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HEADER HYDROLASE 09-OCT-09 3K6K
TITLE CRYSTAL STRUCTURE AT 2.2 ANGSTROM OF HSL-HOMOLOG ESTE7 FROM
TITLE 2 A METAGENOME LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HORMONE SENSITIVE LIPASE HOMOLOG PROTEIN;
COMPND 5 EC: 3.1.1.-;
COMPND 6 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: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR K.Y.HWANG,K.H.NAM
REVDAT 1 27-OCT-09 3K6K 0
JRNL AUTH K.H.NAM,K.H.RHEE,W.H.LEE,B.-C.JEONG,H.K.SONG,
JRNL AUTH 2 K.Y.HWANG
JRNL TITL BIOCHEMICAL AND STRUCTURAL ANALYSIS OF
JRNL TITL 2 HORMONE-SENSITIVE LIPASE HOMOLOG ESTE7; INSIGHT
JRNL TITL 3 INTO THE STABILIZED DIMERIZATION OF HSL-HOMOLOG
JRNL TITL 4 PROTEINS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 84704
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4253
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4950
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 257
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8853
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 433
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.32000
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): 0.236
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.168
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.723
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9075 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12328 ; 1.976 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1172 ; 7.372 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 352 ;39.697 ;24.205
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1501 ;19.700 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;22.529 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1406 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6772 ; 0.009 ; 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): 5852 ; 0.944 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9347 ; 1.737 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3223 ; 2.953 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2981 ; 4.528 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS U VALUES; REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3K6K COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055609.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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 : 84721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.820
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 3DNM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
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 58.57850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.43500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.84950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.43500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.57850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.84950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.57850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.84950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 116.43500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.84950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.57850
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 116.43500
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: RECENTLY, THE DEPOSITORS HAVE CHARACTERIZED THE
REMARK 300 OLIGOMERIC STATE OF THIS PROTEIN. THIS PROTEIN REVEALS THE
REMARK 300 MONOMER AND DIMER FORMATION. BOTH OLIGOMERIC STATE REVEALS THE
REMARK 300 ENZYME ACTIVITY. BASED ON OUR STUDY, BIOLOGICAL ASSEMBLY OF
REMARK 300 ESTE7 ARE FORMING THE MONOMER AND DIMER FORMATION. ESPECIALLY,
REMARK 300 DIMERIC ESTE7 HAVE HIGH ACTIVITY THAN MONOMER ESTE7.
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: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3
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: 4
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: 5
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: 6
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 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 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 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 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 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 PRO C 37
REMARK 465 LEU C 38
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 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 LYS D 15
