HEADER OXIDOREDUCTASE 21-FEB-98 1GSN
TITLE HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.6.4.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: MIXED DISULFIDE BETWEEN C58 AND GLUTATHIONE (GSH 1030)
COMPND 7 SULFENIC ACID GROUP IN CEA63, CEA234, CEA284, CEA423
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SULFHYDRYL OXIDATION, SULFENIC ACID, NITRIC OXIDE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BECKER,S.N.SAVVIDES,M.KEESE,R.H.SCHIRMER,P.A.KARPLUS
REVDAT 4 07-DEC-11 1GSN 1 HEADER HET SEQADV SOURCE
REVDAT 3 13-JUL-11 1GSN 1 VERSN
REVDAT 2 24-FEB-09 1GSN 1 VERSN
REVDAT 1 27-MAY-98 1GSN 0
JRNL AUTH K.BECKER,S.N.SAVVIDES,M.KEESE,R.H.SCHIRMER,P.A.KARPLUS
JRNL TITL ENZYME INACTIVATION THROUGH SULFHYDRYL OXIDATION BY
JRNL TITL 2 PHYSIOLOGIC NO-CARRIERS.
JRNL REF NAT.STRUCT.BIOL. V. 5 267 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9546215
JRNL DOI 10.1038/NSB0498-267
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 57567
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3503
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 519
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.47
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GSN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57567
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
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) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 59.69500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.81500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.69500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.81500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 11630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 163.74430
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 72.18154
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 ALA A 1
REMARK 465 CYS A 2
REMARK 465 ARG A 3
REMARK 465 GLN A 4
REMARK 465 GLU A 5
REMARK 465 PRO A 6
REMARK 465 GLN A 7
REMARK 465 PRO A 8
REMARK 465 GLN A 9
REMARK 465 GLY A 10
REMARK 465 PRO A 11
REMARK 465 PRO A 12
REMARK 465 PRO A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 GLY A 16
REMARK 465 ALA A 17
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 HIS A 52 -119.08 -132.22
REMARK 500 VAL A 61 37.29 -143.42
REMARK 500 LYS A 93 94.98 -49.69
REMARK 500 HIS A 219 -141.63 -120.77
REMARK 500 ASN A 425 -179.22 65.63
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 656 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 662 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH A 713 DISTANCE = 9.03 ANGSTROMS
REMARK 525 HOH A 730 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A 743 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH A 803 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH A 857 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A 935 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH A 947 DISTANCE = 5.45 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1031
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 1030
DBREF 1GSN A 1 478 UNP P00390 GSHR_HUMAN 45 522
SEQRES 1 A 478 ALA CYS ARG GLN GLU PRO GLN PRO GLN GLY PRO PRO PRO
