HEADER HYDROLASE 10-JAN-13 3W4O
TITLE CRYSTAL STRUCTURE OF PENI BETA-LACTAMASE FROM BURKHOLDERIA
TITLE 2 PSEUDOMALLEI AT PH9.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 31-295;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;
SOURCE 3 ORGANISM_TAXID: 272560;
SOURCE 4 STRAIN: K96243;
SOURCE 5 GENE: BPSS0946, PENA, PENI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI 2 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A(+)
KEYWDS BETA-LACTAMASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NUKAGA,N.OHUCHI,K.M.PAPP-WALLACE,M.A.TARACILA,R.A.BONOMO
REVDAT 3 08-NOV-23 3W4O 1 REMARK SEQADV
REVDAT 2 04-SEP-13 3W4O 1 JRNL
REVDAT 1 15-MAY-13 3W4O 0
JRNL AUTH K.M.PAPP-WALLACE,M.A.TARACILA,J.A.GATTA,N.OHUCHI,R.A.BONOMO,
JRNL AUTH 2 M.NUKAGA
JRNL TITL INSIGHTS INTO BETA-LACTAMASES FROM BURKHOLDERIA SPECIES, TWO
JRNL TITL 2 PHYLOGENETICALLY RELATED YET DISTINCT RESISTANCE
JRNL TITL 3 DETERMINANTS
JRNL REF J.BIOL.CHEM. V. 288 19090 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23658015
JRNL DOI 10.1074/JBC.M113.458315
REMARK 2
REMARK 2 RESOLUTION. 1.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.114
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.115
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.153
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2064
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 66491
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.100
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 56129
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1987
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 319
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2320.2
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1939.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 28
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 22240
REMARK 3 NUMBER OF RESTRAINTS : 28349
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.031
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.038
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.080
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.088
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.041
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.021
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.089
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3W4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000095881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68591
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.180
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.040
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2P74
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG8000, 0.1M CHESS, PH 9.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 26.38550
REMARK 290 SMTRY3 2 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: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 25 CD CE NZ
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 44 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 CYS A 69 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 94 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 94 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 94 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 THR A 126 OG1 - CB - CG2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 THR A 126 OG1 - CB - CG2 ANGL. DEV. = -23.3 DEGREES
REMARK 500 THR A 126 CA - CB - OG1 ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR A 126 CA - CB - CG2 ANGL. DEV. = -14.2 DEGREES
