HEADER SUGAR BINDING PROTEIN 18-MAY-12 3VT0
TITLE CRYSTAL STRUCTURE OF CT1,3GAL43A IN COMPLEX WITH LACTOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RICIN B LECTIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 31-520;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 203119;
SOURCE 4 STRAIN: ATCC 27405;
SOURCE 5 GENE: CTHE_0661;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS GH43, CBM13, GALACTAN HYDROLYSIS, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.JIANG,J.FAN,X.WANG,Y.ZHAO,B.HUANG,X.C.ZHANG
REVDAT 3 20-MAR-24 3VT0 1 HETSYN
REVDAT 2 29-JUL-20 3VT0 1 COMPND REMARK SEQADV HET
REVDAT 2 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 2 3 1 SITE ATOM
REVDAT 1 05-DEC-12 3VT0 0
JRNL AUTH D.JIANG,J.FAN,X.WANG,Y.ZHAO,B.HUANG,J.LIU,X.C.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF 1,3GAL43A, AN EXO-BETA-1,3-GALACTANASE
JRNL TITL 2 FROM CLOSTRIDIUM THERMOCELLUM
JRNL REF J.STRUCT.BIOL. V. 180 447 2012
JRNL REFN ISSN 1047-8477
JRNL PMID 22960181
JRNL DOI 10.1016/J.JSB.2012.08.005
REMARK 2
REMARK 2 RESOLUTION. 2.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
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) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 117178
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2115
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 49.2938 - 7.1782 1.00 8109 151 0.2298 0.2455
REMARK 3 2 7.1782 - 5.7003 1.00 7860 146 0.2367 0.2744
REMARK 3 3 5.7003 - 4.9805 1.00 7788 140 0.2310 0.2733
REMARK 3 4 4.9805 - 4.5255 1.00 7709 141 0.1983 0.2043
REMARK 3 5 4.5255 - 4.2013 1.00 7743 142 0.2096 0.2219
REMARK 3 6 4.2013 - 3.9537 1.00 7663 144 0.2246 0.2156
REMARK 3 7 3.9537 - 3.7558 1.00 7692 139 0.2493 0.2362
REMARK 3 8 3.7558 - 3.5924 1.00 7630 138 0.2621 0.2744
REMARK 3 9 3.5924 - 3.4541 1.00 7675 138 0.2827 0.3100
REMARK 3 10 3.4541 - 3.3349 1.00 7640 138 0.2949 0.2997
REMARK 3 11 3.3349 - 3.2307 1.00 7624 141 0.3101 0.3518
REMARK 3 12 3.2307 - 3.1383 1.00 7604 140 0.3356 0.3690
REMARK 3 13 3.1383 - 3.0557 1.00 7630 140 0.3477 0.3447
REMARK 3 14 3.0557 - 2.9812 1.00 7592 135 0.3633 0.3840
REMARK 3 15 2.9812 - 2.9134 0.94 7104 142 0.3843 0.3732
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 31.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 18.74700
REMARK 3 B22 (A**2) : -3.25610
REMARK 3 B33 (A**2) : -15.49100
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 : 0.002 22876
REMARK 3 ANGLE : 0.463 31040
REMARK 3 CHIRALITY : 0.033 3203
REMARK 3 PLANARITY : 0.001 3975
REMARK 3 DIHEDRAL : 9.495 8092
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 3VT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000095463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979150
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.13800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.70300
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE, 2.9-3.3M SODIUM
REMARK 280 CHLORIDE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 53.84700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 202.32800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.18800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 202.32800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.84700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.18800
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, 3, 4, 5, 6
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, G
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H
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: 3
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: C, I
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: 4
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: 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 350
REMARK 350 BIOMOLECULE: 5
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: E, J
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: 6
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: F, K, L
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 MET A -35
REMARK 465 GLY A -34
REMARK 465 SER A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 SER A -25
REMARK 465 SER A -24
REMARK 465 GLY A -23
REMARK 465 LEU A -22
REMARK 465 VAL A -21
REMARK 465 PRO A -20