SEQRES 2 A 478 ALA ALA GLY ALA VAL ALA SER TYR ASP TYR LEU VAL ILE
SEQRES 3 A 478 GLY GLY GLY SER GLY GLY LEU ALA SER ALA ARG ARG ALA
SEQRES 4 A 478 ALA GLU LEU GLY ALA ARG ALA ALA VAL VAL GLU SER HIS
SEQRES 5 A 478 LYS LEU GLY GLY THR CYS VAL ASN VAL GLY CSO VAL PRO
SEQRES 6 A 478 LYS LYS VAL MET TRP ASN THR ALA VAL HIS SER GLU PHE
SEQRES 7 A 478 MET HIS ASP HIS ALA ASP TYR GLY PHE PRO SER CYS GLU
SEQRES 8 A 478 GLY LYS PHE ASN TRP ARG VAL ILE LYS GLU LYS ARG ASP
SEQRES 9 A 478 ALA TYR VAL SER ARG LEU ASN ALA ILE TYR GLN ASN ASN
SEQRES 10 A 478 LEU THR LYS SER HIS ILE GLU ILE ILE ARG GLY HIS ALA
SEQRES 11 A 478 ALA PHE THR SER ASP PRO LYS PRO THR ILE GLU VAL SER
SEQRES 12 A 478 GLY LYS LYS TYR THR ALA PRO HIS ILE LEU ILE ALA THR
SEQRES 13 A 478 GLY GLY MET PRO SER THR PRO HIS GLU SER GLN ILE PRO
SEQRES 14 A 478 GLY ALA SER LEU GLY ILE THR SER ASP GLY PHE PHE GLN
SEQRES 15 A 478 LEU GLU GLU LEU PRO GLY ARG SER VAL ILE VAL GLY ALA
SEQRES 16 A 478 GLY TYR ILE ALA VAL GLU MET ALA GLY ILE LEU SER ALA
SEQRES 17 A 478 LEU GLY SER LYS THR SER LEU MET ILE ARG HIS ASP LYS
SEQRES 18 A 478 VAL LEU ARG SER PHE ASP SER MET ILE SER THR ASN CSO
SEQRES 19 A 478 THR GLU GLU LEU GLU ASN ALA GLY VAL GLU VAL LEU LYS
SEQRES 20 A 478 PHE SER GLN VAL LYS GLU VAL LYS LYS THR LEU SER GLY
SEQRES 21 A 478 LEU GLU VAL SER MET VAL THR ALA VAL PRO GLY ARG LEU
SEQRES 22 A 478 PRO VAL MET THR MET ILE PRO ASP VAL ASP CSO LEU LEU
SEQRES 23 A 478 TRP ALA ILE GLY ARG VAL PRO ASN THR LYS ASP LEU SER
SEQRES 24 A 478 LEU ASN LYS LEU GLY ILE GLN THR ASP ASP LYS GLY HIS
SEQRES 25 A 478 ILE ILE VAL ASP GLU PHE GLN ASN THR ASN VAL LYS GLY
SEQRES 26 A 478 ILE TYR ALA VAL GLY ASP VAL CYS GLY LYS ALA LEU LEU
SEQRES 27 A 478 THR PRO VAL ALA ILE ALA ALA GLY ARG LYS LEU ALA HIS
SEQRES 28 A 478 ARG LEU PHE GLU TYR LYS GLU ASP SER LYS LEU ASP TYR
SEQRES 29 A 478 ASN ASN ILE PRO THR VAL VAL PHE SER HIS PRO PRO ILE
SEQRES 30 A 478 GLY THR VAL GLY LEU THR GLU ASP GLU ALA ILE HIS LYS
SEQRES 31 A 478 TYR GLY ILE GLU ASN VAL LYS THR TYR SER THR SER PHE
SEQRES 32 A 478 THR PRO MET TYR HIS ALA VAL THR LYS ARG LYS THR LYS
SEQRES 33 A 478 CYS VAL MET LYS MET VAL CSO ALA ASN LYS GLU GLU LYS
SEQRES 34 A 478 VAL VAL GLY ILE HIS MET GLN GLY LEU GLY CYS ASP GLU
SEQRES 35 A 478 MET LEU GLN GLY PHE ALA VAL ALA VAL LYS MET GLY ALA
SEQRES 36 A 478 THR LYS ALA ASP PHE ASP ASN THR VAL ALA ILE HIS PRO
SEQRES 37 A 478 THR SER SER GLU GLU LEU VAL THR LEU ARG
MODRES 1GSN CSO A 63 CYS S-HYDROXYCYSTEINE
MODRES 1GSN CSO A 234 CYS S-HYDROXYCYSTEINE
MODRES 1GSN CSO A 284 CYS S-HYDROXYCYSTEINE
MODRES 1GSN CSO A 423 CYS S-HYDROXYCYSTEINE
HET CSO A 63 7
HET CSO A 234 7
HET CSO A 284 7
HET CSO A 423 7
HET PO4 A1031 5
HET FAD A 499 53
HET GSH A1030 20
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM PO4 PHOSPHATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GSH GLUTATHIONE
FORMUL 1 CSO 4(C3 H7 N O3 S)
FORMUL 2 PO4 O4 P 3-
FORMUL 3 FAD C27 H33 N9 O15 P2
FORMUL 4 GSH C10 H17 N3 O6 S
FORMUL 5 HOH *519(H2 O)
HELIX 1 1 SER A 30 GLU A 41 1 12
HELIX 2 2 GLY A 56 ASN A 60 1 5
HELIX 3 3 PRO A 65 ASP A 81 1 17
HELIX 4 4 ALA A 83 TYR A 85 5 3
HELIX 5 5 TRP A 96 SER A 121 1 26
HELIX 6 6 ALA A 171 LEU A 173 5 3
