HEADER LYASE 09-JUL-05 2CZ0
TITLE PHOTO-ACTIVATION STATE OF FE-TYPE NHASE IN AEROBIC CONDITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRILE HYDRATASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NITRILASE, NHASE;
COMPND 5 EC: 4.2.1.84;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NITRILE HYDRATASE SUBUNIT BETA;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: NITRILASE, NHASE;
COMPND 10 EC: 4.2.1.84
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS ERYTHROPOLIS;
SOURCE 3 ORGANISM_TAXID: 1833;
SOURCE 4 STRAIN: N771;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: RHODOCOCCUS ERYTHROPOLIS;
SOURCE 7 ORGANISM_TAXID: 1833;
SOURCE 8 STRAIN: N771
KEYWDS CYSTEINE-SULFINIC ACID, CYSTEINE-SULFENIC ACID, POST-
KEYWDS 2 TRANSLATIONAL MODIFICATION, NITRILE, HYDRATION, NON-HEM
KEYWDS 3 IRON, PHOTO-REACTIVE, OVER-OXIDIZATION, STRUCTURAL GENOMICS,
KEYWDS 4 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 5 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 6 INITIATIVE, RSGI, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KAWANO,K.HASHIMOTO,M.ODAKA,H.NAKAYAMA,K.TAKIO,I.ENDO,
AUTHOR 2 N.KAMIYA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 3 (RSGI)
REVDAT 2 24-FEB-09 2CZ0 1 VERSN
REVDAT 1 09-JAN-06 2CZ0 0
JRNL AUTH Y.KAWANO,K.HASHIMOTO,M.ODAKA,H.NAKAYAMA,K.TAKIO,
JRNL AUTH 2 I.ENDO,N.KAMIYA
JRNL TITL PHOTO-ACTIVATION STATE OF FE-TYPE NHASE IN AEROBIC
JRNL TITL 2 CONDITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.5
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.174
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.173
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 11.200
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 6457
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 57547
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.166
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.165
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 11.200
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 5734
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 51412
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3199
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 391
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3613.00
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 1
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 14533
REMARK 3 NUMBER OF RESTRAINTS : 13368
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.021
REMARK 3 ANGLE DISTANCES (A) : 0.026
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.025
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.047
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.056
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.107
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.062
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.035
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CZ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-05.
REMARK 100 THE RCSB ID CODE IS RCSB024782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.708
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64041
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, MAGNESIUM CHLORIDE, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
