HEADER HYDROLASE 08-SEP-10 2XR0
TITLE ROOM TEMPERATURE X-RAY STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N
TITLE 2 R276N DOUBLE MUTANT BETA-LACTAMASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOHO-1 BETA-LACTAMASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 32-291;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: FULLY PERDEUTERATED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PJEXPRESS 401
KEYWDS HYDROLASE, EXTENDED-SPECTRUM BETA-LACTAMASES, ESBLS, CTX-M-TYPE ESBLS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.TOMANICEK,K.K.WANG,K.L.WEISS,M.P.BLAKELEY,J.COOPER,Y.CHEN,
AUTHOR 2 L.COATES
REVDAT 4 20-DEC-23 2XR0 1 REMARK
REVDAT 3 16-FEB-11 2XR0 1 JRNL
REVDAT 2 29-DEC-10 2XR0 1 JRNL
REVDAT 1 22-DEC-10 2XR0 0
JRNL AUTH S.J.TOMANICEK,K.K.WANG,K.L.WEISS,M.P.BLAKELEY,J.COOPER,
JRNL AUTH 2 Y.CHEN,L.COATES
JRNL TITL THE ACTIVE SITE PROTONATION STATES OF PERDEUTERATED TOHO-1
JRNL TITL 2 BETA-LACTAMASE DETERMINED BY NEUTRON DIFFRACTION SUPPORT A
JRNL TITL 3 ROLE FOR GLU166 AS THE GENERAL BASE IN ACYLATION.
JRNL REF FEBS LETT. V. 585 364 2011
JRNL REFN ISSN 0014-5793
JRNL PMID 21168411
JRNL DOI 10.1016/J.FEBSLET.2010.12.017
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 15956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 800
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.5444 - 3.9951 0.99 2673 143 0.1305 0.1552
REMARK 3 2 3.9951 - 3.1722 0.99 2542 134 0.1247 0.1491
REMARK 3 3 3.1722 - 2.7715 0.98 2517 135 0.1436 0.1957
REMARK 3 4 2.7715 - 2.5183 0.98 2498 131 0.1413 0.1909
REMARK 3 5 2.5183 - 2.3379 0.98 2469 127 0.1319 0.1954
REMARK 3 6 2.3379 - 2.2001 0.97 2457 130 0.1289 0.1913
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 28.96
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05240
REMARK 3 B22 (A**2) : -1.05240
REMARK 3 B33 (A**2) : 2.10470
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2042
REMARK 3 ANGLE : 1.122 2783
REMARK 3 CHIRALITY : 0.070 327
REMARK 3 PLANARITY : 0.005 361
REMARK 3 DIHEDRAL : 13.134 758
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2XR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1290045326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15962
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.83000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 22.00
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: PDB ENTRY 2WYX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 A AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 CITRATE, PD 5.1. PREPARED IN 99.9% D2O AND MIXED 1:1 WITH
REMARK 280 PERDEUTERATED PROTEIN PREPARED IN 20 MM NA MES AT PD 6.1 (PH 6.5)
REMARK 280 .
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 66.22000
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 33.11000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.11000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.22000
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2037 O HOH A 2037 6554 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 69 -137.43 49.64
REMARK 500 VAL A 103 -132.79 -102.81
REMARK 500 ASN A 114 -4.47 80.68
REMARK 500 SER A 220 -127.19 -101.35
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 1291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1293
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IYP RELATED DB: PDB
REMARK 900 TOHO-1 BETA-LACTAMASE IN COMPLEX WITH CEPHALOTHIN
REMARK 900 RELATED ID: 1WE4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLASS A BETA-LACTAMASE TOHO-1 G238CMUTANT
REMARK 900 RELATED ID: 2WYX RELATED DB: PDB
REMARK 900 NEUTRON STRUCTURE OF A CLASS A BETA- LACTAMASE TOHO-1 E166A R274N
REMARK 900 R276N TRIPLE MUTANT
REMARK 900 RELATED ID: 1IYS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLASS A BETA-LACTAMASE TOHO-1
REMARK 900 RELATED ID: 1IYO RELATED DB: PDB
REMARK 900 TOHO-1 BETA-LACTAMASE IN COMPLEX WITH CEFOTAXIME
REMARK 900 RELATED ID: 1BZA RELATED DB: PDB
REMARK 900 BETA-LACTAMASE TOHO-1 FROM ESCHERICHIA COLI TUH12191
REMARK 900 RELATED ID: 1IYQ RELATED DB: PDB
REMARK 900 TOHO-1 BETA-LACTAMASE IN COMPLEX WITH BENZYLPENICILLIN
REMARK 900 RELATED ID: 2XQZ RELATED DB: PDB
REMARK 900 NEUTRON STRUCTURE OF THE PERDEUTERATED TOHO- 1 R274N R276N DOUBLE
REMARK 900 MUTANT BETA-LACTAMASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 2XR0 USES A RESIDUE NUMBERING SCHEME IN WHICH RESIDUE POSITION 58,
REMARK 999 RESIDUE POSITION 239, AND RESIDUE POSITION 253 HAVE NOT BEEN USED -
REMARK 999 GIVING A SMALL MISMATCH BETWEEN THE NUMBER OF RESIDUES IN THE DBREF
REMARK 999 SEQUENCE RANGES BELOW.
