HEADER HYDROLASE 28-MAR-08 2JJB
TITLE FAMILY 37 TREHALASE FROM ESCHERICHIA COLI IN COMPLEX WITH CASUARINE-6-
TITLE 2 O-ALPHA-GLUCOPYRANOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC TREHALASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ALPHA\,ALPHA-TREHALASE, ALPHA\,ALPHA-TREHALOSE
COMPND 5 GLUCOHYDROLASE;
COMPND 6 EC: 3.2.1.28;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE, GLYCOSIDASE, GLYCOSIDE HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.GLOSTER,S.ROBERTS,G.J.DAVIES,F.CARDONA,C.PARMEGGIANI,C.BONACCINI,
AUTHOR 2 P.GRATTERI,L.SIM,D.R.ROSE,A.GOTI
REVDAT 6 13-DEC-23 2JJB 1 HETSYN
REVDAT 5 29-JUL-20 2JJB 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 20-APR-11 2JJB 1 JRNL REMARK
REVDAT 3 21-APR-10 2JJB 1 REMARK HETATM
REVDAT 2 24-NOV-09 2JJB 1 COMPND SOURCE KEYWDS REMARK
REVDAT 2 2 1 HETSYN FORMUL
REVDAT 1 13-JAN-09 2JJB 0
JRNL AUTH F.CARDONA,C.PARMEGGIANI,E.FAGGI,C.BONACCINI,P.GRATTERI,
JRNL AUTH 2 L.SIM,T.M.GLOSTER,S.ROBERTS,G.J.DAVIES,D.R.ROSE,A.GOTI
JRNL TITL TOTAL SYNTHESES OF CASUARINE AND ITS 6-O-ALPHA-GLUCOSIDE:
JRNL TITL 2 COMPLEMENTARY INHIBITION TOWARDS GLYCOSIDE HYDROLASES OF THE
JRNL TITL 3 GH31 AND GH37 FAMILIES.
JRNL REF CHEMISTRY V. 15 1627 2009
JRNL REFN ISSN 0947-6539
JRNL PMID 19123216
JRNL DOI 10.1002/CHEM.200801578
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0065
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 165333
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8658
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11455
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 611
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 302
REMARK 3 SOLVENT ATOMS : 1770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.74000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -1.80000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.327
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17121 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23502 ; 1.383 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2145 ; 5.290 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 865 ;36.523 ;24.855
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2692 ;14.940 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;11.579 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2498 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13367 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 10231 ; 0.679 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16562 ; 1.197 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6890 ; 1.852 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6861 ; 2.823 ; 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 : 1.20
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 2JJB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1290035785.
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 : 3.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 174266
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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 2JF4
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12 MG/ML PROTEIN. CRYSTALLISED FROM
REMARK 280 1.7M AMMONIUM SULPHATE, 0.1M CITRIC ACID BUFFER, PH 3.5.
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 46.24050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.72550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.93150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.72550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.24050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.93150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -311.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -222.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLU A 31
REMARK 465 GLU A 32
REMARK 465 THR A 33
REMARK 465 PRO A 34
REMARK 465 SER A 86
REMARK 465 GLY A 87
REMARK 465 GLU A 103
REMARK 465 GLY A 104
REMARK 465 GLU A 105
REMARK 465 LYS A 106
REMARK 465 GLY A 507
REMARK 465 GLY A 508
REMARK 465 PRO A 547
REMARK 465 THR A 548
REMARK 465 VAL A 549
REMARK 465 LYS A 550
REMARK 465 SER A 551
REMARK 465 ALA A 552
REMARK 465 THR A 553
REMARK 465 THR A 554
REMARK 465 GLN A 555
REMARK 465 PRO A 556
REMARK 465 SER A 557
REMARK 465 THR A 558
REMARK 465 LYS A 559
REMARK 465 GLU A 560
REMARK 465 ALA A 561
REMARK 465 GLN A 562
REMARK 465 PRO A 563
REMARK 465 THR A 564
REMARK 465 PRO A 565
REMARK 465 GLU B 31
REMARK 465 GLU B 32
REMARK 465 THR B 33
REMARK 465 PRO B 34
REMARK 465 GLU B 103
REMARK 465 GLY B 104
REMARK 465 GLU B 105
REMARK 465 LYS B 106
REMARK 465 TYR B 107
REMARK 465 VAL B 108
REMARK 465 PRO B 109
REMARK 465 PRO B 110
REMARK 465 GLY B 504
REMARK 465 THR B 505
REMARK 465 GLY B 506
REMARK 465 GLY B 507
REMARK 465 GLY B 508
REMARK 465 GLY B 509
REMARK 465 GLY B 510
REMARK 465 GLU B 511
REMARK 465 TYR B 512
REMARK 465 THR B 545
REMARK 465 ARG B 546
REMARK 465 PRO B 547
REMARK 465 THR B 548
REMARK 465 VAL B 549
REMARK 465 LYS B 550
REMARK 465 SER B 551
REMARK 465 ALA B 552
REMARK 465 THR B 553
REMARK 465 THR B 554
REMARK 465 GLN B 555
REMARK 465 PRO B 556
REMARK 465 SER B 557
REMARK 465 THR B 558
REMARK 465 LYS B 559
REMARK 465 GLU B 560
REMARK 465 ALA B 561
REMARK 465 GLN B 562
REMARK 465 PRO B 563
REMARK 465 THR B 564
REMARK 465 PRO B 565
REMARK 465 GLU C 31
REMARK 465 GLU C 32
REMARK 465 THR C 33
REMARK 465 PRO C 34
REMARK 465 VAL C 35
REMARK 465 THR C 36
REMARK 465 PRO C 37
REMARK 465 GLY C 504
REMARK 465 THR C 505
REMARK 465 GLY C 506
REMARK 465 GLY C 507
REMARK 465 GLY C 508
REMARK 465 GLY C 509
REMARK 465 GLY C 510
REMARK 465 GLU C 511
REMARK 465 ARG C 546
REMARK 465 PRO C 547
REMARK 465 THR C 548
REMARK 465 VAL C 549
REMARK 465 LYS C 550
REMARK 465 SER C 551
REMARK 465 ALA C 552
REMARK 465 THR C 553
REMARK 465 THR C 554
REMARK 465 GLN C 555
REMARK 465 PRO C 556
REMARK 465 SER C 557
REMARK 465 THR C 558
REMARK 465 LYS C 559
REMARK 465 GLU C 560