REMARK 465 ARG A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 MET A -15
REMARK 465 ALA A -14
REMARK 465 SER A -13
REMARK 465 MET A -12
REMARK 465 THR A -11
REMARK 465 GLY A -10
REMARK 465 GLY A -9
REMARK 465 GLN A -8
REMARK 465 GLN A -7
REMARK 465 MET A -6
REMARK 465 GLY A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 ALA A 31
REMARK 465 ALA A 32
REMARK 465 SER A 494
REMARK 465 SER A 495
REMARK 465 PRO A 496
REMARK 465 GLU A 497
REMARK 465 PRO A 498
REMARK 465 SER A 499
REMARK 465 PRO A 500
REMARK 465 SER A 501
REMARK 465 PRO A 502
REMARK 465 SER A 503
REMARK 465 PRO A 504
REMARK 465 GLN A 505
REMARK 465 VAL A 506
REMARK 465 VAL A 507
REMARK 465 LYS A 508
REMARK 465 GLY A 509
REMARK 465 ASP A 510
REMARK 465 VAL A 511
REMARK 465 ASN A 512
REMARK 465 GLY A 513
REMARK 465 ASP A 514
REMARK 465 LEU A 515
REMARK 465 LYS A 516
REMARK 465 VAL A 517
REMARK 465 ASN A 518
REMARK 465 SER A 519
REMARK 465 THR A 520
REMARK 465 MET B -35
REMARK 465 GLY B -34
REMARK 465 SER B -33
REMARK 465 SER B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 SER B -25
REMARK 465 SER B -24
REMARK 465 GLY B -23
REMARK 465 LEU B -22
REMARK 465 VAL B -21
REMARK 465 PRO B -20
REMARK 465 ARG B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 MET B -15
REMARK 465 ALA B -14
REMARK 465 SER B -13
REMARK 465 MET B -12
REMARK 465 THR B -11
REMARK 465 GLY B -10
REMARK 465 GLY B -9
REMARK 465 GLN B -8
REMARK 465 GLN B -7
REMARK 465 MET B -6
REMARK 465 GLY B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 ALA B 31
REMARK 465 ALA B 32
REMARK 465 SER B 494
REMARK 465 SER B 495
REMARK 465 PRO B 496
REMARK 465 GLU B 497
REMARK 465 PRO B 498
REMARK 465 SER B 499
REMARK 465 PRO B 500
REMARK 465 SER B 501
REMARK 465 PRO B 502
REMARK 465 SER B 503
REMARK 465 PRO B 504
REMARK 465 GLN B 505
REMARK 465 VAL B 506
REMARK 465 VAL B 507
REMARK 465 LYS B 508
REMARK 465 GLY B 509
REMARK 465 ASP B 510
REMARK 465 VAL B 511
REMARK 465 ASN B 512
REMARK 465 GLY B 513
REMARK 465 ASP B 514
REMARK 465 LEU B 515
REMARK 465 LYS B 516
REMARK 465 VAL B 517
REMARK 465 ASN B 518
REMARK 465 SER B 519
REMARK 465 THR B 520
REMARK 465 MET C -35
REMARK 465 GLY C -34
REMARK 465 SER C -33
REMARK 465 SER C -32
REMARK 465 HIS C -31
REMARK 465 HIS C -30
REMARK 465 HIS C -29
REMARK 465 HIS C -28
REMARK 465 HIS C -27
REMARK 465 HIS C -26
REMARK 465 SER C -25
REMARK 465 SER C -24
REMARK 465 GLY C -23
REMARK 465 LEU C -22
REMARK 465 VAL C -21
REMARK 465 PRO C -20
REMARK 465 ARG C -19
REMARK 465 SER C 494
REMARK 465 SER C 495
REMARK 465 PRO C 496
REMARK 465 GLU C 497
REMARK 465 PRO C 498
REMARK 465 SER C 499
REMARK 465 PRO C 500
REMARK 465 SER C 501
REMARK 465 PRO C 502
REMARK 465 SER C 503
REMARK 465 PRO C 504
REMARK 465 GLN C 505
REMARK 465 VAL C 506
REMARK 465 VAL C 507
REMARK 465 LYS C 508
REMARK 465 GLY C 509
REMARK 465 ASP C 510
REMARK 465 VAL C 511
REMARK 465 ASN C 512
REMARK 465 GLY C 513
REMARK 465 ASP C 514
REMARK 465 LEU C 515
REMARK 465 LYS C 516
REMARK 465 VAL C 517
REMARK 465 ASN C 518
REMARK 465 SER C 519
REMARK 465 THR C 520
REMARK 465 MET D -35
REMARK 465 GLY D -34
REMARK 465 SER D -33
REMARK 465 SER D -32
REMARK 465 HIS D -31
REMARK 465 HIS D -30
REMARK 465 HIS D -29
REMARK 465 HIS D -28
REMARK 465 HIS D -27
REMARK 465 HIS D -26
REMARK 465 SER D -25
REMARK 465 SER D -24
REMARK 465 GLY D -23
REMARK 465 LEU D -22
REMARK 465 VAL D -21
REMARK 465 PRO D -20
REMARK 465 ARG D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 MET D -15
REMARK 465 ALA D -14
REMARK 465 SER D -13
REMARK 465 MET D -12
REMARK 465 THR D -11
REMARK 465 GLY D -10
REMARK 465 GLY D -9
REMARK 465 GLN D -8
REMARK 465 GLN D -7
REMARK 465 MET D -6
REMARK 465 GLY D -5
REMARK 465 ARG D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 PHE D 0
REMARK 465 ALA D 31
REMARK 465 ALA D 32
REMARK 465 SER D 494
REMARK 465 SER D 495
REMARK 465 PRO D 496
REMARK 465 GLU D 497
REMARK 465 PRO D 498
REMARK 465 SER D 499
REMARK 465 PRO D 500
REMARK 465 SER D 501
REMARK 465 PRO D 502
REMARK 465 SER D 503
REMARK 465 PRO D 504
REMARK 465 GLN D 505
REMARK 465 VAL D 506
REMARK 465 VAL D 507
REMARK 465 LYS D 508
REMARK 465 GLY D 509
REMARK 465 ASP D 510
REMARK 465 VAL D 511
REMARK 465 ASN D 512
REMARK 465 GLY D 513
REMARK 465 ASP D 514
REMARK 465 LEU D 515
REMARK 465 LYS D 516
REMARK 465 VAL D 517
