HEADER TRANSFERASE 21-NOV-98 1QPO
TITLE QUINOLINATE PHOSPHORIBOSYL TRANSFERASE (QAPRTASE) APO-ENZYME FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: QUINOLINATE ACID PHOSPHORIBOSYL TRANSFERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE, QAPRTASE;
COMPND 5 EC: 2.4.2.19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: NADC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_GENE: NADC
KEYWDS TYPE II PRTASE, DE NOVO NAD BIOSYNTHESIS, PRPP, PHOSPHORIBOSYL
KEYWDS 2 TRANSFERASE, QUINOLINIC ACID, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.SHARMA,C.GRUBMEYER,J.C.SACCHETTINI,TB STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (TBSGC)
REVDAT 6 27-DEC-23 1QPO 1 REMARK
REVDAT 5 13-JUL-11 1QPO 1 VERSN
REVDAT 4 24-FEB-09 1QPO 1 VERSN
REVDAT 3 01-FEB-05 1QPO 1 JRNL AUTHOR KEYWDS REMARK
REVDAT 2 15-DEC-99 1QPO 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 24-NOV-98 1QPO 0
JRNL AUTH V.SHARMA,C.GRUBMEYER,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURE OF QUINOLINIC ACID
JRNL TITL 2 PHOSPHORIBOSYLTRANSFERASE FROM MYCOBACTERIUM TUBERCULOSIS: A
JRNL TITL 3 POTENTIAL TB DRUG TARGET.
JRNL REF STRUCTURE V. 6 1587 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9862811
JRNL DOI 10.1016/S0969-2126(98)00156-7
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 54640
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 284
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.796
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QPO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000000128.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 8.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68930
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 2.820
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.48267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 96.96533
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 ARG C1154 NE - CZ - NH2 ANGL. DEV. = -3.3 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 HIS A 161 -116.98 -102.05
REMARK 500 ALA A 240 71.88 -150.79
REMARK 500 HIS B 661 -109.23 -110.59
REMARK 500 HIS C1161 -114.18 -98.07
REMARK 500 PRO D1586 -70.33 -41.51
REMARK 500 HIS D1661 -120.25 -102.79
REMARK 500 GLU E2104 -69.24 -24.32
REMARK 500 HIS E2161 -106.77 -100.66
REMARK 500 ALA E2240 75.16 -151.29
REMARK 500 PRO F2586 -75.34 -36.03
REMARK 500 HIS F2661 -124.24 -104.65
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 TYR B 525 0.07 SIDE CHAIN
