HEADER HYDROLASE 22-APR-02 1IW8
TITLE CRYSTAL STRUCTURE OF A MUTANT OF ACID PHOSPHATASE FROM ESCHERICHIA
TITLE 2 BLATTAE (G74D/I153T)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACID PHOSPHATASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 1-231;
COMPND 5 EC: 3.1.3.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA BLATTAE;
SOURCE 3 ORGANISM_TAXID: 563;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PUC118
KEYWDS ALL ALPHA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ISHIKAWA,Y.MIHARA,N.SHIMBA,N.OHTSU,H.KAWASAKI,E.SUZUKI,Y.ASANO
REVDAT 5 25-OCT-23 1IW8 1 REMARK
REVDAT 4 10-NOV-21 1IW8 1 REMARK SEQADV
REVDAT 3 04-OCT-17 1IW8 1 REMARK
REVDAT 2 24-FEB-09 1IW8 1 VERSN
REVDAT 1 11-SEP-02 1IW8 0
JRNL AUTH K.ISHIKAWA,Y.MIHARA,N.SHIMBA,N.OHTSU,H.KAWASAKI,E.SUZUKI,
JRNL AUTH 2 Y.ASANO
JRNL TITL ENHANCEMENT OF NUCLEOSIDE PHOSPHORYLATION ACTIVITY IN AN
JRNL TITL 2 ACID PHOSPHATASE
JRNL REF PROTEIN ENG. V. 15 539 2002
JRNL REFN ISSN 0269-2139
JRNL PMID 12200535
JRNL DOI 10.1093/PROTEIN/15.7.539
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.ISHIKAWA,Y.MIHARA,K.GONDOH,E.SUZUKI,Y.ASANO
REMARK 1 TITL X-RAY STRUCTURES OF A NOVEL ACID PHOSPHATASE FROM
REMARK 1 TITL 2 ESCHERICHIA BLATTAE AND ITS COMPLEX WITH THE
REMARK 1 TITL 3 TRANSITION-STATE ANALOG MOLYBDATE
REMARK 1 REF EMBO J. V. 19 2412 2000
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/19.11.2412
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,MOLECULAR
REMARK 3 : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 45889
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2298
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 45889
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 335
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9897
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 314
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.30
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.48
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000005332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-97
REMARK 200 TEMPERATURE (KELVIN) : 288
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200 DATA SCALING SOFTWARE : WEIS, SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45889
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1D2T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, PH 8.4, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
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 68.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -184.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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 LEU A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 VAL A 4
REMARK 465 ALA A 5
REMARK 465 THR A 6
REMARK 465 THR A 134
REMARK 465 THR A 135
REMARK 465 GLU A 136
REMARK 465 GLN A 137
REMARK 465 ASP A 138
REMARK 465 GLN A 229
REMARK 465 LYS A 230
REMARK 465 LYS A 231
REMARK 465 LEU B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 VAL B 4
REMARK 465 ALA B 5
REMARK 465 THR B 135
REMARK 465 GLU B 136
REMARK 465 GLN B 137
REMARK 465 ASP B 138
REMARK 465 LYS B 139
REMARK 465 LEU B 140
REMARK 465 LYS B 231
REMARK 465 LEU C 1
REMARK 465 ALA C 2
REMARK 465 LEU C 3
REMARK 465 VAL C 4
REMARK 465 ALA C 5
REMARK 465 THR C 135
REMARK 465 GLU C 136
REMARK 465 GLN C 137
REMARK 465 ASP C 138
REMARK 465 LYS C 139
REMARK 465 LEU C 140
REMARK 465 HIS C 228
REMARK 465 GLN C 229
REMARK 465 LYS C 230
REMARK 465 LYS C 231
REMARK 465 LEU D 1
REMARK 465 ALA D 2
REMARK 465 LEU D 3
REMARK 465 VAL D 4
