HEADER TRANSFERASE 06-JUN-03 1PL1
TITLE CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE (GST) A1-1 IN
TITLE 2 COMPLEX WITH A DECARBOXY-GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE A1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GTH1, HA SUBUNIT 1, GST-EPSILON, GSTA1-1, GST CLASS-ALPHA;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES
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 DOMAIN1:ALPHA-BETA, DOMAIN2:ALPHA-HELICAL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.GRAHN,E.JAKOBSSON,A.GUSTAFSSON,L.GREHN,B.OLIN,M.WAHLBERG,D.MADSEN,
AUTHOR 2 G.J.KLEYWEGT,B.MANNERVIK
REVDAT 5 07-MAR-18 1PL1 1 REMARK
REVDAT 4 24-FEB-09 1PL1 1 VERSN
REVDAT 3 16-SEP-08 1PL1 1 JRNL
REVDAT 2 14-FEB-06 1PL1 1 AUTHOR JRNL
REVDAT 1 22-JUN-04 1PL1 0
JRNL AUTH E.GRAHN,M.NOVOTNY,E.JAKOBSSON,A.GUSTAFSSON,L.GREHN,B.OLIN,
JRNL AUTH 2 D.MADSEN,M.WAHLBERG,B.MANNERVIK,G.J.KLEYWEGT
JRNL TITL NEW CRYSTAL STRUCTURES OF HUMAN GLUTATHIONE TRANSFERASE A1-1
JRNL TITL 2 SHED LIGHT ON GLUTATHIONE BINDING AND THE CONFORMATION OF
JRNL TITL 3 THE C-TERMINAL HELIX.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 197 2006
JRNL REFN ISSN 0907-4449
JRNL PMID 16421451
JRNL DOI 10.1107/S0907444905039296
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 39448
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4393
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2776
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1400
REMARK 3 BIN FREE R VALUE SET COUNT : 307
REMARK 3 BIN FREE R VALUE : 0.2200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 603
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.31000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.011
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3740 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3557 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5015 ; 1.553 ; 2.016
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8326 ; 0.962 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 440 ; 5.523 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 544 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4007 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 740 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 792 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4098 ; 0.243 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2145 ; 0.095 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 452 ; 0.137 ; 0.200
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): 4 ; 0.141 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 39 ; 0.199 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.141 ; 0.200
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): 2215 ; 0.852 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3578 ; 1.521 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1525 ; 2.378 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1437 ; 3.912 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1PL1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43853
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
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 (%): 44.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS-HCL, DTT, PH 7.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 49.75250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.12350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.75250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.12350