REMARK 465 ALA C 561
REMARK 465 GLN C 562
REMARK 465 PRO C 563
REMARK 465 THR C 564
REMARK 465 PRO C 565
REMARK 465 GLU D 31
REMARK 465 GLU D 32
REMARK 465 THR D 33
REMARK 465 PRO D 34
REMARK 465 SER D 86
REMARK 465 GLU D 103
REMARK 465 GLY D 104
REMARK 465 GLU D 105
REMARK 465 GLY D 504
REMARK 465 THR D 505
REMARK 465 GLY D 506
REMARK 465 GLY D 507
REMARK 465 GLY D 508
REMARK 465 GLY D 509
REMARK 465 GLY D 510
REMARK 465 GLU D 511
REMARK 465 PRO D 547
REMARK 465 THR D 548
REMARK 465 VAL D 549
REMARK 465 LYS D 550
REMARK 465 SER D 551
REMARK 465 ALA D 552
REMARK 465 THR D 553
REMARK 465 THR D 554
REMARK 465 GLN D 555
REMARK 465 PRO D 556
REMARK 465 SER D 557
REMARK 465 THR D 558
REMARK 465 LYS D 559
REMARK 465 GLU D 560
REMARK 465 ALA D 561
REMARK 465 GLN D 562
REMARK 465 PRO D 563
REMARK 465 THR D 564
REMARK 465 PRO D 565
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 GLN A 85 CG CD OE1 NE2
REMARK 470 LYS A 102 CB CG CD CE NZ
REMARK 470 LYS A 135 CB CG CD CE NZ
REMARK 470 LYS A 373 CD CE NZ
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 GLU A 471 CD OE1 OE2
REMARK 470 GLU A 536 CG CD OE1 OE2
REMARK 470 GLN A 537 CD OE1 NE2
REMARK 470 ASN B 84 CB CG OD1 ND2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 LYS B 396 CD CE NZ
REMARK 470 LYS B 416 CG CD CE NZ
REMARK 470 LYS B 470 CD CE NZ
REMARK 470 ARG B 490 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 492 CG CD CE NZ
REMARK 470 LYS B 535 CG CD CE NZ
REMARK 470 GLU C 103 CG CD OE1 OE2
REMARK 470 LYS C 106 CD CE NZ
REMARK 470 LYS C 427 CG CD CE NZ
REMARK 470 LYS C 470 CG CD CE NZ
REMARK 470 GLU C 471 CG CD OE1 OE2
REMARK 470 ARG C 490 CD NE CZ NH1 NH2
REMARK 470 LYS C 492 CG CD CE NZ
REMARK 470 LYS C 535 CG CD CE NZ
REMARK 470 GLU C 536 CB CG CD OE1 OE2
REMARK 470 ALA C 544 CB
REMARK 470 LYS D 102 CD CE NZ
REMARK 470 LYS D 106 CG CD CE NZ
REMARK 470 GLU D 134 CD OE1 OE2
REMARK 470 ARG D 350 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 353 CD CE NZ
REMARK 470 LYS D 373 CG CD CE NZ
REMARK 470 GLN D 383 CG CD OE1 NE2
REMARK 470 LYS D 393 CG CD CE NZ
REMARK 470 LYS D 396 CD CE NZ
REMARK 470 ASN D 399 CB CG OD1 ND2
REMARK 470 LYS D 416 CE NZ
REMARK 470 LYS D 421 CG CD CE NZ
REMARK 470 LYS D 427 CD CE NZ
REMARK 470 LYS D 442 CG CD CE NZ
REMARK 470 LYS D 470 CD CE NZ
REMARK 470 GLU D 471 CB CG CD OE1 OE2
REMARK 470 ARG D 490 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 492 CE NZ
REMARK 470 LYS D 535 CE NZ
REMARK 470 GLN D 537 CG CD OE1 NE2
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 TYR A 158 -70.39 -66.42
REMARK 500 SER A 206 -137.64 -107.55
REMARK 500 LYS A 255 -121.30 46.25
REMARK 500 SER A 280 38.34 -141.25
REMARK 500 TRP A 311 59.22 -96.28
REMARK 500 ARG A 328 52.72 -142.00
REMARK 500 THR A 503 169.86 64.11
REMARK 500 SER B 206 -139.31 -108.91
REMARK 500 LYS B 255 -121.41 45.77
REMARK 500 ARG B 328 53.85 -141.18
REMARK 500 GLN B 537 77.31 -118.06
REMARK 500 GLU C 103 -31.24 -136.41
REMARK 500 TRP C 136 -1.37 77.84
REMARK 500 ARG C 154 33.55 -99.57
REMARK 500 TYR C 158 -71.71 -59.37
REMARK 500 HIS C 173 60.65 -102.98
REMARK 500 SER C 206 -137.19 -105.99
REMARK 500 LYS C 255 -118.60 47.73
REMARK 500 ASP C 357 78.80 -109.08
REMARK 500 ARG D 154 35.46 -96.75
REMARK 500 SER D 206 -137.97 -109.61
REMARK 500 LYS D 255 -117.65 45.19
REMARK 500 ARG D 328 54.84 -141.64
REMARK 500 ARG D 328 57.03 -142.75
REMARK 500 GLN D 469 54.54 -93.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2026 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A2039 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A2060 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A2068 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A2069 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A2074 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A2087 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH A2090 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A2096 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH A2138 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A2141 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH A2160 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A2186 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A2206 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH B2031 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B2040 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B2045 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B2068 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B2072 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B2073 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B2113 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH C2032 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH C2052 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C2055 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C2059 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH C2062 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH C2078 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH C2119 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH D2060 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH D2095 DISTANCE = 7.66 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JG0 RELATED DB: PDB
REMARK 900 FAMILY 37 TREHALASE FROM ESCHERICHIA COLI IN COMPLEX WITH 1-
REMARK 900 THIATREHAZOLIN
REMARK 900 RELATED ID: 2JF4 RELATED DB: PDB
REMARK 900 FAMILY 37 TREHALASE FROM ESCHERICHIA COLI IN COMPLEX WITH
REMARK 900 VALIDOXYLAMINE
REMARK 900 RELATED ID: 2WYN RELATED DB: PDB
REMARK 900 STRUCTURE OF FAMILY 37 TREHALASE FROM ESCHERICHIA COLI IN COMPLEX
REMARK 900 WITH A CASUARINE -6-O-A-D-GLUCOSIDE ANALOGUE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 30 RESIDUES CORRESPOND TO A SIGNAL PEPTIDE THAT
REMARK 999 IS PREDICTED TO HAVE BEEN CLEAVED DURING EXPRESSION OF THE
REMARK 999 PROTEIN.
