HEADER OUTER MEMBRANE 29-JUN-99 1QJP
TITLE HIGH RESOLUTION STRUCTURE OF THE OUTER MEMBRANE PROTEIN A (OMPA)
TITLE 2 TRANSMEMBRANE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANSMEMBRANE DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI BL21(DE3);
SOURCE 3 ORGANISM_TAXID: 469008;
SOURCE 4 GENE: OMPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3B-171
KEYWDS OUTER MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAUTSCH,G.E.SCHULZ
REVDAT 6 13-DEC-23 1QJP 1 REMARK
REVDAT 5 24-JUL-19 1QJP 1 REMARK
REVDAT 4 10-JUL-19 1QJP 1 REMARK
REVDAT 3 24-OCT-18 1QJP 1 SOURCE REMARK
REVDAT 2 24-FEB-09 1QJP 1 VERSN
REVDAT 1 30-JUN-00 1QJP 0
JRNL AUTH A.PAUTSCH,G.E.SCHULZ
JRNL TITL HIGH RESOLUTION STRUCTURE OF THE OMPA MEMBRANE DOMAIN
JRNL REF J.MOL.BIOL. V. 298 273 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10764596
JRNL DOI 10.1006/JMBI.2000.3671
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.PAUTSCH,G.E.SCHULZ
REMARK 1 TITL STRUCTURE OF THE OUTER MEMBRANE PROTEIN A TRANSMEMBRANE
REMARK 1 TITL 2 DOMAIN
REMARK 1 REF NAT.STRUCT.BIOL. V. 5 1013 1998
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 9808047
REMARK 1 DOI 10.1038/2983
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 29702
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1078
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.00
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.070
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.602
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.008 ; 0.010
REMARK 3 ANGLE DISTANCE (A) : 0.037 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.065 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.025 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.175 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.235 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.173 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.200 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 14.900; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 22.800; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 6.823 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 9.204 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.742 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 10.197; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE REGIONS Y18-T30, K64-G70 AND N146
REMARK 3 -N159 WERE DISORDERED AND ARE NOT INCLUDED IN THE MODEL
REMARK 4
REMARK 4 1QJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1290002187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29702
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 1BXW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 10 % MPD, 25 MM KH2PO4
REMARK 280 PH 5.1, PH 5.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 32.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 32.55000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.85000
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 300 REMARK: BIOLOGICAL_UNIT: MONOMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 F23L, Q34K AND K107Y WERE INTRODUCED TO OBTAIN XRAY GRADE
REMARK 400 CRYSTALS
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 TYR A 18
REMARK 465 HIS A 19
REMARK 465 ASP A 20
REMARK 465 THR A 21
REMARK 465 GLY A 22
REMARK 465 PHE A 23
REMARK 465 ILE A 24
REMARK 465 ASN A 25
REMARK 465 ASN A 26
REMARK 465 ASN A 27
REMARK 465 GLY A 28
REMARK 465 PRO A 29
REMARK 465 THR A 30
REMARK 465 LYS A 64
REMARK 465 GLY A 65
REMARK 465 SER A 66
REMARK 465 VAL A 67
REMARK 465 GLU A 68
REMARK 465 ASN A 69
REMARK 465 GLY A 70
REMARK 465 ASN A 146
REMARK 465 ILE A 147
REMARK 465 GLY A 148
REMARK 465 ASP A 149
REMARK 465 ALA A 150