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER C 157 O HOH C 810 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 194 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 203 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 307 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 17 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 120 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 120 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 194 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 194 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 203 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP B 224 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU B 273 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 VAL C 101 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ARG C 225 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU C 273 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG D 194 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG D 194 NE - CZ - NH2 ANGL. DEV. = -5.4 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 THR A 63 -159.94 -143.12
REMARK 500 SER A 157 -115.61 47.18
REMARK 500 LEU A 190 2.17 -68.50
REMARK 500 SER A 193 -12.78 -146.32
REMARK 500 LEU A 212 -39.08 -34.88
REMARK 500 ASP A 278 15.08 59.14
REMARK 500 VAL A 282 55.49 39.48
REMARK 500 ALA B 32 129.70 -35.36
REMARK 500 ASN B 35 62.34 -117.93
REMARK 500 THR B 63 -158.88 -164.59
REMARK 500 ASP B 76 38.31 -88.49
REMARK 500 HIS B 87 161.88 -47.02
REMARK 500 TYR B 91 -5.61 77.05
REMARK 500 ASN B 125 86.79 -151.25
REMARK 500 SER B 157 -129.34 59.60
REMARK 500 GLU B 208 48.77 72.42
REMARK 500 THR B 211 -14.33 -141.40
REMARK 500 GLU B 250 53.15 -99.71
REMARK 500 ILE B 308 76.84 -68.23
REMARK 500 GLU C 30 -6.00 -57.15
REMARK 500 THR C 63 -158.82 -150.54
REMARK 500 TYR C 91 -0.87 66.24
REMARK 500 SER C 157 -129.16 56.54
REMARK 500 SER C 185 56.40 35.29
REMARK 500 VAL C 282 58.62 30.92
REMARK 500 ALA D 32 138.29 -33.95
REMARK 500 ASN D 35 99.10 -160.46
REMARK 500 PRO D 37 -175.00 -65.99
REMARK 500 GLN D 40 -73.33 -71.72
REMARK 500 ARG D 51 8.47 -60.99
REMARK 500 THR D 63 -164.29 -166.58
REMARK 500 TYR D 91 -6.03 85.85
REMARK 500 ASP D 118 69.83 -101.05
REMARK 500 SER D 157 -127.39 48.76
REMARK 500 ALA D 207 69.51 -107.86
REMARK 500 VAL D 233 -35.07 -38.04
REMARK 500 GLU D 250 48.62 -83.34
REMARK 500 ASP D 278 -1.08 76.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP B 210 22.4 L L OUTSIDE RANGE
REMARK 500 ASN B 291 7.4 L L EXPECTING SP3
REMARK 500 SER B 309 24.6 L L OUTSIDE RANGE
REMARK 500 THR C 163 21.9 L L OUTSIDE RANGE
REMARK 500 LYS D 34 23.0 L L OUTSIDE RANGE
REMARK 500 GLU D 124 24.8 L L OUTSIDE RANGE
REMARK 500 THR D 163 23.8 L L OUTSIDE RANGE
REMARK 500 MET D 215 24.5 L L OUTSIDE RANGE
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 323
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 324
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 323
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 324
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 325
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 323
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 324
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 323
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 324
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME D 325
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DNM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT 2.8 ANGSTROM
DBREF 3K6K A 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
DBREF 3K6K B 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
DBREF 3K6K C 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
DBREF 3K6K D 1 309 UNP Q0GMU1 Q0GMU1_9BACT 1 309
SEQADV 3K6K LYS A 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU A 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA A 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA A 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA A 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU A 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K GLU A 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS A 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS A 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS A 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS A 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS A 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS A 322 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LYS B 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU B 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA B 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA B 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA B 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU B 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K GLU B 