REMARK 465 ASN D 518
REMARK 465 SER D 519
REMARK 465 THR D 520
REMARK 465 MET E -35
REMARK 465 GLY E -34
REMARK 465 SER E -33
REMARK 465 SER E -32
REMARK 465 HIS E -31
REMARK 465 HIS E -30
REMARK 465 HIS E -29
REMARK 465 HIS E -28
REMARK 465 HIS E -27
REMARK 465 HIS E -26
REMARK 465 SER E -25
REMARK 465 SER E -24
REMARK 465 GLY E -23
REMARK 465 LEU E -22
REMARK 465 VAL E -21
REMARK 465 PRO E -20
REMARK 465 ARG E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 HIS E -16
REMARK 465 MET E -15
REMARK 465 ALA E -14
REMARK 465 SER E -13
REMARK 465 MET E -12
REMARK 465 THR E -11
REMARK 465 GLY E -10
REMARK 465 GLY E -9
REMARK 465 GLN E -8
REMARK 465 GLN E -7
REMARK 465 MET E -6
REMARK 465 GLY E -5
REMARK 465 ARG E -4
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 GLU E -1
REMARK 465 PHE E 0
REMARK 465 ALA E 31
REMARK 465 ALA E 32
REMARK 465 SER E 494
REMARK 465 SER E 495
REMARK 465 PRO E 496
REMARK 465 GLU E 497
REMARK 465 PRO E 498
REMARK 465 SER E 499
REMARK 465 PRO E 500
REMARK 465 SER E 501
REMARK 465 PRO E 502
REMARK 465 SER E 503
REMARK 465 PRO E 504
REMARK 465 GLN E 505
REMARK 465 VAL E 506
REMARK 465 VAL E 507
REMARK 465 LYS E 508
REMARK 465 GLY E 509
REMARK 465 ASP E 510
REMARK 465 VAL E 511
REMARK 465 ASN E 512
REMARK 465 GLY E 513
REMARK 465 ASP E 514
REMARK 465 LEU E 515
REMARK 465 LYS E 516
REMARK 465 VAL E 517
REMARK 465 ASN E 518
REMARK 465 SER E 519
REMARK 465 THR E 520
REMARK 465 MET F -35
REMARK 465 GLY F -34
REMARK 465 SER F -33
REMARK 465 SER F -32
REMARK 465 HIS F -31
REMARK 465 HIS F -30
REMARK 465 HIS F -29
REMARK 465 HIS F -28
REMARK 465 HIS F -27
REMARK 465 HIS F -26
REMARK 465 SER F -25
REMARK 465 SER F -24
REMARK 465 GLY F -23
REMARK 465 LEU F -22
REMARK 465 VAL F -21
REMARK 465 PRO F -20
REMARK 465 ARG F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 HIS F -16
REMARK 465 MET F -15
REMARK 465 ALA F -14
REMARK 465 SER F -13
REMARK 465 MET F -12
REMARK 465 THR F -11
REMARK 465 GLY F -10
REMARK 465 GLY F -9
REMARK 465 GLN F -8
REMARK 465 GLN F -7
REMARK 465 MET F -6
REMARK 465 GLY F -5
REMARK 465 ARG F -4
REMARK 465 GLY F -3
REMARK 465 SER F -2
REMARK 465 GLU F -1
REMARK 465 PHE F 0
REMARK 465 ALA F 31
REMARK 465 ALA F 32
REMARK 465 SER F 494
REMARK 465 SER F 495
REMARK 465 PRO F 496
REMARK 465 GLU F 497
REMARK 465 PRO F 498
REMARK 465 SER F 499
REMARK 465 PRO F 500
REMARK 465 SER F 501
REMARK 465 PRO F 502
REMARK 465 SER F 503
REMARK 465 PRO F 504
REMARK 465 GLN F 505
REMARK 465 VAL F 506
REMARK 465 VAL F 507
REMARK 465 LYS F 508
REMARK 465 GLY F 509
REMARK 465 ASP F 510
REMARK 465 VAL F 511
REMARK 465 ASN F 512
REMARK 465 GLY F 513
REMARK 465 ASP F 514
REMARK 465 LEU F 515
REMARK 465 LYS F 516
REMARK 465 VAL F 517
REMARK 465 ASN F 518
REMARK 465 SER F 519
REMARK 465 THR F 520
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 ASP A 72 -142.01 -121.26
REMARK 500 MET A 129 -177.67 -170.09
REMARK 500 ILE A 157 -73.61 -103.91
REMARK 500 HIS A 171 60.27 64.52
REMARK 500 ARG A 179 -113.95 -104.34
REMARK 500 TYR A 212 -9.71 69.95
REMARK 500 ARG A 236 -80.54 -126.25
REMARK 500 ASP A 386 103.15 -57.27
REMARK 500 ASP A 480 98.78 -65.22
REMARK 500 ASP B 72 -162.55 -103.58
REMARK 500 ARG B 113 60.16 60.79
REMARK 500 TYR B 137 48.34 -106.19
REMARK 500 ALA B 140 72.96 44.75
REMARK 500 ILE B 157 -80.38 -97.21
REMARK 500 PRO B 162 121.95 -39.85
REMARK 500 THR B 166 1.48 -69.78
REMARK 500 ARG B 179 -111.58 -102.58
REMARK 500 TYR B 212 -0.09 66.79
REMARK 500 SER B 217 -171.85 -172.38
REMARK 500 ALA B 230 63.94 36.82
REMARK 500 ASN B 363 -70.60 -59.17
REMARK 500 ASP B 386 105.26 -58.36
REMARK 500 ASP B 448 -154.77 58.73
REMARK 500 HIS C 51 78.02 -116.23
REMARK 500 ASP C 72 -151.31 -113.37
REMARK 500 ILE C 157 -70.31 -101.22
REMARK 500 HIS C 171 62.29 63.84
REMARK 500 ARG C 179 -114.24 -96.67
REMARK 500 TYR C 212 -0.21 66.36
REMARK 500 GLN C 227 60.35 60.71
REMARK 500 ARG C 236 -85.16 -117.70
REMARK 500 ASN C 237 71.82 -111.98
REMARK 500 PHE C 285 144.20 -173.01
REMARK 500 ASP C 386 108.52 -54.69
REMARK 500 ASP D 72 -140.77 -115.10
REMARK 500 ALA D 103 147.23 -170.87
REMARK 500 ALA D 140 70.71 44.61
REMARK 500 ILE D 157 -71.58 -94.85
REMARK 500 ARG D 179 -110.85 -108.72
REMARK 500 TYR D 212 -5.87 68.11
REMARK 500 ALA D 230 59.94 36.82
REMARK 500 ARG D 236 -93.50 -114.05
