HEADER OXIDOREDUCTASE 04-FEB-16 5I0R
TITLE D-CYSTEINE BOUND C93A MUTANT OF CYSTEINE DIOXYGENASE AT PH 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;
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: 562
KEYWDS CUPIN-FOLD, CYSTEINE TO CYSTEINE SULFINATE, C93-Y157 CROSSLINK, D-
KEYWDS 2 CYSTEINE, CATALYSIS OXIDATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.KEAN,C.M.DRIGGERS,P.A.KARPLUS
REVDAT 3 27-SEP-23 5I0R 1 REMARK
REVDAT 2 03-MAY-17 5I0R 1 REMARK SEQADV ATOM
REVDAT 1 14-DEC-16 5I0R 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. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 46119
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.860
REMARK 3 FREE R VALUE TEST SET COUNT : 4549
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 41.9646 - 4.1935 1.00 1569 168 0.1637 0.1777
REMARK 3 2 4.1935 - 3.3289 1.00 1463 158 0.1423 0.1685
REMARK 3 3 3.3289 - 2.9082 1.00 1423 154 0.1548 0.1649
REMARK 3 4 2.9082 - 2.6424 1.00 1408 169 0.1613 0.2161
REMARK 3 5 2.6424 - 2.4530 1.00 1406 160 0.1591 0.1989
REMARK 3 6 2.4530 - 2.3084 1.00 1392 147 0.1477 0.1729
REMARK 3 7 2.3084 - 2.1928 1.00 1420 138 0.1423 0.1680
REMARK 3 8 2.1928 - 2.0973 1.00 1417 136 0.1406 0.1667
REMARK 3 9 2.0973 - 2.0166 1.00 1358 176 0.1496 0.1858
REMARK 3 10 2.0166 - 1.9470 1.00 1370 170 0.1463 0.1717
REMARK 3 11 1.9470 - 1.8861 1.00 1396 134 0.1511 0.2095
REMARK 3 12 1.8861 - 1.8322 1.00 1403 133 0.1555 0.2023
REMARK 3 13 1.8322 - 1.7840 1.00 1376 140 0.1619 0.2099
REMARK 3 14 1.7840 - 1.7405 1.00 1368 149 0.1770 0.2001
REMARK 3 15 1.7405 - 1.7009 1.00 1361 161 0.1751 0.1925
REMARK 3 16 1.7009 - 1.6647 1.00 1389 150 0.1839 0.2319
REMARK 3 17 1.6647 - 1.6314 1.00 1337 151 0.1752 0.2250
REMARK 3 18 1.6314 - 1.6006 1.00 1382 133 0.1877 0.1957
REMARK 3 19 1.6006 - 1.5720 1.00 1364 162 0.1905 0.2360
REMARK 3 20 1.5720 - 1.5454 1.00 1363 170 0.2134 0.2330
REMARK 3 21 1.5454 - 1.5204 1.00 1376 142 0.2097 0.2655
REMARK 3 22 1.5204 - 1.4970 1.00 1380 144 0.2280 0.2507
REMARK 3 23 1.4970 - 1.4750 1.00 1335 148 0.2423 0.2474
REMARK 3 24 1.4750 - 1.4543 1.00 1345 163 0.2497 0.2712
REMARK 3 25 1.4543 - 1.4346 1.00 1380 145 0.2681 0.3103
REMARK 3 26 1.4346 - 1.4160 1.00 1370 148 0.2865 0.3013
REMARK 3 27 1.4160 - 1.3983 1.00 1363 136 0.3086 0.3204
REMARK 3 28 1.3983 - 1.3814 1.00 1360 155 0.3378 0.3553
REMARK 3 29 1.3814 - 1.3654 1.00 1346 145 0.3622 0.3950
REMARK 3 30 1.3654 - 1.3500 1.00 1350 164 0.3680 0.4078
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) : 19.940
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 1644
REMARK 3 ANGLE : 0.973 2230
REMARK 3 CHIRALITY : 0.080 235
REMARK 3 PLANARITY : 0.006 298
REMARK 3 DIHEDRAL : 13.338 605
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): -17.3205 2.9933 -49.8892
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0754
REMARK 3 T33: 0.0618 T12: -0.0023
REMARK 3 T13: 0.0012 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.7343 L22: 0.6987
REMARK 3 L33: 0.4953 L12: 0.3261
REMARK 3 L13: -0.0553 L23: 0.1237
REMARK 3 S TENSOR
REMARK 3 S11: 0.0254 S12: -0.0143 S13: -0.0194
REMARK 3 S21: 0.0305 S22: -0.0192 S23: -0.0099
REMARK 3 S31: 0.0250 S32: -0.0131 S33: 0.1498
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 5I0R 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_1000216385.
