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HEADER LYASE 23-JUN-14 3WWP
TITLE S-SELECTIVE HYDROXYNITRILE LYASE FROM BALIOSPERMUM MONTANUM (APO2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B, G, L, M, R;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BALIOSPERMUM MONTANUM;
SOURCE 3 ORGANISM_TAXID: 316758;
SOURCE 4 GENE: BMHNL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE FOLD, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NAKANO,M.DADASHIPOUR,Y.ASANO
REVDAT 1 22-OCT-14 3WWP 0
JRNL AUTH S.NAKANO,M.DADASHIPOUR,Y.ASANO
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF HYDROXYNITRILE LYASE
JRNL TITL 2 FROM BALIOSPERMUM MONTANUM WITH CRYSTAL STRUCTURE, MOLECULAR
JRNL TITL 3 DYNAMICS AND ENZYME KINETICS
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1844 2059 2014
JRNL REFN ISSN 0006-3002
JRNL PMID 25220808
JRNL DOI 10.1016/J.BBAPAP.2014.09.004
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 172073
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9074
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12564
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 679
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12464
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 250
REMARK 3 SOLVENT ATOMS : 1849
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.00000
REMARK 3 B33 (A**2) : -0.00000
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): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.514
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12983 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12029 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17632 ; 1.388 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27723 ; 0.739 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1562 ; 6.693 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 612 ;39.970 ;25.098
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2090 ;15.260 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;22.345 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1942 ; 0.231 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14624 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2972 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3WWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-14.
REMARK 100 THE RCSB ID CODE IS RCSB096887.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 181227
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 45.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM SULFATE, 0.1M SODIUM
REMARK 280 CITRATE, 0.5M AMMONIUM SULFATE, PH 5.6, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 95.98100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 130.79050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 95.98100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 130.79050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 95.98100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 130.79050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 95.98100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 130.79050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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: 5250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, L
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 540 LIES ON A SPECIAL POSITION.
REMARK 375 HOH L 499 LIES ON A SPECIAL POSITION.
REMARK 375 HOH L 617 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -24
REMARK 465 ASN A -23
REMARK 465 HIS A -22
REMARK 465 LYS A -21
REMARK 465 VAL A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 ILE A -13
REMARK 465 GLU A -12
REMARK 465 GLY A -11
REMARK 465 ARG A -10
REMARK 465 HIS A -9
REMARK 465 MET A -8
REMARK 465 GLU A -7
REMARK 465 LEU A -6
REMARK 465 GLY A -5
REMARK 465 THR A -4
REMARK 465 LEU A -3
REMARK 465 ALA A 263
REMARK 465 MET B -24
REMARK 465 ASN B -23
REMARK 465 HIS B -22
REMARK 465 LYS B -21
REMARK 465 VAL B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 ILE B -13
REMARK 465 GLU B -12
REMARK 465 GLY B -11
REMARK 465 ARG B -10
REMARK 465 HIS B -9
REMARK 465 MET B -8
REMARK 465 GLU B -7
REMARK 465 LEU B -6
REMARK 465 GLY B -5
REMARK 465 THR B -4
REMARK 465 LEU B -3
REMARK 465 GLU B -2
REMARK 465 LEU B 260
REMARK 465 ALA B 261
REMARK 465 VAL B 262
REMARK 465 ALA B 263
REMARK 465 MET G -24
REMARK 465 ASN G -23
REMARK 465 HIS G -22
REMARK 465 LYS G -21
REMARK 465 VAL G -20
REMARK 465 HIS G -19
REMARK 465 HIS G -18
REMARK 465 HIS G -17
REMARK 465 HIS G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 ILE G -13
REMARK 465 GLU G -12
REMARK 465 GLY G -11
REMARK 465 ARG G -10
REMARK 465 HIS G -9
REMARK 465 MET G -8
REMARK 465 GLU G -7
REMARK 465 LEU G -6
REMARK 465 GLY G -5
REMARK 465 THR G -4