DBREF 2JJB A 31 565 UNP P13482 TREA_ECOLI 31 565
DBREF 2JJB B 31 565 UNP P13482 TREA_ECOLI 31 565
DBREF 2JJB C 31 565 UNP P13482 TREA_ECOLI 31 565
DBREF 2JJB D 31 565 UNP P13482 TREA_ECOLI 31 565
SEQRES 1 A 535 GLU GLU THR PRO VAL THR PRO GLN PRO PRO ASP ILE LEU
SEQRES 2 A 535 LEU GLY PRO LEU PHE ASN ASP VAL GLN ASN ALA LYS LEU
SEQRES 3 A 535 PHE PRO ASP GLN LYS THR PHE ALA ASP ALA VAL PRO ASN
SEQRES 4 A 535 SER ASP PRO LEU MET ILE LEU ALA ASP TYR ARG MET GLN
SEQRES 5 A 535 GLN ASN GLN SER GLY PHE ASP LEU ARG HIS PHE VAL ASN
SEQRES 6 A 535 VAL ASN PHE THR LEU PRO LYS GLU GLY GLU LYS TYR VAL
SEQRES 7 A 535 PRO PRO GLU GLY GLN SER LEU ARG GLU HIS ILE ASP GLY
SEQRES 8 A 535 LEU TRP PRO VAL LEU THR ARG SER THR GLU ASN THR GLU
SEQRES 9 A 535 LYS TRP ASP SER LEU LEU PRO LEU PRO GLU PRO TYR VAL
SEQRES 10 A 535 VAL PRO GLY GLY ARG PHE ARG GLU VAL TYR TYR TRP ASP
SEQRES 11 A 535 SER TYR PHE THR MET LEU GLY LEU ALA GLU SER GLY HIS
SEQRES 12 A 535 TRP ASP LYS VAL ALA ASP MET VAL ALA ASN PHE ALA HIS
SEQRES 13 A 535 GLU ILE ASP THR TYR GLY HIS ILE PRO ASN GLY ASN ARG
SEQRES 14 A 535 SER TYR TYR LEU SER ARG SER GLN PRO PRO PHE PHE ALA
SEQRES 15 A 535 LEU MET VAL GLU LEU LEU ALA GLN HIS GLU GLY ASP ALA
SEQRES 16 A 535 ALA LEU LYS GLN TYR LEU PRO GLN MET GLN LYS GLU TYR
SEQRES 17 A 535 ALA TYR TRP MET ASP GLY VAL GLU ASN LEU GLN ALA GLY
SEQRES 18 A 535 GLN GLN GLU LYS ARG VAL VAL LYS LEU GLN ASP GLY THR
SEQRES 19 A 535 LEU LEU ASN ARG TYR TRP ASP ASP ARG ASP THR PRO ARG
SEQRES 20 A 535 PRO GLU SER TRP VAL GLU ASP ILE ALA THR ALA LYS SER
SEQRES 21 A 535 ASN PRO ASN ARG PRO ALA THR GLU ILE TYR ARG ASP LEU
SEQRES 22 A 535 ARG SER ALA ALA ALA SER GLY TRP ASP PHE SER SER ARG
SEQRES 23 A 535 TRP MET ASP ASN PRO GLN GLN LEU ASN THR LEU ARG THR
SEQRES 24 A 535 THR SER ILE VAL PRO VAL ASP LEU ASN SER LEU MET PHE
SEQRES 25 A 535 LYS MET GLU LYS ILE LEU ALA ARG ALA SER LYS ALA ALA
SEQRES 26 A 535 GLY ASP ASN ALA MET ALA ASN GLN TYR GLU THR LEU ALA
SEQRES 27 A 535 ASN ALA ARG GLN LYS GLY ILE GLU LYS TYR LEU TRP ASN
SEQRES 28 A 535 ASP GLN GLN GLY TRP TYR ALA ASP TYR ASP LEU LYS SER
SEQRES 29 A 535 HIS LYS VAL ARG ASN GLN LEU THR ALA ALA ALA LEU PHE
SEQRES 30 A 535 PRO LEU TYR VAL ASN ALA ALA ALA LYS ASP ARG ALA ASN
SEQRES 31 A 535 LYS MET ALA THR ALA THR LYS THR HIS LEU LEU GLN PRO
SEQRES 32 A 535 GLY GLY LEU ASN THR THR SER VAL LYS SER GLY GLN GLN
SEQRES 33 A 535 TRP ASP ALA PRO ASN GLY TRP ALA PRO LEU GLN TRP VAL
SEQRES 34 A 535 ALA THR GLU GLY LEU GLN ASN TYR GLY GLN LYS GLU VAL
SEQRES 35 A 535 ALA MET ASP ILE SER TRP HIS PHE LEU THR ASN VAL GLN
SEQRES 36 A 535 HIS THR TYR ASP ARG GLU LYS LYS LEU VAL GLU LYS TYR
SEQRES 37 A 535 ASP VAL SER THR THR GLY THR GLY GLY GLY GLY GLY GLU
SEQRES 38 A 535 TYR PRO LEU GLN ASP GLY PHE GLY TRP THR ASN GLY VAL
SEQRES 39 A 535 THR LEU LYS MET LEU ASP LEU ILE CYS PRO LYS GLU GLN
SEQRES 40 A 535 PRO CYS ASP ASN VAL PRO ALA THR ARG PRO THR VAL LYS
SEQRES 41 A 535 SER ALA THR THR GLN PRO SER THR LYS GLU ALA GLN PRO
SEQRES 42 A 535 THR PRO
SEQRES 1 B 535 GLU GLU THR PRO VAL THR PRO GLN PRO PRO ASP ILE LEU
SEQRES 2 B 535 LEU GLY PRO LEU PHE ASN ASP VAL GLN ASN ALA LYS LEU
SEQRES 3 B 535 PHE PRO ASP GLN LYS THR PHE ALA ASP ALA VAL PRO ASN
SEQRES 4 B 535 SER ASP PRO LEU MET ILE LEU ALA ASP TYR ARG MET GLN
SEQRES 5 B 535 GLN ASN GLN SER GLY PHE ASP LEU ARG HIS PHE VAL ASN
SEQRES 6 B 535 VAL ASN PHE THR LEU PRO LYS GLU GLY GLU LYS TYR VAL