DBREF 2XR0 A 28 290 UNP Q47066 BLT1_ECOLX 32 291
SEQADV 2XR0 ASN A 274 UNP Q47066 ARG 275 ENGINEERED MUTATION
SEQADV 2XR0 ASN A 276 UNP Q47066 ARG 277 ENGINEERED MUTATION
SEQRES 1 A 260 SER VAL GLN GLN GLN LEU GLU ALA LEU GLU LYS SER SER
SEQRES 2 A 260 GLY GLY ARG LEU GLY VAL ALA LEU ILE ASN THR ALA ASP
SEQRES 3 A 260 ASN SER GLN ILE LEU TYR ARG ALA ASP GLU ARG PHE ALA
SEQRES 4 A 260 MET CYS SER THR SER LYS VAL MET ALA ALA ALA ALA VAL
SEQRES 5 A 260 LEU LYS GLN SER GLU SER ASP LYS HIS LEU LEU ASN GLN
SEQRES 6 A 260 ARG VAL GLU ILE LYS LYS SER ASP LEU VAL ASN TYR ASN
SEQRES 7 A 260 PRO ILE ALA GLU LYS HIS VAL ASN GLY THR MET THR LEU
SEQRES 8 A 260 ALA GLU LEU GLY ALA ALA ALA LEU GLN TYR SER ASP ASN
SEQRES 9 A 260 THR ALA MET ASN LYS LEU ILE ALA HIS LEU GLY GLY PRO
SEQRES 10 A 260 ASP LYS VAL THR ALA PHE ALA ARG SER LEU GLY ASP GLU
SEQRES 11 A 260 THR PHE ARG LEU ASP ARG THR GLU PRO THR LEU ASN THR
SEQRES 12 A 260 ALA ILE PRO GLY ASP PRO ARG ASP THR THR THR PRO LEU
SEQRES 13 A 260 ALA MET ALA GLN THR LEU LYS ASN LEU THR LEU GLY LYS
SEQRES 14 A 260 ALA LEU ALA GLU THR GLN ARG ALA GLN LEU VAL THR TRP
SEQRES 15 A 260 LEU LYS GLY ASN THR THR GLY SER ALA SER ILE ARG ALA
SEQRES 16 A 260 GLY LEU PRO LYS SER TRP VAL VAL GLY ASP LYS THR GLY
SEQRES 17 A 260 SER GLY ASP TYR GLY THR THR ASN ASP ILE ALA VAL ILE
SEQRES 18 A 260 TRP PRO GLU ASN HIS ALA PRO LEU VAL LEU VAL THR TYR
SEQRES 19 A 260 PHE THR GLN PRO GLU GLN LYS ALA GLU ASN ARG ASN ASP
SEQRES 20 A 260 ILE LEU ALA ALA ALA ALA LYS ILE VAL THR HIS GLY PHE
HET SO4 A1291 5
HET SO4 A1292 5
HET SO4 A1293 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 HOH *154(H2 O)
HELIX 1 1 SER A 28 GLY A 41 1 14
HELIX 2 2 CYS A 69 THR A 71 5 3
HELIX 3 3 SER A 72 GLU A 85 1 14
HELIX 4 4 HIS A 89 ASN A 92 5 4
HELIX 5 5 LYS A 98 LEU A 102 5 5
HELIX 6 6 ILE A 108 VAL A 113 5 6
HELIX 7 7 LEU A 119 TYR A 129 1 11
HELIX 8 8 ASP A 131 GLY A 143 1 13
HELIX 9 9 GLY A 144 LEU A 155 1 12
HELIX 10 10 PRO A 167 THR A 171 5 5
HELIX 11 11 THR A 182 GLY A 196 1 15
HELIX 12 12 ALA A 200 GLY A 213 1 14
HELIX 13 13 SER A 220 LEU A 225 5 6
HELIX 14 14 ARG A 275 THR A 287 1 13
SHEET 1 AA 5 GLN A 56 TYR A 60 0
SHEET 2 AA 5 ARG A 43 ASN A 50 -1 O VAL A 46 N TYR A 60
SHEET 3 AA 5 LEU A 259 THR A 266 -1 O VAL A 260 N ILE A 49
SHEET 4 AA 5 THR A 244 TRP A 251 -1 O THR A 244 N PHE A 265
SHEET 5 AA 5 VAL A 230 SER A 237 -1 O VAL A 230 N TRP A 251
SHEET 1 AB 2 PHE A 66 ALA A 67 0
SHEET 2 AB 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 AC 2 ARG A 94 GLU A 96 0
SHEET 2 AC 2 THR A 116 THR A 118 -1 O MET A 117 N VAL A 95
CISPEP 1 GLU A 166 PRO A 167 0 3.62
SITE 1 AC1 6 TRP A 229 PRO A 252 GLU A 254 ASN A 255
SITE 2 AC1 6 HIS A 256 PHE A 290
SITE 1 AC2 8 SER A 70 SER A 130 LYS A 234 THR A 235
SITE 2 AC2 8 SER A 237 HOH A2149 HOH A2151 HOH A2152
SITE 1 AC3 3 ARG A 178 HOH A2153 HOH A2154
CRYST1 73.500 73.500 99.330 90.00 90.00 120.00 P 32 2 1 6
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 0.013605 0.007855 0.000000 0.00000
SCALE2 0.000000 0.015710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010067 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
