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HEADER HYDROLASE 02-JUL-08 3DNM
TITLE CRYSTAL STRUCTURE HORMONE-SENSITIVE LIPASE FROM A
TITLE 2 METAGENOME LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: ESTE7;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21A;
SOURCE 9 OTHER_DETAILS: THIS PROTEIN WAS PURIFIED FROM METAGENOME
SOURCE 10 LIBRARY(SOIL UNCULTURED BACTERIA)
KEYWDS ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR K.Y.HWANG,K.H.NAM
REVDAT 1 13-JAN-09 3DNM 0
JRNL AUTH K.H.NAM,M.-Y.KIM,S.-J.KIM,A.PRIYADARSHI,S.-T.KWON,
JRNL AUTH 2 B.-S.KOO,S.-H.YOON,K.Y.HWANG
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF A NOVEL
JRNL TITL 2 HORMONE-SENSITIVE LIPASE FROM A METAGENOME LIBRARY
JRNL REF PROTEINS 2008
JRNL REFN ESSN 1097-0134
JRNL PMID 19089974
JRNL DOI 10.1002/PROT.22313
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 40102
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 SET) : 0.233
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2115
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 : 8839
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.87900
REMARK 3 B22 (A**2) : -21.50300
REMARK 3 B33 (A**2) : 12.62400
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 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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.93
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) : 1.213 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.083 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.738 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.704 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 3DNM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB048260.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.23
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42217
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
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 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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1LZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PROPANE, PH 7.0, 0.2M
REMARK 280 AMMONIUM SULFATE, 1M LITHIUM SULFATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 58.66050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.69650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.41400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.69650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.66050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.41400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.66050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.41400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 116.69650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.41400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.66050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 116.69650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 300
REMARK 300 REMARK: THIS PROTEIN WORKS IN MONOMER. BUT
REMARK 300 CRYSTALLOGRAPHICAL DATA SHOWS THE DIMER PROTEIN AS REPORTED
REMARK 300 IN SOME RELATED PAPERS. THE DEPOSITORS CONSIDER THAT THE
REMARK 300 DIMER FORMATION IS CRYSTALLOGRAPHICAL DATA.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -136.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 190.24200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 58.66050
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 126.82800
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -116.69650
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 -58.66050
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 63.41400
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 -116.69650
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -256.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 63.41400
REMARK 350 BIOMT3 2 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 -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 ASN A -6
REMARK 465 ASN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ALA A 3
REMARK 465 MET A 4
REMARK 465 ASP A 5
REMARK 465 GLN A 6
REMARK 465 GLU A 7
REMARK 465 ILE A 8
REMARK 465 GLY A 9
REMARK 465 THR A 10
REMARK 465 VAL A 11
REMARK 465 THR A 12
REMARK 465 LYS A 310
REMARK 465 LEU A 311
REMARK 465 ALA A 312
REMARK 465 ALA A 313
REMARK 465 ALA A 314
REMARK 465 LEU A 315
REMARK 465 GLU A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 ASN B -6
REMARK 465 ASN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ALA B 3
REMARK 465 MET B 4
REMARK 465 ASP B 5
