S.M.WILBANKS
REVDAT 3 22-NOV-17 4Z82 1 REMARK
REVDAT 2 29-JUN-16 4Z82 1 JRNL
REVDAT 1 01-JUN-16 4Z82 0
JRNL AUTH M.FELLNER,E.SIAKKOU,A.S.FAPONLE,E.P.TCHESNOKOV,
JRNL AUTH 2 S.P.DE VISSER,S.M.WILBANKS,G.N.JAMESON
JRNL TITL INFLUENCE OF CYSTEINE 164 ON ACTIVE SITE STRUCTURE IN RAT
JRNL TITL 2 CYSTEINE DIOXYGENASE.
JRNL REF J.BIOL.INORG.CHEM. V. 21 501 2016
JRNL REFN ESSN 1432-1327
JRNL PMID 27193596
JRNL DOI 10.1007/S00775-016-1360-0
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9-1692
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 22818
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2160
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 23.8862 - 4.1857 1.00 2781 126 0.1419 0.1770
REMARK 3 2 4.1857 - 3.3252 0.99 2788 129 0.1486 0.1761
REMARK 3 3 3.3252 - 2.9057 0.99 2740 140 0.1768 0.1676
REMARK 3 4 2.9057 - 2.6404 0.98 2709 163 0.1821 0.2052
REMARK 3 5 2.6404 - 2.4514 0.98 2686 172 0.1954 0.2363
REMARK 3 6 2.4514 - 2.3070 0.98 2694 151 0.1943 0.2437
REMARK 3 7 2.3070 - 2.1915 0.97 2694 136 0.1936 0.2162
REMARK 3 8 2.1915 - 2.0962 0.97 2683 133 0.1925 0.2100
REMARK 3 9 2.0962 - 2.0155 0.96 2652 153 0.1992 0.2319
REMARK 3 10 2.0155 - 1.9460 0.96 2650 149 0.2010 0.2050
REMARK 3 11 1.9460 - 1.8852 0.95 2636 147 0.2118 0.2266
REMARK 3 12 1.8852 - 1.8313 0.95 2673 115 0.2305 0.2947
REMARK 3 13 1.8313 - 1.7831 0.94 2600 152 0.2541 0.3098
REMARK 3 14 1.7831 - 1.7396 0.94 2614 150 0.2439 0.2830
REMARK 3 15 1.7396 - 1.7000 0.93 2544 144 0.2439 0.2713
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.97
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 : 0.008 1594
REMARK 3 ANGLE : 1.102 2161
REMARK 3 CHIRALITY : 0.061 230
REMARK 3 PLANARITY : 0.004 284
REMARK 3 DIHEDRAL : 13.954 584
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 4Z82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.3
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54187
REMARK 200 MONOCHROMATOR : OSMIC VARIMAX OPTICS
REMARK 200 OPTICS : OSMIC VARIMAX OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.0
REMARK 200 DATA SCALING SOFTWARE : D*TREK, AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22847
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 23.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 11.60
REMARK 200 R MERGE FOR SHELL (I) : 0.83200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4KWJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS OF 2 MICROL OF 50 MG/ML
REMARK 280 C164S-CDO (10 MM SODIUM PHOSPHATE, 20 MM NACL, PH 7.5) AND 2
REMARK 280 MICROL RESERVOIR BUFFER CONTAINING SEEDS FROM WT-CDO WERE
REMARK 280 ALLOWED TO EQUILIBRATE ABOVE THE RESERVOIR BUFFER (26% (W/V)
REMARK 280 POLYETHYLENE GLYCOL 4000, 200 MM AMMONIUM ACETATE, 100 MM SODIUM
REMARK 280 CITRATE), PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.11500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 29.01000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.01000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.67250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.01000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.01000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.55750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.01000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.01000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.67250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.01000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.01000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.55750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.11500
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 PHE A 191
REMARK 465 THR 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 536 O HOH A 600 1.81
REMARK 500 O HOH A 592 O HOH A 606 1.81
REMARK 500 O HOH A 605 O HOH A 616 2.16
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 128 -7.34 73.40
REMARK 500 ASN A 128 -7.34 74.76
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 A 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 NE2
REMARK 620 2 HIS A 88 NE2 100.8
REMARK 620 3 HIS A 140 NE2 94.5 89.3
REMARK 620 4 HOH A 401 O 143.1 92.6 120.1
REMARK 620 5 CYS A 302 SG 107.9 150.2 96.3 59.4
REMARK 620 6 CYS A 302 N 90.4 93.6 173.7 54.3 78.5
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 FE2 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CYS A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YYO RELATED DB: PDB
REMARK 900 RESTING STATE OF THE SAME PROTEIN.
DBREF 4Z82 A 1 200 UNP P21816 CDO1_RAT 1 200
SEQADV 4Z82 SER A 164 UNP P21816 CYS 164 ENGINEERED MUTATION
SEQRES 1 A 200 MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA
SEQRES 2 A 200 ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP
SEQRES 3 A 200 GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA
SEQRES 4 A 200 TYR GLU SER ASN PRO ALA GLU TRP ALA LEU 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 ASP SER
SEQRES 8 A 200 HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU
SEQRES 9 A 200 THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET
SEQRES 10 A 200 ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS
SEQRES 11 A 200 ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU
SEQRES 12 A 200 ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU
SEQRES 13 A 200 TYR SER PRO PRO PHE ASP THR SER 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 PHE THR THR SER GLY
SEQRES 16 A 200 SER LEU GLU ASN ASN
HET FE2 A 301 1
HET CYS A 302 7
HETNAM FE2 FE (II) ION
HETNAM CYS CYSTEINE
FORMUL 2 FE2 FE 2+
FORMUL 3 CYS C3 H7 N O2 S
FORMUL 4 HOH *242(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 ASN A 43 ALA A 48 1 6
HELIX 4 AA4 LEU A 49 ALA A 51 5 3
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 ASN A 61 O ILE A 74
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 SER A 164
SHEET 1 AA3 3 LYS A 119 LEU A 125 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 GLU A 143 -1 O GLU A 143 N LYS A 103
LINK NE2 HIS A 86 FE FE2 A 301 1555 1555 2.03
LINK NE2 HIS A 88 FE FE2 A 301 1555 1555 2.21
LINK SG CYS A 93 CE1 TYR A 157 1555 1555 1.98
LINK NE2 HIS A 140 FE FE2 A 301 1555 1555 2.35
LINK FE FE2 A 301 O HOH A 401 1555 1555 2.28
LINK FE FE2 A 301 SG CYS A 302 1555 1555 2.37
LINK FE FE2 A 301 N CYS A 302 1555 1555 2.34
CISPEP 1 SER A 158 PRO A 159 0 -4.18
SITE 1 AC1 5 HIS A 86 HIS A 88 HIS A 140 CYS A 302
SITE 2 AC1 5 HOH A 401
SITE 1 AC2 11 TYR A 58 ARG A 60 LEU A 75 HIS A 86
SITE 2 AC2 11 HIS A 88 HIS A 140 HIS A 155 TYR A 157
SITE 3 AC2 11 MET A 179 FE2 A 301 HOH A 401
CRYST1 58.020 58.020 122.230 90.00 90.00 90.00 P 43 21 2 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 0.017235 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
