HEADER SUGAR BINDING PROTEIN 20-MAY-15 4ZXK
TITLE CARBOHYDRATE BINDING DOMAIN FROM STREPTOCOCCUS PNEUMONIAE NANA
TITLE 2 SIALIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 121-305;
COMPND 5 SYNONYM: NEURAMINIDASE A;
COMPND 6 EC: 3.2.1.18;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 GENE: NANA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SUGAR BINDING PROTEIN, CARBOHYDRATE-BINDING MODULE, SIALIC ACID
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.YANG,H.CONNARIS,J.A.POTTER,G.L.TAYLOR
REVDAT 2 10-JAN-24 4ZXK 1 REMARK
REVDAT 1 27-MAY-15 4ZXK 0
JRNL AUTH L.YANG,H.CONNARIS,J.A.POTTER,G.L.TAYLOR
JRNL TITL CARBOHYDRATE BINDING DOMAIN FROM STREPTOCOCCUS PNEUMONIAE
JRNL TITL 2 NANA SIALIDASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 27743
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1481
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1673
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 318
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : 0.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.53000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.148
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.985
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3086 ; 0.021 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4185 ; 1.988 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 388 ; 7.433 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;41.268 ;24.558
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 551 ;12.806 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;13.724 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 464 ; 0.164 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2360 ; 0.012 ; 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): 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 118 A 305
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9830 12.4110 30.0480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0244 T22: 0.0392
REMARK 3 T33: 0.0063 T12: -0.0125
REMARK 3 T13: 0.0032 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.3958 L22: 1.4483
REMARK 3 L33: 1.5907 L12: -0.3800
REMARK 3 L13: 0.4447 L23: 0.1821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0319 S12: -0.0413 S13: 0.0431
REMARK 3 S21: 0.0179 S22: 0.0070 S23: -0.0759
REMARK 3 S31: 0.0279 S32: 0.0599 S33: -0.0389
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 118 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1670 13.1480 -3.3550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0231 T22: 0.0298
REMARK 3 T33: 0.0110 T12: -0.0057
REMARK 3 T13: -0.0007 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.0942 L22: 1.3485
REMARK 3 L33: 1.2693 L12: -0.2003
REMARK 3 L13: 0.3129 L23: 0.0913
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.0282 S13: -0.0101
REMARK 3 S21: 0.0038 S22: 0.0154 S23: -0.1119
REMARK 3 S31: 0.0384 S32: 0.0700 S33: -0.0275
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4ZXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210025.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29236
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 49.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.06900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2SLI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DL-MALIC ACID, MES, TRIS BASE, PEG
REMARK 280 1500 VALINE, PH 9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 33.49200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A 156 CG - SD - CE ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG A 294 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LYS A 303 CD - CE - NZ ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG B 136 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASN A 190 -6.04 70.35
REMARK 500 PHE A 257 -149.27 -152.85
REMARK 500 ALA A 275 -136.77 52.25
REMARK 500 ASN B 130 -169.18 -160.94
REMARK 500 LEU B 170 -60.48 -93.52
REMARK 500 ASN B 190 -3.74 66.74
REMARK 500 PHE B 257 -145.51 -153.97
REMARK 500 ALA B 275 -133.02 55.29
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4ZXK A 121 305 UNP P62575 NANA_STREE 121 305
DBREF 4ZXK B 121 305 UNP P62575 NANA_STREE 121 305
SEQADV 4ZXK GLY A 118 UNP P62575 EXPRESSION TAG