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 57.00800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.09100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.00800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.09100
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
REMARK 350 TOTAL BURIED SURFACE AREA: 7800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 A1468 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 400 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 SER A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 ILE A 4
REMARK 465 ASP A 5
REMARK 465 HIS A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 VAL A 206
REMARK 465 ALA B 212
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 135 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TYR B 37 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR B 67 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 TYR B 76 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TYR B 76 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 107 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR B 207 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
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 ALA A 164 -130.09 -134.87
REMARK 500 ARG B 141 43.53 -108.67
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 300 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 109 SG
REMARK 620 2 CSD A 112 SG 91.3
REMARK 620 3 SER A 113 N 90.8 96.8
REMARK 620 4 CSD A 114 N 93.7 174.9 83.1
REMARK 620 5 CSD A 114 SG 93.3 94.9 167.5 84.9
REMARK 620 6 HOH A1302 O 176.1 88.1 85.4 86.9 90.6
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 300
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUA A 1301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CYZ RELATED DB: PDB
REMARK 900 FE-TYPE NHASE
REMARK 900 RELATED ID: 2CZ1 RELATED DB: PDB
REMARK 900 FE-TYPE NHASE WITH N-BA
REMARK 900 RELATED ID: AR_001000506.4 RELATED DB: TARGETDB
DBREF 2CZ0 A 1 206 UNP P13448 NHAA_RHOER 1 206
DBREF 2CZ0 B 1 212 UNP P13449 NHAB_RHOER 1 212
SEQADV 2CZ0 CSD A 112 UNP P13448 CYS 112 MODIFIED RESIDUE
SEQADV 2CZ0 CSD A 114 UNP P13448 CYS 114 MODIFIED RESIDUE
SEQRES 1 A 206 SER VAL THR ILE ASP HIS THR THR GLU ASN ALA ALA PRO
SEQRES 2 A 206 ALA GLN ALA PRO VAL SER ASP ARG ALA TRP ALA LEU PHE
SEQRES 3 A 206 ARG ALA LEU ASP GLY LYS GLY LEU VAL PRO ASP GLY TYR
SEQRES 4 A 206 VAL GLU GLY TRP LYS LYS THR PHE GLU GLU ASP PHE SER
SEQRES 5 A 206 PRO ARG ARG GLY ALA GLU LEU VAL ALA ARG ALA TRP THR
SEQRES 6 A 206 ASP PRO GLU PHE ARG GLN LEU LEU LEU THR ASP GLY THR
SEQRES 7 A 206 ALA ALA VAL ALA GLN TYR GLY TYR LEU GLY PRO GLN GLY
SEQRES 8 A 206 GLU TYR ILE VAL ALA VAL GLU ASP THR PRO THR LEU LYS
SEQRES 9 A 206 ASN VAL ILE VAL CYS SER LEU CSD SER CSD THR ALA TRP
SEQRES 10 A 206 PRO ILE LEU GLY LEU PRO PRO THR TRP TYR LYS SER PHE
SEQRES 11 A 206 GLU TYR ARG ALA ARG VAL VAL ARG GLU PRO ARG LYS VAL
SEQRES 12 A 206 LEU SER GLU MET GLY THR GLU ILE ALA SER ASP ILE GLU
SEQRES 13 A 206 ILE ARG VAL TYR ASP THR THR ALA GLU THR ARG TYR MET
SEQRES 14 A 206 VAL LEU PRO GLN ARG PRO ALA GLY THR GLU GLY TRP SER
SEQRES 15 A 206 GLN GLU GLN LEU GLN GLU ILE VAL THR LYS ASP CYS LEU
SEQRES 16 A 206 ILE GLY VAL ALA ILE PRO GLN VAL PRO THR VAL
SEQRES 1 B 212 MET ASP GLY VAL HIS ASP LEU ALA GLY VAL GLN GLY PHE
SEQRES 2 B 212 GLY LYS VAL PRO HIS THR VAL ASN ALA ASP ILE GLY PRO
SEQRES 3 B 212 THR PHE HIS ALA GLU TRP GLU HIS LEU PRO TYR SER LEU
