HEADER OXIDOREDUCTASE 13-AUG-14 4UBG
TITLE RESTING STATE OF RAT CYSTEINE DIOXYGENASE C93G VARIANT
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)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPR-IBA1/RATCDO/C93GFVARIANT
KEYWDS CYSTEINE DIOXYGENASE, NON-HEME MONO-IRON, CUPIN, CYSTEINE TO GLYCINE
KEYWDS 2 SUBSTITUTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,E.P.TCHESNOKOV,G.N.JAMESON,S.M.WILBANKS
REVDAT 6 22-NOV-17 4UBG 1 SOURCE JRNL REMARK
REVDAT 5 25-FEB-15 4UBG 1 REMARK
REVDAT 4 14-JAN-15 4UBG 1 JRNL
REVDAT 3 17-DEC-14 4UBG 1 JRNL
REVDAT 2 03-DEC-14 4UBG 1 JRNL
REVDAT 1 26-NOV-14 4UBG 0
JRNL AUTH C.G.DAVIES,M.FELLNER,E.P.TCHESNOKOV,S.M.WILBANKS,G.N.JAMESON
JRNL TITL THE CYS-TYR CROSS-LINK OF CYSTEINE DIOXYGENASE CHANGES THE
JRNL TITL 2 OPTIMAL PH OF THE REACTION WITHOUT A STRUCTURAL CHANGE.
JRNL REF BIOCHEMISTRY V. 53 7961 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 25390690
JRNL DOI 10.1021/BI501277A
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 14449
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.30
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 4UBG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203143.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953700
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 7.1.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17317
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 52.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.12700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.90
REMARK 200 R MERGE FOR SHELL (I) : 1.24600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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 (%): 41.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS OF 1.5 MICROL OF
REMARK 280 APPROXIMATELY 7 MG/ML C93G-CDO (10MM SODIUMPHOSPHATE, 20MM NACL
REMARK 280 PH 7.5) AND 0.6 MICROL WT-CDO SEEDS IN THEIR OWN GROWTH SOLUTION
REMARK 280 (25% (W/V) POLYETHYLENE GLYCOL 1500, 13MM SUCCINATE, 44MM
REMARK 280 SODIUMPHOSPHATE, 44MM GLYCINE) AND 1.5 MICROL RESERVOIR BUFFER
REMARK 280 WERE ALLOWED TO EQUILIBRATE ABOVE THE RESERVOIR BUFFER (26% (W/V)
REMARK 280 POLYETHYLENE GLYCOL 4000, 200 MM AMMONIUM ACETATE, 100 MM
REMARK 280 SODIUM CITRATE)., PH 6.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 61.36500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.92000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.92000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.04750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.92000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.92000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.68250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.92000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.92000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 92.04750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.92000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.92000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.68250
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 61.36500
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 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 465 SER A 201
REMARK 465 ALA A 202
REMARK 465 TRP A 203
REMARK 465 SER A 204
REMARK 465 HIS A 205
REMARK 465 PRO A 206
REMARK 465 GLN A 207
REMARK 465 PHE A 208
REMARK 465 GLU A 209
REMARK 465 LYS A 210