REMARK 500 ASN D 237 71.15 -116.09
REMARK 500 THR D 248 45.81 -142.39
REMARK 500 LYS D 362 -72.50 -58.54
REMARK 500 SER D 433 105.79 -57.80
REMARK 500 ASP D 448 4.38 -62.40
REMARK 500 ILE D 453 177.94 -59.23
REMARK 500 TRP D 467 16.22 59.57
REMARK 500 THR D 484 28.58 -76.95
REMARK 500
REMARK 500 THIS ENTRY HAS 73 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VSF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 1,3GAL43A, AN EXO-BETA-1,3-GALACTANASE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM
REMARK 900 RELATED ID: 3VSZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CT1,3GAL43A IN COMPLEX WITH GALACTAN
REMARK 900 RELATED ID: 3VT1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CT1,3GAL43A IN COMPLEX WITH GALACTOSE
REMARK 900 RELATED ID: 3VT2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CT1,3GAL43A IN COMPLEX WITH ISOPROPY-BETA-D-
REMARK 900 THIOGALACTOSIDE
DBREF 3VT0 A 31 520 UNP A3DD67 A3DD67_CLOTH 31 520
DBREF 3VT0 B 31 520 UNP A3DD67 A3DD67_CLOTH 31 520
DBREF 3VT0 C 31 520 UNP A3DD67 A3DD67_CLOTH 31 520
DBREF 3VT0 D 31 520 UNP A3DD67 A3DD67_CLOTH 31 520
DBREF 3VT0 E 31 520 UNP A3DD67 A3DD67_CLOTH 31 520
DBREF 3VT0 F 31 520 UNP A3DD67 A3DD67_CLOTH 31 520
SEQADV 3VT0 MET A -35 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -34 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -33 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -32 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -31 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -30 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -29 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -28 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -27 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -26 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -25 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -24 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -23 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 LEU A -22 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 VAL A -21 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PRO A -20 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG A -19 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -18 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -17 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS A -16 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET A -15 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ALA A -14 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -13 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET A -12 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 THR A -11 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -10 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -9 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN A -8 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN A -7 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET A -6 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -5 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG A -4 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY A -3 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER A -2 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLU A -1 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PHE A 0 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET B -35 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -34 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -33 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -32 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -31 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -30 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -29 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -28 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -27 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -26 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -25 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -24 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -23 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 LEU B -22 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 VAL B -21 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PRO B -20 