REMARK 465 ALA D 5
REMARK 465 THR D 6
REMARK 465 THR D 134
REMARK 465 THR D 135
REMARK 465 GLU D 136
REMARK 465 GLN D 137
REMARK 465 ASP D 138
REMARK 465 LYS D 139
REMARK 465 LEU D 140
REMARK 465 GLN D 229
REMARK 465 LYS D 230
REMARK 465 LYS D 231
REMARK 465 LEU E 1
REMARK 465 ALA E 2
REMARK 465 LEU E 3
REMARK 465 VAL E 4
REMARK 465 ALA E 5
REMARK 465 THR E 6
REMARK 465 THR E 134
REMARK 465 THR E 135
REMARK 465 GLU E 136
REMARK 465 GLN E 137
REMARK 465 ASP E 138
REMARK 465 LYS E 139
REMARK 465 LEU E 140
REMARK 465 HIS E 228
REMARK 465 GLN E 229
REMARK 465 LYS E 230
REMARK 465 LYS E 231
REMARK 465 LEU F 1
REMARK 465 ALA F 2
REMARK 465 LEU F 3
REMARK 465 VAL F 4
REMARK 465 ALA F 5
REMARK 465 THR F 135
REMARK 465 GLU F 136
REMARK 465 GLN F 137
REMARK 465 ASP F 138
REMARK 465 LYS F 139
REMARK 465 LEU F 140
REMARK 465 GLN F 229
REMARK 465 LYS F 230
REMARK 465 LYS F 231
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 53 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 53 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 53 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 56 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 56 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 168 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 168 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 183 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 56 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 112 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 112 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 168 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 175 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG C 175 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG C 183 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG D 56 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG D 56 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 60 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG D 60 NE - CZ - NH2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG E 53 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG E 53 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG E 175 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG E 175 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG F 53 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG F 53 NE - CZ - NH2 ANGL. DEV. = 3.2 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 ASP A 9 -165.21 -170.64
REMARK 500 ALA A 92 68.38 -165.37
REMARK 500 THR A 131 -167.60 -107.65
REMARK 500 ASN A 143 -165.23 -128.21
REMARK 500 ASP B 9 -166.14 -169.55
REMARK 500 ALA B 92 67.05 -159.85
REMARK 500 ASN B 143 -164.22 -129.73
REMARK 500 ASP C 9 -166.14 -171.13
REMARK 500 ALA C 92 67.66 -160.99
REMARK 500 MET C 119 48.14 39.52
REMARK 500 ASN C 133 55.42 -119.14
REMARK 500 ASN C 143 -163.73 -127.50
REMARK 500 ASN D 8 153.49 -47.87
REMARK 500 ASP D 9 -166.96 -169.01
REMARK 500 ALA D 92 66.35 -164.65
REMARK 500 THR D 131 -168.43 -104.36
REMARK 500 ASN D 143 -164.23 -129.03
REMARK 500 ASP E 9 -167.28 -170.06
REMARK 500 ALA E 92 68.33 -161.94
REMARK 500 ASN E 143 -162.11 -126.63
REMARK 500 ASP F 9 -165.29 -169.34
REMARK 500 ALA F 92 68.00 -163.22
REMARK 500 ASN F 133 79.95 -118.18
REMARK 500 ASN F 143 -163.67 -129.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D2T RELATED DB: PDB
REMARK 900 1D2T CONTAINS THE WILD-TYPE OF THE SAME PROTEIN.
REMARK 900 RELATED ID: 1EOI RELATED DB: PDB
REMARK 900 1EOI CONTAINS THE WILD-TYPE OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 MOLYBDATE.