HELIX 7 7 SER A 177 GLN A 182 1 6
HELIX 8 8 TYR A 197 ALA A 208 1 12
HELIX 9 9 SER A 228 ASN A 240 1 13
HELIX 10 10 LYS A 296 LEU A 298 5 3
HELIX 11 11 LEU A 300 LYS A 302 5 3
HELIX 12 12 GLY A 330 CYS A 333 5 4
HELIX 13 13 THR A 339 PHE A 354 1 16
HELIX 14 14 GLU A 384 TYR A 391 1 8
HELIX 15 15 ILE A 393 ASN A 395 5 3
HELIX 16 16 MET A 406 VAL A 410 5 5
HELIX 17 17 CYS A 440 MET A 453 1 14
HELIX 18 18 LYS A 457 ASP A 461 1 5
HELIX 19 19 SER A 471 VAL A 475 5 5
SHEET 1 A 4 ALA A 19 TYR A 21 0
SHEET 2 A 4 LYS A 145 ALA A 149 1 N THR A 148 O ALA A 19
SHEET 3 A 4 THR A 139 VAL A 142 -1 N VAL A 142 O LYS A 145
SHEET 4 A 4 ALA A 130 PHE A 132 -1 N ALA A 131 O GLU A 141
SHEET 1 B 5 ILE A 326 ALA A 328 0
SHEET 2 B 5 ILE A 152 ILE A 154 1 N ILE A 152 O TYR A 327
SHEET 3 B 5 TYR A 23 ILE A 26 1 N LEU A 24 O LEU A 153
SHEET 4 B 5 ALA A 46 GLU A 50 1 N ALA A 47 O TYR A 23
SHEET 5 B 5 GLU A 124 ARG A 127 1 N GLU A 124 O VAL A 48
SHEET 1 C 2 GLY A 158 PRO A 160 0
SHEET 2 C 2 ARG A 291 PRO A 293 -1 N VAL A 292 O MET A 159
SHEET 1 D 3 ARG A 189 VAL A 193 0
SHEET 2 D 3 LYS A 212 MET A 216 1 N LYS A 212 O SER A 190
SHEET 3 D 3 GLU A 244 LEU A 246 1 N GLU A 244 O LEU A 215
SHEET 1 E 3 VAL A 275 ILE A 279 0
SHEET 2 E 3 LEU A 261 THR A 267 -1 N THR A 267 O VAL A 275
SHEET 3 E 3 SER A 249 LYS A 256 -1 N LYS A 255 O GLU A 262
SHEET 1 F 5 THR A 369 VAL A 371 0
SHEET 2 F 5 ILE A 377 GLY A 381 -1 N THR A 379 O THR A 369
SHEET 3 F 5 GLY A 432 GLN A 436 -1 N MET A 435 O GLY A 378
SHEET 4 F 5 CYS A 417 VAL A 422 -1 N VAL A 422 O GLY A 432
SHEET 5 F 5 TYR A 399 PHE A 403 -1 N PHE A 403 O CYS A 417
SSBOND 1 CYS A 90 CYS A 90 1555 2656 2.13
LINK N CSO A 63 C GLY A 62 1555 1555 1.33
LINK C CSO A 63 N VAL A 64 1555 1555 1.33
LINK N CSO A 234 C ASN A 233 1555 1555 1.32
LINK C CSO A 234 N THR A 235 1555 1555 1.33
LINK N CSO A 284 C ASP A 283 1555 1555 1.33
LINK C CSO A 284 N LEU A 285 1555 1555 1.33
LINK N CSO A 423 C VAL A 422 1555 1555 1.33
LINK C CSO A 423 N ALA A 424 1555 1555 1.33
LINK SG2 GSH A1030 SG CYS A 58 1555 1555 2.13
CISPEP 1 HIS A 374 PRO A 375 0 -7.45
CISPEP 2 HIS A 467 PRO A 468 0 -5.85
SITE 1 AC1 7 ARG A 218 HIS A 219 ARG A 224 HOH A 519
SITE 2 AC1 7 HOH A 590 HOH A 615 HOH A 851
SITE 1 AC2 36 GLY A 27 GLY A 29 SER A 30 GLY A 31
SITE 2 AC2 36 GLU A 50 SER A 51 HIS A 52 GLY A 56
SITE 3 AC2 36 THR A 57 CYS A 58 CSO A 63 LYS A 66
SITE 4 AC2 36 GLY A 128 HIS A 129 ALA A 130 ALA A 155
SITE 5 AC2 36 THR A 156 GLY A 157 TYR A 197 ARG A 291
SITE 6 AC2 36 GLY A 330 ASP A 331 LEU A 337 LEU A 338
SITE 7 AC2 36 THR A 339 PRO A 340 HIS A 467 PRO A 468
SITE 8 AC2 36 HOH A 502 HOH A 504 HOH A 510 HOH A 515
SITE 9 AC2 36 HOH A 554 HOH A 826 HOH A 859 HOH A 864
SITE 1 AC3 17 SER A 30 ALA A 34 ARG A 37 CYS A 58
SITE 2 AC3 17 VAL A 59 TYR A 114 THR A 339 ILE A 343
SITE 3 AC3 17 ARG A 347 HIS A 467 THR A 476 HOH A 516
SITE 4 AC3 17 HOH A 558 HOH A 560 HOH A 810 HOH A 812
SITE 5 AC3 17 HOH A1026
CRYST1 119.390 63.630 84.720 90.00 58.43 90.00 C 1 2 1 4
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 0.008376 0.000000 -0.005147 0.00000
SCALE2 0.000000 0.015716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013854 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