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 OE1 GLU A 38 O HOH A 567 1.84
REMARK 500 O HOH A 408 O HOH A 454 1.89
REMARK 500 O HOH A 545 O HOH A 612 1.90
REMARK 500 OD1 ASN A 175 O HOH A 589 1.90
REMARK 500 ND1 HIS A 173 O HOH A 587 1.91
REMARK 500 NH2 ARG A 10 O HOH A 610 1.94
REMARK 500 NE2 GLN A 65 O HOH A 615 1.97
REMARK 500 OD2 ASP A 26 O HOH A 401 2.00
REMARK 500 O LYS A 112 O HOH A 606 2.03
REMARK 500 O HOH A 446 O HOH A 457 2.04
REMARK 500 O HOH A 468 O HOH A 582 2.06
REMARK 500 O HOH A 531 O HOH A 536 2.07
REMARK 500 O HOH A 578 O HOH A 581 2.10
REMARK 500 O THR A 171 O HOH A 564 2.10
REMARK 500 NH2 ARG A 123 O HOH A 500 2.10
REMARK 500 O HOH A 408 O HOH A 463 2.15
REMARK 500 NZ LYS A 112 O HOH A 402 2.17
REMARK 500 O HOH A 554 O HOH A 568 2.19
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 46.89 39.75
REMARK 500 ASN A 128 -12.48 74.64
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 600 DISTANCE = 6.01 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 NA A 310 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 9 O
REMARK 620 2 HOH A 501 O 124.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 54 O
REMARK 620 2 ARG A 57 O 75.4
REMARK 620 3 CYS A 76 O 164.2 98.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 308 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 62 O
REMARK 620 2 SER A 183 OG 130.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 309 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 82 O
REMARK 620 2 HOH A 482 O 118.0
REMARK 620 N 1
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 104.6
REMARK 620 3 HIS A 140 NE2 91.4 95.3
REMARK 620 4 HOH A 562 O 146.6 98.9 109.9
REMARK 620 5 HOH A 563 O 94.0 160.9 88.3 62.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 101 O
REMARK 620 2 ASN A 144 OD1 71.8
REMARK 620 3 GLU A 149 O 146.3 77.6
REMARK 620 4 HOH A 414 O 95.7 119.2 111.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 103 O
REMARK 620 2 THR A 105 OG1 117.5
REMARK 620 3 GLU A 143 OE1 122.1 104.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 135 OD1
REMARK 620 2 GLY A 138 O 125.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 306 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 532 O
REMARK 620 2 HOH A 516 O 92.8
REMARK 620 N 1
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 NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 310
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UBH RELATED DB: PDB
DBREF 4UBG A 1 200 UNP P21816 CDO1_RAT 1 200
SEQADV 4UBG GLY A 93 UNP P21816 CYS 93 ENGINEERED MUTATION
SEQADV 4UBG SER A 201 UNP P21816 EXPRESSION TAG
SEQADV 4UBG ALA A 202 UNP P21816 EXPRESSION TAG
SEQADV 4UBG TRP A 203 UNP P21816 EXPRESSION TAG
SEQADV 4UBG SER A 204 UNP P21816 EXPRESSION TAG
SEQADV 4UBG HIS A 205 UNP P21816 EXPRESSION TAG
SEQADV 4UBG PRO A 206 UNP P21816 EXPRESSION TAG
SEQADV 4UBG GLN A 207 UNP P21816 EXPRESSION TAG
SEQADV 4UBG PHE A 208 UNP P21816 EXPRESSION TAG
SEQADV 4UBG GLU A 209 UNP P21816 EXPRESSION TAG
SEQADV 4UBG LYS A 210 UNP P21816 EXPRESSION TAG
SEQRES 1 A 210 MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA
SEQRES 2 A 210 ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP
SEQRES 3 A 210 GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA
SEQRES 4 A 210 TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS
SEQRES 5 A 210 PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN
SEQRES 6 A 210 GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY
SEQRES 7 A 210 GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER
SEQRES 8 A 210 HIS GLY PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU
SEQRES 9 A 210 THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET
SEQRES 10 A 210 ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS
SEQRES 11 A 210 ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU
SEQRES 12 A 210 ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU
SEQRES 13 A 210 TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN
SEQRES 14 A 210 ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS
SEQRES 15 A 210 SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY
SEQRES 16 A 210 SER LEU GLU ASN ASN SER ALA TRP SER HIS PRO GLN PHE
SEQRES 17 A 210 GLU LYS
HET FE2 A 301 1
HET NA A 302 1
HET NA A 303 1
HET NA A 304 1
HET NA A 305 1
HET NA A 306 1
HET NA A 307 1
HET NA A 308 1
HET NA A 309 1
HET NA A 310 1
HETNAM FE2 FE (II) ION
HETNAM NA SODIUM ION
FORMUL 2 FE2 FE 2+
FORMUL 3 NA 9(NA 1+)
FORMUL 12 HOH *215(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
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 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 LEU A 139 N PHE A 107
LINK O PRO A 9 NA NA A 310 1555 1555 2.54
LINK O ASP A 54 NA NA A 302 1555 1555 2.88
LINK O ARG A 57 NA NA A 302 1555 1555 2.87
LINK O LEU A 62 NA NA A 308 1555 1555 2.85
LINK O CYS A 76 NA NA A 302 1555 1555 2.98
LINK O GLY A 82 NA NA A 309 1555 1555 2.90
LINK NE2 HIS A 86 FE FE2 A 301 1555 1555 2.09
LINK NE2 HIS A 88 FE FE2 A 301 1555 1555 2.31
LINK O ASN A 101 NA NA A 304 1555 1555 3.16
LINK O LYS A 103 NA NA A 305 1555 1555 3.01
LINK OG1 THR A 105 NA NA A 305 1555 1555 2.62
LINK OD1 ASP A 135 NA NA A 303 1555 1555 2.60
LINK O GLY A 138 NA NA A 303 1555 1555 2.58
LINK NE2 HIS A 140 FE FE2 A 301 1555 1555 2.24
LINK OE1 GLU A 143 NA NA A 305 1555 1555 2.63
LINK OD1 ASN A 144 NA NA A 304 1555 1555 2.73
LINK O GLU A 149 NA NA A 304 1555 1555 2.94
LINK O THR A 180 NA NA A 307 1555 1555 3.11
LINK OG SER A 183 NA NA A 308 1555 1555 2.80
LINK FE FE2 A 301 O HOH A 562 1555 1555 1.89
LINK FE FE2 A 301 O HOH A 563 1555 1555 2.59
LINK NA NA A 304 O HOH A 414 1555 1555 2.85
LINK NA NA A 306 O HOH A 532 1555 1555 2.88
LINK NA NA A 306 O HOH A 516 1555 1555 2.80
LINK NA NA A 309 O HOH A 482 1555 1555 2.97
LINK NA NA A 310 O HOH A 501 1555 1555 2.95
CISPEP 1 SER A 158 PRO A 159 0 -3.38
SITE 1 AC1 5 HIS A 86 HIS A 88 HIS A 140 HOH A 562
SITE 2 AC1 5 HOH A 563
SITE 1 AC2 4 PHE A 53 ASP A 54 ARG A 57 CYS A 76
SITE 1 AC3 5 ASP A 87 HIS A 88 ASN A 134 ASP A 135
SITE 2 AC3 5 GLY A 138
SITE 1 AC4 5 ASN A 101 ASN A 144 SER A 146 GLU A 149
SITE 2 AC4 5 HOH A 414
SITE 1 AC5 4 LYS A 103 THR A 105 ARG A 141 GLU A 143
SITE 1 AC6 6 THR A 11 LEU A 12 ALA A 13 GLU A 46
SITE 2 AC6 6 HOH A 516 HOH A 532
SITE 1 AC7 5 TYR A 56 THR A 59 ARG A 60 THR A 180
SITE 2 AC7 5 HIS A 182
SITE 1 AC8 6 TYR A 50 LEU A 62 SER A 183 LYS A 184
SITE 2 AC8 6 PHE A 185 GLY A 186
SITE 1 AC9 5 ARG A 57 TYR A 58 HIS A 81 GLY A 82
SITE 2 AC9 5 HOH A 482
SITE 1 AD1 5 LYS A 8 PRO A 9 TYR A 40 GLU A 41
SITE 2 AD1 5 HOH A 501
CRYST1 57.840 57.840 122.730 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 0.017289 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008148 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