REMARK 465 HIS A 151
REMARK 465 THR A 152
REMARK 465 ILE A 153
REMARK 465 GLY A 154
REMARK 465 THR A 155
REMARK 465 ARG A 156
REMARK 465 PRO A 157
REMARK 465 ASP A 158
REMARK 465 ASN A 159
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 60 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TYR A 85 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 89 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 90 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 LEU A 91 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU A 139 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 C8E A 1174
REMARK 615 C8E A 1175
REMARK 615 C8E A 1177
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A1172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A1173
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A1174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A1175
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A1176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A1177
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BXW RELATED DB: PDB
DBREF 1QJP A 1 171 UNP P02934 OMPA_ECOLI 22 192
SEQADV 1QJP PHE A 23 UNP P02934 LEU 44 ENGINEERED MUTATION
SEQADV 1QJP LYS A 34 UNP P02934 GLN 55 ENGINEERED MUTATION
SEQADV 1QJP TYR A 107 UNP P02934 LYS 128 ENGINEERED MUTATION
SEQRES 1 A 171 ALA PRO LYS ASP ASN THR TRP TYR THR GLY ALA LYS LEU
SEQRES 2 A 171 GLY TRP SER GLN TYR HIS ASP THR GLY PHE ILE ASN ASN
SEQRES 3 A 171 ASN GLY PRO THR HIS GLU ASN LYS LEU GLY ALA GLY ALA
SEQRES 4 A 171 PHE GLY GLY TYR GLN VAL ASN PRO TYR VAL GLY PHE GLU
SEQRES 5 A 171 MET GLY TYR ASP TRP LEU GLY ARG MET PRO TYR LYS GLY
SEQRES 6 A 171 SER VAL GLU ASN GLY ALA TYR LYS ALA GLN GLY VAL GLN
SEQRES 7 A 171 LEU THR ALA LYS LEU GLY TYR PRO ILE THR ASP ASP LEU
SEQRES 8 A 171 ASP ILE TYR THR ARG LEU GLY GLY MET VAL TRP ARG ALA
SEQRES 9 A 171 ASP THR TYR SER ASN VAL TYR GLY LYS ASN HIS ASP THR
SEQRES 10 A 171 GLY VAL SER PRO VAL PHE ALA GLY GLY VAL GLU TYR ALA
SEQRES 11 A 171 ILE THR PRO GLU ILE ALA THR ARG LEU GLU TYR GLN TRP
SEQRES 12 A 171 THR ASN ASN ILE GLY ASP ALA HIS THR ILE GLY THR ARG
SEQRES 13 A 171 PRO ASP ASN GLY MET LEU SER LEU GLY VAL SER TYR ARG
SEQRES 14 A 171 PHE GLY
HET C8E A1172 21
HET C8E A1173 21
HET C8E A1174 21
HET C8E A1175 21
HET C8E A1176 21
HET C8E A1177 21
HETNAM C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
FORMUL 2 C8E 6(C16 H34 O5)
FORMUL 8 HOH *64(H2 O)
SHEET 1 A 9 LYS A 34 GLN A 44 0
SHEET 2 A 9 THR A 6 SER A 16 -1 N SER A 16 O LYS A 34
SHEET 3 A 9 MET A 161 ARG A 169 -1 N TYR A 168 O THR A 9
SHEET 4 A 9 ILE A 135 THR A 144 -1 N GLN A 142 O MET A 161
SHEET 5 A 9 LYS A 113 THR A 132 -1 N THR A 132 O ILE A 135
SHEET 6 A 9 LEU A 91 TYR A 107 -1 N THR A 106 O ASN A 114
SHEET 7 A 9 TYR A 72 PRO A 86 -1 N TYR A 85 O ILE A 93
SHEET 8 A 9 VAL A 49 ARG A 60 -1 N LEU A 58 O ALA A 74
SHEET 9 A 9 LYS A 34 ASN A 46 -1 N ASN A 46 O VAL A 49
SITE 1 AC1 6 TYR A 43 PHE A 51 LEU A 79 PRO A 121
SITE 2 AC1 6 ASN A 145 C8E A1175
SITE 1 AC2 5 LEU A 13 GLN A 17 ILE A 131 THR A 137
SITE 2 AC2 5 LEU A 139
SITE 1 AC3 7 TYR A 48 LEU A 83 GLY A 84 TYR A 85
SITE 2 AC3 7 ILE A 93 TYR A 94 THR A 95
SITE 1 AC4 4 VAL A 77 GLY A 99 VAL A 101 C8E A1172
SITE 1 AC5 10 ALA A 11 LEU A 13 LEU A 35 GLY A 36
SITE 2 AC5 10 ALA A 37 GLY A 38 TRP A 57 GLY A 59
SITE 3 AC5 10 ARG A 60 MET A 61
SITE 1 AC6 4 ASN A 46 THR A 95 TRP A 143 ASN A 145
CRYST1 65.100 79.700 50.200 90.00 94.30 90.00 C 1 2 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 0.015361 0.000000 0.001155 0.00000
SCALE2 0.000000 0.012547 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019976 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