DBREF 1IW8 A 1 231 UNP Q9S1A6 Q9S1A6_ESCBL 19 249
DBREF 1IW8 B 1 231 UNP Q9S1A6 Q9S1A6_ESCBL 19 249
DBREF 1IW8 C 1 231 UNP Q9S1A6 Q9S1A6_ESCBL 19 249
DBREF 1IW8 D 1 231 UNP Q9S1A6 Q9S1A6_ESCBL 19 249
DBREF 1IW8 E 1 231 UNP Q9S1A6 Q9S1A6_ESCBL 19 249
DBREF 1IW8 F 1 231 UNP Q9S1A6 Q9S1A6_ESCBL 19 249
SEQADV 1IW8 ASP A 74 UNP Q9S1A6 GLY 92 ENGINEERED MUTATION
SEQADV 1IW8 THR A 153 UNP Q9S1A6 ILE 171 ENGINEERED MUTATION
SEQADV 1IW8 ASP B 74 UNP Q9S1A6 GLY 92 ENGINEERED MUTATION
SEQADV 1IW8 THR B 153 UNP Q9S1A6 ILE 171 ENGINEERED MUTATION
SEQADV 1IW8 ASP C 74 UNP Q9S1A6 GLY 92 ENGINEERED MUTATION
SEQADV 1IW8 THR C 153 UNP Q9S1A6 ILE 171 ENGINEERED MUTATION
SEQADV 1IW8 ASP D 74 UNP Q9S1A6 GLY 92 ENGINEERED MUTATION
SEQADV 1IW8 THR D 153 UNP Q9S1A6 ILE 171 ENGINEERED MUTATION
SEQADV 1IW8 ASP E 74 UNP Q9S1A6 GLY 92 ENGINEERED MUTATION
SEQADV 1IW8 THR E 153 UNP Q9S1A6 ILE 171 ENGINEERED MUTATION
SEQADV 1IW8 ASP F 74 UNP Q9S1A6 GLY 92 ENGINEERED MUTATION
SEQADV 1IW8 THR F 153 UNP Q9S1A6 ILE 171 ENGINEERED MUTATION
SEQRES 1 A 231 LEU ALA LEU VAL ALA THR GLY ASN ASP THR THR THR LYS
SEQRES 2 A 231 PRO ASP LEU TYR TYR LEU LYS ASN SER GLU ALA ILE ASN
SEQRES 3 A 231 SER LEU ALA LEU LEU PRO PRO PRO PRO ALA VAL GLY SER
SEQRES 4 A 231 ILE ALA PHE LEU ASN ASP GLN ALA MET TYR GLU GLN GLY
SEQRES 5 A 231 ARG LEU LEU ARG ASN THR GLU ARG GLY LYS LEU ALA ALA
SEQRES 6 A 231 GLU ASP ALA ASN LEU SER SER GLY ASP VAL ALA ASN ALA
SEQRES 7 A 231 PHE SER GLY ALA PHE GLY SER PRO ILE THR GLU LYS ASP
SEQRES 8 A 231 ALA PRO ALA LEU HIS LYS LEU LEU THR ASN MET ILE GLU
SEQRES 9 A 231 ASP ALA GLY ASP LEU ALA THR ARG SER ALA LYS ASP HIS
SEQRES 10 A 231 TYR MET ARG ILE ARG PRO PHE ALA PHE TYR GLY VAL SER
SEQRES 11 A 231 THR CYS ASN THR THR GLU GLN ASP LYS LEU SER LYS ASN
SEQRES 12 A 231 GLY SER TYR PRO SER GLY HIS THR SER THR GLY TRP ALA
SEQRES 13 A 231 THR ALA LEU VAL LEU ALA GLU ILE ASN PRO GLN ARG GLN
SEQRES 14 A 231 ASN GLU ILE LEU LYS ARG GLY TYR GLU LEU GLY GLN SER
SEQRES 15 A 231 ARG VAL ILE CYS GLY TYR HIS TRP GLN SER ASP VAL ASP
SEQRES 16 A 231 ALA ALA ARG VAL VAL GLY SER ALA VAL VAL ALA THR LEU