REMARK 500 TYR D1525 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE SULFATE ION OCCUPIES THE 5'-PHOSPHATE BINDING SITE
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 2985
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2986
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2987
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 2988
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2989
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2990
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1596 RELATED DB: TARGETDB
DBREF 1QPO A 2 285 UNP O06594 NADC_MYCTU 2 285
DBREF 1QPO B 502 785 UNP O06594 NADC_MYCTU 2 285
DBREF 1QPO C 1002 1285 UNP O06594 NADC_MYCTU 2 285
DBREF 1QPO D 1502 1785 UNP O06594 NADC_MYCTU 2 285
DBREF 1QPO E 2002 2285 UNP O06594 NADC_MYCTU 2 285
DBREF 1QPO F 2502 2785 UNP O06594 NADC_MYCTU 2 285
SEQRES 1 A 284 GLY LEU SER ASP TRP GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 A 284 ILE ALA ARG GLY LEU ASP GLU ASP LEU ARG TYR GLY PRO
SEQRES 3 A 284 ASP VAL THR THR LEU ALA THR VAL PRO ALA SER ALA THR
SEQRES 4 A 284 THR THR ALA SER LEU VAL THR ARG GLU ALA GLY VAL VAL
SEQRES 5 A 284 ALA GLY LEU ASP VAL ALA LEU LEU THR LEU ASN GLU VAL
SEQRES 6 A 284 LEU GLY THR ASN GLY TYR ARG VAL LEU ASP ARG VAL GLU
SEQRES 7 A 284 ASP GLY ALA ARG VAL PRO PRO GLY GLU ALA LEU MET THR
SEQRES 8 A 284 LEU GLU ALA GLN THR ARG GLY LEU LEU THR ALA GLU ARG
SEQRES 9 A 284 THR MET LEU ASN LEU VAL GLY HIS LEU SER GLY ILE ALA
SEQRES 10 A 284 THR ALA THR ALA ALA TRP VAL ASP ALA VAL ARG GLY THR
SEQRES 11 A 284 LYS ALA LYS ILE ARG ASP THR ARG LYS THR LEU PRO GLY
SEQRES 12 A 284 LEU ARG ALA LEU GLN LYS TYR ALA VAL ARG THR GLY GLY
SEQRES 13 A 284 GLY VAL ASN HIS ARG LEU GLY LEU GLY ASP ALA ALA LEU
SEQRES 14 A 284 ILE LYS ASP ASN HIS VAL ALA ALA ALA GLY SER VAL VAL
SEQRES 15 A 284 ASP ALA LEU ARG ALA VAL ARG ASN ALA ALA PRO ASP LEU
SEQRES 16 A 284 PRO CYS GLU VAL GLU VAL ASP SER LEU GLU GLN LEU ASP
SEQRES 17 A 284 ALA VAL LEU PRO GLU LYS PRO GLU LEU ILE LEU LEU ASP
SEQRES 18 A 284 ASN PHE ALA VAL TRP GLN THR GLN THR ALA VAL GLN ARG
SEQRES 19 A 284 ARG ASP SER ARG ALA PRO THR VAL MET LEU GLU SER SER
SEQRES 20 A 284 GLY GLY LEU SER LEU GLN THR ALA ALA THR TYR ALA GLU
SEQRES 21 A 284 THR GLY VAL ASP TYR LEU ALA VAL GLY ALA LEU THR HIS
SEQRES 22 A 284 SER VAL ARG VAL LEU ASP ILE GLY LEU ASP MET
SEQRES 1 B 284 GLY LEU SER ASP TRP GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 B 284 ILE ALA ARG GLY LEU ASP GLU ASP LEU ARG TYR GLY PRO