REMARK 465 GLN B 6
REMARK 465 GLU B 7
REMARK 465 ILE B 8
REMARK 465 GLY B 9
REMARK 465 THR B 10
REMARK 465 VAL B 11
REMARK 465 THR B 12
REMARK 465 SER B 309
REMARK 465 LYS B 310
REMARK 465 LEU B 311
REMARK 465 ALA B 312
REMARK 465 ALA B 313
REMARK 465 ALA B 314
REMARK 465 LEU B 315
REMARK 465 GLU B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 MET C -13
REMARK 465 ALA C -12
REMARK 465 SER C -11
REMARK 465 MET C -10
REMARK 465 THR C -9
REMARK 465 GLY C -8
REMARK 465 GLY C -7
REMARK 465 ASN C -6
REMARK 465 ASN C -5
REMARK 465 MET C -4
REMARK 465 GLY C -3
REMARK 465 ARG C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 ALA C 3
REMARK 465 MET C 4
REMARK 465 ASP C 5
REMARK 465 GLN C 6
REMARK 465 GLU C 7
REMARK 465 ILE C 8
REMARK 465 GLY C 9
REMARK 465 THR C 10
REMARK 465 VAL C 11
REMARK 465 THR C 12
REMARK 465 ASP C 13
REMARK 465 GLU C 33
REMARK 465 LYS C 34
REMARK 465 ASN C 35
REMARK 465 LEU C 36
REMARK 465 SER C 309
REMARK 465 LYS C 310
REMARK 465 LEU C 311
REMARK 465 ALA C 312
REMARK 465 ALA C 313
REMARK 465 ALA C 314
REMARK 465 LEU C 315
REMARK 465 GLU C 316
REMARK 465 HIS C 317
REMARK 465 HIS C 318
REMARK 465 HIS C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 MET D -13
REMARK 465 ALA D -12
REMARK 465 SER D -11
REMARK 465 MET D -10
REMARK 465 THR D -9
REMARK 465 GLY D -8
REMARK 465 GLY D -7
REMARK 465 ASN D -6
REMARK 465 ASN D -5
REMARK 465 MET D -4
REMARK 465 GLY D -3
REMARK 465 ARG D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 ALA D 3
REMARK 465 MET D 4
REMARK 465 ASP D 5
REMARK 465 GLN D 6
REMARK 465 GLU D 7
REMARK 465 ILE D 8
REMARK 465 GLY D 9
REMARK 465 THR D 10
REMARK 465 VAL D 11
REMARK 465 THR D 12
REMARK 465 ASP D 13
REMARK 465 THR D 14
REMARK 465 GLU D 33
REMARK 465 LYS D 34
REMARK 465 ASN D 35
REMARK 465 SER D 309
REMARK 465 LYS D 310
REMARK 465 LEU D 311
REMARK 465 ALA D 312
REMARK 465 ALA D 313
REMARK 465 ALA D 314
REMARK 465 LEU D 315
REMARK 465 GLU D 316
REMARK 465 HIS D 317
REMARK 465 HIS D 318
REMARK 465 HIS D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
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 PRO A 18 -59.71 -29.59
REMARK 500 ALA A 32 152.32 -49.93
REMARK 500 LYS A 34 -73.04 -62.62
REMARK 500 CYS A 49 12.26 -61.37
REMARK 500 THR A 63 -156.15 -119.00
REMARK 500 SER A 97 -76.40 -51.35
REMARK 500 THR A 98 -36.87 -32.51
REMARK 500 GLN A 109 9.64 -68.81
REMARK 500 ASP A 118 64.72 -102.64
REMARK 500 SER A 157 -120.20 51.88
REMARK 500 PRO A 178 172.59 -57.48
REMARK 500 LEU A 192 36.81 37.25
REMARK 500 LEU A 206 -61.27 -132.07
REMARK 500 THR A 211 -70.39 -61.65
REMARK 500 GLU A 223 171.77 -53.25
REMARK 500 VAL A 233 -1.03 -59.70
REMARK 500 ASP A 236 76.67 -103.31
REMARK 500 LEU A 237 6.46 -61.39
REMARK 500 ASP A 278 17.14 46.50
REMARK 500 GLN A 284 -5.73 -58.89
REMARK 500 PRO B 18 -34.60 -39.68
REMARK 500 LYS B 31 34.81 -91.34
REMARK 500 GLU B 33 105.49 -52.55
REMARK 500 LYS B 34 -71.26 -45.08
REMARK 500 ASN B 35 54.18 -114.53
REMARK 500 CYS B 49 -2.73 -54.53
REMARK 500 THR B 63 -156.15 -103.82
REMARK 500 CYS B 70 168.20 175.15
REMARK 500 ALA B 74 -176.15 -175.87
REMARK 500 ALA B 78 133.98 -175.42
REMARK 500 ALA B 80 6.80 -64.40
REMARK 500 TYR B 91 -14.53 70.25
REMARK 500 SER B 97 -74.14 -58.05
REMARK 500 THR B 98 -25.03 -36.04
REMARK 500 ASP B 118 66.59 -102.48
REMARK 500 ALA B 129 -71.33 -46.69
REMARK 500 SER B 157 -123.34 46.44
REMARK 500 LEU B 190 3.00 -65.70
REMARK 500 SER B 198 -76.53 -79.44
REMARK 500 ALA B 201 -37.16 -36.50
REMARK 500 PRO B 209 -71.93 -47.21
REMARK 500 THR B 211 -38.86 -39.86
REMARK 500 LEU B 212 -76.43 -85.27
REMARK 500 ASP B 278 14.06 49.27
REMARK 500 GLN B 284 4.89 -55.48
REMARK 500 LEU C 38 4.66 83.47
REMARK 500 ASP C 39 21.94 49.85
REMARK 500 ARG C 42 9.87 -64.60
REMARK 500 ALA C 43 -59.49 -123.00
REMARK 500 ALA C 55 109.81 -53.55
REMARK 500 THR C 63 -156.56 -151.98
REMARK 500 TYR C 91 -4.54 65.61
REMARK 500 SER C 93 -156.17 -144.81
REMARK 500 PRO C 128 38.89 -94.64
REMARK 500 SER C 157 -124.02 35.40
REMARK 500 THR C 164 -70.69 -67.23
REMARK 500 LEU C 192 53.11 35.46
REMARK 500 ASP C 202 54.59 -100.86
REMARK 500 ARG C 203 -16.18 -148.80
REMARK 500 LEU C 206 -67.22 -102.19
REMARK 500 PRO C 209 -75.70 -37.69
REMARK 500 GLU C 250 51.44 -103.87
REMARK 500 VAL C 282 65.80 31.96
REMARK 500 PHE C 289 -69.14 -99.10
REMARK 500 ARG C 307 -73.98 -54.32
REMARK 500 PRO D 37 154.87 -45.79
REMARK 500 ALA D 47 -70.62 -50.41
REMARK 500 ALA D 55 127.16 -31.84
REMARK 500 THR D 63 -153.19 -152.51
REMARK 500 ALA D 74 147.04 -173.06
REMARK 500 TYR D 91 -6.21 71.73