SEQRES 17 A 231 HIS THR ASN PRO ALA PHE GLN GLN GLN LEU GLN LYS ALA
SEQRES 18 A 231 LYS ALA GLU PHE ALA GLN HIS GLN LYS LYS
SEQRES 1 B 231 LEU ALA LEU VAL ALA THR GLY ASN ASP THR THR THR LYS
SEQRES 2 B 231 PRO ASP LEU TYR TYR LEU LYS ASN SER GLU ALA ILE ASN
SEQRES 3 B 231 SER LEU ALA LEU LEU PRO PRO PRO PRO ALA VAL GLY SER
SEQRES 4 B 231 ILE ALA PHE LEU ASN ASP GLN ALA MET TYR GLU GLN GLY
SEQRES 5 B 231 ARG LEU LEU ARG ASN THR GLU ARG GLY LYS LEU ALA ALA
SEQRES 6 B 231 GLU ASP ALA ASN LEU SER SER GLY ASP VAL ALA ASN ALA
SEQRES 7 B 231 PHE SER GLY ALA PHE GLY SER PRO ILE THR GLU LYS ASP
SEQRES 8 B 231 ALA PRO ALA LEU HIS LYS LEU LEU THR ASN MET ILE GLU
SEQRES 9 B 231 ASP ALA GLY ASP LEU ALA THR ARG SER ALA LYS ASP HIS
SEQRES 10 B 231 TYR MET ARG ILE ARG PRO PHE ALA PHE TYR GLY VAL SER
SEQRES 11 B 231 THR CYS ASN THR THR GLU GLN ASP LYS LEU SER LYS ASN
SEQRES 12 B 231 GLY SER TYR PRO SER GLY HIS THR SER THR GLY TRP ALA
SEQRES 13 B 231 THR ALA LEU VAL LEU ALA GLU ILE ASN PRO GLN ARG GLN
SEQRES 14 B 231 ASN GLU ILE LEU LYS ARG GLY TYR GLU LEU GLY GLN SER
SEQRES 15 B 231 ARG VAL ILE CYS GLY TYR HIS TRP GLN SER ASP VAL ASP
SEQRES 16 B 231 ALA ALA ARG VAL VAL GLY SER ALA VAL VAL ALA THR LEU
SEQRES 17 B 231 HIS THR ASN PRO ALA PHE GLN GLN GLN LEU GLN LYS ALA
SEQRES 18 B 231 LYS ALA GLU PHE ALA GLN HIS GLN LYS LYS
SEQRES 1 C 231 LEU ALA LEU VAL ALA THR GLY ASN ASP THR THR THR LYS
SEQRES 2 C 231 PRO ASP LEU TYR TYR LEU LYS ASN SER GLU ALA ILE ASN
SEQRES 3 C 231 SER LEU ALA LEU LEU PRO PRO PRO PRO ALA VAL GLY SER
SEQRES 4 C 231 ILE ALA PHE LEU ASN ASP GLN ALA MET TYR GLU GLN GLY
SEQRES 5 C 231 ARG LEU LEU ARG ASN THR GLU ARG GLY LYS LEU ALA ALA
SEQRES 6 C 231 GLU ASP ALA ASN LEU SER SER GLY ASP VAL ALA ASN ALA
SEQRES 7 C 231 PHE SER GLY ALA PHE GLY SER PRO ILE THR GLU LYS ASP
SEQRES 8 C 231 ALA PRO ALA LEU HIS LYS LEU LEU THR ASN MET ILE GLU
SEQRES 9 C 231 ASP ALA GLY ASP LEU ALA THR ARG SER ALA LYS ASP HIS
SEQRES 10 C 231 TYR MET ARG ILE ARG PRO PHE ALA PHE TYR GLY VAL SER
SEQRES 11 C 231 THR CYS ASN THR THR GLU GLN ASP LYS LEU SER LYS ASN
SEQRES 12 C 231 GLY SER TYR PRO SER GLY HIS THR SER THR GLY TRP ALA