SEQRES 3 B 284 ASP VAL THR THR LEU ALA THR VAL PRO ALA SER ALA THR
SEQRES 4 B 284 THR THR ALA SER LEU VAL THR ARG GLU ALA GLY VAL VAL
SEQRES 5 B 284 ALA GLY LEU ASP VAL ALA LEU LEU THR LEU ASN GLU VAL
SEQRES 6 B 284 LEU GLY THR ASN GLY TYR ARG VAL LEU ASP ARG VAL GLU
SEQRES 7 B 284 ASP GLY ALA ARG VAL PRO PRO GLY GLU ALA LEU MET THR
SEQRES 8 B 284 LEU GLU ALA GLN THR ARG GLY LEU LEU THR ALA GLU ARG
SEQRES 9 B 284 THR MET LEU ASN LEU VAL GLY HIS LEU SER GLY ILE ALA
SEQRES 10 B 284 THR ALA THR ALA ALA TRP VAL ASP ALA VAL ARG GLY THR
SEQRES 11 B 284 LYS ALA LYS ILE ARG ASP THR ARG LYS THR LEU PRO GLY
SEQRES 12 B 284 LEU ARG ALA LEU GLN LYS TYR ALA VAL ARG THR GLY GLY
SEQRES 13 B 284 GLY VAL ASN HIS ARG LEU GLY LEU GLY ASP ALA ALA LEU
SEQRES 14 B 284 ILE LYS ASP ASN HIS VAL ALA ALA ALA GLY SER VAL VAL
SEQRES 15 B 284 ASP ALA LEU ARG ALA VAL ARG ASN ALA ALA PRO ASP LEU
SEQRES 16 B 284 PRO CYS GLU VAL GLU VAL ASP SER LEU GLU GLN LEU ASP
SEQRES 17 B 284 ALA VAL LEU PRO GLU LYS PRO GLU LEU ILE LEU LEU ASP
SEQRES 18 B 284 ASN PHE ALA VAL TRP GLN THR GLN THR ALA VAL GLN ARG
SEQRES 19 B 284 ARG ASP SER ARG ALA PRO THR VAL MET LEU GLU SER SER
SEQRES 20 B 284 GLY GLY LEU SER LEU GLN THR ALA ALA THR TYR ALA GLU
SEQRES 21 B 284 THR GLY VAL ASP TYR LEU ALA VAL GLY ALA LEU THR HIS
SEQRES 22 B 284 SER VAL ARG VAL LEU ASP ILE GLY LEU ASP MET
SEQRES 1 C 284 GLY LEU SER ASP TRP GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 C 284 ILE ALA ARG GLY LEU ASP GLU ASP LEU ARG TYR GLY PRO
SEQRES 3 C 284 ASP VAL THR THR LEU ALA THR VAL PRO ALA SER ALA THR
SEQRES 4 C 284 THR THR ALA SER LEU VAL THR ARG GLU ALA GLY VAL VAL
SEQRES 5 C 284 ALA GLY LEU ASP VAL ALA LEU LEU THR LEU ASN GLU VAL
SEQRES 6 C 284 LEU GLY THR ASN GLY TYR ARG VAL LEU ASP ARG VAL GLU
SEQRES 7 C 284 ASP GLY ALA ARG VAL PRO PRO GLY GLU ALA LEU MET THR
SEQRES 8 C 284 LEU GLU ALA GLN THR ARG GLY LEU LEU THR ALA GLU ARG
SEQRES 9 C 284 THR MET LEU ASN LEU VAL GLY HIS LEU SER GLY ILE ALA
SEQRES 10 C 284 THR ALA THR ALA ALA TRP VAL ASP ALA VAL ARG GLY THR
SEQRES 11 C 284 LYS ALA LYS ILE ARG ASP THR ARG LYS THR LEU PRO GLY
SEQRES 12 C 284 LEU ARG ALA LEU GLN LYS TYR ALA VAL ARG THR GLY GLY
SEQRES 13 C 284 GLY VAL ASN HIS ARG LEU GLY LEU GLY ASP ALA ALA LEU
SEQRES 14 C 284 ILE LYS ASP ASN HIS VAL ALA ALA ALA GLY SER VAL VAL
SEQRES 15 C 284 ASP ALA LEU ARG ALA VAL ARG ASN ALA ALA PRO ASP LEU