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 : 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 : 46343
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 41.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 53.50
REMARK 200 R MERGE (I) : 0.24600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 36.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
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: 4EIO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.13
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 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 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 876 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 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 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 836 O HOH A 888 1.94
REMARK 500 O HOH A 761 O HOH A 796 2.00
REMARK 500 OXT DCY A 502 O HOH A 601 2.06
REMARK 500 O HOH A 604 O HOH A 733 2.14
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 O HOH A 748 O HOH A 821 8554 2.18
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 -11.90 78.42
REMARK 500 ASN A 128 -11.50 75.96
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 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 NE2
REMARK 620 2 HIS A 88 NE2 98.9
REMARK 620 3 HIS A 140 NE2 88.8 96.7
REMARK 620 4 DCY A 502 N 43.5 116.4 122.9
REMARK 620 5 DCY A 502 N 45.8 113.0 127.3 4.6
REMARK 620 6 DCY A 502 SG 86.7 171.7 89.5 63.9 66.8
REMARK 620 7 DCY A 502 SG 122.9 127.2 113.4 83.0 82.6 44.7
REMARK 620 N 1 2 3 4 5 6
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 DCY A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I0S RELATED DB: PDB
REMARK 900 RELATED ID: 5I0U RELATED DB: PDB
REMARK 900 RELATED ID: 5I0T RELATED DB: PDB
DBREF 5I0R A 1 200 UNP P21816 CDO1_RAT 1 200
SEQADV 5I0R ALA A 93 UNP P21816 CYS 93 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 ALA 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 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 PHE THR THR SER GLY
SEQRES 16 A 200 SER LEU GLU ASN ASN
HET FE A 501 1
HET DCY A 502 26
HET CL A 503 1
HETNAM FE FE (III) ION
HETNAM DCY D-CYSTEINE
HETNAM CL CHLORIDE ION
FORMUL 2 FE FE 3+
FORMUL 3 DCY C3 H7 N O2 S
FORMUL 4 CL CL 1-
FORMUL 5 HOH *321(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 CYS 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 NE2AHIS A 86 FE FE A 501 1555 1555 2.14
LINK NE2 HIS A 88 FE FE A 501 1555 1555 2.04
LINK NE2 HIS A 140 FE FE A 501 1555 1555 2.04
LINK FE FE A 501 N BDCY A 502 1555 1555 2.04
LINK FE FE A 501 N CDCY A 502 1555 1555 2.08
LINK FE FE A 501 SG CDCY A 502 1555 1555 2.62
LINK FE FE A 501 SG BDCY A 502 1555 1555 2.19
CISPEP 1 SER A 158 PRO A 159 0 -6.47
SITE 1 AC1 5 HIS A 86 HIS A 88 HIS A 140 DCY A 502
SITE 2 AC1 5 CL A 503
SITE 1 AC2 14 TYR A 58 SER A 83 HIS A 86 HIS A 88
SITE 2 AC2 14 HIS A 140 VAL A 142 HIS A 155 TYR A 157
SITE 3 AC2 14 MET A 179 FE A 501 CL A 503 HOH A 601
SITE 4 AC2 14 HOH A 667 HOH A 746
SITE 1 AC3 7 HIS A 88 HIS A 140 HIS A 155 TYR A 157
SITE 2 AC3 7 FE A 501 DCY A 502 HOH A 685
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