REMARK 500 THR A 126 CA - CB - CG2 ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG A 165 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP A 197 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 PRO A 254 O - C - N ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR A 264 CB - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 284 CG - CD - NE ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG A 284 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH2 ANGL. DEV. = -6.1 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 CYS A 69 -140.91 46.64
REMARK 500 GLU A 87 77.07 -153.51
REMARK 500 ARG A 220 -120.79 -113.39
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 NHE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OV5 RELATED DB: PDB
REMARK 900 BETA-LACTAMASE WITH SIMILAR SUBSTRATE SPECIFICITY
REMARK 900 RELATED ID: 3W4P RELATED DB: PDB
REMARK 900 RELATED ID: 3W4Q RELATED DB: PDB
DBREF 3W4O A 25 291 UNP H7C785 H7C785_BURPS 31 295
SEQADV 3W4O MET A 24 UNP H7C785 INITIATING METHIONINE
SEQRES 1 A 266 MET LYS ASN VAL ALA ALA ALA GLU ARG GLN LEU ARG GLU
SEQRES 2 A 266 LEU GLU SER THR PHE ASP GLY ARG LEU GLY PHE VAL ALA
SEQRES 3 A 266 LEU ASP THR ALA THR GLY ALA ARG ILE ALA HIS ARG GLY
SEQRES 4 A 266 ASP GLU ARG PHE PRO PHE CYS SER THR SER LYS MET MET
SEQRES 5 A 266 LEU CYS ALA ALA VAL LEU ALA ARG SER ALA GLY GLU PRO
SEQRES 6 A 266 ALA LEU LEU GLN ARG ARG ILE ALA TYR ALA LYS GLY ASP
SEQRES 7 A 266 LEU ILE ARG TYR SER PRO ILE THR GLU GLN HIS VAL GLY
SEQRES 8 A 266 ALA GLY MET SER VAL ALA GLU LEU CYS ALA ALA THR LEU
SEQRES 9 A 266 GLN TYR SER ASP ASN THR ALA ALA ASN LEU LEU ILE ALA
SEQRES 10 A 266 LEU LEU GLY GLY PRO GLN THR VAL THR ALA TYR ALA ARG
SEQRES 11 A 266 SER ILE GLY ASP ALA THR PHE ARG LEU ASP ARG ARG GLU
SEQRES 12 A 266 PRO GLU LEU ASN THR ALA LEU PRO GLY ASP GLU ARG ASP
SEQRES 13 A 266 THR THR THR PRO ALA ALA MET ALA ALA SER VAL HIS ARG
SEQRES 14 A 266 LEU LEU VAL GLY ASP ALA LEU GLY ALA ALA GLN ARG ALA
SEQRES 15 A 266 GLN LEU ASN ALA TRP MET LEU GLY ASN LYS THR GLY ASP
SEQRES 16 A 266 ALA ARG ILE ARG ALA GLY VAL PRO ALA ASP TRP ARG VAL
SEQRES 17 A 266 ALA ASP LYS THR GLY THR GLY ASP TYR GLY THR ALA ASN
SEQRES 18 A 266 ASP ILE GLY VAL ALA TYR PRO PRO ASN ARG ALA PRO ILE
SEQRES 19 A 266 VAL PHE ILE VAL TYR THR THR MET ARG ASN PRO ASN ALA
SEQRES 20 A 266 GLN ALA ARG ASP ASP VAL ILE ALA SER ALA THR ARG ILE
SEQRES 21 A 266 ALA ALA ARG ALA PHE ALA
HET NHE A 301 13
HET GOL A 302 6
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NHE C8 H17 N O3 S
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *319(H2 O)
HELIX 1 1 MET A 24 SER A 39 1 16
HELIX 2 2 THR A 71 ALA A 85 1 15
HELIX 3 3 GLU A 87 GLN A 92 5 6
HELIX 4 4 ALA A 98 LEU A 102 5 5
HELIX 5 5 ILE A 108 VAL A 113 1 6
HELIX 6 6 VAL A 119 SER A 130 1 12
HELIX 7 7 ASP A 131 GLY A 143 1 13
HELIX 8 8 GLY A 144 ILE A 155 1 12
HELIX 9 9 PRO A 167 THR A 171 5 5
HELIX 10 10 THR A 182 VAL A 195 1 14
HELIX 11 11 GLY A 200 GLY A 213 1 14
HELIX 12 12 ARG A 220 VAL A 225 1 6
HELIX 13 13 ASP A 276 PHE A 290 1 15
SHEET 1 A 5 ARG A 57 HIS A 60 0
SHEET 2 A 5 GLY A 43 ASP A 51 -1 N ALA A 49 O ILE A 58
SHEET 3 A 5 ILE A 259 MET A 267 -1 O TYR A 264 N GLY A 46
SHEET 4 A 5 ALA A 244 TYR A 251 -1 N ALA A 250 O ILE A 259
SHEET 5 A 5 ARG A 230 THR A 237 -1 N ARG A 230 O TYR A 251
SHEET 1 B 2 PHE A 66 PRO A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 ARG A 94 ILE A 95 0
SHEET 2 C 2 MET A 117 SER A 118 -1 O MET A 117 N ILE A 95
CISPEP 1 GLU A 166 PRO A 167 0 -3.02
SITE 1 AC1 9 LYS A 25 ARG A 83 LEU A 90 ARG A 93
SITE 2 AC1 9 LEU A 141 HOH A 587 HOH A 610 HOH A 758
SITE 3 AC1 9 HOH A 764
SITE 1 AC2 8 LEU A 212 ARG A 222 ARG A 230 VAL A 231
SITE 2 AC2 8 ASN A 271 HOH A 514 HOH A 531 HOH A 620
CRYST1 41.395 52.771 50.471 90.00 92.55 90.00 P 1 21 1 2
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 0.024158 0.000000 0.001076 0.00000
SCALE2 0.000000 0.018950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019833 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