SEQRES 16 C 284 PRO CYS GLU VAL GLU VAL ASP SER LEU GLU GLN LEU ASP
SEQRES 17 C 284 ALA VAL LEU PRO GLU LYS PRO GLU LEU ILE LEU LEU ASP
SEQRES 18 C 284 ASN PHE ALA VAL TRP GLN THR GLN THR ALA VAL GLN ARG
SEQRES 19 C 284 ARG ASP SER ARG ALA PRO THR VAL MET LEU GLU SER SER
SEQRES 20 C 284 GLY GLY LEU SER LEU GLN THR ALA ALA THR TYR ALA GLU
SEQRES 21 C 284 THR GLY VAL ASP TYR LEU ALA VAL GLY ALA LEU THR HIS
SEQRES 22 C 284 SER VAL ARG VAL LEU ASP ILE GLY LEU ASP MET
SEQRES 1 D 284 GLY LEU SER ASP TRP GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 D 284 ILE ALA ARG GLY LEU ASP GLU ASP LEU ARG TYR GLY PRO
SEQRES 3 D 284 ASP VAL THR THR LEU ALA THR VAL PRO ALA SER ALA THR
SEQRES 4 D 284 THR THR ALA SER LEU VAL THR ARG GLU ALA GLY VAL VAL
SEQRES 5 D 284 ALA GLY LEU ASP VAL ALA LEU LEU THR LEU ASN GLU VAL
SEQRES 6 D 284 LEU GLY THR ASN GLY TYR ARG VAL LEU ASP ARG VAL GLU
SEQRES 7 D 284 ASP GLY ALA ARG VAL PRO PRO GLY GLU ALA LEU MET THR
SEQRES 8 D 284 LEU GLU ALA GLN THR ARG GLY LEU LEU THR ALA GLU ARG
SEQRES 9 D 284 THR MET LEU ASN LEU VAL GLY HIS LEU SER GLY ILE ALA
SEQRES 10 D 284 THR ALA THR ALA ALA TRP VAL ASP ALA VAL ARG GLY THR
SEQRES 11 D 284 LYS ALA LYS ILE ARG ASP THR ARG LYS THR LEU PRO GLY
SEQRES 12 D 284 LEU ARG ALA LEU GLN LYS TYR ALA VAL ARG THR GLY GLY
SEQRES 13 D 284 GLY VAL ASN HIS ARG LEU GLY LEU GLY ASP ALA ALA LEU
SEQRES 14 D 284 ILE LYS ASP ASN HIS VAL ALA ALA ALA GLY SER VAL VAL
SEQRES 15 D 284 ASP ALA LEU ARG ALA VAL ARG ASN ALA ALA PRO ASP LEU
SEQRES 16 D 284 PRO CYS GLU VAL GLU VAL ASP SER LEU GLU GLN LEU ASP
SEQRES 17 D 284 ALA VAL LEU PRO GLU LYS PRO GLU LEU ILE LEU LEU ASP
SEQRES 18 D 284 ASN PHE ALA VAL TRP GLN THR GLN THR ALA VAL GLN ARG
SEQRES 19 D 284 ARG ASP SER ARG ALA PRO THR VAL MET LEU GLU SER SER
SEQRES 20 D 284 GLY GLY LEU SER LEU GLN THR ALA ALA THR TYR ALA GLU
SEQRES 21 D 284 THR GLY VAL ASP TYR LEU ALA VAL GLY ALA LEU THR HIS
SEQRES 22 D 284 SER VAL ARG VAL LEU ASP ILE GLY LEU ASP MET
SEQRES 1 E 284 GLY LEU SER ASP TRP GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 E 284 ILE ALA ARG GLY LEU ASP GLU ASP LEU ARG TYR GLY PRO
SEQRES 3 E 284 ASP VAL THR THR LEU ALA THR VAL PRO ALA SER ALA THR
SEQRES 4 E 284 THR THR ALA SER LEU VAL THR ARG GLU ALA GLY VAL VAL
SEQRES 5 E 284 ALA GLY LEU ASP VAL ALA LEU LEU THR LEU ASN GLU VAL
SEQRES 6 E 284 LEU GLY THR ASN GLY TYR ARG VAL LEU ASP ARG VAL GLU
SEQRES 7 E 284 ASP GLY ALA ARG VAL PRO PRO GLY GLU ALA LEU MET THR