REMARK 465 LEU G -3
REMARK 465 LEU G 260
REMARK 465 ALA G 261
REMARK 465 VAL G 262
REMARK 465 ALA G 263
REMARK 465 MET L -24
REMARK 465 ASN L -23
REMARK 465 HIS L -22
REMARK 465 LYS L -21
REMARK 465 VAL L -20
REMARK 465 HIS L -19
REMARK 465 HIS L -18
REMARK 465 HIS L -17
REMARK 465 HIS L -16
REMARK 465 HIS L -15
REMARK 465 HIS L -14
REMARK 465 ILE L -13
REMARK 465 GLU L -12
REMARK 465 GLY L -11
REMARK 465 ARG L -10
REMARK 465 HIS L -9
REMARK 465 MET L -8
REMARK 465 GLU L -7
REMARK 465 LEU L -6
REMARK 465 GLY L -5
REMARK 465 THR L -4
REMARK 465 LEU L -3
REMARK 465 GLU L -2
REMARK 465 ALA L 256
REMARK 465 SER L 257
REMARK 465 ASP L 258
REMARK 465 LEU L 259
REMARK 465 LEU L 260
REMARK 465 ALA L 261
REMARK 465 VAL L 262
REMARK 465 ALA L 263
REMARK 465 MET M -24
REMARK 465 ASN M -23
REMARK 465 HIS M -22
REMARK 465 LYS M -21
REMARK 465 VAL M -20
REMARK 465 HIS M -19
REMARK 465 HIS M -18
REMARK 465 HIS M -17
REMARK 465 HIS M -16
REMARK 465 HIS M -15
REMARK 465 HIS M -14
REMARK 465 ILE M -13
REMARK 465 GLU M -12
REMARK 465 GLY M -11
REMARK 465 ARG M -10
REMARK 465 HIS M -9
REMARK 465 MET M -8
REMARK 465 GLU M -7
REMARK 465 LEU M -6
REMARK 465 GLY M -5
REMARK 465 THR M -4
REMARK 465 LEU M -3
REMARK 465 GLU M -2
REMARK 465 SER M 257
REMARK 465 ASP M 258
REMARK 465 LEU M 259
REMARK 465 LEU M 260
REMARK 465 ALA M 261
REMARK 465 VAL M 262
REMARK 465 ALA M 263
REMARK 465 MET R -24
REMARK 465 ASN R -23
REMARK 465 HIS R -22
REMARK 465 LYS R -21
REMARK 465 VAL R -20
REMARK 465 HIS R -19
REMARK 465 HIS R -18
REMARK 465 HIS R -17
REMARK 465 HIS R -16
REMARK 465 HIS R -15
REMARK 465 HIS R -14
REMARK 465 ILE R -13
REMARK 465 GLU R -12
REMARK 465 GLY R -11
REMARK 465 ARG R -10
REMARK 465 HIS R -9
REMARK 465 MET R -8
REMARK 465 GLU R -7
REMARK 465 LEU R -6
REMARK 465 GLY R -5
REMARK 465 THR R -4
REMARK 465 LEU R -3
REMARK 465 GLU R -2
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 O HOH L 733 O HOH L 736 1.57
REMARK 500 O HOH G 436 O HOH G 648 1.67
REMARK 500 O HOH M 439 O HOH M 542 1.72
REMARK 500 O HOH B 776 O HOH B 777 1.74
REMARK 500 O HOH A 791 O HOH A 808 1.78
REMARK 500 O HOH B 775 O HOH B 777 1.82
REMARK 500 O GLU B 205 NH2 ARG B 212 1.87
REMARK 500 SG CYS R 229 O HOH R 699 1.92
REMARK 500 CB ILE B 163 O HOH B 783 1.92
REMARK 500 O2 EDO B 302 O HOH B 786 1.95
REMARK 500 O HOH B 449 O HOH B 669 1.95
REMARK 500 CB ASN A 135 O HOH A 792 1.95
REMARK 500 O HOH M 521 O HOH M 534 1.99
REMARK 500 O HOH L 516 O HOH L 720 1.99
REMARK 500 O HOH L 635 O HOH L 737 2.00
REMARK 500 O HOH G 529 O HOH G 634 2.02
REMARK 500 SG CYS G 229 O HOH G 638 2.03
REMARK 500 SG CYS A 229 O HOH A 791 2.03
REMARK 500 O HOH L 646 O HOH L 718 2.05
REMARK 500 O GLU M 55 O HOH M 505 2.05
REMARK 500 SG CYS L 229 O HOH L 736 2.06
REMARK 500 O HOH L 599 O HOH L 672 2.07
REMARK 500 O3 SO4 R 306 O HOH R 607 2.07
REMARK 500 O HOH A 578 O HOH A 779 2.08
REMARK 500 NE1 TRP R 217 O2 SO4 R 307 2.08
REMARK 500 SG CYS B 229 O HOH B 727 2.08
REMARK 500 O1 EDO B 302 O HOH B 786 2.08
REMARK 500 SG CYS M 229 O HOH M 478 2.09
REMARK 500 O HOH A 652 O HOH A 764 2.12
REMARK 500 O HOH G 635 O HOH G 638 2.13
REMARK 500 O3 SO4 L 307 O HOH L 734 2.13
REMARK 500 O HOH L 628 O HOH L 739 2.13
REMARK 500 NZ LYS L 170 O HOH L 628 2.13
REMARK 500 O HOH A 607 O HOH A 809 2.14
REMARK 500 ND2 ASN G 243 O1 CIT G 301 2.14
REMARK 500 CD1 LEU R 260 O HOH A 807 2.14
REMARK 500 O GLY L 139 O HOH L 685 2.15
REMARK 500 O HOH A 700 O HOH R 697 2.15
REMARK 500 O LEU L 186 O HOH L 639 2.15
REMARK 500 O HOH B 649 O HOH B 693 2.16
REMARK 500 O HOH R 601 O HOH R 604 2.16
REMARK 500 O HOH B 587 O HOH B 726 2.16
REMARK 500 O HOH A 715 O HOH A 794 2.16
REMARK 500 O HOH A 517 O HOH A 699 2.16
REMARK 500 O4 SO4 A 308 O HOH A 787 2.16
REMARK 500 C ASN L 140 O HOH L 601 2.17
REMARK 500 O1 EDO R 302 O HOH R 698 2.17
REMARK 500 O2 EDO L 303 O HOH L 738 2.17
REMARK 500 CD1 PHE A 178 O HOH A 806 2.17
REMARK 500 O HOH A 705 O HOH A 735 2.18
REMARK 500
REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH M 492 O HOH M 492 6445 1.93
REMARK 500 O HOH A 761 O HOH B 539 4554 2.05
REMARK 500 O HOH L 563 O HOH L 642 6445 2.17
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 LEU A 88 CB - CG - CD1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 199 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG B 212 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 212 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG L 199 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG R 199 NE - CZ - NH2 ANGL. DEV. = -5.3 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 CYS A 13 -17.45 81.05
REMARK 500 HIS A 14 -169.00 -105.89
REMARK 500 SER A 80 -117.87 51.81
REMARK 500 ASN A 104 52.34 38.57
REMARK 500 LYS A 129 -115.90 48.38
REMARK 500 PHE A 158 42.50 -98.90