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG B -19 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -18 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -17 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS B -16 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET B -15 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ALA B -14 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -13 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET B -12 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 THR B -11 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -10 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -9 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN B -8 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN B -7 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET B -6 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -5 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG B -4 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY B -3 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER B -2 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLU B -1 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PHE B 0 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET C -35 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -34 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -33 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -32 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -31 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -30 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -29 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -28 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -27 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -26 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -25 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -24 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -23 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 LEU C -22 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 VAL C -21 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PRO C -20 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG C -19 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -18 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -17 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS C -16 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET C -15 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ALA C -14 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -13 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET C -12 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 THR C -11 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -10 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -9 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN C -8 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN C -7 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET C -6 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -5 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG C -4 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY C -3 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER C -2 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLU C -1 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PHE C 0 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET D -35 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -34 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -33 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -32 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -31 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -30 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -29 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -28 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -27 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -26 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -25 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -24 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -23 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 LEU D -22 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 VAL D -21 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PRO D -20 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG D -19 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -18 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -17 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS D -16 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET D -15 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ALA D -14 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -13 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET D -12 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 THR D -11 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -10 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -9 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN D -8 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN D -7 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET D -6 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -5 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG D -4 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY D -3 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER D -2 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLU D -1 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PHE D 0 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET E -35 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -34 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -33 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -32 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -31 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -30 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -29 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -28 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -27 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -26 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -25 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -24 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -23 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 LEU E -22 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 VAL E -21 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PRO E -20 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG E -19 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -18 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -17 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS E -16 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET E -15 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ALA E -14 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -13 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET E -12 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 THR E -11 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -10 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -9 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN E -8 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN E -7 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET E -6 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -5 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG E -4 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY E -3 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER E -2 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLU E -1 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PHE E 0 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET F -35 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -34 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -33 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -32 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -31 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -30 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -29 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -28 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -27 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -26 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -25 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -24 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -23 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 LEU F -22 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 VAL F -21 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PRO