SEQRES 8 E 284 LEU GLU ALA GLN THR ARG GLY LEU LEU THR ALA GLU ARG
SEQRES 9 E 284 THR MET LEU ASN LEU VAL GLY HIS LEU SER GLY ILE ALA
SEQRES 10 E 284 THR ALA THR ALA ALA TRP VAL ASP ALA VAL ARG GLY THR
SEQRES 11 E 284 LYS ALA LYS ILE ARG ASP THR ARG LYS THR LEU PRO GLY
SEQRES 12 E 284 LEU ARG ALA LEU GLN LYS TYR ALA VAL ARG THR GLY GLY
SEQRES 13 E 284 GLY VAL ASN HIS ARG LEU GLY LEU GLY ASP ALA ALA LEU
SEQRES 14 E 284 ILE LYS ASP ASN HIS VAL ALA ALA ALA GLY SER VAL VAL
SEQRES 15 E 284 ASP ALA LEU ARG ALA VAL ARG ASN ALA ALA PRO ASP LEU
SEQRES 16 E 284 PRO CYS GLU VAL GLU VAL ASP SER LEU GLU GLN LEU ASP
SEQRES 17 E 284 ALA VAL LEU PRO GLU LYS PRO GLU LEU ILE LEU LEU ASP
SEQRES 18 E 284 ASN PHE ALA VAL TRP GLN THR GLN THR ALA VAL GLN ARG
SEQRES 19 E 284 ARG ASP SER ARG ALA PRO THR VAL MET LEU GLU SER SER
SEQRES 20 E 284 GLY GLY LEU SER LEU GLN THR ALA ALA THR TYR ALA GLU
SEQRES 21 E 284 THR GLY VAL ASP TYR LEU ALA VAL GLY ALA LEU THR HIS
SEQRES 22 E 284 SER VAL ARG VAL LEU ASP ILE GLY LEU ASP MET
SEQRES 1 F 284 GLY LEU SER ASP TRP GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 F 284 ILE ALA ARG GLY LEU ASP GLU ASP LEU ARG TYR GLY PRO
SEQRES 3 F 284 ASP VAL THR THR LEU ALA THR VAL PRO ALA SER ALA THR
SEQRES 4 F 284 THR THR ALA SER LEU VAL THR ARG GLU ALA GLY VAL VAL
SEQRES 5 F 284 ALA GLY LEU ASP VAL ALA LEU LEU THR LEU ASN GLU VAL
SEQRES 6 F 284 LEU GLY THR ASN GLY TYR ARG VAL LEU ASP ARG VAL GLU
SEQRES 7 F 284 ASP GLY ALA ARG VAL PRO PRO GLY GLU ALA LEU MET THR
SEQRES 8 F 284 LEU GLU ALA GLN THR ARG GLY LEU LEU THR ALA GLU ARG
SEQRES 9 F 284 THR MET LEU ASN LEU VAL GLY HIS LEU SER GLY ILE ALA
SEQRES 10 F 284 THR ALA THR ALA ALA TRP VAL ASP ALA VAL ARG GLY THR
SEQRES 11 F 284 LYS ALA LYS ILE ARG ASP THR ARG LYS THR LEU PRO GLY
SEQRES 12 F 284 LEU ARG ALA LEU GLN LYS TYR ALA VAL ARG THR GLY GLY
SEQRES 13 F 284 GLY VAL ASN HIS ARG LEU GLY LEU GLY ASP ALA ALA LEU
SEQRES 14 F 284 ILE LYS ASP ASN HIS VAL ALA ALA ALA GLY SER VAL VAL
SEQRES 15 F 284 ASP ALA LEU ARG ALA VAL ARG ASN ALA ALA PRO ASP LEU
SEQRES 16 F 284 PRO CYS GLU VAL GLU VAL ASP SER LEU GLU GLN LEU ASP
SEQRES 17 F 284 ALA VAL LEU PRO GLU LYS PRO GLU LEU ILE LEU LEU ASP
SEQRES 18 F 284 ASN PHE ALA VAL TRP GLN THR GLN THR ALA VAL GLN ARG
SEQRES 19 F 284 ARG ASP SER ARG ALA PRO THR VAL MET LEU GLU SER SER
SEQRES 20 F 284 GLY GLY LEU SER LEU GLN THR ALA ALA THR TYR ALA GLU
SEQRES 21 F 284 THR GLY VAL ASP TYR LEU ALA VAL GLY ALA LEU THR HIS
SEQRES 22 F 284 SER VAL ARG VAL LEU ASP ILE GLY LEU ASP MET