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS B 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS B 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS B 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS B 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS B 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS B 322 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LYS C 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU C 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA C 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA C 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA C 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU C 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K GLU C 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS C 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS C 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS C 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS C 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS C 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS C 322 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LYS D 310 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU D 311 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA D 312 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA D 313 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K ALA D 314 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K LEU D 315 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K GLU D 316 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS D 317 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS D 318 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS D 319 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS D 320 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS D 321 UNP Q0GMU1 EXPRESSION TAG
SEQADV 3K6K HIS D 322 UNP Q0GMU1 EXPRESSION TAG
SEQRES 1 A 322 MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR ASP
SEQRES 2 A 322 THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU LYS
SEQRES 3 A 322 ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU ASP
SEQRES 4 A 322 GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG PHE
SEQRES 5 A 322 PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP LEU
SEQRES 6 A 322 GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY ALA
SEQRES 7 A 322 GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY TYR
SEQRES 8 A 322 ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR THR
SEQRES 9 A 322 GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER LEU
SEQRES 10 A 322 ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA ALA
SEQRES 11 A 322 VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU LYS
SEQRES 12 A 322 THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY ASP
SEQRES 13 A 322 SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU LYS
SEQRES 14 A 322 ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU VAL
SEQRES 15 A 322 MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG TRP
SEQRES 16 A 322 SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA GLU
SEQRES 17 A 322 PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL GLY
SEQRES 18 A 322 GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL TYR
SEQRES 19 A 322 ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS VAL
SEQRES 20 A 322 GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR LEU
SEQRES 21 A 322 ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU LEU
SEQRES 22 A 322 LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET TYR
SEQRES 23 A 322 GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS GLU
SEQRES 24 A 322 ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU ALA
SEQRES 25 A 322 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 322 MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR ASP
SEQRES 2 B 322 THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU LYS
SEQRES 3 B 322 ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU ASP
SEQRES 4 B 322 GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG PHE
SEQRES 5 B 322 PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP LEU
SEQRES 6 B 322 GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY ALA
SEQRES 7 B 322 GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY TYR
SEQRES 8 B 322 ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR THR
SEQRES 9 B 322 GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER LEU
SEQRES 10 B 322 ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA ALA
SEQRES 11 B 322 VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU LYS
SEQRES 12 B 322 THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY ASP