SEQRES 13 C 231 THR ALA LEU VAL LEU ALA GLU ILE ASN PRO GLN ARG GLN
SEQRES 14 C 231 ASN GLU ILE LEU LYS ARG GLY TYR GLU LEU GLY GLN SER
SEQRES 15 C 231 ARG VAL ILE CYS GLY TYR HIS TRP GLN SER ASP VAL ASP
SEQRES 16 C 231 ALA ALA ARG VAL VAL GLY SER ALA VAL VAL ALA THR LEU
SEQRES 17 C 231 HIS THR ASN PRO ALA PHE GLN GLN GLN LEU GLN LYS ALA
SEQRES 18 C 231 LYS ALA GLU PHE ALA GLN HIS GLN LYS LYS
SEQRES 1 D 231 LEU ALA LEU VAL ALA THR GLY ASN ASP THR THR THR LYS
SEQRES 2 D 231 PRO ASP LEU TYR TYR LEU LYS ASN SER GLU ALA ILE ASN
SEQRES 3 D 231 SER LEU ALA LEU LEU PRO PRO PRO PRO ALA VAL GLY SER
SEQRES 4 D 231 ILE ALA PHE LEU ASN ASP GLN ALA MET TYR GLU GLN GLY
SEQRES 5 D 231 ARG LEU LEU ARG ASN THR GLU ARG GLY LYS LEU ALA ALA
SEQRES 6 D 231 GLU ASP ALA ASN LEU SER SER GLY ASP VAL ALA ASN ALA
SEQRES 7 D 231 PHE SER GLY ALA PHE GLY SER PRO ILE THR GLU LYS ASP
SEQRES 8 D 231 ALA PRO ALA LEU HIS LYS LEU LEU THR ASN MET ILE GLU
SEQRES 9 D 231 ASP ALA GLY ASP LEU ALA THR ARG SER ALA LYS ASP HIS
SEQRES 10 D 231 TYR MET ARG ILE ARG PRO PHE ALA PHE TYR GLY VAL SER
SEQRES 11 D 231 THR CYS ASN THR THR GLU GLN ASP LYS LEU SER LYS ASN
SEQRES 12 D 231 GLY SER TYR PRO SER GLY HIS THR SER THR GLY TRP ALA
SEQRES 13 D 231 THR ALA LEU VAL LEU ALA GLU ILE ASN PRO GLN ARG GLN
SEQRES 14 D 231 ASN GLU ILE LEU LYS ARG GLY TYR GLU LEU GLY GLN SER
SEQRES 15 D 231 ARG VAL ILE CYS GLY TYR HIS TRP GLN SER ASP VAL ASP
SEQRES 16 D 231 ALA ALA ARG VAL VAL GLY SER ALA VAL VAL ALA THR LEU
SEQRES 17 D 231 HIS THR ASN PRO ALA PHE GLN GLN GLN LEU GLN LYS ALA
SEQRES 18 D 231 LYS ALA GLU PHE ALA GLN HIS GLN LYS LYS
SEQRES 1 E 231 LEU ALA LEU VAL ALA THR GLY ASN ASP THR THR THR LYS
SEQRES 2 E 231 PRO ASP LEU TYR TYR LEU LYS ASN SER GLU ALA ILE ASN
SEQRES 3 E 231 SER LEU ALA LEU LEU PRO PRO PRO PRO ALA VAL GLY SER
SEQRES 4 E 231 ILE ALA PHE LEU ASN ASP GLN ALA MET TYR GLU GLN GLY
SEQRES 5 E 231 ARG LEU LEU ARG ASN THR GLU ARG GLY LYS LEU ALA ALA
SEQRES 6 E 231 GLU ASP ALA ASN LEU SER SER GLY ASP VAL ALA ASN ALA
SEQRES 7 E 231 PHE SER GLY ALA PHE GLY SER PRO ILE THR GLU LYS ASP
SEQRES 8 E 231 ALA PRO ALA LEU HIS LYS LEU LEU THR ASN MET ILE GLU
