HEADER OXIDOREDUCTASE 04-FEB-16 5I0T
TITLE THIOSULFATE BOUND CYSTEINE DIOXYGENASE AT PH 6.8
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: 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: 562
KEYWDS CUPIN-FOLD, CYSTEINE TO CYSTEINE SULFINATE, C93-Y157 CROSSLINK,
KEYWDS 2 CATALYSIS OXIDATION, OXIDOREDUCTASE, THIOSULFATE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.KEAN,C.M.DRIGGERS,P.A.KARPLUS
REVDAT 1 14-DEC-16 5I0T 0
JRNL AUTH C.M.DRIGGERS,K.M.KEAN,L.L.HIRSCHBERGER,R.B.COOLEY,
JRNL AUTH 2 M.H.STIPANUK,P.A.KARPLUS
JRNL TITL STRUCTURE-BASED INSIGHTS INTO THE ROLE OF THE CYS-TYR
JRNL TITL 2 CROSSLINK AND INHIBITOR RECOGNITION BY MAMMALIAN CYSTEINE
JRNL TITL 3 DIOXYGENASE.
JRNL REF J. MOL. BIOL. V. 428 3999 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27477048
JRNL DOI 10.1016/J.JMB.2016.07.012
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2386: ???)
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 44156
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.810
REMARK 3 FREE R VALUE TEST SET COUNT : 4333
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 30.6076 - 4.2532 1.00 1497 164 0.1666 0.1733
REMARK 3 2 4.2532 - 3.3773 1.00 1395 146 0.1444 0.1830
REMARK 3 3 3.3773 - 2.9508 1.00 1381 153 0.1529 0.1725
REMARK 3 4 2.9508 - 2.6812 1.00 1356 148 0.1550 0.2036
REMARK 3 5 2.6812 - 2.4891 1.00 1324 166 0.1526 0.1796
REMARK 3 6 2.4891 - 2.3424 1.00 1354 139 0.1507 0.2119
REMARK 3 7 2.3424 - 2.2251 1.00 1331 141 0.1463 0.1874
REMARK 3 8 2.2251 - 2.1283 1.00 1355 133 0.1424 0.1884
REMARK 3 9 2.1283 - 2.0464 1.00 1306 161 0.1517 0.1776
REMARK 3 10 2.0464 - 1.9758 1.00 1317 156 0.1522 0.1863
REMARK 3 11 1.9758 - 1.9140 1.00 1337 137 0.1572 0.1890
REMARK 3 12 1.9140 - 1.8593 1.00 1316 132 0.1654 0.2123
REMARK 3 13 1.8593 - 1.8104 1.00 1336 138 0.1630 0.2122
REMARK 3 14 1.8104 - 1.7662 1.00 1328 135 0.1755 0.2216
REMARK 3 15 1.7662 - 1.7260 1.00 1327 135 0.1804 0.2060
REMARK 3 16 1.7260 - 1.6893 1.00 1304 149 0.1843 0.2054
REMARK 3 17 1.6893 - 1.6555 1.00 1308 140 0.1823 0.2149
REMARK 3 18 1.6555 - 1.6243 1.00 1326 154 0.1786 0.2221
REMARK 3 19 1.6243 - 1.5953 1.00 1289 135 0.1902 0.2000
REMARK 3 20 1.5953 - 1.5682 1.00 1307 151 0.1960 0.2439
REMARK 3 21 1.5682 - 1.5429 1.00 1291 157 0.2104 0.2375
REMARK 3 22 1.5429 - 1.5192 1.00 1307 135 0.2250 0.2891
REMARK 3 23 1.5192 - 1.4969 1.00 1329 141 0.2403 0.2326
REMARK 3 24 1.4969 - 1.4758 1.00 1286 139 0.2600 0.2464
REMARK 3 25 1.4758 - 1.4558 1.00 1294 155 0.2701 0.3051
REMARK 3 26 1.4558 - 1.4369 1.00 1306 143 0.2838 0.2899
REMARK 3 27 1.4369 - 1.4190 1.00 1305 149 0.2820 0.2873
REMARK 3 28 1.4190 - 1.4019 1.00 1294 125 0.2957 0.3338
REMARK 3 29 1.4019 - 1.3856 1.00 1309 148 0.3203 0.3084
REMARK 3 30 1.3856 - 1.3700 1.00 1308 128 0.3360 0.3769
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.010 1657
REMARK 3 ANGLE : 1.092 2257
REMARK 3 CHIRALITY : 0.082 238
REMARK 3 PLANARITY : 0.006 299
REMARK 3 DIHEDRAL : 12.846 611
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND RESID 5 THROUGH 190
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2405 2.9606 -49.6222
REMARK 3 T TENSOR
REMARK 3 T11: 0.0951 T22: 0.1124
REMARK 3 T33: 0.1087 T12: 0.0008
REMARK 3 T13: -0.0055 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.8901 L22: 1.0160
REMARK 3 L33: 0.8696 L12: 0.3980
REMARK 3 L13: -0.1774 L23: 0.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.0175 S13: -0.0511
REMARK 3 S21: 0.0456 S22: -0.0152 S23: -0.0030
REMARK 3 S31: 0.0628 S32: -0.0333 S33: -0.0002
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 5I0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000216397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44485
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 30.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 27.30