SEQADV 4ZXK ALA A 119 UNP P62575 EXPRESSION TAG
SEQADV 4ZXK MET A 120 UNP P62575 EXPRESSION TAG
SEQADV 4ZXK GLY B 118 UNP P62575 EXPRESSION TAG
SEQADV 4ZXK ALA B 119 UNP P62575 EXPRESSION TAG
SEQADV 4ZXK MET B 120 UNP P62575 EXPRESSION TAG
SEQRES 1 A 188 GLY ALA MET VAL ILE GLU LYS GLU ASP VAL GLU THR ASN
SEQRES 2 A 188 ALA SER ASN GLY GLN ARG VAL ASP LEU SER SER GLU LEU
SEQRES 3 A 188 ASP LYS LEU LYS LYS LEU GLU ASN ALA THR VAL HIS MET
SEQRES 4 A 188 GLU PHE LYS PRO ASP ALA LYS ALA PRO ALA PHE TYR ASN
SEQRES 5 A 188 LEU PHE SER VAL SER SER ALA THR LYS LYS ASP GLU TYR
SEQRES 6 A 188 PHE THR MET ALA VAL TYR ASN ASN THR ALA THR LEU GLU
SEQRES 7 A 188 GLY ARG GLY SER ASP GLY LYS GLN PHE TYR ASN ASN TYR
SEQRES 8 A 188 ASN ASP ALA PRO LEU LYS VAL LYS PRO GLY GLN TRP ASN
SEQRES 9 A 188 SER VAL THR PHE THR VAL GLU LYS PRO THR ALA GLU LEU
SEQRES 10 A 188 PRO LYS GLY ARG VAL ARG LEU TYR VAL ASN GLY VAL LEU
SEQRES 11 A 188 SER ARG THR SER LEU ARG SER GLY ASN PHE ILE LYS ASP
SEQRES 12 A 188 MET PRO ASP VAL THR HIS VAL GLN ILE GLY ALA THR LYS
SEQRES 13 A 188 ARG ALA ASN ASN THR VAL TRP GLY SER ASN LEU GLN ILE
SEQRES 14 A 188 ARG ASN LEU THR VAL TYR ASN ARG ALA LEU THR PRO GLU
SEQRES 15 A 188 GLU VAL GLN LYS ARG SER
SEQRES 1 B 188 GLY ALA MET VAL ILE GLU LYS GLU ASP VAL GLU THR ASN
SEQRES 2 B 188 ALA SER ASN GLY GLN ARG VAL ASP LEU SER SER GLU LEU
SEQRES 3 B 188 ASP LYS LEU LYS LYS LEU GLU ASN ALA THR VAL HIS MET
SEQRES 4 B 188 GLU PHE LYS PRO ASP ALA LYS ALA PRO ALA PHE TYR ASN
SEQRES 5 B 188 LEU PHE SER VAL SER SER ALA THR LYS LYS ASP GLU TYR
SEQRES 6 B 188 PHE THR MET ALA VAL TYR ASN ASN THR ALA THR LEU GLU
SEQRES 7 B 188 GLY ARG GLY SER ASP GLY LYS GLN PHE TYR ASN ASN TYR
SEQRES 8 B 188 ASN ASP ALA PRO LEU LYS VAL LYS PRO GLY GLN TRP ASN
SEQRES 9 B 188 SER VAL THR PHE THR VAL GLU LYS PRO THR ALA GLU LEU
SEQRES 10 B 188 PRO LYS GLY ARG VAL ARG LEU TYR VAL ASN GLY VAL LEU
SEQRES 11 B 188 SER ARG THR SER LEU ARG SER GLY ASN PHE ILE LYS ASP
SEQRES 12 B 188 MET PRO ASP VAL THR HIS VAL GLN ILE GLY ALA THR LYS
SEQRES 13 B 188 ARG ALA ASN ASN THR VAL TRP GLY SER ASN LEU GLN ILE
SEQRES 14 B 188 ARG ASN LEU THR VAL TYR ASN ARG ALA LEU THR PRO GLU
SEQRES 15 B 188 GLU VAL GLN LYS ARG SER
FORMUL 3 HOH *318(H2 O)
HELIX 1 AA1 ASN A 130 GLY A 134 5 5
HELIX 2 AA2 GLU A 142 LYS A 148 1 7
HELIX 3 AA3 PHE A 257 MET A 261 5 5
HELIX 4 AA4 THR A 297 SER A 305 1 9
HELIX 5 AA5 ASN B 130 GLY B 134 5 5
HELIX 6 AA6 GLU B 142 LYS B 147 1 6
HELIX 7 AA7 PHE B 257 MET B 261 5 5
HELIX 8 AA8 THR B 297 SER B 305 1 9
SHEET 1 AA1 6 MET A 120 THR A 129 0
SHEET 2 AA1 6 LEU A 284 TYR A 292 -1 O VAL A 291 N VAL A 121
SHEET 3 AA1 6 ALA A 152 PRO A 160 -1 N HIS A 155 O THR A 290
SHEET 4 AA1 6 ASN A 221 GLU A 228 -1 O PHE A 225 N VAL A 154
SHEET 5 AA1 6 ARG A 238 VAL A 243 -1 O TYR A 242 N THR A 224
SHEET 6 AA1 6 VAL A 246 SER A 251 -1 O SER A 248 N LEU A 241
SHEET 1 AA2 5 ARG A 136 ASP A 138 0
SHEET 2 AA2 5 HIS A 266 GLY A 270 -1 O ILE A 269 N VAL A 137
SHEET 3 AA2 5 PHE A 167 SER A 174 -1 N SER A 174 O HIS A 266
SHEET 4 AA2 5 TYR A 182 TYR A 188 -1 O MET A 185 N LEU A 170
SHEET 5 AA2 5 THR A 191 ARG A 197 -1 O THR A 193 N ALA A 186
SHEET 1 AA3 2 THR A 272 ARG A 274 0
SHEET 2 AA3 2 ASN A 277 VAL A 279 -1 O VAL A 279 N THR A 272
SHEET 1 AA4 6 MET B 120 THR B 129 0
SHEET 2 AA4 6 LEU B 284 TYR B 292 -1 O ILE B 286 N VAL B 127
SHEET 3 AA4 6 ALA B 152 PRO B 160 -1 N HIS B 155 O THR B 290
SHEET 4 AA4 6 ASN B 221 GLU B 228 -1 O PHE B 225 N VAL B 154
SHEET 5 AA4 6 ARG B 238 VAL B 243 -1 O TYR B 242 N THR B 224
SHEET 6 AA4 6 VAL B 246 SER B 251 -1 O SER B 251 N VAL B 239
SHEET 1 AA5 5 ARG B 136 ASP B 138 0
SHEET 2 AA5 5 HIS B 266 GLY B 270 -1 O ILE B 269 N VAL B 137
SHEET 3 AA5 5 PHE B 167 SER B 174 -1 N SER B 172 O GLN B 268
SHEET 4 AA5 5 TYR B 182 TYR B 188 -1 O MET B 185 N LEU B 170
SHEET 5 AA5 5 THR B 191 ARG B 197 -1 O THR B 193 N ALA B 186
SHEET 1 AA6 2 THR B 272 ARG B 274 0
SHEET 2 AA6 2 ASN B 277 VAL B 279 -1 O VAL B 279 N THR B 272
CRYST1 39.234 66.984 66.792 90.00 92.43 90.00 P 1 21 1 4
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 0.025488 0.000000 0.001083 0.00000
SCALE2 0.000000 0.014929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014985 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