SEQRES 13 B 322 SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU LYS
SEQRES 14 B 322 ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU VAL
SEQRES 15 B 322 MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG TRP
SEQRES 16 B 322 SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA GLU
SEQRES 17 B 322 PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL GLY
SEQRES 18 B 322 GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL TYR
SEQRES 19 B 322 ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS VAL
SEQRES 20 B 322 GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR LEU
SEQRES 21 B 322 ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU LEU
SEQRES 22 B 322 LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET TYR
SEQRES 23 B 322 GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS GLU
SEQRES 24 B 322 ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU ALA
SEQRES 25 B 322 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 322 MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR ASP
SEQRES 2 C 322 THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU LYS
SEQRES 3 C 322 ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU ASP
SEQRES 4 C 322 GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG PHE
SEQRES 5 C 322 PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP LEU
SEQRES 6 C 322 GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY ALA
SEQRES 7 C 322 GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY TYR
SEQRES 8 C 322 ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR THR
SEQRES 9 C 322 GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER LEU
SEQRES 10 C 322 ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA ALA
SEQRES 11 C 322 VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU LYS
SEQRES 12 C 322 THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY ASP
SEQRES 13 C 322 SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU LYS
SEQRES 14 C 322 ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU VAL
SEQRES 15 C 322 MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG TRP
SEQRES 16 C 322 SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA GLU
SEQRES 17 C 322 PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL GLY
SEQRES 18 C 322 GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL TYR
SEQRES 19 C 322 ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS VAL
SEQRES 20 C 322 GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR LEU
SEQRES 21 C 322 ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU LEU
SEQRES 22 C 322 LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET TYR
SEQRES 23 C 322 GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS GLU
SEQRES 24 C 322 ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU ALA
SEQRES 25 C 322 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 322 MET GLY ALA MET ASP GLN GLU ILE GLY THR VAL THR ASP
SEQRES 2 D 322 THR LYS MET ASP PRO ARG ASP PHE LEU GLN LEU LEU LYS
SEQRES 3 D 322 ILE ASN ALA GLU LYS ALA GLU LYS ASN LEU PRO LEU ASP
SEQRES 4 D 322 GLN LYS ARG ALA GLY MET GLU ALA LEU CYS GLU ARG PHE
SEQRES 5 D 322 PRO ARG ALA GLU GLY VAL GLU LEU THR LEU THR ASP LEU
SEQRES 6 D 322 GLY GLY VAL PRO CYS ILE ARG GLN ALA THR ASP GLY ALA
SEQRES 7 D 322 GLY ALA ALA HIS ILE LEU TYR PHE HIS GLY GLY GLY TYR
SEQRES 8 D 322 ILE SER GLY SER PRO SER THR HIS LEU VAL LEU THR THR
SEQRES 9 D 322 GLN LEU ALA LYS GLN SER SER ALA THR LEU TRP SER LEU
SEQRES 10 D 322 ASP TYR ARG LEU ALA PRO GLU ASN PRO PHE PRO ALA ALA
SEQRES 11 D 322 VAL ASP ASP CYS VAL ALA ALA TYR ARG ALA LEU LEU LYS
SEQRES 12 D 322 THR ALA GLY SER ALA ASP ARG ILE ILE ILE ALA GLY ASP
SEQRES 13 D 322 SER ALA GLY GLY GLY LEU THR THR ALA SER MET LEU LYS
SEQRES 14 D 322 ALA LYS GLU ASP GLY LEU PRO MET PRO ALA GLY LEU VAL
SEQRES 15 D 322 MET LEU SER PRO PHE VAL ASP LEU THR LEU SER ARG TRP
SEQRES 16 D 322 SER ASN SER ASN LEU ALA ASP ARG ASP PHE LEU ALA GLU
SEQRES 17 D 322 PRO ASP THR LEU GLY GLU MET SER GLU LEU TYR VAL GLY
SEQRES 18 D 322 GLY GLU ASP ARG LYS ASN PRO LEU ILE SER PRO VAL TYR
SEQRES 19 D 322 ALA ASP LEU SER GLY LEU PRO GLU MET LEU ILE HIS VAL
SEQRES 20 D 322 GLY SER GLU GLU ALA LEU LEU SER ASP SER THR THR LEU
SEQRES 21 D 322 ALA GLU ARG ALA GLY ALA ALA GLY VAL SER VAL GLU LEU
SEQRES 22 D 322 LYS ILE TRP PRO ASP MET PRO HIS VAL PHE GLN MET TYR
SEQRES 23 D 322 GLY LYS PHE VAL ASN ALA ALA ASP ILE SER ILE LYS GLU
SEQRES 24 D 322 ILE CYS HIS TRP ILE SER ALA ARG ILE SER LYS LEU ALA
SEQRES 25 D 322 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 323 5
HET SO4 A 324 5
HET SO4 B 323 5
HET SO4 B 324 5
HET SO4 B 325 5
HET SO4 C 323 5
HET SO4 C 324 5
HET SO4 D 323 5
HET SO4 D 324 5
HET BME D 325 4