REMARK 500 SER D 93 -148.48 -113.84
REMARK 500 LYS D 108 -72.99 -52.70
REMARK 500 GLN D 109 0.16 -61.09
REMARK 500 SER D 147 130.51 174.01
REMARK 500 SER D 157 -125.16 41.54
REMARK 500 PRO D 178 -175.86 -62.72
REMARK 500 SER D 185 57.27 37.41
REMARK 500 LEU D 190 39.41 -84.12
REMARK 500 LEU D 192 58.54 38.27
REMARK 500 ASN D 197 -39.74 -37.55
REMARK 500 ASP D 202 2.60 -67.90
REMARK 500 LEU D 206 -52.12 -135.99
REMARK 500 ALA D 207 55.83 -92.81
REMARK 500 GLU D 250 47.21 -94.56
REMARK 500 HIS D 281 125.11 -39.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 332 DISTANCE = 5.00 ANGSTROMS
REMARK 525 HOH C 348 DISTANCE = 8.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 325
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 323
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 324
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 330
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 323
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 324
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 325
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 326
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 327
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 328
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 329
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME C 325
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 323
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 324
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME D 326
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 323
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 324
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 325
DBREF 3DNM A 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
DBREF 3DNM B 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
DBREF 3DNM C 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
DBREF 3DNM D 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
SEQADV 3DNM MET A -13 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA A -12 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER A -11 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET A -10 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM THR A -9 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY A -8 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY A -7 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN A -6 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN A -5 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET A -4 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY A -3 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ARG A -2 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY A -1 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER A 0 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LYS A 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU A 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA A 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA A 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA A 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU A 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLU A 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS A 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS A 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS A 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS A 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS A 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS A 322 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET B -13 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA B -12 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER B -11 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET B -10 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM THR B -9 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY B -8 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY B -7 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN B -6 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN B -5 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET B -4 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY B -3 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ARG B -2 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY B -1 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER B 0 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LYS B 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU B 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA B 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA B 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA B 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU B 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLU B 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS B 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS B 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS B 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS B 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS B 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS B 322 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET C -13 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA C -12 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER C -11 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET C -10 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM THR C -9 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY C -8 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY C -7 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN C -6 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN C -5 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET C -4 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY C -3 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ARG C -2 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY C -1 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER C 0 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LYS C 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU C 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA C 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA C 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA C 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU C 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLU C 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS C 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS C 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS C 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS C 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS C 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS C 322 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET D -13 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA D -12 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER D -11 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET D -10 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM THR D -9 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY D -8 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY D -7 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN D -6 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ASN D -5 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM MET D -4 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY D -3 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ARG D -2 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLY D -1 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM SER D 0 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LYS D 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU D 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA D 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA D 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM ALA D 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM LEU D 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM GLU D 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS D 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS D 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS D 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS D 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS D 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3DNM HIS D 322 UNP Q0GMU1 EXPRESSION TAG
SEQRES 1 A 336 MET ALA SER MET THR GLY GLY ASN ASN MET GLY ARG GLY
SEQRES 2 A 336 SER MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR
SEQRES 3 A 336 ASP THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU
SEQRES 4 A 336 LYS ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU
SEQRES 5 A 336 ASP GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG
SEQRES 6 A 336 PHE PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP
SEQRES 7 A 336 LEU GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY
SEQRES 8 A 336 ALA GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY
SEQRES 9 A 336 TYR ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR
SEQRES 10 A 336 THR GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER
SEQRES 11 A 336 LEU ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA
SEQRES 12 A 336 ALA VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU
SEQRES 13 A 336 LYS THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY
SEQRES 14 A 336 ASP SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU
SEQRES 15 A 336 LYS ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU
SEQRES 16 A 336 VAL MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG
SEQRES 17 A 336 TRP SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA
SEQRES 18 A 336 GLU PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL
SEQRES 19 A 336 GLY GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL
SEQRES 20 A 336 TYR ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS
SEQRES 21 A 336 VAL GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR
SEQRES 22 A 336 LEU ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU
SEQRES 23 A 336 LEU LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET
SEQRES 24 A 336 TYR GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS
SEQRES 25 A 336 GLU ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU
SEQRES 26 A 336 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 336 MET ALA SER MET THR GLY GLY ASN ASN MET GLY ARG GLY
SEQRES 2 B 336 SER MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR
SEQRES 3 B 336 ASP THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU
SEQRES 4 B 336 LYS ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU
SEQRES 5 B 336 ASP GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG
SEQRES 6 B 336 PHE PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP
SEQRES 7 B 336 LEU GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY
SEQRES 8 B 336 ALA GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY
SEQRES 9 B 336 TYR ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR
SEQRES 10 B 336 THR GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER
SEQRES 11 B 336 LEU ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA
SEQRES 12 B 336 ALA VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU
SEQRES 13 B 336 LYS THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY
SEQRES 14 B 336 ASP SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU
SEQRES 15 B 336 LYS ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU
SEQRES 16 B 336 VAL MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG
SEQRES 17 B 336 TRP SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA
SEQRES 18 B 336 GLU PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL
SEQRES 19 B 336 GLY GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL
SEQRES 20 B 336 TYR ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS
SEQRES 21 B 336 VAL GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR
SEQRES 22 B 336 LEU ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU
SEQRES 23 B 336 LEU LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET
SEQRES 24 B 336 TYR GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS
SEQRES 25 B 336 GLU ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU
SEQRES 26 B 336 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 336 MET ALA SER MET THR GLY GLY ASN ASN MET GLY ARG GLY
SEQRES 2 C 336 SER MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR
SEQRES 3 C 336 ASP THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU
SEQRES 4 C 336 LYS ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU
SEQRES 5 C 336 ASP GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG
SEQRES 6 C 336 PHE PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP
SEQRES 7 C 336 LEU GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY
SEQRES 8 C 336 ALA GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY
SEQRES 9 C 336 TYR ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR
SEQRES 10 C 336 THR GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER
SEQRES 11 C 336 LEU ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA
SEQRES 12 C 336 ALA VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU
SEQRES 13 C 336 LYS THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY
SEQRES 14 C 336 ASP SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU
SEQRES 15 C 336 LYS ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU
SEQRES 16 C 336 VAL MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG
SEQRES 17 C 336 TRP SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA
SEQRES 18 C 336 GLU PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL
SEQRES 19 C 336 GLY GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL
SEQRES 20 C 336 TYR ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS
SEQRES 21 C 336 VAL GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR
SEQRES 22 C 336 LEU ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU
SEQRES 23 C 336 LEU LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET
SEQRES 24 C 336 TYR GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS
SEQRES 25 C 336 GLU ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU
SEQRES 26 C 336 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 336 MET ALA SER MET THR GLY GLY ASN ASN MET GLY ARG GLY
SEQRES 2 D 336 SER MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR
SEQRES 3 D 336 ASP THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU
SEQRES 4 D 336 LYS ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU
SEQRES 5 D 336 ASP GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG
SEQRES 6 D 336 PHE PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP
SEQRES 7 D 336 LEU GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY
SEQRES 8 D 336 ALA GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY
SEQRES 9 D 336 TYR ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR
SEQRES 10 D 336 THR GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER
SEQRES 11 D 336 LEU ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA
SEQRES 12 D 336 ALA VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU
SEQRES 13 D 336 LYS THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY
SEQRES 14 D 336 ASP SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU
SEQRES 15 D 336 LYS ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU
SEQRES 16 D 336 VAL MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG
SEQRES 17 D 336 TRP SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA
SEQRES 18 D 336 GLU PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL
SEQRES 19 D 336 GLY GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL
SEQRES 20 D 336 TYR ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS
SEQRES 21 D 336 VAL GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR
SEQRES 22 D 336 LEU ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU
SEQRES 23 D 336 LEU LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET
SEQRES 24 D 336 TYR GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS
SEQRES 25 D 336 GLU ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU
SEQRES 26 D 336 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET BME A 325 4
HET SO4 A 323 5
HET SO4 A 324 5
HET BME B 330 4
HET SO4 B 323 5
HET SO4 B 324 5
HET SO4 B 325 5
HET SO4 B 326 5
HET SO4 B 327 5
HET SO4 B 328 5
HET SO4 B 329 5
HET BME C 325 4
HET SO4 C 323 5
HET SO4 C 324 5
HET BME D 326 4
HET SO4 D 323 5
HET SO4 D 324 5
HET SO4 D 325 5
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM SO4 SULFATE ION
FORMUL 5 BME 4(C2 H6 O S)
FORMUL 6 SO4 14(O4 S 2-)
FORMUL 23 HOH *204(H2 O)
HELIX 1 1 ASP A 17 LYS A 31 1 15
HELIX 2 2 PRO A 37 CYS A 49 1 13
HELIX 3 3 HIS A 99 GLN A 109 1 11
HELIX 4 4 PRO A 128 GLY A 146 1 19
HELIX 5 5 SER A 147 ASP A 149 5 3
HELIX 6 6 SER A 157 GLY A 174 1 18
HELIX 7 7 ARG A 194 LEU A 200 1 7
HELIX 8 8 ALA A 201 ASP A 204 5 4
HELIX 9 9 GLU A 208 GLY A 221 1 14
HELIX 10 10 SER A 231 ALA A 235 5 5
HELIX 11 11 LEU A 253 ALA A 267 1 15
HELIX 12 12 VAL A 282 TYR A 286 5 5
HELIX 13 13 VAL A 290 ILE A 308 1 19
HELIX 14 14 ASP B 17 LYS B 31 1 15
HELIX 15 15 PRO B 37 GLU B 50 1 14
HELIX 16 16 HIS B 99 SER B 110 1 12
HELIX 17 17 PRO B 128 GLY B 146 1 19
HELIX 18 18 SER B 147 ASP B 149 5 3
HELIX 19 19 SER B 157 ASP B 173 1 17
HELIX 20 20 ARG B 194 ALA B 201 1 8
HELIX 21 21 ASP B 202 ASP B 204 5 3
HELIX 22 22 GLU B 208 GLY B 213 1 6
HELIX 23 23 SER B 216 GLY B 221 1 6
HELIX 24 24 SER B 231 ALA B 235 5 5
HELIX 25 25 LEU B 253 ALA B 267 1 15
HELIX 26 26 VAL B 282 TYR B 286 5 5
HELIX 27 27 VAL B 290 ILE B 308 1 19
HELIX 28 28 ASP C 17 LYS C 31 1 15
HELIX 29 29 GLN C 40 CYS C 49 1 10
HELIX 30 30 PRO C 96 THR C 98 5 3
HELIX 31 31 HIS C 99 SER C 111 1 13
HELIX 32 32 PRO C 128 GLY C 146 1 19
HELIX 33 33 SER C 147 ASP C 149 5 3
HELIX 34 34 ALA C 158 GLY C 174 1 17
HELIX 35 35 ARG C 194 LEU C 200 1 7
HELIX 36 36 GLU C 208 GLY C 221 1 14
HELIX 37 37 SER C 231 ALA C 235 5 5
HELIX 38 38 LEU C 253 ALA C 267 1 15
HELIX 39 39 VAL C 282 TYR C 286 5 5
HELIX 40 40 ASN C 291 ILE C 308 1 18
HELIX 41 41 ASP D 17 LYS D 31 1 15
HELIX 42 42 PRO D 37 GLU D 50 1 14
HELIX 43 43 HIS D 99 SER D 111 1 13
