HEADER HYDROLASE 20-FEB-07 2OXN
TITLE VIBRIO CHOLERAE FAMILY 3 GLYCOSIDE HYDROLASE (NAGZ) IN COMPLEX WITH
TITLE 2 PUGNAC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-HEXOSAMINIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: N-ACETYL-BETA-GLUCOSAMINIDASE, BETA-N-ACETYLHEXOSAMINIDASE;
COMPND 5 EC: 3.2.1.52;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 GENE: NAGZ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS TIM-BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BALCEWICH,B.L.MARK
REVDAT 5 30-AUG-23 2OXN 1 REMARK SEQADV
REVDAT 4 02-JUL-14 2OXN 1 CONECT HETATM LINK VERSN
REVDAT 3 23-MAR-10 2OXN 1 JRNL
REVDAT 2 24-FEB-09 2OXN 1 VERSN
REVDAT 1 12-JUN-07 2OXN 0
JRNL AUTH K.A.STUBBS,M.BALCEWICH,B.L.MARK,D.J.VOCADLO
JRNL TITL SMALL MOLECULE INHIBITORS OF A GLYCOSIDE HYDROLASE ATTENUATE
JRNL TITL 2 INDUCIBLE AMPC-MEDIATED BETA-LACTAM RESISTANCE.
JRNL REF J.BIOL.CHEM. V. 282 21382 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17439950
JRNL DOI 10.1074/JBC.M700084200
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 35779
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1783
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2309
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2592
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 381
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 0.50000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.108
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.615
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2681 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1814 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3625 ; 1.298 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4405 ; 0.905 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 334 ; 5.639 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;35.772 ;24.077
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 449 ;11.905 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;11.768 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 387 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3038 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 548 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 561 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2009 ; 0.200 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1298 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1343 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 242 ; 0.132 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.218 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.321 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.135 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2152 ; 1.137 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 681 ; 0.203 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2634 ; 1.171 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1171 ; 2.397 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 991 ; 3.394 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041711.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35787
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 55.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.16700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.400
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: 1TR9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 20000, 100MM BIS-TRIS, PH 5.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 24.36700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.44700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.92500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.44700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.36700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.92500
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: MONOMERIC
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 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 HIS A 334
REMARK 465 HIS A 335
REMARK 465 HIS A 336
REMARK 465 HIS A 337
REMARK 465 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 717 O HOH A 880 2.06
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 LYS A 54 19.12 59.91
REMARK 500 ASN A 89 41.11 -98.32
REMARK 500 ILE A 127 -71.87 -92.06
REMARK 500 LYS A 275 71.08 -155.25
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 OAN A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TR9 RELATED DB: PDB
