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HEADER HYDROLASE/HYDROLASE INHIBITOR 14-JUN-12 4FLM
TITLE S-FORMYLGLUTATHIONE HYDROLASE W197I VARIANT CONTAINING COPPER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-FORMYLGLUTATHIONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FGH;
COMPND 5 EC: 3.1.2.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YJL068C, HRE299, J1102;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDATION SENSOR MOTIF, ESTERASE ACTIVITY ACTIVATION, ESTERASE
KEYWDS 2 ACTIVITY INHIBITION, CYSTEINE SULFINIC ACID, CYS-60, HYDROLASE-
KEYWDS 3 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.LEGLER,C.B.MILLARD
REVDAT 1 05-SEP-12 4FLM 0
JRNL AUTH P.M.LEGLER,D.H.LEARY,W.J.HERVEY,C.B.MILLARD
JRNL TITL A ROLE FOR HIS-160 IN PEROXIDE INHIBITION OF S. CEREVISIAE
JRNL TITL 2 S-FORMYLGLUTATHIONE HYDROLASE: EVIDENCE FOR AN OXIDATION
JRNL TITL 3 SENSITIVE MOTIF.
JRNL REF ARCH.BIOCHEM.BIOPHYS. 2012
JRNL REFN ESSN 1096-0384
JRNL PMID 22906720
JRNL DOI 10.1016/J.ABB.2012.08.001
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19408
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 + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1047
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.41
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1461
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4638
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : -0.09000
REMARK 3 B13 (A**2) : -0.07000
REMARK 3 B23 (A**2) : -0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 2.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.305
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4797 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6499 ; 1.202 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 573 ; 6.419 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 235 ;32.835 ;24.213
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 759 ;16.287 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;14.959 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 665 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3724 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4FLM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20473
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410
REMARK 200 RESOLUTION RANGE LOW (A) : 42.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.160
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11500
REMARK 200 FOR THE DATA SET : 12.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.43
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39670
REMARK 200 FOR SHELL : 3.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM ACETATE, 0.085 M
REMARK 280 SODIUM ACETATE TRIHYDRATE, PH 4.6, 25.5% PEG4000, 15% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 2030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 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 PHE A 43
REMARK 465 PRO A 44
REMARK 465 ARG A 45
REMARK 465 ASP A 92
REMARK 465 GLU A 93
REMARK 465 VAL A 94
REMARK 465 ALA A 95
REMARK 465 ASN A 96
REMARK 465 ASP A 97
REMARK 465 PRO A 98
REMARK 465 GLU A 99
REMARK 465 PHE B 43
REMARK 465 PRO B 44
REMARK 465 ARG B 45
REMARK 465 ASN B 46
REMARK 465 ASP B 97
REMARK 465 PRO B 98
REMARK 465 GLU B 99
REMARK 465 GLY B 100
REMARK 465 LYS B 143
REMARK 465 ASN B 144
REMARK 465 GLY B 145
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 CYS A 10 -131.17 45.88
REMARK 500 LYS A 25 14.58 54.02
REMARK 500 GLN A 41 68.01 -117.29
REMARK 500 THR A 59 -29.30 88.69
REMARK 500 ALA A 108 35.97 -152.54
REMARK 500 PHE A 110 14.29 59.68
REMARK 500 LYS A 131 -60.92 -125.46
REMARK 500 ASP A 153 -73.65 -94.31
REMARK 500 SDP A 161 -115.84 61.63
REMARK 500 GLU A 208 41.77 -109.14
REMARK 500 ASP A 264 -2.00 77.12
REMARK 500 ASP A 275 -146.46 -106.66