HETNAM SO4 SULFATE ION
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 5 SO4 9(O4 S 2-)
FORMUL 14 BME C2 H6 O S
FORMUL 15 HOH *433(H2 O)
HELIX 1 1 ASP A 17 LYS A 31 1 15
HELIX 2 2 PRO A 37 GLU A 50 1 14
HELIX 3 3 SER A 95 SER A 111 1 17
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 ASP A 173 1 17
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 GLY A 287 5 6
HELIX 13 13 VAL A 290 ALA A 306 1 17
HELIX 14 14 ASP B 17 ALA B 32 1 16
HELIX 15 15 PRO B 37 GLU B 50 1 14
HELIX 16 16 HIS B 99 SER B 111 1 13
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 LEU B 200 1 7
HELIX 21 21 ALA B 201 ASP B 204 5 4
HELIX 22 22 GLU B 208 GLY B 221 1 14
HELIX 23 23 SER B 231 ALA B 235 5 5
HELIX 24 24 LEU B 253 ALA B 267 1 15
HELIX 25 25 VAL B 282 GLY B 287 5 6
HELIX 26 26 VAL B 290 ILE B 308 1 19
HELIX 27 27 ASP C 17 GLU C 30 1 14
HELIX 28 28 GLN C 40 ARG C 51 1 12
HELIX 29 29 HIS C 99 SER C 111 1 13
HELIX 30 30 PRO C 128 GLY C 146 1 19
HELIX 31 31 SER C 147 ASP C 149 5 3
HELIX 32 32 SER C 157 ASP C 173 1 17
HELIX 33 33 ARG C 194 LEU C 200 1 7
HELIX 34 34 ALA C 201 ASP C 204 5 4
HELIX 35 35 GLU C 208 GLY C 221 1 14
HELIX 36 36 SER C 231 ALA C 235 5 5
HELIX 37 37 LEU C 253 ALA C 267 1 15
HELIX 38 38 VAL C 282 TYR C 286 5 5
HELIX 39 39 VAL C 290 SER C 309 1 20
HELIX 40 40 ASP D 17 LYS D 31 1 15
HELIX 41 41 PRO D 37 ARG D 51 1 15
HELIX 42 42 HIS D 99 SER D 111 1 13
HELIX 43 43 PRO D 128 GLY D 146 1 19
HELIX 44 44 SER D 147 ASP D 149 5 3
HELIX 45 45 ALA D 158 ASP D 173 1 16
HELIX 46 46 ARG D 194 LEU D 200 1 7
HELIX 47 47 GLU D 208 GLY D 221 1 14
HELIX 48 48 SER D 231 ALA D 235 5 5
HELIX 49 49 LEU D 253 ALA D 267 1 15
HELIX 50 50 VAL D 282 TYR D 286 5 5
HELIX 51 51 ASN D 291 ILE D 308 1 18
SHEET 1 A32 GLU A 59 LEU A 65 0
SHEET 2 A32 VAL A 68 ALA A 74 -1 O CYS A 70 N THR A 63
SHEET 3 A32 THR A 113 LEU A 117 -1 O LEU A 114 N GLN A 73
SHEET 4 A32 HIS A 82 PHE A 86 1 N ILE A 83 O TRP A 115
SHEET 5 A32 ILE A 151 ASP A 156 1 O ILE A 152 N LEU A 84
SHEET 6 A32 GLY A 180 LEU A 184 1 O VAL A 182 N ILE A 153
SHEET 7 A32 MET A 243 GLY A 248 1 O HIS A 246 N MET A 183
SHEET 8 A32 VAL A 271 TRP A 276 1 O TRP A 276 N VAL A 247
SHEET 9 A32 VAL B 271 PRO B 280 -1 O LEU B 273 N LEU A 273
SHEET 10 A32 MET B 243 GLU B 250 1 N ILE B 245 O GLU B 272
SHEET 11 A32 GLY B 180 LEU B 184 1 N MET B 183 O LEU B 244
SHEET 12 A32 ILE B 151 ASP B 156 1 N GLY B 155 O LEU B 184
SHEET 13 A32 ALA B 81 PHE B 86 1 N LEU B 84 O ALA B 154
SHEET 14 A32 ALA B 112 LEU B 117 1 O TRP B 115 N ILE B 83
SHEET 15 A32 VAL B 68 ALA B 74 -1 N GLN B 73 O LEU B 114
SHEET 16 A32 GLU B 59 LEU B 65 -1 N GLU B 59 O ALA B 74
SHEET 17 A32 VAL C 58 LEU C 65 -1 O LEU C 62 N LEU B 60
SHEET 18 A32 VAL C 68 THR C 75 -1 O ALA C 74 N GLU C 59
SHEET 19 A32 THR C 113 LEU C 117 -1 O SER C 116 N ILE C 71
SHEET 20 A32 HIS C 82 PHE C 86 1 N ILE C 83 O TRP C 115
SHEET 21 A32 ILE C 151 ASP C 156 1 O ALA C 154 N LEU C 84
SHEET 22 A32 GLY C 180 LEU C 184 1 O VAL C 182 N ILE C 153
SHEET 23 A32 MET C 243 GLY C 248 1 O LEU C 244 N MET C 183
SHEET 24 A32 VAL C 271 TRP C 276 1 O TRP C 276 N VAL C 247
SHEET 25 A32 VAL D 271 PRO D 280 -1 O LEU D 273 N LEU C 273
SHEET 26 A32 MET D 243 GLU D 250 1 N ILE D 245 O GLU D 272
SHEET 27 A32 GLY D 180 LEU D 184 1 N MET D 183 O LEU D 244
SHEET 28 A32 ILE D 151 ASP D 156 1 N ILE D 153 O VAL D 182
SHEET 29 A32 HIS D 82 PHE D 86 1 N LEU D 84 O ILE D 152
SHEET 30 A32 THR D 113 LEU D 117 1 O TRP D 115 N ILE D 83
SHEET 31 A32 VAL D 68 ALA D 74 -1 N GLN D 73 O LEU D 114
SHEET 32 A32 GLU D 59 LEU D 65 -1 N GLU D 59 O ALA D 74
CISPEP 1 ALA A 122 PRO A 123 0 4.84
CISPEP 2 PHE A 127 PRO A 128 0 8.45
CISPEP 3 ALA B 122 PRO B 123 0 3.08
CISPEP 4 PHE B 127 PRO B 128 0 10.53
CISPEP 5 ALA C 122 PRO C 123 0 0.07
CISPEP 6 PHE C 127 PRO C 128 0 10.74
CISPEP 7 ALA D 122 PRO D 123 0 4.37
CISPEP 8 PHE D 127 PRO D 128 0 9.44
SITE 1 AC1 6 ARG A 54 ALA A 55 GLU A 56 GLN A 105
SITE 2 AC1 6 LYS A 108 HOH A 411
SITE 1 AC2 3 ARG A 194 TYR A 234 ARG A 263
SITE 1 AC3 3 GLU B 56 GLN B 105 LYS B 108
SITE 1 AC4 2 SER B 305 ILE B 308
SITE 1 AC5 5 THR A 258 THR A 259 THR B 258 THR B 259
SITE 2 AC5 5 GLU B 262
SITE 1 AC6 3 GLU C 56 GLN C 105 LYS C 108
SITE 1 AC7 3 ARG C 194 TYR C 234 ARG C 263
SITE 1 AC8 4 ALA D 55 GLU D 56 GLN D 105 LYS D 108
SITE 1 AC9 4 ARG D 194 TYR D 234 ARG D 263 HOH D 338
SITE 1 BC1 3 SER D 157 LEU D 206 HIS D 281
CRYST1 117.157 127.699 232.870 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 0.008536 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007831 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004294 0.00000
TER 2236 SER A 309
TER 4472 SER B 309
TER 6651 SER C 309
TER 8857 ILE D 308
MASTER 574 0 10 51 32 0 12 6 9335 4 49 100
END |