REMARK 200 R MERGE (I) : 0.18300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4IEO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE PH 5.6, 24%
REMARK 280 PEG 4000, 0.15 M AMMONIUM ACETATE, PH 6.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 61.20000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.80000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.80000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.80000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.60000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.80000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.80000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.60000
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 61.20000
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 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 ARG A 10 CZ NH1 NH2
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 LYS A 184 CE NZ
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 HH22 ARG A 60 O2 THJ A 502 1.34
REMARK 500 O HOH A 638 O HOH A 816 2.00
REMARK 500 O HOH A 756 O HOH A 848 2.05
REMARK 500 O HOH A 676 O HOH A 831 2.07
REMARK 500 O HOH A 795 O HOH A 827 2.07
REMARK 500 O HOH A 739 O HOH A 897 2.09
REMARK 500 NH2 ARG A 60 O2 THJ A 502 2.11
REMARK 500 O HOH A 650 O HOH A 799 2.16
REMARK 500 O CYS A 130 O HOH A 602 2.19
REMARK 500 O HOH A 754 O HOH A 878 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLN A 55 HH22 ARG A 188 7554 1.59
REMARK 500 O HOH A 876 O HOH A 908 6554 2.13
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 67 55.35 -108.49
REMARK 500 ASN A 128 -6.28 73.14
REMARK 500 ASN A 128 -12.60 73.14
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 501 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 98.9 97.4
REMARK 620 4 THJ A 502 S2 100.9 141.3 110.3
REMARK 620 5 THJ A 502 O3 80.2 86.2 176.4 66.6
REMARK 620 6 HOH A 727 O 133.9 118.7 98.6 33.1 79.8
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 FE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue THJ A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I0R RELATED DB: PDB
REMARK 900 RELATED ID: 5I0S RELATED DB: PDB
REMARK 900 RELATED ID: 5I0U RELATED DB: PDB
DBREF 5I0T A 1 200 UNP P21816 CDO1_RAT 1 200
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 CSS 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
MODRES 5I0T CSS A 164 CYS MODIFIED RESIDUE
HET CSS A 164 22
HET FE A 501 1
HET THJ A 502 5
HETNAM CSS S-MERCAPTOCYSTEINE
HETNAM FE FE (III) ION
HETNAM THJ THIOSULFATE
FORMUL 1 CSS C3 H7 N O2 S2
FORMUL 2 FE FE 3+
FORMUL 3 THJ O3 S2 2-
FORMUL 4 HOH *313(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 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 CSS A 164
SHEET 1 AA3 3 SER A 121 LEU A 125 0
SHEET 2 AA3 3 LEU A 102 PHE A 107 -1 N LEU A 102 O LEU A 125
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 FE A 501 1555 1555 2.03
LINK NE2 HIS A 88 FE FE A 501 1555 1555 2.12
LINK SG CYS A 93 CE1 TYR A 157 1555 1555 1.80
LINK NE2 HIS A 140 FE FE A 501 1555 1555 2.09
LINK C THR A 163 N ACSS A 164 1555 1555 1.33
LINK C THR A 163 N BCSS A 164 1555 1555 1.33
LINK C ACSS A 164 N HIS A 165 1555 1555 1.33
LINK C BCSS A 164 N HIS A 165 1555 1555 1.33
LINK FE FE A 501 S2 ATHJ A 502 1555 1555 2.32
LINK FE FE A 501 O3 ATHJ A 502 1555 1555 2.80
LINK FE FE A 501 O AHOH A 727 1555 1555 2.04
CISPEP 1 SER A 158 PRO A 159 0 -6.92
SITE 1 AC1 5 HIS A 86 HIS A 88 HIS A 140 THJ A 502
SITE 2 AC1 5 HOH A 727
SITE 1 AC2 11 TYR A 58 ARG A 60 HIS A 86 HIS A 88
SITE 2 AC2 11 HIS A 140 HIS A 155 TYR A 157 FE A 501
SITE 3 AC2 11 HOH A 712 HOH A 727 HOH A 845
CRYST1 57.600 57.600 122.400 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 0.017361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008170 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