F -20 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG F -19 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -18 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -17 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 HIS F -16 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET F -15 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ALA F -14 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -13 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET F -12 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 THR F -11 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -10 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -9 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN F -8 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLN F -7 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 MET F -6 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -5 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 ARG F -4 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLY F -3 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 SER F -2 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 GLU F -1 UNP A3DD67 EXPRESSION TAG
SEQADV 3VT0 PHE F 0 UNP A3DD67 EXPRESSION TAG
SEQRES 1 A 526 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 526 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 526 GLY GLN GLN MET GLY ARG GLY SER GLU PHE ALA ALA GLU
SEQRES 4 A 526 GLY VAL ILE VAL ASN GLY THR GLN PHE LYS ASP THR SER
SEQRES 5 A 526 GLY ASN VAL ILE HIS ALA HIS GLY GLY GLY MET LEU LYS
SEQRES 6 A 526 HIS GLY ASP TYR TYR TYR TRP TYR GLY GLU TYR ARG ASP
SEQRES 7 A 526 ASP SER ASN LEU PHE LEU GLY VAL SER CYS TYR ARG SER
SEQRES 8 A 526 LYS ASP LEU VAL ASN TRP GLU TYR ARG GLY GLU VAL LEU
SEQRES 9 A 526 SER ARG ASN SER ALA PRO GLU LEU ASN HIS CYS ASN ILE
SEQRES 10 A 526 GLU ARG PRO LYS VAL MET TYR ASN ALA SER THR GLY GLU
SEQRES 11 A 526 PHE VAL MET TRP MET HIS TRP GLU ASN GLY ILE ASN TYR
SEQRES 12 A 526 GLY GLN ALA ARG ALA ALA VAL ALA TYR SER LYS THR PRO
SEQRES 13 A 526 ASP GLY LYS PHE THR TYR ILE ARG SER PHE ARG PRO MET
SEQRES 14 A 526 GLN ASP THR GLY VAL MET ASP HIS GLY LEU PRO GLY TYR
SEQRES 15 A 526 MET SER ARG ASP CYS ASN VAL PHE VAL ASP THR ASP GLY
SEQRES 16 A 526 LYS GLY TYR PHE ILE SER ALA ALA ASN GLU ASN MET ASP
SEQRES 17 A 526 LEU HIS LEU TYR GLU LEU THR PRO ASP TYR LYS ASN ILE
SEQRES 18 A 526 ALA SER LEU LYS ALA LYS LEU PHE VAL GLY GLN GLN ARG
SEQRES 19 A 526 GLU ALA PRO CYS LEU ILE LYS ARG ASN GLY TYR TYR TYR
SEQRES 20 A 526 LEU ILE THR SER GLY CYS THR GLY TRP ASN PRO ASN GLN
SEQRES 21 A 526 ALA LYS TYR ALA TYR SER LYS ASP LEU ALA SER GLY TRP
SEQRES 22 A 526 SER GLN LEU TYR ASN LEU GLY ASN SER THR THR TYR ARG
SEQRES 23 A 526 SER GLN PRO THR PHE ILE ILE PRO VAL GLN GLY SER SER
SEQRES 24 A 526 GLY THR SER TYR LEU TYR MET GLY ASP ARG TRP ALA GLY
SEQRES 25 A 526 ALA TRP GLY GLY LYS VAL ASN ASP SER GLN TYR VAL TRP
SEQRES 26 A 526 LEU PRO LEU ASN PHE ILE SER ASP THR THR LEU GLU LEU
SEQRES 27 A 526 PRO TYR TYR ASP SER VAL LYS ILE ASP ALA SER SER GLY
SEQRES 28 A 526 ILE ILE SER GLU TYR ILE PRO ASP THR THR ARG TYR LYS
SEQRES 29 A 526 LEU VAL ASN LYS ASN SER GLY LYS VAL LEU ASP VAL LEU
SEQRES 30 A 526 ASP GLY SER VAL ASP ASN ALA ALA GLN ILE VAL GLN TRP
SEQRES 31 A 526 THR ASP ASN GLY SER LEU SER GLN GLN TRP TYR LEU VAL
SEQRES 32 A 526 ASP VAL GLY GLY GLY TYR LYS LYS ILE VAL ASN VAL LYS
SEQRES 33 A 526 SER GLY ARG ALA LEU ASP VAL LYS ASP GLU SER LYS GLU
SEQRES 34 A 526 ASP GLY GLY VAL LEU ILE GLN TYR THR SER ASN GLY GLY
SEQRES 35 A 526 TYR ASN GLN HIS TRP LYS PHE THR ASP ILE GLY ASP GLY
SEQRES 36 A 526 TYR TYR LYS ILE SER SER ARG HIS CYS GLY LYS LEU ILE
SEQRES 37 A 526 ASP VAL ARG LYS TRP SER THR GLU ASP GLY GLY ILE ILE
SEQRES 38 A 526 GLN GLN TRP SER ASP ALA GLY GLY THR ASN GLN HIS TRP
SEQRES 39 A 526 LYS LEU VAL LEU VAL SER SER PRO GLU PRO SER PRO SER
SEQRES 40 A 526 PRO SER PRO GLN VAL VAL LYS GLY ASP VAL ASN GLY ASP
SEQRES 41 A 526 LEU LYS VAL ASN SER THR
SEQRES 1 B 526 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 526 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 526 GLY GLN GLN MET GLY ARG GLY SER GLU PHE ALA ALA GLU
SEQRES 4 B 526 GLY VAL ILE VAL ASN GLY THR GLN PHE LYS ASP THR SER