REMARK 500 CYS B 10 -132.68 52.26
REMARK 500 THR B 59 -14.66 81.29
REMARK 500 ALA B 108 44.17 -150.16
REMARK 500 PHE B 110 19.86 51.08
REMARK 500 GLN B 124 60.25 -105.73
REMARK 500 LYS B 131 -66.11 -120.61
REMARK 500 ASP B 153 -77.47 -94.42
REMARK 500 SDP B 161 -113.63 65.22
REMARK 500 LYS B 249 62.12 34.14
REMARK 500 ASP B 275 -147.48 -106.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 143 ASN A 144 148.01
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 CU B 301 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 1 N
REMARK 620 2 HIS B 140 ND1 116.9
REMARK 620 3 MET B 1 O 70.6 96.4
REMARK 620 4 HOH B 473 O 104.5 104.7 157.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 301 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 140 ND1
REMARK 620 2 MET A 1 O 96.7
REMARK 620 3 HOH A 454 O 124.5 138.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C6B RELATED DB: PDB
REMARK 900 S-FORMYLGLUTATHIONE HYDROLASE W197I VARIANT CONTAINING A
REMARK 900 CYSTEINE SULFENIC ACID
REMARK 900 RELATED ID: 1PV1 RELATED DB: PDB
REMARK 900 S-FORMYLGLUTATHIONE HYDROLASE
REMARK 900 RELATED ID: 4FOL RELATED DB: PDB
REMARK 900 S-FORMYLGLUTATHIONE HYDROLASE VARIANT H160I
DBREF 4FLM A 1 299 UNP P40363 SFGH_YEAST 1 299
DBREF 4FLM B 1 299 UNP P40363 SFGH_YEAST 1 299
SEQADV 4FLM ILE A 197 UNP P40363 TRP 197 ENGINEERED MUTATION
SEQADV 4FLM ILE B 197 UNP P40363 TRP 197 ENGINEERED MUTATION
SEQRES 1 A 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 A 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 A 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 A 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 A 299 PHE TYR LEU SER GLY LEU THR CSD THR PRO ASP ASN ALA
SEQRES 6 A 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 A 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 A 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 A 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 A 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 A 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 A 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 A 299 ILE THR GLY HIS SDP MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 A 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 A 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 A 299 PRO ILE GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 A 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 A 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 A 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 A 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 A 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 A 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 A 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
SEQRES 1 B 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 B 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 B 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 B 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 B 299 PHE TYR LEU SER GLY LEU THR CSD THR PRO ASP ASN ALA
SEQRES 6 B 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 B 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 B 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 B 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 B 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 B 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 B 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 B 299 ILE THR GLY HIS SDP MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 B 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 B 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 B 299 PRO ILE GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 B 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 B 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 B 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 B 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 B 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 B 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 B 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
