HEADER TRANSFERASE 24-OCT-11 3UBK
TITLE CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE (TARGET EFI-501770) FROM
TITLE 2 LEPTOSPIRA INTERROGANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEPTOSPIRA INTERROGANS SEROVAR LAI;
SOURCE 3 ORGANISM_TAXID: 189518;
SOURCE 4 STRAIN: 56601;
SOURCE 5 GENE: GST, LA_2623;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS TRANSFERASE, GSH BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,R.D.SEIDEL,
AUTHOR 2 E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,H.J.IMKER,
AUTHOR 3 R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO,(EFI) ENZYME FUNCTION INITIATIVE
REVDAT 2 29-FEB-12 3UBK 1 AUTHOR JRNL
REVDAT 1 09-NOV-11 3UBK 0
JRNL AUTH Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,
JRNL AUTH 2 R.D.SEIDEL,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,
JRNL AUTH 3 J.HAMMONDS,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM
JRNL TITL 2 LEPTOSPIRA INTERROGANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 43745
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1407
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2938
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3317
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.99000
REMARK 3 B22 (A**2) : 1.99000
REMARK 3 B33 (A**2) : -3.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.537
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3494 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4742 ; 1.012 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 433 ; 4.743 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;30.544 ;24.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 641 ;13.484 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.152 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 534 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2568 ; 0.005 ; 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): 2110 ; 3.026 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3448 ; 4.468 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1384 ; 6.533 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1283 ; 9.909 ; 7.000
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 3UBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB068548.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46029
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 15.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : 0.84000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3CBU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, PH 5.5, 2M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 87.80400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 131.70600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.90200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 87.80400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.90200
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 131.70600
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: 5010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 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 MET A -1
REMARK 465 PRO A 111
REMARK 465 ALA A 112
REMARK 465 ALA A 113
REMARK 465 LYS A 114
REMARK 465 VAL A 115
REMARK 465 LYS A 214
REMARK 465 THR A 215
REMARK 465 LYS A 216
REMARK 465 ILE A 217
REMARK 465 GLY A 218
REMARK 465 ALA A 219
REMARK 465 GLU A 220
REMARK 465 ASN A 221
REMARK 465 LEU A 222
REMARK 465 TYR A 223
REMARK 465 PHE A 224
REMARK 465 GLN A 225
REMARK 465 SER A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 HIS A 229
REMARK 465 HIS A 230
REMARK 465 HIS A 231
REMARK 465 HIS A 232
REMARK 465 TRP A 233
REMARK 465 SER A 234
REMARK 465 HIS A 235
REMARK 465 PRO A 236
REMARK 465 GLN A 237
REMARK 465 PHE A 238
REMARK 465 GLU A 239
REMARK 465 LYS A 240
REMARK 465 MET B -1
REMARK 465 LEU B 110
REMARK 465 PRO B 111
REMARK 465 ALA B 112
REMARK 465 ALA B 113
REMARK 465 LYS B 114
REMARK 465 VAL B 115
REMARK 465 ARG B 212
REMARK 465 ALA B 213
REMARK 465 LYS B 214
REMARK 465 THR B 215
REMARK 465 LYS B 216
REMARK 465 ILE B 217
REMARK 465 GLY B 218
REMARK 465 ALA B 219
REMARK 465 GLU B 220
REMARK 465 ASN B 221
REMARK 465 LEU B 222
REMARK 465 TYR B 223
REMARK 465 PHE B 224
REMARK 465 GLN B 225
REMARK 465 SER B 226
REMARK 465 HIS B 227
REMARK 465 HIS B 228
REMARK 465 HIS B 229
REMARK 465 HIS B 230
REMARK 465 HIS B 231
REMARK 465 HIS B 232
REMARK 465 TRP B 233