SEQRES 7 B 535 PRO PRO GLU GLY GLN SER LEU ARG GLU HIS ILE ASP GLY
SEQRES 8 B 535 LEU TRP PRO VAL LEU THR ARG SER THR GLU ASN THR GLU
SEQRES 9 B 535 LYS TRP ASP SER LEU LEU PRO LEU PRO GLU PRO TYR VAL
SEQRES 10 B 535 VAL PRO GLY GLY ARG PHE ARG GLU VAL TYR TYR TRP ASP
SEQRES 11 B 535 SER TYR PHE THR MET LEU GLY LEU ALA GLU SER GLY HIS
SEQRES 12 B 535 TRP ASP LYS VAL ALA ASP MET VAL ALA ASN PHE ALA HIS
SEQRES 13 B 535 GLU ILE ASP THR TYR GLY HIS ILE PRO ASN GLY ASN ARG
SEQRES 14 B 535 SER TYR TYR LEU SER ARG SER GLN PRO PRO PHE PHE ALA
SEQRES 15 B 535 LEU MET VAL GLU LEU LEU ALA GLN HIS GLU GLY ASP ALA
SEQRES 16 B 535 ALA LEU LYS GLN TYR LEU PRO GLN MET GLN LYS GLU TYR
SEQRES 17 B 535 ALA TYR TRP MET ASP GLY VAL GLU ASN LEU GLN ALA GLY
SEQRES 18 B 535 GLN GLN GLU LYS ARG VAL VAL LYS LEU GLN ASP GLY THR
SEQRES 19 B 535 LEU LEU ASN ARG TYR TRP ASP ASP ARG ASP THR PRO ARG
SEQRES 20 B 535 PRO GLU SER TRP VAL GLU ASP ILE ALA THR ALA LYS SER
SEQRES 21 B 535 ASN PRO ASN ARG PRO ALA THR GLU ILE TYR ARG ASP LEU
SEQRES 22 B 535 ARG SER ALA ALA ALA SER GLY TRP ASP PHE SER SER ARG
SEQRES 23 B 535 TRP MET ASP ASN PRO GLN GLN LEU ASN THR LEU ARG THR
SEQRES 24 B 535 THR SER ILE VAL PRO VAL ASP LEU ASN SER LEU MET PHE
SEQRES 25 B 535 LYS MET GLU LYS ILE LEU ALA ARG ALA SER LYS ALA ALA
SEQRES 26 B 535 GLY ASP ASN ALA MET ALA ASN GLN TYR GLU THR LEU ALA
SEQRES 27 B 535 ASN ALA ARG GLN LYS GLY ILE GLU LYS TYR LEU TRP ASN
SEQRES 28 B 535 ASP GLN GLN GLY TRP TYR ALA ASP TYR ASP LEU LYS SER
SEQRES 29 B 535 HIS LYS VAL ARG ASN GLN LEU THR ALA ALA ALA LEU PHE
SEQRES 30 B 535 PRO LEU TYR VAL ASN ALA ALA ALA LYS ASP ARG ALA ASN
SEQRES 31 B 535 LYS MET ALA THR ALA THR LYS THR HIS LEU LEU GLN PRO
SEQRES 32 B 535 GLY GLY LEU ASN THR THR SER VAL LYS SER GLY GLN GLN
SEQRES 33 B 535 TRP ASP ALA PRO ASN GLY TRP ALA PRO LEU GLN TRP VAL
SEQRES 34 B 535 ALA THR GLU GLY LEU GLN ASN TYR GLY GLN LYS GLU VAL
SEQRES 35 B 535 ALA MET ASP ILE SER TRP HIS PHE LEU THR ASN VAL GLN
SEQRES 36 B 535 HIS THR TYR ASP ARG GLU LYS LYS LEU VAL GLU LYS TYR
SEQRES 37 B 535 ASP VAL SER THR THR GLY THR GLY GLY GLY GLY GLY GLU
SEQRES 38 B 535 TYR PRO LEU GLN ASP GLY PHE GLY TRP THR ASN GLY VAL
SEQRES 39 B 535 THR LEU LYS MET LEU ASP LEU ILE CYS PRO LYS GLU GLN
SEQRES 40 B 535 PRO CYS ASP ASN VAL PRO ALA THR ARG PRO THR VAL LYS
SEQRES 41 B 535 SER ALA THR THR GLN PRO SER THR LYS GLU ALA GLN PRO
SEQRES 42 B 535 THR PRO
SEQRES 1 C 535 GLU GLU THR PRO VAL THR PRO GLN PRO PRO ASP ILE LEU
SEQRES 2 C 535 LEU GLY PRO LEU PHE ASN ASP VAL GLN ASN ALA LYS LEU
SEQRES 3 C 535 PHE PRO ASP GLN LYS THR PHE ALA ASP ALA VAL PRO ASN
SEQRES 4 C 535 SER ASP PRO LEU MET ILE LEU ALA ASP TYR ARG MET GLN
SEQRES 5 C 535 GLN ASN GLN SER GLY PHE ASP LEU ARG HIS PHE VAL ASN
SEQRES 6 C 535 VAL ASN PHE THR LEU PRO LYS GLU GLY GLU LYS TYR VAL
SEQRES 7 C 535 PRO PRO GLU GLY GLN SER LEU ARG GLU HIS ILE ASP GLY
SEQRES 8 C 535 LEU TRP PRO VAL LEU THR ARG SER THR GLU ASN THR GLU
SEQRES 9 C 535 LYS TRP ASP SER LEU LEU PRO LEU PRO GLU PRO TYR VAL
SEQRES 10 C 535 VAL PRO GLY GLY ARG PHE ARG GLU VAL TYR TYR TRP ASP
SEQRES 11 C 535 SER TYR PHE THR MET LEU GLY LEU ALA GLU SER GLY HIS
SEQRES 12 C 535 TRP ASP LYS VAL ALA ASP MET VAL ALA ASN PHE ALA HIS
SEQRES 13 C 535 GLU ILE ASP THR TYR GLY HIS ILE PRO ASN GLY ASN ARG
SEQRES 14 C 535 SER TYR TYR LEU SER ARG SER GLN PRO PRO PHE PHE ALA
SEQRES 15 C 535 LEU MET VAL GLU LEU LEU ALA GLN HIS GLU GLY ASP ALA