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: 5250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19730 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 A1000 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1002 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 983 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 MET B 1
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 ARG A 13 -70.29 -63.75
REMARK 500 GLN A 67 116.72 76.99
REMARK 500 ASP A 171 108.74 -165.90
REMARK 500 GLU B 3 149.05 171.12
REMARK 500 GLN B 67 112.01 76.20
REMARK 500 ASP B 171 111.33 -167.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABY A 654
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABY B 655
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PKW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE A1-1 IN COMPLEX
REMARK 900 WITH GLUTATHIONE
REMARK 900 RELATED ID: 1PKZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE A1-1 COMPLEXED
REMARK 900 WITH 2-HYDROXYETHYL DISULFIDE
REMARK 900 RELATED ID: 1PL2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE A1-1 T68E MUTANT
REMARK 900 IN COMPLEX WITH DECARBOXY-GLUTATHIONE
DBREF 1PL1 A 1 222 UNP P08263 GSTA1_HUMAN 1 222
DBREF 1PL1 B 1 222 UNP P08263 GSTA1_HUMAN 1 222
SEQADV 1PL1 CSO A 112 UNP P08263 CYS 111 MODIFIED RESIDUE
SEQADV 1PL1 CSO B 112 UNP P08263 CYS 111 MODIFIED RESIDUE
SEQRES 1 A 222 MET ALA GLU LYS PRO LYS LEU HIS TYR PHE ASN ALA ARG
SEQRES 2 A 222 GLY ARG MET GLU SER THR ARG TRP LEU LEU ALA ALA ALA
SEQRES 3 A 222 GLY VAL GLU PHE GLU GLU LYS PHE ILE LYS SER ALA GLU
SEQRES 4 A 222 ASP LEU ASP LYS LEU ARG ASN ASP GLY TYR LEU MET PHE
SEQRES 5 A 222 GLN GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU
SEQRES 6 A 222 VAL GLN THR ARG ALA ILE LEU ASN TYR ILE ALA SER LYS
SEQRES 7 A 222 TYR ASN LEU TYR GLY LYS ASP ILE LYS GLU ARG ALA LEU
SEQRES 8 A 222 ILE ASP MET TYR ILE GLU GLY ILE ALA ASP LEU GLY GLU
SEQRES 9 A 222 MET ILE LEU LEU LEU PRO VAL CSO PRO PRO GLU GLU LYS
SEQRES 10 A 222 ASP ALA LYS LEU ALA LEU ILE LYS GLU LYS ILE LYS ASN
SEQRES 11 A 222 ARG TYR PHE PRO ALA PHE GLU LYS VAL LEU LYS SER HIS
SEQRES 12 A 222 GLY GLN ASP TYR LEU VAL GLY ASN LYS LEU SER ARG ALA
SEQRES 13 A 222 ASP ILE HIS LEU VAL GLU LEU LEU TYR TYR VAL GLU GLU
SEQRES 14 A 222 LEU ASP SER SER LEU ILE SER SER PHE PRO LEU LEU LYS
SEQRES 15 A 222 ALA LEU LYS THR ARG ILE SER ASN LEU PRO THR VAL LYS
SEQRES 16 A 222 LYS PHE LEU GLN PRO GLY SER PRO ARG LYS PRO PRO MET
SEQRES 17 A 222 ASP GLU LYS SER LEU GLU GLU ALA ARG LYS ILE PHE ARG
SEQRES 18 A 222 PHE
SEQRES 1 B 222 MET ALA GLU LYS PRO LYS LEU HIS TYR PHE ASN ALA ARG
SEQRES 2 B 222 GLY ARG MET GLU SER THR ARG TRP LEU LEU ALA ALA ALA
SEQRES 3 B 222 GLY VAL GLU PHE GLU GLU LYS PHE ILE LYS SER ALA GLU
SEQRES 4 B 222 ASP LEU ASP LYS LEU ARG ASN ASP GLY TYR LEU MET PHE
SEQRES 5 B 222 GLN GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU
SEQRES 6 B 222 VAL GLN THR ARG ALA ILE LEU ASN TYR ILE ALA SER LYS
SEQRES 7 B 222 TYR ASN LEU TYR GLY LYS ASP ILE LYS GLU ARG ALA LEU
SEQRES 8 B 222 ILE ASP MET TYR ILE GLU GLY ILE ALA ASP LEU GLY GLU