REMARK 465 SER B 234
REMARK 465 HIS B 235
REMARK 465 PRO B 236
REMARK 465 GLN B 237
REMARK 465 PHE B 238
REMARK 465 GLU B 239
REMARK 465 LYS B 240
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 55 CG OD1 OD2
REMARK 470 ARG A 89 CD NE CZ NH1 NH2
REMARK 470 LEU B 210 CG CD1 CD2
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 PHE A 73 75.01 -118.09
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 SO4 A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 243
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 243
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UBL RELATED DB: PDB
REMARK 900 RELATED ID: EFI-501770 RELATED DB: TARGETTRACK
DBREF 3UBK A 1 218 UNP Q8F2Y8 Q8F2Y8_LEPIN 1 218
DBREF 3UBK B 1 218 UNP Q8F2Y8 Q8F2Y8_LEPIN 1 218
SEQADV 3UBK MET A -1 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK VAL A 0 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK ALA A 219 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLU A 220 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK ASN A 221 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK LEU A 222 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK TYR A 223 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK PHE A 224 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLN A 225 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK SER A 226 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 227 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 228 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 229 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 230 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 231 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 232 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK TRP A 233 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK SER A 234 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS A 235 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK PRO A 236 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLN A 237 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK PHE A 238 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLU A 239 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK LYS A 240 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK MET B -1 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK VAL B 0 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK ALA B 219 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLU B 220 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK ASN B 221 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK LEU B 222 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK TYR B 223 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK PHE B 224 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLN B 225 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK SER B 226 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 227 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 228 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 229 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 230 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 231 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 232 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK TRP B 233 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK SER B 234 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK HIS B 235 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK PRO B 236 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLN B 237 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK PHE B 238 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK GLU B 239 UNP Q8F2Y8 EXPRESSION TAG
SEQADV 3UBK LYS B 240 UNP Q8F2Y8 EXPRESSION TAG
SEQRES 1 A 242 MET VAL MET ILE LYS LEU HIS GLY ALA SER ILE SER ASN
SEQRES 2 A 242 TYR VAL ASN LYS VAL LYS LEU GLY ILE LEU GLU LYS GLY
SEQRES 3 A 242 LEU GLU TYR GLU GLN ILE ARG ILE ALA PRO SER GLN GLU
SEQRES 4 A 242 GLU ASP PHE LEU LYS ILE SER PRO MET GLY LYS ILE PRO
SEQRES 5 A 242 VAL LEU GLU MET ASP GLY LYS PHE ILE PHE GLU SER GLY
SEQRES 6 A 242 ALA ILE LEU GLU PHE LEU ASP THR ILE PHE PRO GLN THR
SEQRES 7 A 242 PRO LYS LEU ILE PRO GLU ASP PRO TRP GLU ALA ALA ARG
SEQRES 8 A 242 VAL ARG GLU ILE SER THR ILE ILE GLU THR TYR LEU ASP
SEQRES 9 A 242 ILE PRO ALA ARG ARG ILE TYR LEU PRO ALA ALA LYS VAL