HET SO4 A2985 5
HET SO4 B2986 5
HET SO4 C2987 5
HET SO4 D2990 5
HET SO4 E2989 5
HET SO4 F2988 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 6(O4 S 2-)
FORMUL 13 HOH *284(H2 O)
HELIX 1 1 ASP A 5 LEU A 23 1 19
HELIX 2 2 VAL A 29 THR A 34 1 6
HELIX 3 3 LEU A 56 LEU A 67 1 12
HELIX 4 4 THR A 97 ALA A 127 1 31
HELIX 5 5 ARG A 146 THR A 155 1 10
HELIX 6 6 ASP A 173 ALA A 179 1 7
HELIX 7 7 VAL A 182 ALA A 192 1 11
HELIX 8 8 LEU A 205 GLU A 214 1 10
HELIX 9 9 VAL A 226 ARG A 239 1 14
HELIX 10 10 ALA A 256 THR A 262 1 7
HELIX 11 11 GLY A 270 LEU A 272 5 3
HELIX 12 12 ASP B 505 LEU B 523 1 19
HELIX 13 13 VAL B 529 THR B 534 1 6
HELIX 14 14 LEU B 556 LEU B 567 1 12
HELIX 15 15 THR B 597 ALA B 627 1 31
HELIX 16 16 ARG B 646 THR B 655 1 10
HELIX 17 17 ASP B 673 ALA B 679 1 7
HELIX 18 18 VAL B 682 ALA B 692 1 11
HELIX 19 19 LEU B 705 GLU B 714 1 10
HELIX 20 20 VAL B 726 ARG B 739 1 14
HELIX 21 21 ALA B 756 THR B 762 1 7
HELIX 22 22 GLY B 770 LEU B 772 5 3
HELIX 23 23 ASP C 1005 LEU C 1023 1 19
HELIX 24 24 VAL C 1029 THR C 1034 1 6
HELIX 25 25 LEU C 1056 LEU C 1067 1 12
HELIX 26 26 THR C 1097 ALA C 1127 1 31
HELIX 27 27 ARG C 1146 THR C 1155 1 10
HELIX 28 28 ASP C 1173 ALA C 1179 1 7
HELIX 29 29 VAL C 1182 ALA C 1192 1 11
HELIX 30 30 LEU C 1205 GLU C 1214 1 10
HELIX 31 31 VAL C 1226 ARG C 1239 1 14
HELIX 32 32 ALA C 1256 THR C 1262 1 7
HELIX 33 33 GLY C 1270 LEU C 1272 5 3
HELIX 34 34 ASP D 1505 LEU D 1523 1 19
HELIX 35 35 VAL D 1529 THR D 1534 1 6
HELIX 36 36 LEU D 1556 LEU D 1567 1 12
HELIX 37 37 THR D 1597 ALA D 1627 1 31
HELIX 38 38 ARG D 1646 THR D 1655 1 10
HELIX 39 39 ASP D 1673 ALA D 1679 1 7
HELIX 40 40 VAL D 1682 ALA D 1692 1 11
HELIX 41 41 LEU D 1705 GLU D 1714 1 10
HELIX 42 42 VAL D 1726 ARG D 1739 1 14
HELIX 43 43 ALA D 1756 THR D 1762 1 7
HELIX 44 44 GLY D 1770 LEU D 1772 5 3
HELIX 45 45 ASP E 2005 LEU E 2023 1 19
HELIX 46 46 VAL E 2029 THR E 2034 1 6
HELIX 47 47 LEU E 2056 LEU E 2067 1 12
HELIX 48 48 THR E 2097 ALA E 2127 1 31
HELIX 49 49 ARG E 2146 THR E 2155 1 10
HELIX 50 50 ASP E 2173 ALA E 2179 1 7
HELIX 51 51 VAL E 2182 ALA E 2192 1 11
HELIX 52 52 LEU E 2205 GLU E 2214 1 10
HELIX 53 53 VAL E 2226 ARG E 2239 1 14
HELIX 54 54 ALA E 2256 THR E 2262 1 7
HELIX 55 55 GLY E 2270 LEU E 2272 5 3
HELIX 56 56 ASP F 2505 LEU F 2523 1 19
HELIX 57 57 VAL F 2529 THR F 2534 1 6
HELIX 58 58 LEU F 2556 LEU F 2567 1 12
HELIX 59 59 THR F 2597 ALA F 2627 1 31
HELIX 60 60 ARG F 2646 THR F 2655 1 10