SEQRES 16 C 535 ALA LEU LYS GLN TYR LEU PRO GLN MET GLN LYS GLU TYR
SEQRES 17 C 535 ALA TYR TRP MET ASP GLY VAL GLU ASN LEU GLN ALA GLY
SEQRES 18 C 535 GLN GLN GLU LYS ARG VAL VAL LYS LEU GLN ASP GLY THR
SEQRES 19 C 535 LEU LEU ASN ARG TYR TRP ASP ASP ARG ASP THR PRO ARG
SEQRES 20 C 535 PRO GLU SER TRP VAL GLU ASP ILE ALA THR ALA LYS SER
SEQRES 21 C 535 ASN PRO ASN ARG PRO ALA THR GLU ILE TYR ARG ASP LEU
SEQRES 22 C 535 ARG SER ALA ALA ALA SER GLY TRP ASP PHE SER SER ARG
SEQRES 23 C 535 TRP MET ASP ASN PRO GLN GLN LEU ASN THR LEU ARG THR
SEQRES 24 C 535 THR SER ILE VAL PRO VAL ASP LEU ASN SER LEU MET PHE
SEQRES 25 C 535 LYS MET GLU LYS ILE LEU ALA ARG ALA SER LYS ALA ALA
SEQRES 26 C 535 GLY ASP ASN ALA MET ALA ASN GLN TYR GLU THR LEU ALA
SEQRES 27 C 535 ASN ALA ARG GLN LYS GLY ILE GLU LYS TYR LEU TRP ASN
SEQRES 28 C 535 ASP GLN GLN GLY TRP TYR ALA ASP TYR ASP LEU LYS SER
SEQRES 29 C 535 HIS LYS VAL ARG ASN GLN LEU THR ALA ALA ALA LEU PHE
SEQRES 30 C 535 PRO LEU TYR VAL ASN ALA ALA ALA LYS ASP ARG ALA ASN
SEQRES 31 C 535 LYS MET ALA THR ALA THR LYS THR HIS LEU LEU GLN PRO
SEQRES 32 C 535 GLY GLY LEU ASN THR THR SER VAL LYS SER GLY GLN GLN
SEQRES 33 C 535 TRP ASP ALA PRO ASN GLY TRP ALA PRO LEU GLN TRP VAL
SEQRES 34 C 535 ALA THR GLU GLY LEU GLN ASN TYR GLY GLN LYS GLU VAL
SEQRES 35 C 535 ALA MET ASP ILE SER TRP HIS PHE LEU THR ASN VAL GLN
SEQRES 36 C 535 HIS THR TYR ASP ARG GLU LYS LYS LEU VAL GLU LYS TYR
SEQRES 37 C 535 ASP VAL SER THR THR GLY THR GLY GLY GLY GLY GLY GLU
SEQRES 38 C 535 TYR PRO LEU GLN ASP GLY PHE GLY TRP THR ASN GLY VAL
SEQRES 39 C 535 THR LEU LYS MET LEU ASP LEU ILE CYS PRO LYS GLU GLN
SEQRES 40 C 535 PRO CYS ASP ASN VAL PRO ALA THR ARG PRO THR VAL LYS
SEQRES 41 C 535 SER ALA THR THR GLN PRO SER THR LYS GLU ALA GLN PRO
SEQRES 42 C 535 THR PRO
SEQRES 1 D 535 GLU GLU THR PRO VAL THR PRO GLN PRO PRO ASP ILE LEU
SEQRES 2 D 535 LEU GLY PRO LEU PHE ASN ASP VAL GLN ASN ALA LYS LEU
SEQRES 3 D 535 PHE PRO ASP GLN LYS THR PHE ALA ASP ALA VAL PRO ASN
SEQRES 4 D 535 SER ASP PRO LEU MET ILE LEU ALA ASP TYR ARG MET GLN
SEQRES 5 D 535 GLN ASN GLN SER GLY PHE ASP LEU ARG HIS PHE VAL ASN
SEQRES 6 D 535 VAL ASN PHE THR LEU PRO LYS GLU GLY GLU LYS TYR VAL
SEQRES 7 D 535 PRO PRO GLU GLY GLN SER LEU ARG GLU HIS ILE ASP GLY
SEQRES 8 D 535 LEU TRP PRO VAL LEU THR ARG SER THR GLU ASN THR GLU
SEQRES 9 D 535 LYS TRP ASP SER LEU LEU PRO LEU PRO GLU PRO TYR VAL
SEQRES 10 D 535 VAL PRO GLY GLY ARG PHE ARG GLU VAL TYR TYR TRP ASP
SEQRES 11 D 535 SER TYR PHE THR MET LEU GLY LEU ALA GLU SER GLY HIS
SEQRES 12 D 535 TRP ASP LYS VAL ALA ASP MET VAL ALA ASN PHE ALA HIS
SEQRES 13 D 535 GLU ILE ASP THR TYR GLY HIS ILE PRO ASN GLY ASN ARG
SEQRES 14 D 535 SER TYR TYR LEU SER ARG SER GLN PRO PRO PHE PHE ALA
SEQRES 15 D 535 LEU MET VAL GLU LEU LEU ALA GLN HIS GLU GLY ASP ALA
SEQRES 16 D 535 ALA LEU LYS GLN TYR LEU PRO GLN MET GLN LYS GLU TYR
SEQRES 17 D 535 ALA TYR TRP MET ASP GLY VAL GLU ASN LEU GLN ALA GLY
SEQRES 18 D 535 GLN GLN GLU LYS ARG VAL VAL LYS LEU GLN ASP GLY THR
SEQRES 19 D 535 LEU LEU ASN ARG TYR TRP ASP ASP ARG ASP THR PRO ARG
SEQRES 20 D 535 PRO GLU SER TRP VAL GLU ASP ILE ALA THR ALA LYS SER
SEQRES 21 D 535 ASN PRO ASN ARG PRO ALA THR GLU ILE TYR ARG ASP LEU
SEQRES 22 D 535 ARG SER ALA ALA ALA SER GLY TRP ASP PHE SER SER ARG
SEQRES 23 D 535 TRP MET ASP ASN PRO GLN GLN LEU ASN THR LEU ARG THR
SEQRES 24 D 535 THR SER ILE VAL PRO VAL ASP LEU ASN SER LEU MET PHE