SEQRES 9 E 231 ASP ALA GLY ASP LEU ALA THR ARG SER ALA LYS ASP HIS
SEQRES 10 E 231 TYR MET ARG ILE ARG PRO PHE ALA PHE TYR GLY VAL SER
SEQRES 11 E 231 THR CYS ASN THR THR GLU GLN ASP LYS LEU SER LYS ASN
SEQRES 12 E 231 GLY SER TYR PRO SER GLY HIS THR SER THR GLY TRP ALA
SEQRES 13 E 231 THR ALA LEU VAL LEU ALA GLU ILE ASN PRO GLN ARG GLN
SEQRES 14 E 231 ASN GLU ILE LEU LYS ARG GLY TYR GLU LEU GLY GLN SER
SEQRES 15 E 231 ARG VAL ILE CYS GLY TYR HIS TRP GLN SER ASP VAL ASP
SEQRES 16 E 231 ALA ALA ARG VAL VAL GLY SER ALA VAL VAL ALA THR LEU
SEQRES 17 E 231 HIS THR ASN PRO ALA PHE GLN GLN GLN LEU GLN LYS ALA
SEQRES 18 E 231 LYS ALA GLU PHE ALA GLN HIS GLN LYS LYS
SEQRES 1 F 231 LEU ALA LEU VAL ALA THR GLY ASN ASP THR THR THR LYS
SEQRES 2 F 231 PRO ASP LEU TYR TYR LEU LYS ASN SER GLU ALA ILE ASN
SEQRES 3 F 231 SER LEU ALA LEU LEU PRO PRO PRO PRO ALA VAL GLY SER
SEQRES 4 F 231 ILE ALA PHE LEU ASN ASP GLN ALA MET TYR GLU GLN GLY
SEQRES 5 F 231 ARG LEU LEU ARG ASN THR GLU ARG GLY LYS LEU ALA ALA
SEQRES 6 F 231 GLU ASP ALA ASN LEU SER SER GLY ASP VAL ALA ASN ALA
SEQRES 7 F 231 PHE SER GLY ALA PHE GLY SER PRO ILE THR GLU LYS ASP
SEQRES 8 F 231 ALA PRO ALA LEU HIS LYS LEU LEU THR ASN MET ILE GLU
SEQRES 9 F 231 ASP ALA GLY ASP LEU ALA THR ARG SER ALA LYS ASP HIS
SEQRES 10 F 231 TYR MET ARG ILE ARG PRO PHE ALA PHE TYR GLY VAL SER
SEQRES 11 F 231 THR CYS ASN THR THR GLU GLN ASP LYS LEU SER LYS ASN
SEQRES 12 F 231 GLY SER TYR PRO SER GLY HIS THR SER THR GLY TRP ALA
SEQRES 13 F 231 THR ALA LEU VAL LEU ALA GLU ILE ASN PRO GLN ARG GLN
SEQRES 14 F 231 ASN GLU ILE LEU LYS ARG GLY TYR GLU LEU GLY GLN SER
SEQRES 15 F 231 ARG VAL ILE CYS GLY TYR HIS TRP GLN SER ASP VAL ASP
SEQRES 16 F 231 ALA ALA ARG VAL VAL GLY SER ALA VAL VAL ALA THR LEU
SEQRES 17 F 231 HIS THR ASN PRO ALA PHE GLN GLN GLN LEU GLN LYS ALA
SEQRES 18 F 231 LYS ALA GLU PHE ALA GLN HIS GLN LYS LYS
HET SO4 A1001 5
HET SO4 B1002 5
HET SO4 C1003 5
HET SO4 D1004 5
HET SO4 E1005 5
HET SO4 F1006 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 6(O4 S 2-)
FORMUL 13 HOH *314(H2 O)
HELIX 1 1 LYS A 20 ALA A 24 5 5
HELIX 2 2 ASN A 26 LEU A 31 1 6