HELIX 61 61 ASP F 2673 ALA F 2679 1 7
HELIX 62 62 VAL F 2682 ALA F 2692 1 11
HELIX 63 63 LEU F 2705 LEU F 2712 1 8
HELIX 64 64 VAL F 2726 ARG F 2739 1 14
HELIX 65 65 ALA F 2756 THR F 2762 1 7
HELIX 66 66 GLY F 2770 LEU F 2772 5 3
SHEET 1 A 4 ILE A 281 ASP A 284 0
SHEET 2 A 4 THR A 40 THR A 47 -1 N VAL A 46 O GLY A 282
SHEET 3 A 4 ALA A 89 GLN A 96 -1 N ALA A 95 O THR A 41
SHEET 4 A 4 TYR A 72 ARG A 77 -1 N ASP A 76 O THR A 92
SHEET 1 B 6 LYS A 134 ARG A 136 0
SHEET 2 B 6 TYR A 266 ALA A 268 1 N LEU A 267 O LYS A 134
SHEET 3 B 6 MET A 244 SER A 248 1 N SER A 247 O TYR A 266
SHEET 4 B 6 LEU A 218 ASP A 222 1 N ILE A 219 O MET A 244
SHEET 5 B 6 CYS A 198 VAL A 202 1 N VAL A 200 O LEU A 218
SHEET 6 B 6 ALA A 169 ILE A 171 1 N ALA A 169 O GLU A 199
SHEET 1 C 4 ILE B 781 ASP B 784 0
SHEET 2 C 4 THR B 540 THR B 547 -1 N VAL B 546 O GLY B 782
SHEET 3 C 4 ALA B 589 GLN B 596 -1 N ALA B 595 O THR B 541
SHEET 4 C 4 TYR B 572 ARG B 577 -1 N ASP B 576 O THR B 592
SHEET 1 D 6 LYS B 634 ARG B 636 0
SHEET 2 D 6 TYR B 766 ALA B 768 1 N LEU B 767 O LYS B 634
SHEET 3 D 6 MET B 744 SER B 748 1 N SER B 747 O TYR B 766
SHEET 4 D 6 LEU B 718 ASP B 722 1 N ILE B 719 O MET B 744
SHEET 5 D 6 CYS B 698 VAL B 702 1 N VAL B 700 O LEU B 718
SHEET 6 D 6 ALA B 669 ILE B 671 1 N ALA B 669 O GLU B 699
SHEET 1 E 4 ILE C1281 ASP C1284 0
SHEET 2 E 4 THR C1040 THR C1047 -1 N VAL C1046 O GLY C1282
SHEET 3 E 4 ALA C1089 GLN C1096 -1 N ALA C1095 O THR C1041
SHEET 4 E 4 TYR C1072 ARG C1077 -1 N ASP C1076 O THR C1092
SHEET 1 F 6 LYS C1134 ARG C1136 0
SHEET 2 F 6 TYR C1266 ALA C1268 1 N LEU C1267 O LYS C1134
SHEET 3 F 6 MET C1244 SER C1248 1 N SER C1247 O TYR C1266
SHEET 4 F 6 LEU C1218 ASP C1222 1 N ILE C1219 O MET C1244
SHEET 5 F 6 CYS C1198 VAL C1202 1 N VAL C1200 O LEU C1218
SHEET 6 F 6 ALA C1169 ILE C1171 1 N ALA C1169 O GLU C1199
SHEET 1 G 4 ILE D1781 ASP D1784 0
SHEET 2 G 4 THR D1540 THR D1547 -1 N VAL D1546 O GLY D1782
SHEET 3 G 4 ALA D1589 GLN D1596 -1 N ALA D1595 O THR D1541
SHEET 4 G 4 TYR D1572 ARG D1577 -1 N ASP D1576 O THR D1592
SHEET 1 H 2 LYS D1634 ARG D1636 0
SHEET 2 H 2 TYR D1766 ALA D1768 1 N LEU D1767 O LYS D1634
SHEET 1 I 4 ALA D1669 ILE D1671 0
SHEET 2 I 4 CYS D1698 VAL D1702 1 N GLU D1699 O ALA D1669
SHEET 3 I 4 LEU D1718 ASP D1722 1 N LEU D1718 O VAL D1700
SHEET 4 I 4 MET D1744 SER D1748 1 N MET D1744 O ILE D1719
SHEET 1 J 4 ILE E2281 ASP E2284 0
SHEET 2 J 4 THR E2040 THR E2047 -1 N VAL E2046 O GLY E2282