SEQRES 25 D 535 LYS MET GLU LYS ILE LEU ALA ARG ALA SER LYS ALA ALA
SEQRES 26 D 535 GLY ASP ASN ALA MET ALA ASN GLN TYR GLU THR LEU ALA
SEQRES 27 D 535 ASN ALA ARG GLN LYS GLY ILE GLU LYS TYR LEU TRP ASN
SEQRES 28 D 535 ASP GLN GLN GLY TRP TYR ALA ASP TYR ASP LEU LYS SER
SEQRES 29 D 535 HIS LYS VAL ARG ASN GLN LEU THR ALA ALA ALA LEU PHE
SEQRES 30 D 535 PRO LEU TYR VAL ASN ALA ALA ALA LYS ASP ARG ALA ASN
SEQRES 31 D 535 LYS MET ALA THR ALA THR LYS THR HIS LEU LEU GLN PRO
SEQRES 32 D 535 GLY GLY LEU ASN THR THR SER VAL LYS SER GLY GLN GLN
SEQRES 33 D 535 TRP ASP ALA PRO ASN GLY TRP ALA PRO LEU GLN TRP VAL
SEQRES 34 D 535 ALA THR GLU GLY LEU GLN ASN TYR GLY GLN LYS GLU VAL
SEQRES 35 D 535 ALA MET ASP ILE SER TRP HIS PHE LEU THR ASN VAL GLN
SEQRES 36 D 535 HIS THR TYR ASP ARG GLU LYS LYS LEU VAL GLU LYS TYR
SEQRES 37 D 535 ASP VAL SER THR THR GLY THR GLY GLY GLY GLY GLY GLU
SEQRES 38 D 535 TYR PRO LEU GLN ASP GLY PHE GLY TRP THR ASN GLY VAL
SEQRES 39 D 535 THR LEU LYS MET LEU ASP LEU ILE CYS PRO LYS GLU GLN
SEQRES 40 D 535 PRO CYS ASP ASN VAL PRO ALA THR ARG PRO THR VAL LYS
SEQRES 41 D 535 SER ALA THR THR GLN PRO SER THR LYS GLU ALA GLN PRO
SEQRES 42 D 535 THR PRO
HET 3CU A1547 13
HET GLC A1548 12
HET SO4 A1549 5
HET SO4 A1550 5
HET SO4 A1551 5
HET SO4 A1552 5
HET SO4 A1553 5
HET SO4 A1554 5
HET SO4 A1555 5
HET SO4 A1556 5
HET SO4 A1557 5
HET SO4 A1558 5
HET SO4 A1559 5
HET SO4 A1560 5
HET EDO A1561 4
HET 3CU B1545 13
HET GLC B1546 12
HET SO4 B1547 5
HET SO4 B1548 5
HET SO4 B1549 5
HET SO4 B1550 5
HET SO4 B1551 5
HET SO4 B1552 5
HET SO4 B1553 5
HET EDO B1554 4
HET 3CU C1546 13
HET GLC C1547 12
HET SO4 C1548 5
HET SO4 C1549 5
HET SO4 C1550 5
HET SO4 C1551 5
HET SO4 C1552 5
HET SO4 C1553 5
HET SO4 C1554 5
HET SO4 C1555 5
HET SO4 C1556 5
HET SO4 C1557 5
HET SO4 C1558 5
HET EDO C1559 4
HET 3CU D1547 13
HET GLC D1548 12
HET SO4 D1549 5
HET SO4 D1550 5
HET SO4 D1551 5
HET SO4 D1552 5
HET SO4 D1553 5
HET SO4 D1554 5
HET SO4 D1555 5
HET SO4 D1556 5
HETNAM 3CU CASUARINE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN 3CU (1R,2R,3R,6S,7S,7AR)-3-(HYDROXYMETHYL)HEXAHYDRO-1H-
HETSYN 2 3CU PYRROLIZINE-1,2,6,7-TETROL
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 3CU 4(C8 H15 N O5)
FORMUL 6 GLC 4(C6 H12 O6)
FORMUL 7 SO4 38(O4 S 2-)
FORMUL 19 EDO 3(C2 H6 O2)
FORMUL 54 HOH *1770(H2 O)
HELIX 1 1 PRO A 39 LEU A 44 1 6
HELIX 2 2 GLY A 45 ALA A 54 1 10
HELIX 3 3 GLN A 60 ASP A 65 1 6
HELIX 4 4 ASP A 71 ASN A 84 1 14
HELIX 5 5 ASP A 89 ASN A 97 1 9
HELIX 6 6 SER A 114 TRP A 123 1 10
HELIX 7 7 TYR A 157 SER A 171 1 15
HELIX 8 8 HIS A 173 GLY A 192 1 20
HELIX 9 9 SER A 200 LEU A 203 5 4
HELIX 10 10 PHE A 210 GLY A 223 1 14
HELIX 11 11 ASP A 224 MET A 242 1 19
HELIX 12 12 GLY A 244 LEU A 248 5 5
HELIX 13 13 ARG A 277 GLU A 279 5 3
HELIX 14 14 SER A 280 SER A 290 1 11
HELIX 15 15 PRO A 295 GLY A 310 1 16
HELIX 16 16 SER A 314 TRP A 317 5 4
HELIX 17 17 GLN A 323 THR A 326 5 4
HELIX 18 18 ARG A 328 THR A 330 5 3
HELIX 19 19 PRO A 334 ALA A 355 1 22
HELIX 20 20 ASP A 357 LEU A 379 1 23
HELIX 21 21 ALA A 403 ALA A 405 5 3
HELIX 22 22 LEU A 406 VAL A 411 1 6
HELIX 23 23 ALA A 415 LEU A 430 1 16
HELIX 24 24 TRP A 453 ASN A 466 1 14
HELIX 25 25 GLN A 469 LYS A 492 1 24
HELIX 26 26 PHE A 518 CYS A 533 1 16
HELIX 27 27 PRO B 39 LEU B 44 1 6
HELIX 28 28 GLY B 45 ALA B 54 1 10
HELIX 29 29 GLN B 60 ASP B 65 1 6
HELIX 30 30 ASP B 71 ASN B 84 1 14
HELIX 31 31 ASP B 89 ASN B 97 1 9
HELIX 32 32 SER B 114 LEU B 126 1 13