REMARK 500 ILE A 209 -42.08 -130.28
REMARK 500 SER A 211 151.60 -36.87
REMARK 500 LYS A 236 72.47 -106.40
REMARK 500 LYS A 241 57.64 -142.65
REMARK 500 CYS B 13 -14.66 82.03
REMARK 500 HIS B 14 -168.54 -109.05
REMARK 500 SER B 80 -118.43 56.24
REMARK 500 ASN B 104 56.28 36.01
REMARK 500 LYS B 129 -123.25 55.70
REMARK 500 PHE B 158 46.40 -104.44
REMARK 500 ILE B 209 -41.66 -131.09
REMARK 500 TYR B 222 84.56 -151.94
REMARK 500 LYS B 236 70.48 -106.20
REMARK 500 CYS G 13 -14.09 79.69
REMARK 500 HIS G 14 -159.32 -106.32
REMARK 500 SER G 80 -119.35 48.78
REMARK 500 ASN G 104 54.19 36.97
REMARK 500 ASP G 109 -165.21 -118.87
REMARK 500 LYS G 129 -120.31 53.58
REMARK 500 PHE G 158 47.77 -100.43
REMARK 500 ILE G 209 -39.99 -131.24
REMARK 500 TYR G 222 84.36 -154.21
REMARK 500 LYS G 236 73.40 -101.40
REMARK 500 CYS L 13 -13.15 85.96
REMARK 500 SER L 80 -116.51 55.01
REMARK 500 TYR L 93 51.05 -140.70
REMARK 500 ASN L 104 55.27 39.14
REMARK 500 ASP L 109 -166.90 -118.85
REMARK 500 LYS L 129 -122.34 52.95
REMARK 500 ILE L 157 -62.04 -95.21
REMARK 500 PHE L 158 43.79 -93.11
REMARK 500 ILE L 209 -41.35 -131.95
REMARK 500 SER L 232 12.41 57.22
REMARK 500 ASP L 234 -159.35 -85.87
REMARK 500 LYS L 236 76.02 -100.75
REMARK 500 CYS M 13 -15.41 85.50
REMARK 500 HIS M 14 -167.02 -110.05
REMARK 500 SER M 80 -124.41 47.86
REMARK 500 ASN M 104 56.30 33.72
REMARK 500 LYS M 129 -118.46 53.30
REMARK 500 PHE M 158 43.43 -99.38
REMARK 500 TYR M 222 79.38 -162.38
REMARK 500 LYS M 236 72.29 -105.64
REMARK 500 LYS M 241 56.09 -146.78
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP L 141 THR L 142 147.78
REMARK 500 VAL R 262 ALA R 263 141.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 199 0.19 SIDE CHAIN
REMARK 500 ARG B 199 0.15 SIDE CHAIN
REMARK 500 ARG L 199 0.15 SIDE CHAIN
REMARK 500 ARG R 199 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN G 135 10.58
REMARK 500 ASN L 135 11.58
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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: (10X,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 THR B 142 24.3 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 CIT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT M 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT R 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL R 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WWO RELATED DB: PDB
DBREF 3WWP A 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
DBREF 3WWP B 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
DBREF 3WWP G 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
DBREF 3WWP L 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
DBREF 3WWP M 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
DBREF 3WWP R 1 263 UNP D1MX73 D1MX73_9ROSI 1 263
SEQADV 3WWP MET A -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ASN A -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LYS A -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP VAL A -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ILE A -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU A -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY A -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ARG A -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS A -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET A -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU A -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU A -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY A -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP THR A -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU A -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU A -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY A -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP PHE A 0 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET B -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ASN B -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LYS B -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP VAL B -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ILE B -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU B -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY B -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ARG B -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS B -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET B -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU B -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU B -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY B -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP THR B -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU B -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU B -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY B -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP PHE B 0 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET G -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ASN G -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LYS G -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP VAL G -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ILE G -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU G -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY G -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ARG G -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS G -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET G -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU G -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU G -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY G -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP THR G -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU G -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU G -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY G -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP PHE G 0 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET L -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ASN L -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LYS L -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP VAL L -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ILE L -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU L -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY L -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ARG L -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS L -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET L -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU L -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU L -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY L -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP THR L -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU L -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU L -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY L -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP PHE L 0 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET M -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ASN M -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LYS M -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP VAL M -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ILE M -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU M -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY M -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ARG M -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS M -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET M -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU M -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU M -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY M -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP THR M -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU M -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU M -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY M -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP PHE M 0 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET R -24 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ASN R -23 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -22 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LYS R -21 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP VAL R -20 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -19 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -18 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -17 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -16 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -15 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -14 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ILE R -13 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU R -12 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY R -11 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP ARG R -10 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP HIS R -9 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP MET R -8 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU R -7 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU R -6 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY R -5 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP THR R -4 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP LEU R -3 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLU R -2 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP GLY R -1 UNP D1MX73 EXPRESSION TAG
SEQADV 3WWP PHE R 0 UNP D1MX73 EXPRESSION TAG
SEQRES 1 A 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 A 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 A 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 A 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 A 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 A 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 A 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 A 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 A 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 A 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 A 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 A 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 A 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 A 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 A 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 A 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 A 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 A 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 A 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 A 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 A 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 A 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 A 288 VAL ALA
SEQRES 1 B 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 B 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 B 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 B 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 B 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 B 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 B 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 B 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 B 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 B 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 B 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 B 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 B 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 B 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 B 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 B 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 B 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 B 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 B 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 B 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 B 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 B 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 B 288 VAL ALA
SEQRES 1 G 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 G 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 G 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 G 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 G 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 G 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 G 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 G 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 G 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 G 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 G 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 G 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 G 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 G 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 G 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 G 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 G 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 G 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 G 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 G 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 G 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 G 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 G 288 VAL ALA
SEQRES 1 L 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 L 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 L 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 L 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 L 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 L 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 L 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 L 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 L 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 L 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 L 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 L 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 L 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 L 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 L 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 L 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 L 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 L 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 L 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 L 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 L 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 L 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 L 288 VAL ALA