SHEET 3 J 4 ALA E2089 GLN E2096 -1 N ALA E2095 O THR E2041
SHEET 4 J 4 TYR E2072 ARG E2077 -1 N ASP E2076 O THR E2092
SHEET 1 K 6 LYS E2134 ARG E2136 0
SHEET 2 K 6 TYR E2266 ALA E2268 1 N LEU E2267 O LYS E2134
SHEET 3 K 6 MET E2244 SER E2248 1 N SER E2247 O TYR E2266
SHEET 4 K 6 LEU E2218 ASP E2222 1 N ILE E2219 O MET E2244
SHEET 5 K 6 CYS E2198 VAL E2202 1 N VAL E2200 O LEU E2218
SHEET 6 K 6 ALA E2169 ILE E2171 1 N ALA E2169 O GLU E2199
SHEET 1 L 4 ILE F2781 ASP F2784 0
SHEET 2 L 4 THR F2540 THR F2547 -1 N VAL F2546 O GLY F2782
SHEET 3 L 4 ALA F2589 GLN F2596 -1 N ALA F2595 O THR F2541
SHEET 4 L 4 TYR F2572 ARG F2577 -1 N ASP F2576 O THR F2592
SHEET 1 M 6 LYS F2634 ARG F2636 0
SHEET 2 M 6 TYR F2766 ALA F2768 1 N LEU F2767 O LYS F2634
SHEET 3 M 6 MET F2744 SER F2748 1 N SER F2747 O TYR F2766
SHEET 4 M 6 LEU F2718 ASP F2722 1 N ILE F2719 O MET F2744
SHEET 5 M 6 CYS F2698 VAL F2702 1 N VAL F2700 O LEU F2718
SHEET 6 M 6 ALA F2669 ILE F2671 1 N ALA F2669 O GLU F2699
SITE 1 AC1 6 LYS A 140 GLY A 249 GLY A 270 ALA A 271
SITE 2 AC1 6 HIS A 274 HOH A3236
SITE 1 AC2 5 LYS B 640 GLY B 749 GLY B 770 HIS B 774
SITE 2 AC2 5 HOH B3153
SITE 1 AC3 6 LYS C1140 GLY C1249 GLY C1270 ALA C1271
SITE 2 AC3 6 HIS C1274 HOH C3026
SITE 1 AC4 6 LYS F2640 GLY F2749 GLY F2770 HIS F2774
SITE 2 AC4 6 HOH F3033 HOH F3034
SITE 1 AC5 5 LYS E2140 GLY E2249 GLY E2270 HIS E2274
SITE 2 AC5 5 HOH E3060
SITE 1 AC6 5 LYS D1640 GLY D1749 GLY D1770 HIS D1774
SITE 2 AC6 5 HOH D3184
CRYST1 100.584 100.584 145.448 90.00 90.00 120.00 P 31 18
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 0.009942 0.005740 0.000000 0.00000
SCALE2 0.000000 0.011480 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006875 0.00000
MTRIX1 1 -0.268881 0.962759 0.028253 -35.33130 1
MTRIX2 1 0.962679 0.267687 0.039910 26.18780 1
MTRIX3 1 0.030860 0.037930 -0.998804 23.97180 1
MTRIX1 2 -0.499252 -0.863757 -0.068348 71.21530 1
MTRIX2 2 0.866331 -0.498966 -0.022418 71.22330 1
MTRIX3 2 -0.014739 -0.070404 0.997410 3.63770 1
MTRIX1 3 0.971049 -0.237395 0.026600 13.03780 1
MTRIX2 3 -0.235939 -0.970547 -0.048699 114.35990 1
MTRIX3 3 0.037378 0.041013 -0.998459 23.96080 1
MTRIX1 4 -0.491247 0.871016 0.002660 -26.84260 1
MTRIX2 4 -0.869985 -0.490512 -0.050244 96.80360 1
MTRIX3 4 -0.042458 -0.026996 0.998733 1.80890 1
MTRIX1 5 -0.694767 -0.719164 -0.010111 65.11820 1
MTRIX2 5 -0.719165 0.694435 0.023711 27.49500 1
MTRIX3 5 -0.010031 0.023746 -0.999668 26.04130 1
(ATOM LINES ARE NOT SHOWN.)
END