HELIX 33 33 TYR B 157 SER B 171 1 15
HELIX 34 34 HIS B 173 GLY B 192 1 20
HELIX 35 35 SER B 200 LEU B 203 5 4
HELIX 36 36 PHE B 210 GLY B 223 1 14
HELIX 37 37 ASP B 224 MET B 242 1 19
HELIX 38 38 GLY B 244 LEU B 248 5 5
HELIX 39 39 ARG B 277 GLU B 279 5 3
HELIX 40 40 SER B 280 SER B 290 1 11
HELIX 41 41 PRO B 295 SER B 309 1 15
HELIX 42 42 SER B 314 TRP B 317 5 4
HELIX 43 43 GLN B 323 THR B 326 5 4
HELIX 44 44 ARG B 328 THR B 330 5 3
HELIX 45 45 PRO B 334 ALA B 355 1 22
HELIX 46 46 ASP B 357 LEU B 379 1 23
HELIX 47 47 ALA B 403 ALA B 405 5 3
HELIX 48 48 LEU B 406 VAL B 411 1 6
HELIX 49 49 ALA B 415 LEU B 430 1 16
HELIX 50 50 TRP B 453 TYR B 467 1 15
HELIX 51 51 GLN B 469 LYS B 492 1 24
HELIX 52 52 PHE B 518 CYS B 533 1 16
HELIX 53 53 PRO C 39 GLY C 45 1 7
HELIX 54 54 GLY C 45 ALA C 54 1 10
HELIX 55 55 ASP C 59 ASP C 65 1 7
HELIX 56 56 ASP C 71 GLN C 83 1 13
HELIX 57 57 ASP C 89 ASN C 97 1 9
HELIX 58 58 SER C 114 TRP C 123 1 10
HELIX 59 59 TYR C 157 SER C 171 1 15
HELIX 60 60 HIS C 173 GLY C 192 1 20
HELIX 61 61 SER C 200 LEU C 203 5 4
HELIX 62 62 PHE C 210 GLY C 223 1 14
HELIX 63 63 GLY C 223 TYR C 230 1 8
HELIX 64 64 TYR C 230 MET C 242 1 13
HELIX 65 65 GLY C 244 LEU C 248 5 5
HELIX 66 66 ARG C 277 GLU C 279 5 3
HELIX 67 67 SER C 280 SER C 290 1 11
HELIX 68 68 PRO C 295 SER C 309 1 15
HELIX 69 69 SER C 314 TRP C 317 5 4
HELIX 70 70 GLN C 323 THR C 326 5 4
HELIX 71 71 ARG C 328 THR C 330 5 3
HELIX 72 72 PRO C 334 ALA C 355 1 22
HELIX 73 73 ASP C 357 LEU C 379 1 23
HELIX 74 74 ALA C 403 ALA C 405 5 3
HELIX 75 75 LEU C 406 VAL C 411 1 6
HELIX 76 76 ALA C 415 LEU C 430 1 16
HELIX 77 77 TRP C 453 TYR C 467 1 15
HELIX 78 78 GLN C 469 LYS C 492 1 24
HELIX 79 79 PHE C 518 CYS C 533 1 16
HELIX 80 80 PRO D 39 GLY D 45 1 7
HELIX 81 81 GLY D 45 ALA D 54 1 10
HELIX 82 82 GLN D 60 ASP D 65 1 6
HELIX 83 83 ASP D 71 ASN D 84 1 14
HELIX 84 84 ASP D 89 ASN D 97 1 9
HELIX 85 85 SER D 114 TRP D 123 1 10
HELIX 86 86 TYR D 157 SER D 171 1 15
HELIX 87 87 HIS D 173 GLY D 192 1 20
HELIX 88 88 SER D 200 LEU D 203 5 4
HELIX 89 89 PHE D 210 GLY D 223 1 14
HELIX 90 90 GLY D 223 ASP D 243 1 21
HELIX 91 91 GLY D 244 LEU D 248 5 5
HELIX 92 92 ARG D 277 GLU D 279 5 3
HELIX 93 93 SER D 280 SER D 290 1 11
HELIX 94 94 PRO D 295 SER D 309 1 15
HELIX 95 95 SER D 314 TRP D 317 5 4
HELIX 96 96 GLN D 323 THR D 326 5 4
HELIX 97 97 ARG D 328 THR D 330 5 3
HELIX 98 98 PRO D 334 GLY D 356 1 23
HELIX 99 99 ASP D 357 LEU D 379 1 23
HELIX 100 100 ALA D 403 ALA D 405 5 3
HELIX 101 101 LEU D 406 VAL D 411 1 6
HELIX 102 102 ALA D 415 LEU D 430 1 16
HELIX 103 103 TRP D 453 TYR D 467 1 15
HELIX 104 104 GLN D 469 LYS D 492 1 24
HELIX 105 105 PHE D 518 CYS D 533 1 16
SHEET 1 AA 2 VAL A 67 PRO A 68 0
SHEET 2 AA 2 PHE A 98 THR A 99 -1 O THR A 99 N VAL A 67
SHEET 1 AB 2 THR A 127 ARG A 128 0
SHEET 2 AB 2 TYR A 146 VAL A 147 -1 O TYR A 146 N ARG A 128
SHEET 1 AC 3 GLN A 252 GLU A 254 0
SHEET 2 AC 3 VAL A 257 LYS A 259 -1 O VAL A 257 N GLU A 254
SHEET 3 AC 3 LEU A 265 ASN A 267 -1 O LEU A 266 N VAL A 258
SHEET 1 AD 3 ILE A 332 VAL A 333 0
SHEET 2 AD 3 TYR A 390 ASP A 391 -1 O TYR A 390 N VAL A 333
SHEET 3 AD 3 LYS A 396 VAL A 397 -1 O LYS A 396 N ASP A 391
SHEET 1 AE 2 TRP A 380 ASN A 381 0
SHEET 2 AE 2 TRP A 386 TYR A 387 -1 O TRP A 386 N ASN A 381
SHEET 1 AF 2 LEU A 431 GLN A 432 0
SHEET 2 AF 2 GLY A 435 LEU A 436 -1 O GLY A 435 N GLN A 432
SHEET 1 AG 2 ASN A 451 GLY A 452 0