SEQRES 9 B 222 MET ILE LEU LEU LEU PRO VAL CSO PRO PRO GLU GLU LYS
SEQRES 10 B 222 ASP ALA LYS LEU ALA LEU ILE LYS GLU LYS ILE LYS ASN
SEQRES 11 B 222 ARG TYR PHE PRO ALA PHE GLU LYS VAL LEU LYS SER HIS
SEQRES 12 B 222 GLY GLN ASP TYR LEU VAL GLY ASN LYS LEU SER ARG ALA
SEQRES 13 B 222 ASP ILE HIS LEU VAL GLU LEU LEU TYR TYR VAL GLU GLU
SEQRES 14 B 222 LEU ASP SER SER LEU ILE SER SER PHE PRO LEU LEU LYS
SEQRES 15 B 222 ALA LEU LYS THR ARG ILE SER ASN LEU PRO THR VAL LYS
SEQRES 16 B 222 LYS PHE LEU GLN PRO GLY SER PRO ARG LYS PRO PRO MET
SEQRES 17 B 222 ASP GLU LYS SER LEU GLU GLU ALA ARG LYS ILE PHE ARG
SEQRES 18 B 222 PHE
MODRES 1PL1 CSO A 112 CYS S-HYDROXYCYSTEINE
MODRES 1PL1 CSO B 112 CYS S-HYDROXYCYSTEINE
HET CSO A 112 7
HET CSO B 112 7
HET CL A 702 1
HET ABY A 654 26
HET CL B 701 1
HET ABY B 655 26
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM CL CHLORIDE ION
HETNAM ABY N-(4-AMINOBUTANOYL)-S-(4-METHOXYBENZYL)-L-
HETNAM 2 ABY CYSTEINYLGLYCINE
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 3 CL 2(CL 1-)
FORMUL 4 ABY 2(C17 H25 N3 O5 S)
FORMUL 7 HOH *603(H2 O)
HELIX 1 1 MET A 16 ALA A 26 1 11
HELIX 2 2 SER A 37 ASP A 47 1 11
HELIX 3 3 GLN A 67 TYR A 79 1 13
HELIX 4 4 ASP A 85 LEU A 109 1 25
HELIX 5 5 PRO A 110 CSO A 112 5 3
HELIX 6 6 PRO A 113 GLU A 115 5 3
HELIX 7 7 GLU A 116 ARG A 131 1 16
HELIX 8 8 ARG A 131 GLY A 144 1 14
HELIX 9 9 SER A 154 ASP A 171 1 18
HELIX 10 10 PHE A 178 ASN A 190 1 13
HELIX 11 11 LEU A 191 GLN A 199 1 9
HELIX 12 12 ASP A 209 ARG A 221 1 13
HELIX 13 13 ARG B 13 ARG B 15 5 3
HELIX 14 14 MET B 16 ALA B 26 1 11
HELIX 15 15 SER B 37 ASP B 47 1 11
HELIX 16 16 GLN B 67 TYR B 79 1 13
HELIX 17 17 ASP B 85 LEU B 109 1 25
HELIX 18 18 PRO B 110 CSO B 112 5 3
HELIX 19 19 PRO B 113 GLU B 115 5 3
HELIX 20 20 GLU B 116 ARG B 131 1 16
HELIX 21 21 ARG B 131 GLY B 144 1 14
HELIX 22 22 SER B 154 ASP B 171 1 18
HELIX 23 23 PHE B 178 LEU B 191 1 14
HELIX 24 24 LEU B 191 GLN B 199 1 9
HELIX 25 25 ASP B 209 ARG B 221 1 13
SHEET 1 A 4 GLU A 31 PHE A 34 0
SHEET 2 A 4 LYS A 6 TYR A 9 1 N LEU A 7 O LYS A 33
SHEET 3 A 4 MET A 57 ILE A 60 -1 O MET A 57 N HIS A 8
SHEET 4 A 4 MET A 63 VAL A 66 -1 O LEU A 65 N VAL A 58
SHEET 1 B 4 GLU B 31 PHE B 34 0
SHEET 2 B 4 LYS B 6 TYR B 9 1 N LEU B 7 O GLU B 31
SHEET 3 B 4 MET B 57 ILE B 60 -1 O MET B 57 N HIS B 8
SHEET 4 B 4 MET B 63 VAL B 66 -1 O LEU B 65 N VAL B 58
LINK C VAL A 111 N CSO A 112 1555 1555 1.34
LINK C CSO A 112 N PRO A 113 1555 1555 1.35
LINK C VAL B 111 N CSO B 112 1555 1555 1.32
LINK C CSO B 112 N PRO B 113 1555 1555 1.34
CISPEP 1 VAL A 55 PRO A 56 0 3.56
CISPEP 2 VAL B 55 PRO B 56 0 0.99
SITE 1 AC1 3 PRO B 56 THR B 68 ABY B 655
SITE 1 AC2 3 PRO A 56 THR A 68 ABY A 654
SITE 1 AC3 13 TYR A 9 ARG A 45 GLN A 54 VAL A 55
SITE 2 AC3 13 GLN A 67 LEU A 107 MET A 208 PHE A 220
SITE 3 AC3 13 CL A 702 HOH A 818 HOH A 849 ASP B 101
SITE 4 AC3 13 ARG B 131
SITE 1 AC4 16 ASP A 101 ARG A 131 TYR B 9 ARG B 45
SITE 2 AC4 16 GLN B 54 VAL B 55 GLN B 67 LEU B 107
SITE 3 AC4 16 MET B 208 PHE B 220 CL B 701 HOH B 727
SITE 4 AC4 16 HOH B 746 HOH B 770 HOH B 898 HOH B 935
CRYST1 99.505 90.247 51.130 90.00 93.67 90.00 C 1 2 1 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 0.010050 0.000000 0.000645 0.00000
SCALE2 0.000000 0.011081 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