SEQRES 1 M 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 M 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 M 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 M 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 M 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 M 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 M 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 M 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 M 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 M 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 M 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 M 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 M 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 M 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 M 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 M 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 M 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 M 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 M 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 M 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 M 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 M 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 M 288 VAL ALA
SEQRES 1 R 288 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 R 288 GLY ARG HIS MET GLU LEU GLY THR LEU GLU GLY PHE MET
SEQRES 3 R 288 VAL SER ALA HIS PHE ILE LEU ILE HIS THR ILE CYS HIS
SEQRES 4 R 288 GLY ALA TRP LEU TRP TYR LYS LEU ILE PRO LEU LEU GLN
SEQRES 5 R 288 SER ALA GLY HIS ASN ALA THR ALA ILE ASP LEU VAL ALA
SEQRES 6 R 288 SER GLY ILE ASP PRO ARG GLN LEU GLU GLN ILE GLY THR
SEQRES 7 R 288 TRP GLU GLN TYR SER GLU PRO LEU PHE THR LEU ILE GLU
SEQRES 8 R 288 SER ILE PRO GLU GLY LYS LYS VAL ILE LEU VAL GLY GLU
SEQRES 9 R 288 SER GLY GLY GLY ILE ASN ILE ALA LEU ALA ALA GLU LYS
SEQRES 10 R 288 TYR PRO GLU LYS VAL SER ALA LEU VAL PHE HIS ASN ALA
SEQRES 11 R 288 LEU MET PRO ASP ILE ASP HIS SER PRO ALA PHE VAL TYR
SEQRES 12 R 288 LYS LYS PHE SER GLU VAL PHE THR ASP TRP LYS ASP SER
SEQRES 13 R 288 ILE PHE SER ASN TYR THR TYR GLY ASN ASP THR VAL THR
SEQRES 14 R 288 ALA VAL GLU LEU GLY ASP ARG THR LEU ALA GLU ASN ILE
SEQRES 15 R 288 PHE SER ASN SER PRO ILE GLU ASP VAL GLU LEU ALA LYS
SEQRES 16 R 288 HIS LEU VAL ARG LYS GLY SER PHE PHE GLU GLN ASP LEU
SEQRES 17 R 288 ASP THR LEU PRO ASN PHE THR SER GLU GLY TYR GLY SER
SEQRES 18 R 288 ILE ARG ARG VAL TYR VAL TYR GLY GLU GLU ASP GLN ILE
SEQRES 19 R 288 PHE SER ARG ASP PHE GLN LEU TRP GLN ILE ASN ASN TYR
SEQRES 20 R 288 LYS PRO ASP LYS VAL TYR CYS VAL PRO SER ALA ASP HIS
SEQRES 21 R 288 LYS ILE GLN ILE SER LYS VAL ASN GLU LEU ALA GLN ILE
SEQRES 22 R 288 LEU GLN GLU VAL ALA ASN SER ALA SER ASP LEU LEU ALA
SEQRES 23 R 288 VAL ALA
HET CIT A 301 13
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HET EDO A 305 4
HET SO4 A 306 5
HET SO4 A 307 5
HET SO4 A 308 5
HET CL A 309 1
HET CIT B 301 13
HET EDO B 302 4
HET EDO B 303 4
HET EDO B 304 4
HET EDO B 305 4
HET SO4 B 306 5
HET SO4 B 307 5
HET SO4 B 308 5
HET SO4 B 309 5
HET SO4 B 310 5
HET CL B 311 1
HET CIT G 301 13
HET EDO G 302 4
HET EDO G 303 4
HET SO4 G 304 5
HET SO4 G 305 5
HET SO4 G 306 5
HET CL G 307 1
HET CIT L 301 13
HET EDO L 302 4
HET EDO L 303 4
HET EDO L 304 4
HET EDO L 305 4
HET SO4 L 306 5
HET SO4 L 307 5
HET SO4 L 308 5
HET CL L 309 1
HET CIT M 301 13
HET EDO M 302 4
HET EDO M 303 4
HET EDO M 304 4
HET CL M 305 1
HET CIT R 301 13
HET EDO R 302 4
HET EDO R 303 4
HET SO4 R 304 5
HET SO4 R 305 5
HET SO4 R 306 5
HET SO4 R 307 5
HET CL R 308 1
HETNAM CIT CITRIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 CIT 6(C6 H8 O7)
FORMUL 8 EDO 19(C2 H6 O2)
FORMUL 12 SO4 18(O4 S 2-)
FORMUL 15 CL 6(CL 1-)
FORMUL 56 HOH *1849(H2 O)
HELIX 1 1 GLY A 15 TYR A 20 5 6
HELIX 2 2 LYS A 21 ALA A 29 1 9
HELIX 3 3 GLN A 47 ILE A 51 5 5
HELIX 4 4 THR A 53 SER A 58 1 6
HELIX 5 5 SER A 58 SER A 67 1 10
HELIX 6 6 GLY A 81 TYR A 93 1 13
HELIX 7 7 ALA A 115 PHE A 125 1 11
HELIX 8 8 GLY A 149 ASN A 156 1 8
HELIX 9 9 PRO A 162 HIS A 171 1 10
HELIX 10 10 PHE A 179 LEU A 186 1 8
HELIX 11 11 GLY A 193 ILE A 197 5 5
HELIX 12 12 SER A 211 TYR A 222 1 12
HELIX 13 13 LYS A 236 LYS A 241 1 6
HELIX 14 14 LYS A 241 ALA A 261 1 21
HELIX 15 15 GLY B 15 TYR B 20 5 6
HELIX 16 16 LYS B 21 ALA B 29 1 9
HELIX 17 17 GLN B 47 ILE B 51 5 5
HELIX 18 18 THR B 53 SER B 58 1 6