SHEET 2 AG 2 TYR A 498 ASP A 499 -1 O TYR A 498 N GLY A 452
SHEET 1 BA 2 VAL B 67 PRO B 68 0
SHEET 2 BA 2 PHE B 98 THR B 99 -1 O THR B 99 N VAL B 67
SHEET 1 BB 2 THR B 127 ARG B 128 0
SHEET 2 BB 2 TYR B 146 VAL B 147 -1 O TYR B 146 N ARG B 128
SHEET 1 BC 3 GLN B 253 GLU B 254 0
SHEET 2 BC 3 VAL B 257 LYS B 259 -1 O VAL B 257 N GLU B 254
SHEET 3 BC 3 LEU B 265 ASN B 267 -1 O LEU B 266 N VAL B 258
SHEET 1 BD 3 ILE B 332 VAL B 333 0
SHEET 2 BD 3 TYR B 390 ASP B 391 -1 O TYR B 390 N VAL B 333
SHEET 3 BD 3 LYS B 396 VAL B 397 -1 O LYS B 396 N ASP B 391
SHEET 1 BE 2 TRP B 380 ASN B 381 0
SHEET 2 BE 2 TRP B 386 TYR B 387 -1 O TRP B 386 N ASN B 381
SHEET 1 BF 2 LEU B 431 GLN B 432 0
SHEET 2 BF 2 GLY B 435 LEU B 436 -1 O GLY B 435 N GLN B 432
SHEET 1 BG 2 ASN B 451 GLY B 452 0
SHEET 2 BG 2 TYR B 498 ASP B 499 -1 O TYR B 498 N GLY B 452
SHEET 1 CA 2 VAL C 67 PRO C 68 0
SHEET 2 CA 2 PHE C 98 THR C 99 -1 O THR C 99 N VAL C 67
SHEET 1 CB 2 THR C 127 ARG C 128 0
SHEET 2 CB 2 TYR C 146 VAL C 147 -1 O TYR C 146 N ARG C 128
SHEET 1 CC 3 GLN C 252 GLU C 254 0
SHEET 2 CC 3 VAL C 257 LYS C 259 -1 O VAL C 257 N GLU C 254
SHEET 3 CC 3 LEU C 265 ASN C 267 -1 O LEU C 266 N VAL C 258
SHEET 1 CD 3 ILE C 332 VAL C 333 0
SHEET 2 CD 3 TYR C 390 ASP C 391 -1 O TYR C 390 N VAL C 333
SHEET 3 CD 3 LYS C 396 VAL C 397 -1 O LYS C 396 N ASP C 391
SHEET 1 CE 2 TRP C 380 ASN C 381 0
SHEET 2 CE 2 TRP C 386 TYR C 387 -1 O TRP C 386 N ASN C 381
SHEET 1 CF 2 LEU C 431 GLN C 432 0
SHEET 2 CF 2 GLY C 435 LEU C 436 -1 O GLY C 435 N GLN C 432
SHEET 1 CG 2 ASN C 451 GLY C 452 0
SHEET 2 CG 2 TYR C 498 ASP C 499 -1 O TYR C 498 N GLY C 452
SHEET 1 DA 2 VAL D 67 PRO D 68 0
SHEET 2 DA 2 PHE D 98 THR D 99 -1 O THR D 99 N VAL D 67
SHEET 1 DB 2 THR D 127 ARG D 128 0
SHEET 2 DB 2 TYR D 146 VAL D 147 -1 O TYR D 146 N ARG D 128
SHEET 1 DC 3 GLN D 252 GLU D 254 0
SHEET 2 DC 3 VAL D 257 LYS D 259 -1 O VAL D 257 N GLU D 254
SHEET 3 DC 3 LEU D 265 ASN D 267 -1 O LEU D 266 N VAL D 258
SHEET 1 DD 3 ILE D 332 VAL D 333 0
SHEET 2 DD 3 TYR D 390 ASP D 391 -1 O TYR D 390 N VAL D 333
SHEET 3 DD 3 LYS D 396 VAL D 397 -1 O LYS D 396 N ASP D 391
SHEET 1 DE 2 TRP D 380 ASN D 381 0
SHEET 2 DE 2 TRP D 386 TYR D 387 -1 O TRP D 386 N ASN D 381
SHEET 1 DF 2 LEU D 431 GLN D 432 0
SHEET 2 DF 2 GLY D 435 LEU D 436 -1 O GLY D 435 N GLN D 432
SHEET 1 DG 2 ASN D 451 GLY D 452 0
SHEET 2 DG 2 TYR D 498 ASP D 499 -1 O TYR D 498 N GLY D 452
SSBOND 1 CYS A 533 CYS A 539 1555 1555 2.06
SSBOND 2 CYS B 533 CYS B 539 1555 1555 2.05
SSBOND 3 CYS C 533 CYS C 539 1555 1555 2.05
SSBOND 4 CYS D 533 CYS D 539 1555 1555 2.06
LINK C6 3CU A1547 O1 GLC A1548 1555 1555 1.46
LINK C6 3CU B1545 O1 GLC B1546 1555 1555 1.46
LINK C6 3CU C1546 O1 GLC C1547 1555 1555 1.46
LINK C6 3CU D1547 O1 GLC D1548 1555 1555 1.46
CISPEP 1 ASP A 312 PHE A 313 0 -2.63
CISPEP 2 ALA A 449 PRO A 450 0 3.04
CISPEP 3 GLY A 517 PHE A 518 0 -7.89
CISPEP 4 ASP B 312 PHE B 313 0 -0.39
CISPEP 5 ALA B 449 PRO B 450 0 -0.48
CISPEP 6 GLY B 517 PHE B 518 0 -10.34
CISPEP 7 ASP C 312 PHE C 313 0 -4.62
CISPEP 8 ALA C 449 PRO C 450 0 2.71
CISPEP 9 GLY C 517 PHE C 518 0 -10.18
CISPEP 10 ASP D 312 PHE D 313 0 3.41
CISPEP 11 ALA D 449 PRO D 450 0 3.22
CISPEP 12 GLY D 517 PHE D 518 0 -11.66
CRYST1 92.481 117.863 203.451 90.00 90.00 90.00 P 21 21 21 16
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 0.010813 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004915 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