SEQRES 10 A 242 SER PRO GLU ILE VAL GLU GLU VAL HIS SER THR LEU VAL
SEQRES 11 A 242 LYS GLY ILE LYS ALA LEU GLN ARG VAL VAL ARG PHE SER
SEQRES 12 A 242 PRO TYR ILE ALA GLY ASN VAL PHE THR LEU ALA ASP CYS
SEQRES 13 A 242 SER GLY PHE ALA HIS LEU SER VAL LEU ASP GLU GLU LEU
SEQRES 14 A 242 ARG PRO PHE TYR PRO ASN ASN HIS PRO LEU ASP LEU LEU
SEQRES 15 A 242 ASN GLY TRP LYS GLU TYR PHE VAL PHE MET LYS THR LYS
SEQRES 16 A 242 ALA GLY PRO ALA LEU VAL GLU LYS ASP LYS GLN ILE LEU
SEQRES 17 A 242 LYS LYS ILE LEU ALA ARG ALA LYS THR LYS ILE GLY ALA
SEQRES 18 A 242 GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS
SEQRES 19 A 242 TRP SER HIS PRO GLN PHE GLU LYS
SEQRES 1 B 242 MET VAL MET ILE LYS LEU HIS GLY ALA SER ILE SER ASN
SEQRES 2 B 242 TYR VAL ASN LYS VAL LYS LEU GLY ILE LEU GLU LYS GLY
SEQRES 3 B 242 LEU GLU TYR GLU GLN ILE ARG ILE ALA PRO SER GLN GLU
SEQRES 4 B 242 GLU ASP PHE LEU LYS ILE SER PRO MET GLY LYS ILE PRO
SEQRES 5 B 242 VAL LEU GLU MET ASP GLY LYS PHE ILE PHE GLU SER GLY
SEQRES 6 B 242 ALA ILE LEU GLU PHE LEU ASP THR ILE PHE PRO GLN THR
SEQRES 7 B 242 PRO LYS LEU ILE PRO GLU ASP PRO TRP GLU ALA ALA ARG
SEQRES 8 B 242 VAL ARG GLU ILE SER THR ILE ILE GLU THR TYR LEU ASP
SEQRES 9 B 242 ILE PRO ALA ARG ARG ILE TYR LEU PRO ALA ALA LYS VAL
SEQRES 10 B 242 SER PRO GLU ILE VAL GLU GLU VAL HIS SER THR LEU VAL
SEQRES 11 B 242 LYS GLY ILE LYS ALA LEU GLN ARG VAL VAL ARG PHE SER
SEQRES 12 B 242 PRO TYR ILE ALA GLY ASN VAL PHE THR LEU ALA ASP CYS
SEQRES 13 B 242 SER GLY PHE ALA HIS LEU SER VAL LEU ASP GLU GLU LEU
SEQRES 14 B 242 ARG PRO PHE TYR PRO ASN ASN HIS PRO LEU ASP LEU LEU
SEQRES 15 B 242 ASN GLY TRP LYS GLU TYR PHE VAL PHE MET LYS THR LYS
SEQRES 16 B 242 ALA GLY PRO ALA LEU VAL GLU LYS ASP LYS GLN ILE LEU
SEQRES 17 B 242 LYS LYS ILE LEU ALA ARG ALA LYS THR LYS ILE GLY ALA
SEQRES 18 B 242 GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS
SEQRES 19 B 242 TRP SER HIS PRO GLN PHE GLU LYS
HET SO4 A 241 5
HET SO4 A 242 5
HET SO4 A 243 5
HET GOL A 244 6
HET CL A 245 1
HET GOL A 246 6
HET GOL A 247 6
HET CL A 248 1
HET SO4 B 241 5
HET CL B 242 1
HET CL B 243 1
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 7 CL 4(CL 1-)
FORMUL 14 HOH *175(H2 O)
HELIX 1 1 SER A 10 GLY A 24 1 15
HELIX 2 2 GLU A 37 LYS A 42 1 6
HELIX 3 3 GLU A 61 PHE A 73 1 13
HELIX 4 4 ASP A 83 TYR A 100 1 18
HELIX 5 5 LEU A 101 LEU A 110 1 10
HELIX 6 6 PRO A 117 VAL A 138 1 22
HELIX 7 7 THR A 150 ARG A 168 1 19
HELIX 8 8 HIS A 175 LEU A 180 5 6
HELIX 9 9 GLY A 182 THR A 192 1 11
HELIX 10 10 LYS A 193 ARG A 212 1 20
HELIX 11 11 SER B 10 GLY B 24 1 15
HELIX 12 12 GLU B 37 LYS B 42 1 6
HELIX 13 13 GLU B 61 PHE B 73 1 13
HELIX 14 14 ASP B 83 LEU B 101 1 19
HELIX 15 15 LEU B 101 ARG B 106 1 6
HELIX 16 16 PRO B 117 GLN B 135 1 19
HELIX 17 17 THR B 150 LEU B 167 1 18
HELIX 18 18 HIS B 175 LEU B 180 5 6
HELIX 19 19 GLY B 182 LYS B 193 1 12
HELIX 20 20 LYS B 193 LEU B 210 1 18
SHEET 1 A 4 TYR A 27 ILE A 30 0
SHEET 2 A 4 ILE A 2 HIS A 5 1 N LEU A 4 O GLU A 28
SHEET 3 A 4 VAL A 51 MET A 54 -1 O GLU A 53 N LYS A 3
SHEET 4 A 4 LYS A 57 ILE A 59 -1 O LYS A 57 N MET A 54
SHEET 1 B 4 TYR B 27 ILE B 30 0
SHEET 2 B 4 ILE B 2 HIS B 5 1 N LEU B 4 O ILE B 30
SHEET 3 B 4 VAL B 51 MET B 54 -1 O VAL B 51 N HIS B 5
SHEET 4 B 4 LYS B 57 ILE B 59 -1 O ILE B 59 N LEU B 52
CISPEP 1 ILE A 49 PRO A 50 0 2.95
CISPEP 2 THR A 76 PRO A 77 0 -2.11
CISPEP 3 SER A 141 PRO A 142 0 2.34
CISPEP 4 ILE B 49 PRO B 50 0 6.84
CISPEP 5 THR B 76 PRO B 77 0 0.61
CISPEP 6 SER B 141 PRO B 142 0 -0.23
SITE 1 AC1 4 LYS A 193 ALA A 194 HOH A 250 HOH A 326
SITE 1 AC2 7 GLN A 75 THR A 76 HOH A 262 HOH A 323
SITE 2 AC2 7 LYS B 78 GLU B 82 HOH B 254
SITE 1 AC3 5 LEU A 180 GLY A 182 TRP A 183 LYS A 184
SITE 2 AC3 5 GLU A 185
SITE 1 AC4 5 MET A 1 ILE A 2 GLU A 26 HOH A 321
SITE 2 AC4 5 ASP B 83
SITE 1 AC5 2 SER A 8 ARG A 31
SITE 1 AC6 4 TYR A 27 GLN A 29 ASP A 202 HOH A 277
SITE 1 AC7 7 SER A 141 PRO A 142 GLU A 185 TYR A 186
SITE 2 AC7 7 PHE A 189 HOH A 292 HOH A 311
SITE 1 AC8 3 SER A 10 ASN A 11 ARG A 106
SITE 1 AC9 6 LEU B 180 ASN B 181 GLY B 182 TRP B 183
SITE 2 AC9 6 LYS B 184 GLU B 185
SITE 1 BC1 3 SER B 8 ARG B 31 LEU B 206
SITE 1 BC2 2 SER B 10 ARG B 106
CRYST1 82.843 82.843 175.608 90.00 90.00 90.00 P 43 2 2 16
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 0.012071 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005695 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