HELIX 3 3 SER A 39 ARG A 56 1 18
HELIX 4 4 THR A 58 LEU A 70 1 13
HELIX 5 5 SER A 71 VAL A 75 5 5
HELIX 6 6 ALA A 76 ALA A 78 5 3
HELIX 7 7 PHE A 79 GLY A 84 1 6
HELIX 8 8 ALA A 92 ASN A 101 1 10
HELIX 9 9 MET A 102 ASP A 108 1 7
HELIX 10 10 THR A 111 MET A 119 1 9
HELIX 11 11 ARG A 122 TYR A 127 1 6
HELIX 12 12 SER A 148 ASN A 165 1 18
HELIX 13 13 ARG A 168 CYS A 186 1 19
HELIX 14 14 TRP A 190 HIS A 209 1 20
HELIX 15 15 ASN A 211 HIS A 228 1 18
HELIX 16 16 LYS B 20 ALA B 24 5 5
HELIX 17 17 ASN B 26 LEU B 31 1 6
HELIX 18 18 SER B 39 ARG B 56 1 18
HELIX 19 19 THR B 58 ALA B 68 1 11
HELIX 20 20 ASN B 69 LEU B 70 5 2
HELIX 21 21 SER B 71 VAL B 75 5 5
HELIX 22 22 ALA B 76 ALA B 78 5 3
HELIX 23 23 PHE B 79 GLY B 84 1 6
HELIX 24 24 ALA B 92 ASN B 101 1 10
HELIX 25 25 MET B 102 ASP B 108 1 7
HELIX 26 26 THR B 111 MET B 119 1 9
HELIX 27 27 ARG B 122 GLY B 128 1 7
HELIX 28 28 SER B 148 ASN B 165 1 18
HELIX 29 29 ARG B 168 CYS B 186 1 19
HELIX 30 30 TRP B 190 HIS B 209 1 20
HELIX 31 31 ASN B 211 HIS B 228 1 18
HELIX 32 32 LYS C 20 ALA C 24 5 5
HELIX 33 33 ASN C 26 LEU C 31 1 6
HELIX 34 34 SER C 39 ARG C 56 1 18
HELIX 35 35 THR C 58 LEU C 70 1 13
HELIX 36 36 SER C 71 ALA C 78 5 8
HELIX 37 37 PHE C 79 GLY C 84 1 6
HELIX 38 38 ALA C 92 ASN C 101 1 10
HELIX 39 39 MET C 102 ASP C 108 1 7
HELIX 40 40 THR C 111 MET C 119 1 9
HELIX 41 41 ARG C 122 GLY C 128 1 7
HELIX 42 42 SER C 148 ASN C 165 1 18
HELIX 43 43 ARG C 168 CYS C 186 1 19
HELIX 44 44 TRP C 190 HIS C 209 1 20
HELIX 45 45 ASN C 211 GLN C 227 1 17
HELIX 46 46 LYS D 20 ALA D 24 5 5
HELIX 47 47 ASN D 26 LEU D 31 1 6
HELIX 48 48 SER D 39 ARG D 56 1 18
HELIX 49 49 THR D 58 LEU D 70 1 13
HELIX 50 50 SER D 71 VAL D 75 5 5
HELIX 51 51 ALA D 76 ALA D 78 5 3
HELIX 52 52 PHE D 79 GLY D 84 1 6
HELIX 53 53 ALA D 92 ASN D 101 1 10
HELIX 54 54 MET D 102 ASP D 108 1 7
HELIX 55 55 THR D 111 MET D 119 1 9
HELIX 56 56 ARG D 122 GLY D 128 1 7
HELIX 57 57 SER D 148 ASN D 165 1 18
HELIX 58 58 ARG D 168 CYS D 186 1 19
HELIX 59 59 TRP D 190 HIS D 209 1 20
HELIX 60 60 ASN D 211 HIS D 228 1 18
HELIX 61 61 LYS E 20 ALA E 24 5 5
HELIX 62 62 ASN E 26 LEU E 31 1 6
HELIX 63 63 SER E 39 ARG E 56 1 18