HELIX 19 19 SER B 58 SER B 67 1 10
HELIX 20 20 GLY B 81 TYR B 93 1 13
HELIX 21 21 ALA B 115 PHE B 125 1 11
HELIX 22 22 GLY B 149 ASN B 156 1 8
HELIX 23 23 PRO B 162 HIS B 171 1 10
HELIX 24 24 PHE B 179 LEU B 186 1 8
HELIX 25 25 GLY B 193 ILE B 197 5 5
HELIX 26 26 SER B 211 TYR B 222 1 12
HELIX 27 27 LYS B 236 LYS B 241 1 6
HELIX 28 28 LYS B 241 SER B 257 1 17
HELIX 29 29 GLY G 15 TYR G 20 5 6
HELIX 30 30 LYS G 21 ALA G 29 1 9
HELIX 31 31 GLN G 47 ILE G 51 5 5
HELIX 32 32 THR G 53 SER G 58 1 6
HELIX 33 33 SER G 58 SER G 67 1 10
HELIX 34 34 GLY G 81 TYR G 93 1 13
HELIX 35 35 ALA G 115 PHE G 125 1 11
HELIX 36 36 GLY G 149 ASN G 156 1 8
HELIX 37 37 PRO G 162 HIS G 171 1 10
HELIX 38 38 PHE G 179 ASP G 184 1 6
HELIX 39 39 GLY G 193 ILE G 197 5 5
HELIX 40 40 SER G 211 TYR G 222 1 12
HELIX 41 41 LYS G 236 LYS G 241 1 6
HELIX 42 42 LYS G 241 SER G 257 1 17
HELIX 43 43 GLY L 15 TYR L 20 5 6
HELIX 44 44 LEU L 22 ALA L 29 1 8
HELIX 45 45 GLN L 47 ILE L 51 5 5
HELIX 46 46 THR L 53 SER L 58 1 6
HELIX 47 47 SER L 58 SER L 67 1 10
HELIX 48 48 GLY L 81 TYR L 93 1 13
HELIX 49 49 ALA L 115 PHE L 125 1 11
HELIX 50 50 GLY L 149 ASN L 156 1 8
HELIX 51 51 PRO L 162 HIS L 171 1 10
HELIX 52 52 PHE L 179 LEU L 186 1 8
HELIX 53 53 GLY L 193 ILE L 197 5 5
HELIX 54 54 SER L 211 TYR L 222 1 12
HELIX 55 55 LYS L 236 LYS L 241 1 6
HELIX 56 56 LYS L 241 SER L 255 1 15
HELIX 57 57 GLY M 15 TYR M 20 5 6
HELIX 58 58 LYS M 21 ALA M 29 1 9
HELIX 59 59 GLN M 47 ILE M 51 5 5
HELIX 60 60 THR M 53 SER M 58 1 6
HELIX 61 61 SER M 58 SER M 67 1 10
HELIX 62 62 GLY M 81 TYR M 93 1 13
HELIX 63 63 ALA M 115 PHE M 125 1 11
HELIX 64 64 GLY M 149 ASN M 156 1 8
HELIX 65 65 PRO M 162 HIS M 171 1 10
HELIX 66 66 PHE M 179 ASP M 184 1 6
HELIX 67 67 GLY M 193 ILE M 197 5 5
HELIX 68 68 SER M 211 TYR M 222 1 12
HELIX 69 69 LYS M 236 LYS M 241 1 6
HELIX 70 70 LYS M 241 ALA M 256 1 16
HELIX 71 71 GLY R 15 TYR R 20 5 6
HELIX 72 72 LEU R 22 ALA R 29 1 8
HELIX 73 73 GLN R 47 ILE R 51 5 5
HELIX 74 74 THR R 53 SER R 58 1 6
HELIX 75 75 SER R 58 SER R 67 1 10
HELIX 76 76 GLY R 81 TYR R 93 1 13
HELIX 77 77 ALA R 115 PHE R 125 1 11
HELIX 78 78 GLY R 149 ASN R 156 1 8
HELIX 79 79 PRO R 162 HIS R 171 1 10
HELIX 80 80 PHE R 179 ASP R 184 1 6
HELIX 81 81 GLY R 193 ILE R 197 5 5
HELIX 82 82 SER R 211 TYR R 222 1 12
HELIX 83 83 LYS R 236 LYS R 241 1 6
HELIX 84 84 LYS R 241 ASN R 254 1 14
SHEET 1 A 2 GLY A -1 VAL A 2 0
SHEET 2 A 2 PHE R 0 SER R 3 -1 O SER R 3 N GLY A -1
SHEET 1 B 6 ASN A 32 ALA A 35 0
SHEET 2 B 6 HIS A 5 ILE A 9 1 N PHE A 6 O ASN A 32
SHEET 3 B 6 VAL A 74 GLU A 79 1 O VAL A 77 N ILE A 7
SHEET 4 B 6 VAL A 97 HIS A 103 1 O VAL A 101 N LEU A 76
SHEET 5 B 6 ARG A 198 GLY A 204 1 O VAL A 202 N PHE A 102
SHEET 6 B 6 LYS A 226 VAL A 230 1 O VAL A 230 N TYR A 203
SHEET 1 C 2 ILE A 132 TYR A 138 0
SHEET 2 C 2 ASP A 141 GLU A 147 -1 O VAL A 143 N TYR A 136
SHEET 1 D 8 ASN B 32 ALA B 35 0
SHEET 2 D 8 HIS B 5 ILE B 9 1 N PHE B 6 O ASN B 32
SHEET 3 D 8 VAL B 74 GLU B 79 1 O VAL B 77 N ILE B 9
SHEET 4 D 8 VAL B 97 HIS B 103 1 O VAL B 101 N LEU B 76
SHEET 5 D 8 ARG B 198 GLY B 204 1 O VAL B 202 N PHE B 102
SHEET 6 D 8 LYS B 226 VAL B 230 1 O TYR B 228 N TYR B 201
SHEET 7 D 8 ILE L 132 TYR L 138 -1 O ASN L 135 N VAL B 227
SHEET 8 D 8 ASP L 141 GLU L 147 -1 O VAL L 143 N TYR L 136
SHEET 1 E 2 ILE B 132 TYR B 138 0
SHEET 2 E 2 ASP B 141 GLU B 147 -1 O VAL B 143 N TYR B 136
SHEET 1 F 6 ASN G 32 ALA G 35 0
SHEET 2 F 6 HIS G 5 ILE G 9 1 N PHE G 6 O ASN G 32
SHEET 3 F 6 VAL G 74 GLU G 79 1 O VAL G 77 N ILE G 9
SHEET 4 F 6 VAL G 97 HIS G 103 1 O VAL G 101 N LEU G 76
SHEET 5 F 6 ARG G 199 GLY G 204 1 O VAL G 202 N PHE G 102
SHEET 6 F 6 LYS G 226 VAL G 230 1 O TYR G 228 N TYR G 201
SHEET 1 G 3 ILE G 132 TYR G 138 0
SHEET 2 G 3 ASP G 141 GLU G 147 -1 O VAL G 143 N TYR G 136
SHEET 3 G 3 GLY G 176 SER G 177 -1 O GLY G 176 N VAL G 146
SHEET 1 H 6 ASN L 32 ALA L 35 0
SHEET 2 H 6 HIS L 5 ILE L 9 1 N LEU L 8 O THR L 34
SHEET 3 H 6 VAL L 74 GLU L 79 1 O ILE L 75 N ILE L 7
SHEET 4 H 6 VAL L 97 HIS L 103 1 O VAL L 101 N LEU L 76
SHEET 5 H 6 ARG L 198 GLY L 204 1 O VAL L 202 N PHE L 102
SHEET 6 H 6 LYS L 226 VAL L 230 1 O VAL L 230 N TYR L 203
SHEET 1 I 6 ASN M 32 ALA M 35 0
SHEET 2 I 6 HIS M 5 ILE M 9 1 N LEU M 8 O THR M 34
SHEET 3 I 6 VAL M 74 GLU M 79 1 O ILE M 75 N HIS M 5
SHEET 4 I 6 VAL M 97 HIS M 103 1 O VAL M 101 N LEU M 76
SHEET 5 I 6 ARG M 198 GLY M 204 1 O VAL M 202 N PHE M 102
SHEET 6 I 6 LYS M 226 VAL M 230 1 O LYS M 226 N TYR M 201
SHEET 1 J 2 ILE M 132 TYR M 138 0
SHEET 2 J 2 ASP M 141 GLU M 147 -1 O VAL M 143 N TYR M 136
SHEET 1 K 6 ASN R 32 ALA R 35 0
SHEET 2 K 6 HIS R 5 ILE R 9 1 N LEU R 8 O THR R 34
SHEET 3 K 6 VAL R 74 GLU R 79 1 O VAL R 77 N ILE R 9
SHEET 4 K 6 VAL R 97 HIS R 103 1 O VAL R 101 N LEU R 76