REMARK 900 VIBRIO CHOLERAE NAGZ
REMARK 900 RELATED ID: 1Y65 RELATED DB: PDB
REMARK 900 VIBRIO CHOLERAE NAGZ PRODUCT COMPLEX
DBREF 2OXN A 1 330 UNP Q9KU37 NAGZ_VIBCH 1 330
SEQADV 2OXN HIS A 331 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 332 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 333 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 334 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 335 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 336 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 337 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 338 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 339 UNP Q9KU37 EXPRESSION TAG
SEQADV 2OXN HIS A 340 UNP Q9KU37 EXPRESSION TAG
SEQRES 1 A 340 MET GLY PRO LEU TRP LEU ASP VAL ALA GLY TYR GLU LEU
SEQRES 2 A 340 SER ALA GLU ASP ARG GLU ILE LEU GLN HIS PRO THR VAL
SEQRES 3 A 340 GLY GLY VAL ILE LEU PHE GLY ARG ASN TYR HIS ASP ASN
SEQRES 4 A 340 GLN GLN LEU LEU ALA LEU ASN LYS ALA ILE ARG GLN ALA
SEQRES 5 A 340 ALA LYS ARG PRO ILE LEU ILE GLY VAL ASP GLN GLU GLY
SEQRES 6 A 340 GLY ARG VAL GLN ARG PHE ARG GLU GLY PHE SER ARG ILE
SEQRES 7 A 340 PRO PRO ALA GLN TYR TYR ALA ARG ALA GLU ASN GLY VAL
SEQRES 8 A 340 GLU LEU ALA GLU GLN GLY GLY TRP LEU MET ALA ALA GLU
SEQRES 9 A 340 LEU ILE ALA HIS ASP VAL ASP LEU SER PHE ALA PRO VAL
SEQRES 10 A 340 LEU ASP MET GLY PHE ALA CYS LYS ALA ILE GLY ASN ARG
SEQRES 11 A 340 ALA PHE GLY GLU ASP VAL GLN THR VAL LEU LYS HIS SER
SEQRES 12 A 340 SER ALA PHE LEU ARG GLY MET LYS ALA VAL GLY MET ALA
SEQRES 13 A 340 THR THR GLY LYS HIS PHE PRO GLY HIS GLY ALA VAL ILE
SEQRES 14 A 340 ALA ASP SER HIS LEU GLU THR PRO TYR ASP GLU ARG GLU
SEQRES 15 A 340 THR ILE ALA GLN ASP MET ALA ILE PHE ARG ALA GLN ILE
SEQRES 16 A 340 GLU ALA GLY VAL LEU ASP ALA MET MET PRO ALA HIS VAL
SEQRES 17 A 340 VAL TYR PRO HIS TYR ASP ALA GLN PRO ALA SER GLY SER
SEQRES 18 A 340 SER TYR TRP LEU LYS GLN VAL LEU ARG GLU GLU LEU GLY
SEQRES 19 A 340 PHE LYS GLY ILE VAL PHE SER ASP ASP LEU SER MET GLU
SEQRES 20 A 340 GLY ALA ALA VAL MET GLY GLY PRO VAL GLU ARG SER HIS
SEQRES 21 A 340 GLN ALA LEU VAL ALA GLY CYS ASP MET ILE LEU ILE CYS
SEQRES 22 A 340 ASN LYS ARG GLU ALA ALA VAL GLU VAL LEU ASP ASN LEU
SEQRES 23 A 340 PRO ILE MET GLU VAL PRO GLN ALA GLU ALA LEU LEU LYS
SEQRES 24 A 340 LYS GLN GLN PHE SER TYR SER GLU LEU LYS ARG LEU GLU
SEQRES 25 A 340 ARG TRP GLN GLN ALA SER ALA ASN MET GLN ARG LEU ILE
SEQRES 26 A 340 GLU GLN PHE SER GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 27 A 340 HIS HIS
HET OAN A 501 25
HETNAM OAN O-(2-ACETAMIDO-2-DEOXY D-GLUCOPYRANOSYLIDENE) AMINO-N-
HETNAM 2 OAN PHENYLCARBAMATE
HETSYN OAN PUGNAC
FORMUL 2 OAN C15 H19 N3 O7
FORMUL 3 HOH *381(H2 O)
HELIX 1 1 SER A 14 GLN A 22 1 9
HELIX 2 2 PHE A 32 TYR A 36 5 5
HELIX 3 3 ASP A 38 LYS A 54 1 17
HELIX 4 4 PRO A 80 ALA A 87 5 8
HELIX 5 5 ASN A 89 ALA A 107 1 19
HELIX 6 6 ILE A 127 ALA A 131 5 5
HELIX 7 7 ASP A 135 VAL A 153 1 19
HELIX 8 8 ILE A 184 GLY A 198 1 15
HELIX 9 9 PRO A 217 GLY A 220 5 4
HELIX 10 10 SER A 221 LYS A 226 1 6
HELIX 11 11 SER A 245 GLU A 247 5 3
HELIX 12 12 GLY A 248 GLY A 253 1 6
HELIX 13 13 GLY A 254 GLY A 266 1 13
HELIX 14 14 LYS A 275 LEU A 286 1 12
HELIX 15 15 VAL A 291 LEU A 298 5 8
HELIX 16 16 SER A 304 ARG A 310 1 7
HELIX 17 17 LEU A 311 SER A 329 1 19
SHEET 1 A 8 LEU A 112 SER A 113 0
SHEET 2 A 8 LEU A 58 VAL A 61 1 N ILE A 59 O LEU A 112
SHEET 3 A 8 VAL A 26 LEU A 31 1 N LEU A 31 O GLY A 60
SHEET 4 A 8 LEU A 4 LEU A 6 1 N LEU A 4 O GLY A 27
SHEET 5 A 8 MET A 269 LEU A 271 1 O ILE A 270 N TRP A 5
SHEET 6 A 8 ILE A 238 ASP A 243 1 O VAL A 239 N MET A 269
SHEET 7 A 8 ALA A 202 PRO A 205 1 N MET A 203 O PHE A 240
SHEET 8 A 8 THR A 158 PHE A 162 1 N GLY A 159 O MET A 204
SHEET 1 B 2 GLN A 63 GLY A 65 0
SHEET 2 B 2 VAL A 68 GLN A 69 -1 O VAL A 68 N GLY A 65
CISPEP 1 ALA A 115 PRO A 116 0 7.78
CISPEP 2 LYS A 160 HIS A 161 0 -0.73
CISPEP 3 PHE A 162 PRO A 163 0 1.58
SITE 1 AC1 11 GLU A 19 GLN A 22 ILE A 30 ASP A 62
SITE 2 AC1 11 ARG A 130 LYS A 160 HIS A 161 MET A 204
SITE 3 AC1 11 ASP A 243 MET A 246 HOH A 846
CRYST1 48.734 67.850 96.894 90.00 90.00 90.00 P 21 21 21 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 0.020520 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014738 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010321 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