HELIX 64 64 THR E 58 LEU E 70 1 13
HELIX 65 65 SER E 71 VAL E 75 5 5
HELIX 66 66 ALA E 76 ALA E 78 5 3
HELIX 67 67 PHE E 79 GLY E 84 1 6
HELIX 68 68 ALA E 92 ASN E 101 1 10
HELIX 69 69 MET E 102 ASP E 108 1 7
HELIX 70 70 THR E 111 MET E 119 1 9
HELIX 71 71 ARG E 122 GLY E 128 1 7
HELIX 72 72 SER E 148 ASN E 165 1 18
HELIX 73 73 ARG E 168 CYS E 186 1 19
HELIX 74 74 TRP E 190 HIS E 209 1 20
HELIX 75 75 ASN E 211 GLN E 227 1 17
HELIX 76 76 LYS F 20 ALA F 24 5 5
HELIX 77 77 ASN F 26 LEU F 31 1 6
HELIX 78 78 SER F 39 ARG F 56 1 18
HELIX 79 79 THR F 58 LEU F 70 1 13
HELIX 80 80 SER F 71 VAL F 75 5 5
HELIX 81 81 ALA F 76 ALA F 78 5 3
HELIX 82 82 PHE F 79 GLY F 84 1 6
HELIX 83 83 ALA F 92 ASN F 101 1 10
HELIX 84 84 MET F 102 ASP F 108 1 7
HELIX 85 85 THR F 111 MET F 119 1 9
HELIX 86 86 ARG F 122 GLY F 128 1 7
HELIX 87 87 SER F 148 ASN F 165 1 18
HELIX 88 88 ARG F 168 CYS F 186 1 19
HELIX 89 89 TRP F 190 HIS F 209 1 20
HELIX 90 90 ASN F 211 HIS F 228 1 18
SSBOND 1 CYS A 132 CYS A 186 1555 1555 2.01
SSBOND 2 CYS B 132 CYS B 186 1555 1555 2.03
SSBOND 3 CYS C 132 CYS C 186 1555 1555 2.02
SSBOND 4 CYS D 132 CYS D 186 1555 1555 2.03
SSBOND 5 CYS E 132 CYS E 186 1555 1555 2.02
SSBOND 6 CYS F 132 CYS F 186 1555 1555 2.03
CISPEP 1 TYR A 146 PRO A 147 0 0.11
CISPEP 2 TYR B 146 PRO B 147 0 -0.98
CISPEP 3 TYR C 146 PRO C 147 0 -0.55
CISPEP 4 TYR D 146 PRO D 147 0 0.95
CISPEP 5 TYR E 146 PRO E 147 0 -0.06
CISPEP 6 TYR F 146 PRO F 147 0 0.23
SITE 1 AC1 6 LYS A 115 ARG A 122 SER A 148 GLY A 149
SITE 2 AC1 6 HIS A 150 HIS A 189
SITE 1 AC2 5 LYS B 115 ARG B 122 GLY B 149 HIS B 150
SITE 2 AC2 5 HIS B 189
SITE 1 AC3 6 LYS C 115 ARG C 122 SER C 148 GLY C 149
SITE 2 AC3 6 HIS C 150 HIS C 189
SITE 1 AC4 5 LYS D 115 ARG D 122 GLY D 149 HIS D 150
SITE 2 AC4 5 HIS D 189
SITE 1 AC5 5 LYS E 115 ARG E 122 GLY E 149 HIS E 150
SITE 2 AC5 5 HIS E 189
SITE 1 AC6 6 LYS F 115 ARG F 122 SER F 148 GLY F 149
SITE 2 AC6 6 HIS F 150 HIS F 189
CRYST1 137.800 168.200 58.400 90.00 90.00 90.00 P 21 21 21 24
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 0.007257 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
