HEADER TRANSFERASE 06-NOV-01 1KBN
TITLE GLUTATHIONE TRANSFERASE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE P;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 TRANSFERASE, MULTIGENE FAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ROSSJOHN,M.W.PARKER
REVDAT 5 10-NOV-21 1KBN 1 REMARK SEQADV
REVDAT 4 07-DEC-11 1KBN 1 HET HETATM HETNAM
REVDAT 3 13-JUL-11 1KBN 1 VERSN
REVDAT 2 24-FEB-09 1KBN 1 VERSN
REVDAT 1 11-NOV-03 1KBN 0
JRNL AUTH J.ROSSJOHN,M.W.PARKER
JRNL TITL CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 29965
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.360
REMARK 3 FREE R VALUE TEST SET COUNT : 1606
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 : 3256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 321
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 1KBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014783.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 34.43650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.70950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.38750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.70950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.43650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.38750
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: 4500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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 70 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 70 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH2 ANGL. DEV. = -7.5 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 GLN A 64 112.33 83.90
REMARK 500 LEU A 78 52.38 -118.41
REMARK 500 TYR A 79 44.83 -142.45
REMARK 500 ASN A 110 71.54 -154.57
REMARK 500 THR A 141 -104.89 -113.55
REMARK 500 CYS A 169 -9.21 -59.00
REMARK 500 GLN B 64 111.93 84.53
REMARK 500 LEU B 78 51.77 -119.03
REMARK 500 TYR B 79 44.52 -141.84
REMARK 500 ASN B 110 71.30 -154.45
REMARK 500 THR B 141 -105.12 -113.63
REMARK 500 CYS B 169 -9.89 -59.60
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 GSH A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2201
DBREF 1KBN A 1 209 UNP P09211 GSTP1_HUMAN 1 209
DBREF 1KBN B 1 209 UNP P09211 GSTP1_HUMAN 1 209
SEQADV 1KBN ALA A 148 UNP P09211 ILE 148 ENGINEERED MUTATION
SEQADV 1KBN ALA A 153 UNP P09211 TYR 153 ENGINEERED MUTATION
SEQADV 1KBN ALA B 148 UNP P09211 ILE 148 ENGINEERED MUTATION
SEQADV 1KBN ALA B 153 UNP P09211 TYR 153 ENGINEERED MUTATION
SEQRES 1 A 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 A 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 A 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES 4 A 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES 5 A 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 A 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES 7 A 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES 8 A 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES 9 A 209 SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES 10 A 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES 11 A 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES 12 A 209 VAL GLY ASP GLN ALA SER PHE ALA ASP ALA ASN LEU LEU
SEQRES 13 A 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES 14 A 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES 15 A 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES 16 A 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 A 209 GLN
SEQRES 1 B 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 B 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 B 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES 4 B 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES 5 B 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 B 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES 7 B 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES 8 B 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES 9 B 209 SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES 10 B 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES 11 B 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES 12 B 209 VAL GLY ASP GLN ALA SER PHE ALA ASP ALA ASN LEU LEU
SEQRES 13 B 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES 14 B 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES 15 B 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES 16 B 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 B 209 GLN
HET GSH A1001 20
HET MES A1101 12
HET GOL A1201 6
HET GSH B2001 20
HET MES B2101 12
HET GOL B2201 6
HETNAM GSH GLUTATHIONE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GSH 2(C10 H17 N3 O6 S)
FORMUL 4 MES 2(C6 H13 N O4 S)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 9 HOH *321(H2 O)
HELIX 1 1 ARG A 11 ARG A 13 5 3
HELIX 2 2 CYS A 14 GLN A 24 1 11
HELIX 3 3 THR A 34 GLU A 40 1 7
HELIX 4 4 GLY A 41 CYS A 47 1 7
HELIX 5 5 GLN A 64 GLY A 77 1 14
HELIX 6 6 ASP A 82 ASN A 110 1 29
HELIX 7 7 ASN A 110 GLN A 135 1 26
HELIX 8 8 ASN A 136 LYS A 140 5 5
HELIX 9 9 SER A 149 ALA A 166 1 18
HELIX 10 10 PHE A 173 ARG A 186 1 14
HELIX 11 11 ARG A 186 SER A 195 1 10
HELIX 12 12 SER A 195 ASN A 200 1 6
HELIX 13 13 ARG B 11 ARG B 13 5 3
HELIX 14 14 CYS B 14 GLN B 24 1 11
HELIX 15 15 THR B 34 GLU B 40 1 7
HELIX 16 16 GLY B 41 CYS B 47 1 7
HELIX 17 17 GLN B 64 GLY B 77 1 14
HELIX 18 18 ASP B 82 ASN B 110 1 29
HELIX 19 19 ASN B 110 GLN B 135 1 26
HELIX 20 20 ASN B 136 LYS B 140 5 5
HELIX 21 21 SER B 149 ALA B 166 1 18
HELIX 22 22 PHE B 173 ARG B 186 1 14
HELIX 23 23 ARG B 186 SER B 195 1 10
HELIX 24 24 SER B 195 ASN B 200 1 6
SHEET 1 A 4 TRP A 28 VAL A 32 0
SHEET 2 A 4 TYR A 3 TYR A 7 1 N VAL A 5 O GLU A 31
SHEET 3 A 4 LYS A 54 ASP A 57 -1 O LYS A 54 N VAL A 6
SHEET 4 A 4 LEU A 60 TYR A 63 -1 O LEU A 62 N PHE A 55
SHEET 1 B 4 TRP B 28 VAL B 32 0
SHEET 2 B 4 TYR B 3 TYR B 7 1 N VAL B 5 O GLU B 31
SHEET 3 B 4 LYS B 54 ASP B 57 -1 O LYS B 54 N VAL B 6
SHEET 4 B 4 LEU B 60 TYR B 63 -1 O LEU B 62 N PHE B 55
CISPEP 1 PRO A 1 PRO A 2 0 0.00
CISPEP 2 LEU A 52 PRO A 53 0 0.46
CISPEP 3 PRO B 1 PRO B 2 0 0.57
CISPEP 4 LEU B 52 PRO B 53 0 0.25
SITE 1 AC1 17 TYR A 7 PHE A 8 ARG A 13 TRP A 38
SITE 2 AC1 17 LYS A 44 GLN A 51 LEU A 52 PRO A 53
SITE 3 AC1 17 GLN A 64 SER A 65 HOH A1214 HOH A1236
SITE 4 AC1 17 HOH A1252 HOH A1258 HOH A1339 HOH A1341
SITE 5 AC1 17 ASP B 98
SITE 1 AC2 14 ASP A 98 TYR B 7 PHE B 8 ARG B 13
SITE 2 AC2 14 TRP B 38 LYS B 44 GLN B 51 LEU B 52
SITE 3 AC2 14 GLN B 64 SER B 65 HOH B2208 HOH B2239
SITE 4 AC2 14 HOH B2254 HOH B2340
SITE 1 AC3 6 TRP A 28 GLU A 30 PHE A 192 GLU A 197
SITE 2 AC3 6 HOH A1268 ALA B 172
SITE 1 AC4 7 ASP A 171 TRP B 28 GLU B 30 PHE B 192
SITE 2 AC4 7 GLU B 197 HOH B2219 HOH B2345
SITE 1 AC5 4 ASP A 23 ALA A 153 LEU A 183 ARG A 186
SITE 1 AC6 4 ASP B 23 ALA B 153 LEU B 183 ARG B 186
CRYST1 68.873 78.775 89.419 90.00 90.00 90.00 P 21 21 21 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 0.014519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012694 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011183 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