MODRES 4FLM CSD A 60 CYS 3-SULFINOALANINE
MODRES 4FLM SDP A 161 SER
MODRES 4FLM CSD B 60 CYS 3-SULFINOALANINE
MODRES 4FLM SDP B 161 SER
HET CSD A 60 8
HET SDP A 161 14
HET CSD B 60 8
HET SDP B 161 14
HET CU A 301 1
HET CU B 301 1
HETNAM CSD 3-SULFINOALANINE
HETNAM SDP 2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC ACID
HETNAM CU COPPER (II) ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 1 SDP 2(C7 H16 N O6 P)
FORMUL 3 CU 2(CU 2+)
FORMUL 5 HOH *133(H2 O)
HELIX 1 1 PRO A 35 ALA A 40 1 6
HELIX 2 2 PRO A 62 ALA A 69 1 8
HELIX 3 3 PHE A 70 GLY A 79 1 10
HELIX 4 4 GLN A 124 LYS A 131 1 8
HELIX 5 5 LYS A 131 ASN A 142 1 12
HELIX 6 6 SDP A 161 GLY A 174 1 14
HELIX 7 7 ASN A 191 ASN A 194 5 4
HELIX 8 8 VAL A 195 GLY A 207 1 13
HELIX 9 9 GLU A 209 ALA A 215 1 7
HELIX 10 10 ASP A 217 ILE A 222 1 6
HELIX 11 11 LYS A 223 ILE A 225 5 3
HELIX 12 12 PHE A 243 LEU A 248 1 6
HELIX 13 13 GLU A 251 VAL A 257 1 7
HELIX 14 14 SER A 277 LEU A 296 1 20
HELIX 15 15 PRO B 35 ALA B 40 5 6
HELIX 16 16 THR B 61 ALA B 69 1 9
HELIX 17 17 PHE B 70 GLY B 79 1 10
HELIX 18 18 GLN B 124 LYS B 131 1 8
HELIX 19 19 LYS B 131 ASN B 142 1 12
HELIX 20 20 SDP B 161 GLY B 174 1 14
HELIX 21 21 TYR B 175 LYS B 178 5 4
HELIX 22 22 ASN B 191 ASN B 194 5 4
HELIX 23 23 VAL B 195 GLY B 207 1 13
HELIX 24 24 TRP B 213 TYR B 216 5 4
HELIX 25 25 ASP B 217 ILE B 222 1 6
HELIX 26 26 LYS B 223 ILE B 225 5 3
HELIX 27 27 PRO B 250 VAL B 257 1 8
HELIX 28 28 SER B 277 LEU B 296 1 20
SHEET 1 A 9 LYS A 2 VAL A 9 0
SHEET 2 A 9 GLY A 12 ASN A 20 -1 O LEU A 14 N PHE A 7
SHEET 3 A 9 SER A 27 LEU A 34 -1 O VAL A 30 N LEU A 17
SHEET 4 A 9 ALA A 81 PRO A 85 -1 O PHE A 84 N ASN A 31
SHEET 5 A 9 ILE A 49 LEU A 55 1 N PRO A 50 O ALA A 81
SHEET 6 A 9 LEU A 149 GLY A 159 1 O THR A 158 N PHE A 53
SHEET 7 A 9 SER A 182 PHE A 186 1 O PHE A 186 N GLY A 159
SHEET 8 A 9 ILE A 233 GLY A 238 1 O LEU A 234 N ALA A 185
SHEET 9 A 9 VAL A 266 VAL A 271 1 O GLU A 267 N ILE A 233
SHEET 1 B 9 LYS B 2 VAL B 9 0
SHEET 2 B 9 GLY B 12 ASN B 20 -1 O LYS B 16 N LYS B 5
SHEET 3 B 9 SER B 27 LEU B 34 -1 O MET B 28 N HIS B 19
SHEET 4 B 9 ALA B 81 PHE B 84 -1 O PHE B 84 N ASN B 31
SHEET 5 B 9 THR B 51 LEU B 55 1 N VAL B 52 O VAL B 83
SHEET 6 B 9 VAL B 155 GLY B 159 1 O ALA B 156 N THR B 51
SHEET 7 B 9 SER B 182 PHE B 186 1 O PHE B 186 N GLY B 159
SHEET 8 B 9 ILE B 233 GLY B 238 1 O LEU B 234 N ALA B 185
SHEET 9 B 9 VAL B 266 VAL B 271 1 O VAL B 271 N VAL B 237
LINK C THR A 59 N CSD A 60 1555 1555 1.33
LINK C CSD A 60 N THR A 61 1555 1555 1.33
LINK C HIS A 160 N SDP A 161 1555 1555 1.34
LINK C SDP A 161 N MET A 162 1555 1555 1.34
LINK C THR B 59 N CSD B 60 1555 1555 1.34
LINK C CSD B 60 N THR B 61 1555 1555 1.34
LINK C HIS B 160 N SDP B 161 1555 1555 1.34
LINK C SDP B 161 N MET B 162 1555 1555 1.34
LINK N MET B 1 CU CU B 301 1555 1555 1.87
LINK ND1 HIS B 140 CU CU B 301 1555 1555 2.07
LINK ND1 HIS A 140 CU CU A 301 1555 1555 2.09
LINK O MET A 1 CU CU A 301 1555 1555 2.39
LINK O MET B 1 CU CU B 301 1555 1555 2.61
LINK CU CU B 301 O HOH B 473 1555 1555 2.11
LINK CU CU A 301 O HOH A 454 1555 1555 2.31
CISPEP 1 GLU A 117 PRO A 118 0 -2.53
CISPEP 2 GLU B 117 PRO B 118 0 6.87
SITE 1 AC1 3 MET A 1 HIS A 140 HOH A 454
SITE 1 AC2 3 MET B 1 HIS B 140 HOH B 473
CRYST1 48.826 49.203 66.845 73.92 80.44 62.60 P 1 2
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 0.020481 -0.010616 -0.001045 0.00000
SCALE2 0.000000 0.022892 -0.005387 0.00000
SCALE3 0.000000 0.000000 0.015585 0.00000
TER 2328 ILE A 299
TER 4660 ILE B 299
MASTER 341 0 6 28 18 0 2 6 4773 2 61 46
END |