HELIX 44 44 PRO D 128 GLY D 146 1 19
HELIX 45 45 SER D 147 ASP D 149 5 3
HELIX 46 46 SER D 157 ASP D 173 1 17
HELIX 47 47 TRP D 195 ASN D 199 5 5
HELIX 48 48 LEU D 200 ASP D 204 5 5
HELIX 49 49 GLU D 208 GLY D 221 1 14
HELIX 50 50 SER D 231 ALA D 235 5 5
HELIX 51 51 LEU D 253 ALA D 266 1 14
HELIX 52 52 VAL D 282 GLY D 287 5 6
HELIX 53 53 ASN D 291 ALA D 306 1 16
SHEET 1 A16 GLU A 59 LEU A 65 0
SHEET 2 A16 VAL A 68 ALA A 74 -1 O VAL A 68 N LEU A 65
SHEET 3 A16 THR A 113 LEU A 117 -1 O LEU A 114 N GLN A 73
SHEET 4 A16 HIS A 82 PHE A 86 1 N ILE A 83 O TRP A 115
SHEET 5 A16 ILE A 151 ASP A 156 1 O ALA A 154 N PHE A 86
SHEET 6 A16 LEU A 181 LEU A 184 1 O VAL A 182 N ILE A 153
SHEET 7 A16 MET A 243 GLU A 250 1 O LEU A 244 N LEU A 181
SHEET 8 A16 VAL A 271 PRO A 280 1 O GLU A 272 N ILE A 245
SHEET 9 A16 VAL B 271 TRP B 276 -1 O LEU B 273 N LEU A 273
SHEET 10 A16 MET B 243 GLY B 248 1 N VAL B 247 O TRP B 276
SHEET 11 A16 GLY B 180 LEU B 184 1 N MET B 183 O LEU B 244
SHEET 12 A16 ILE B 151 ASP B 156 1 N ILE B 153 O GLY B 180
SHEET 13 A16 HIS B 82 PHE B 86 1 N LEU B 84 O ALA B 154
SHEET 14 A16 THR B 113 LEU B 117 1 O TRP B 115 N ILE B 83
SHEET 15 A16 VAL B 68 ALA B 74 -1 N GLN B 73 O LEU B 114
SHEET 16 A16 ASP B 64 LEU B 65 -1 N LEU B 65 O VAL B 68
SHEET 1 B32 GLU A 59 LEU A 65 0
SHEET 2 B32 VAL A 68 ALA A 74 -1 O VAL A 68 N LEU A 65
SHEET 3 B32 THR A 113 LEU A 117 -1 O LEU A 114 N GLN A 73
SHEET 4 B32 HIS A 82 PHE A 86 1 N ILE A 83 O TRP A 115
SHEET 5 B32 ILE A 151 ASP A 156 1 O ALA A 154 N PHE A 86
SHEET 6 B32 LEU A 181 LEU A 184 1 O VAL A 182 N ILE A 153
SHEET 7 B32 MET A 243 GLU A 250 1 O LEU A 244 N LEU A 181
SHEET 8 B32 VAL A 271 PRO A 280 1 O GLU A 272 N ILE A 245
SHEET 9 B32 VAL B 271 TRP B 276 -1 O LEU B 273 N LEU A 273
SHEET 10 B32 MET B 243 GLY B 248 1 N VAL B 247 O TRP B 276
SHEET 11 B32 GLY B 180 LEU B 184 1 N MET B 183 O LEU B 244
SHEET 12 B32 ILE B 151 ASP B 156 1 N ILE B 153 O GLY B 180
SHEET 13 B32 HIS B 82 PHE B 86 1 N LEU B 84 O ALA B 154
SHEET 14 B32 THR B 113 LEU B 117 1 O TRP B 115 N ILE B 83
SHEET 15 B32 VAL B 68 ALA B 74 -1 N GLN B 73 O LEU B 114
SHEET 16 B32 GLU B 59 THR B 61 -1 N THR B 61 O ARG B 72
SHEET 17 B32 VAL C 58 LEU C 65 -1 O LEU C 62 N LEU B 60
SHEET 18 B32 VAL C 68 THR C 75 -1 O ALA C 74 N GLU C 59
SHEET 19 B32 THR C 113 LEU C 117 -1 O LEU C 114 N GLN C 73
SHEET 20 B32 HIS C 82 PHE C 86 1 N ILE C 83 O TRP C 115
SHEET 21 B32 ILE C 151 ASP C 156 1 O ALA C 154 N LEU C 84
SHEET 22 B32 GLY C 180 LEU C 184 1 O VAL C 182 N ILE C 153
SHEET 23 B32 MET C 243 GLU C 250 1 O LEU C 244 N LEU C 181
SHEET 24 B32 VAL C 271 PRO C 280 1 O TRP C 276 N VAL C 247
SHEET 25 B32 VAL D 271 PRO D 280 -1 O LEU D 273 N LEU C 273
SHEET 26 B32 MET D 243 GLU D 250 1 N GLU D 250 O MET D 279
SHEET 27 B32 GLY D 180 LEU D 184 1 N MET D 183 O LEU D 244
SHEET 28 B32 ILE D 151 ASP D 156 1 N GLY D 155 O LEU D 184
SHEET 29 B32 HIS D 82 PHE D 86 1 N LEU D 84 O ALA D 154
SHEET 30 B32 THR D 113 LEU D 117 1 O LEU D 117 N TYR D 85
SHEET 31 B32 VAL D 68 THR D 75 -1 N GLN D 73 O LEU D 114
SHEET 32 B32 VAL D 58 LEU D 65 -1 N GLU D 59 O ALA D 74
CISPEP 1 ALA A 122 PRO A 123 0 0.27
CISPEP 2 PHE A 127 PRO A 128 0 0.11
CISPEP 3 ALA B 122 PRO B 123 0 0.19
CISPEP 4 PHE B 127 PRO B 128 0 0.10
CISPEP 5 ALA C 122 PRO C 123 0 0.02
CISPEP 6 PHE C 127 PRO C 128 0 0.29
CISPEP 7 ALA D 122 PRO D 123 0 0.42
CISPEP 8 PHE D 127 PRO D 128 0 0.14
SITE 1 AC1 4 GLY A 90 SER A 157 LEU A 206 HIS A 281
SITE 1 AC2 4 ALA A 55 GLU A 56 GLN A 105 LYS A 108
SITE 1 AC3 4 ARG A 194 TYR A 234 ARG A 263 TRP B 195
SITE 1 AC4 4 SER B 157 LEU B 206 HIS B 281 HOH B 385
SITE 1 AC5 4 ALA B 55 GLU B 56 GLN B 105 LYS B 108
SITE 1 AC6 6 THR A 258 THR A 259 GLU A 262 THR B 258
SITE 2 AC6 6 THR B 259 GLU B 262
SITE 1 AC7 4 ARG B 194 LYS B 226 TYR B 234 ARG B 263
SITE 1 AC8 3 ARG B 19 LEU B 22 GLN B 23
SITE 1 AC9 5 ASP B 39 GLN B 40 ASP C 118 LEU C 121
SITE 2 AC9 5 HOH C 371
SITE 1 BC1 3 ASP B 118 TYR B 119 ARG B 120
SITE 1 BC2 4 ASP B 64 THR B 144 HOH B 378 HOH B 379
SITE 1 BC3 6 GLY C 90 SER C 157 ALA C 207 MET C 215
SITE 2 BC3 6 HIS C 281 HOH C 359
SITE 1 BC4 3 GLU C 56 GLN C 105 LYS C 108
SITE 1 BC5 3 ARG C 194 TYR C 234 ARG C 263
SITE 1 BC6 4 SER D 157 LEU D 206 MET D 215 HIS D 281
SITE 1 BC7 4 ALA D 55 GLU D 56 GLN D 105 LYS D 108
SITE 1 BC8 3 ARG D 194 TYR D 234 ARG D 263
SITE 1 BC9 1 MET D 177
CRYST1 117.321 126.828 233.393 90.00 90.00 90.00 I 21 21 21 32
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 0.008524 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004285 0.00000 |