SHEET 5 K 6 ARG R 198 GLY R 204 1 O VAL R 200 N LEU R 100
SHEET 6 K 6 LYS R 226 VAL R 230 1 O TYR R 228 N TYR R 203
SHEET 1 L 2 ILE R 132 TYR R 138 0
SHEET 2 L 2 ASP R 141 GLU R 147 -1 O VAL R 143 N TYR R 136
SITE 1 AC1 13 SER A 240 LYS A 241 VAL A 242 ASN A 243
SITE 2 AC1 13 GLU A 244 HOH A 423 HOH A 431 HOH A 463
SITE 3 AC1 13 HOH A 527 HOH A 599 HOH A 739 HOH A 787
SITE 4 AC1 13 HOH R 545
SITE 1 AC2 5 THR A 11 SER A 80 ILE A 209 CL A 309
SITE 2 AC2 5 HOH A 793
SITE 1 AC3 8 VAL A 124 ASP A 213 HOH A 467 HOH A 758
SITE 2 AC3 8 HOH A 760 GLU L 66 EDO L 304 HOH L 687
SITE 1 AC4 7 TYR A 136 THR A 137 HOH A 680 HOH A 696
SITE 2 AC4 7 HOH A 715 HOH A 794 HOH A 810
SITE 1 AC5 5 TYR A 118 TRP A 128 PHE A 178 HOH A 453
SITE 2 AC5 5 HOH A 635
SITE 1 AC6 8 HIS A 112 SER A 113 HOH A 459 HOH A 485
SITE 2 AC6 8 HOH A 615 HOH A 619 HOH A 689 HOH A 734
SITE 1 AC7 5 LYS A 129 ARG A 151 HOH A 443 HOH A 533
SITE 2 AC7 5 HOH A 747
SITE 1 AC8 5 ASN A 160 SER A 232 LYS A 241 HOH A 673
SITE 2 AC8 5 HOH A 787
SITE 1 AC9 4 THR A 11 HIS A 235 LYS A 236 EDO A 302
SITE 1 BC1 9 SER B 240 LYS B 241 VAL B 242 ASN B 243
SITE 2 BC1 9 GLU B 244 HOH B 410 HOH B 562 HOH B 567
SITE 3 BC1 9 HOH B 690
SITE 1 BC2 6 THR B 11 SER B 80 PHE B 178 CL B 311
SITE 2 BC2 6 HOH B 613 HOH B 786
SITE 1 BC3 8 ILE A 43 ASP A 44 GLN A 47 ARG A 174
SITE 2 BC3 8 ASP B 44 PRO B 45 GLN B 47 ARG B 174
SITE 1 BC4 7 LEU B 88 GLU B 91 LEU B 186 PRO B 187
SITE 2 BC4 7 PHE B 189 HOH B 634 HOH B 717
SITE 1 BC5 5 TYR B 118 PHE B 178 HOH B 421 HOH B 463
SITE 2 BC5 5 HOH B 744
SITE 1 BC6 4 HIS B 112 SER B 113 HOH B 565 HOH B 588
SITE 1 BC7 3 ARG B 151 HOH B 471 HOH B 534
SITE 1 BC8 6 LYS B 226 HOH B 542 HOH B 605 HOH B 686
SITE 2 BC8 6 GLU L 49 LYS L 175
SITE 1 BC9 9 SER B 3 ALA B 4 HIS B 5 LYS B 72
SITE 2 BC9 9 HOH B 440 HOH B 454 HOH B 481 HOH B 528
SITE 3 BC9 9 HOH B 723
SITE 1 CC1 5 PHE B 116 TRP B 217 HOH B 480 HOH B 560
SITE 2 CC1 5 HOH B 789
SITE 1 CC2 4 THR B 11 HIS B 235 LYS B 236 EDO B 302
SITE 1 CC3 10 SER G 240 LYS G 241 VAL G 242 ASN G 243
SITE 2 CC3 10 GLU G 244 HOH G 408 HOH G 491 HOH G 531
SITE 3 CC3 10 HOH G 537 HOH G 592
SITE 1 CC4 3 THR G 11 SER G 80 CL G 307
SITE 1 CC5 6 TYR G 118 TRP G 128 PHE G 133 PHE G 178
SITE 2 CC5 6 HOH G 459 HOH G 539
SITE 1 CC6 3 HIS G 112 SER G 113 HOH G 602
SITE 1 CC7 4 LYS G 129 ARG G 151 HOH G 464 HOH G 553
SITE 1 CC8 9 SER G 3 ALA G 4 HIS G 5 LYS G 72
SITE 2 CC8 9 HOH G 426 HOH G 438 HOH G 453 HOH G 533
SITE 3 CC8 9 HOH G 631
SITE 1 CC9 4 ILE G 157 HIS G 235 LYS G 236 EDO G 302
SITE 1 DC1 12 SER L 240 LYS L 241 VAL L 242 ASN L 243
SITE 2 DC1 12 GLU L 244 HOH L 415 HOH L 429 HOH L 530
SITE 3 DC1 12 HOH L 617 HOH L 634 HOH L 695 HOH L 734
SITE 1 DC2 5 THR L 11 SER L 80 PHE L 178 CL L 309
SITE 2 DC2 5 HOH L 583
SITE 1 DC3 9 ASP G 44 GLN G 47 ARG G 174 ILE L 43
SITE 2 DC3 9 ASP L 44 PRO L 45 GLN L 47 ARG L 174
SITE 3 DC3 9 HOH L 738
SITE 1 DC4 7 LYS A 120 VAL A 124 PHE A 214 TRP A 217
SITE 2 DC4 7 EDO A 303 GLU L 66 TYR L 93
SITE 1 DC5 6 TYR L 118 TRP L 128 VAL L 146 PHE L 178
SITE 2 DC5 6 HOH L 436 HOH L 458
SITE 1 DC6 5 HIS L 112 SER L 113 HOH L 540 HOH L 566
SITE 2 DC6 5 HOH L 714
SITE 1 DC7 6 ASN L 160 SER L 232 LYS L 241 HOH L 579
SITE 2 DC7 6 HOH L 626 HOH L 734
SITE 1 DC8 4 PHE L 116 LYS L 120 TRP L 217 HOH L 527
SITE 1 DC9 5 THR L 11 ILE L 157 HIS L 235 LYS L 236
SITE 2 DC9 5 EDO L 302
SITE 1 EC1 8 SER M 240 LYS M 241 VAL M 242 ASN M 243
SITE 2 EC1 8 GLU M 244 HOH M 409 HOH M 429 HOH M 516
SITE 1 EC2 4 THR M 11 SER M 80 CL M 305 HOH M 539
SITE 1 EC3 10 ILE M 43 ASP M 44 PRO M 45 GLN M 47
SITE 2 EC3 10 ARG M 174 ILE R 43 ASP R 44 PRO R 45
SITE 3 EC3 10 GLN R 47 ARG R 174
SITE 1 EC4 5 TYR M 118 TRP M 128 PHE M 133 PHE M 178
SITE 2 EC4 5 HOH M 475
SITE 1 EC5 4 THR M 11 HIS M 235 LYS M 236 EDO M 302
SITE 1 EC6 11 SER R 240 LYS R 241 VAL R 242 ASN R 243
SITE 2 EC6 11 GLU R 244 HOH R 410 HOH R 468 HOH R 545
SITE 3 EC6 11 HOH R 560 HOH R 567 HOH R 586
SITE 1 EC7 5 THR R 11 SER R 80 PHE R 178 CL R 308
SITE 2 EC7 5 HOH R 698
SITE 1 EC8 6 TYR R 118 TRP R 128 VAL R 146 PHE R 178
SITE 2 EC8 6 HOH R 464 HOH R 500
SITE 1 EC9 4 HIS R 112 SER R 113 HOH R 546 HOH R 618
SITE 1 FC1 8 LYS G 226 LYS R 175 HOH R 515 HOH R 540
SITE 2 FC1 8 HOH R 554 HOH R 581 HOH R 631 HOH R 634
SITE 1 FC2 4 ASN R 160 SER R 232 LYS R 241 HOH R 607
SITE 1 FC3 4 LYS R 120 TRP R 217 HOH R 523 HOH R 553
SITE 1 FC4 5 THR R 11 ILE R 157 HIS R 235 LYS R 236
SITE 2 FC4 5 EDO R 302
CRYST1 191.962 261.581 91.987 90.00 90.00 90.00 C 2 2 2 48
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 0.005209 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010871 0.00000
TER 2105 VAL A 262
TER 4181 LEU B 259
TER 6266 LEU G 259
TER 8315 SER L 255
TER 10369 ALA M 256
TER 12470 ALA R 263
MASTER 898 0 49 84 51 0 94 614563 6 244 138
END |