SEQRES 4 B 212 MET PHE ALA GLY VAL ALA GLU LEU GLY ALA PHE SER VAL
SEQRES 5 B 212 ASP GLU VAL ARG TYR VAL VAL GLU ARG MET GLU PRO ARG
SEQRES 6 B 212 HIS TYR MET MET THR PRO TYR TYR GLU ARG TYR VAL ILE
SEQRES 7 B 212 GLY VAL ALA THR LEU MET VAL GLU LYS GLY ILE LEU THR
SEQRES 8 B 212 GLN ASP GLU LEU GLU SER LEU ALA GLY GLY PRO PHE PRO
SEQRES 9 B 212 LEU SER ARG PRO SER GLU SER GLU GLY ARG PRO ALA PRO
SEQRES 10 B 212 VAL GLU THR THR THR PHE GLU VAL GLY GLN ARG VAL ARG
SEQRES 11 B 212 VAL ARG ASP GLU TYR VAL PRO GLY HIS ILE ARG MET PRO
SEQRES 12 B 212 ALA TYR CYS ARG GLY ARG VAL GLY THR ILE SER HIS ARG
SEQRES 13 B 212 THR THR GLU LYS TRP PRO PHE PRO ASP ALA ILE GLY HIS
SEQRES 14 B 212 GLY ARG ASN ASP ALA GLY GLU GLU PRO THR TYR HIS VAL
SEQRES 15 B 212 LYS PHE ALA ALA GLU GLU LEU PHE GLY SER ASP THR ASP
SEQRES 16 B 212 GLY GLY SER VAL VAL VAL ASP LEU PHE GLU GLY TYR LEU
SEQRES 17 B 212 GLU PRO ALA ALA
MODRES 2CZ0 CSD A 112 CYS 3-SULFINOALANINE
MODRES 2CZ0 CSD A 114 CYS 3-SULFINOALANINE
HET CSD A 112 8
HET CSD A 114 8
HET FE A 300 1
HET BUA A1301 12
HETNAM CSD 3-SULFINOALANINE
HETNAM FE FE (III) ION
HETNAM BUA BUTANOIC ACID
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 FE FE 3+
FORMUL 4 BUA C4 H8 O2
FORMUL 5 HOH *391(H2 O)
HELIX 1 1 PRO A 17 GLY A 31 1 15
HELIX 2 2 GLY A 38 ASP A 50 1 13
HELIX 3 3 SER A 52 ASP A 66 1 15
HELIX 4 4 ASP A 66 ASP A 76 1 11
HELIX 5 5 ASP A 76 TYR A 84 1 9
HELIX 6 6 ALA A 116 GLY A 121 1 6
HELIX 7 7 PRO A 124 SER A 129 1 6
HELIX 8 8 SER A 129 VAL A 136 1 8
HELIX 9 9 GLU A 139 GLY A 148 1 10
HELIX 10 10 SER A 182 GLU A 188 1 7
HELIX 11 11 THR A 191 GLY A 197 1 7
HELIX 12 12 HIS B 34 GLU B 46 1 13
HELIX 13 13 SER B 51 ARG B 61 1 11
HELIX 14 14 GLU B 63 THR B 70 1 8
HELIX 15 15 PRO B 71 LYS B 87 1 17
HELIX 16 16 THR B 91 GLY B 100 1 10
HELIX 17 17 PRO B 143 ARG B 147 5 5
HELIX 18 18 PHE B 163 GLY B 168 1 6
HELIX 19 19 ALA B 186 GLY B 191 1 6
SHEET 1 A 2 ILE A 94 GLU A 98 0
SHEET 2 A 2 ARG A 167 LEU A 171 1 O LEU A 171 N VAL A 97
SHEET 1 B 7 LEU A 103 VAL A 108 0
SHEET 2 B 7 GLU A 156 ASP A 161 1 O GLU A 156 N LYS A 104
SHEET 3 B 7 SER B 198 PHE B 204 1 O VAL B 200 N VAL A 159
SHEET 4 B 7 THR B 179 ALA B 185 -1 N PHE B 184 O VAL B 199
SHEET 5 B 7 VAL B 150 ARG B 156 -1 N SER B 154 O HIS B 181
SHEET 6 B 7 ARG B 128 VAL B 131 -1 N VAL B 129 O GLY B 151
SHEET 7 B 7 LEU B 208 PRO B 210 -1 O GLU B 209 N ARG B 130
LINK FE FE A 300 SG CYS A 109 1555 1555 2.28
LINK FE FE A 300 SG CSD A 112 1555 1555 2.20
LINK FE FE A 300 N SER A 113 1555 1555 2.01
LINK FE FE A 300 N CSD A 114 1555 1555 1.95
LINK FE FE A 300 SG CSD A 114 1555 1555 2.15
LINK C LEU A 111 N CSD A 112 1555 1555 1.34
LINK C CSD A 112 N SER A 113 1555 1555 1.34
LINK C SER A 113 N CSD A 114 1555 1555 1.34
LINK C CSD A 114 N THR A 115 1555 1555 1.32
LINK FE FE A 300 O HOH A1302 1555 1555 2.05
SITE 1 AC1 5 CYS A 109 CSD A 112 SER A 113 CSD A 114
SITE 2 AC1 5 HOH A1302
SITE 1 AC2 10 GLN A 90 CSD A 114 TRP A 117 HOH A1302
SITE 2 AC2 10 HOH A1370 MET B 40 VAL B 52 ARG B 56
SITE 3 AC2 10 TYR B 72 TYR B 76
CRYST1 114.016 60.182 81.573 90.00 125.15 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 0.008771 0.000000 0.006176 0.00000
SCALE2 0.000000 0.016616 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014993 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