SEQRES 5 B 526 GLY ASN VAL ILE HIS ALA HIS GLY GLY GLY MET LEU LYS
SEQRES 6 B 526 HIS GLY ASP TYR TYR TYR TRP TYR GLY GLU TYR ARG ASP
SEQRES 7 B 526 ASP SER ASN LEU PHE LEU GLY VAL SER CYS TYR ARG SER
SEQRES 8 B 526 LYS ASP LEU VAL ASN TRP GLU TYR ARG GLY GLU VAL LEU
SEQRES 9 B 526 SER ARG ASN SER ALA PRO GLU LEU ASN HIS CYS ASN ILE
SEQRES 10 B 526 GLU ARG PRO LYS VAL MET TYR ASN ALA SER THR GLY GLU
SEQRES 11 B 526 PHE VAL MET TRP MET HIS TRP GLU ASN GLY ILE ASN TYR
SEQRES 12 B 526 GLY GLN ALA ARG ALA ALA VAL ALA TYR SER LYS THR PRO
SEQRES 13 B 526 ASP GLY LYS PHE THR TYR ILE ARG SER PHE ARG PRO MET
SEQRES 14 B 526 GLN ASP THR GLY VAL MET ASP HIS GLY LEU PRO GLY TYR
SEQRES 15 B 526 MET SER ARG ASP CYS ASN VAL PHE VAL ASP THR ASP GLY
SEQRES 16 B 526 LYS GLY TYR PHE ILE SER ALA ALA ASN GLU ASN MET ASP
SEQRES 17 B 526 LEU HIS LEU TYR GLU LEU THR PRO ASP TYR LYS ASN ILE
SEQRES 18 B 526 ALA SER LEU LYS ALA LYS LEU PHE VAL GLY GLN GLN ARG
SEQRES 19 B 526 GLU ALA PRO CYS LEU ILE LYS ARG ASN GLY TYR TYR TYR
SEQRES 20 B 526 LEU ILE THR SER GLY CYS THR GLY TRP ASN PRO ASN GLN
SEQRES 21 B 526 ALA LYS TYR ALA TYR SER LYS ASP LEU ALA SER GLY TRP
SEQRES 22 B 526 SER GLN LEU TYR ASN LEU GLY ASN SER THR THR TYR ARG
SEQRES 23 B 526 SER GLN PRO THR PHE ILE ILE PRO VAL GLN GLY SER SER
SEQRES 24 B 526 GLY THR SER TYR LEU TYR MET GLY ASP ARG TRP ALA GLY
SEQRES 25 B 526 ALA TRP GLY GLY LYS VAL ASN ASP SER GLN TYR VAL TRP
SEQRES 26 B 526 LEU PRO LEU ASN PHE ILE SER ASP THR THR LEU GLU LEU
SEQRES 27 B 526 PRO TYR TYR ASP SER VAL LYS ILE ASP ALA SER SER GLY
SEQRES 28 B 526 ILE ILE SER GLU TYR ILE PRO ASP THR THR ARG TYR LYS
SEQRES 29 B 526 LEU VAL ASN LYS ASN SER GLY LYS VAL LEU ASP VAL LEU
SEQRES 30 B 526 ASP GLY SER VAL ASP ASN ALA ALA GLN ILE VAL GLN TRP
SEQRES 31 B 526 THR ASP ASN GLY SER LEU SER GLN GLN TRP TYR LEU VAL
SEQRES 32 B 526 ASP VAL GLY GLY GLY TYR LYS LYS ILE VAL ASN VAL LYS
SEQRES 33 B 526 SER GLY ARG ALA LEU ASP VAL LYS ASP GLU SER LYS GLU
SEQRES 34 B 526 ASP GLY GLY VAL LEU ILE GLN TYR THR SER ASN GLY GLY
SEQRES 35 B 526 TYR ASN GLN HIS TRP LYS PHE THR ASP ILE GLY ASP GLY
SEQRES 36 B 526 TYR TYR LYS ILE SER SER ARG HIS CYS GLY LYS LEU ILE
SEQRES 37 B 526 ASP VAL ARG LYS TRP SER THR GLU ASP GLY GLY ILE ILE
SEQRES 38 B 526 GLN GLN TRP SER ASP ALA GLY GLY THR ASN GLN HIS TRP
SEQRES 39 B 526 LYS LEU VAL LEU VAL SER SER PRO GLU PRO SER PRO SER
SEQRES 40 B 526 PRO SER PRO GLN VAL VAL LYS GLY ASP VAL ASN GLY ASP
SEQRES 41 B 526 LEU LYS VAL ASN SER THR
SEQRES 1 C 526 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 526 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 C 526 GLY GLN GLN MET GLY ARG GLY SER GLU PHE ALA ALA GLU
SEQRES 4 C 526 GLY VAL ILE VAL ASN GLY THR GLN PHE LYS ASP THR SER
SEQRES 5 C 526 GLY ASN VAL ILE HIS ALA HIS GLY GLY GLY MET LEU LYS
SEQRES 6 C 526 HIS GLY ASP TYR TYR TYR TRP TYR GLY GLU TYR ARG ASP
SEQRES 7 C 526 ASP SER ASN LEU PHE LEU GLY VAL SER CYS TYR ARG SER
SEQRES 8 C 526 LYS ASP LEU VAL ASN TRP GLU TYR ARG GLY GLU VAL LEU
SEQRES 9 C 526 SER ARG ASN SER ALA PRO GLU LEU ASN HIS CYS ASN ILE
SEQRES 10 C 526 GLU ARG PRO LYS VAL MET TYR ASN ALA SER THR GLY GLU
SEQRES 11 C 526 PHE VAL MET TRP MET HIS TRP GLU ASN GLY ILE ASN TYR
SEQRES 12 C 526 GLY GLN ALA ARG ALA ALA VAL ALA TYR SER LYS THR PRO
SEQRES 13 C 526 ASP GLY LYS PHE THR TYR ILE ARG SER PHE ARG PRO MET
SEQRES 14 C 526 GLN ASP THR GLY VAL MET ASP HIS GLY LEU PRO GLY TYR
SEQRES 15 C 526 MET SER ARG ASP CYS ASN VAL PHE VAL ASP THR ASP GLY
SEQRES 16 C 526 LYS GLY TYR PHE ILE SER ALA ALA ASN GLU ASN MET ASP
SEQRES 17 C 526 LEU HIS LEU TYR GLU LEU THR PRO ASP TYR LYS ASN ILE
SEQRES 18 C 526 ALA SER LEU LYS ALA LYS LEU PHE VAL GLY GLN GLN ARG
SEQRES 19 C 526 GLU ALA PRO CYS LEU ILE LYS ARG ASN GLY TYR TYR TYR
SEQRES 20 C 526 LEU ILE THR SER GLY CYS THR GLY TRP ASN PRO ASN GLN
SEQRES 21 C 526 ALA LYS TYR ALA TYR SER LYS ASP LEU ALA SER GLY TRP
SEQRES 22 C 526 SER GLN LEU TYR ASN LEU GLY ASN SER THR THR TYR ARG
SEQRES 23 C 526 SER GLN PRO THR PHE ILE ILE PRO VAL GLN GLY SER SER
SEQRES 24 C 526 GLY THR SER TYR LEU TYR MET GLY ASP ARG TRP ALA GLY
SEQRES 25 C 526 ALA TRP GLY GLY LYS VAL ASN ASP SER GLN TYR VAL TRP
SEQRES 26 C 526 LEU PRO LEU ASN PHE ILE SER ASP THR THR LEU GLU LEU
SEQRES 27 C 526 PRO TYR TYR ASP SER VAL LYS ILE ASP ALA SER SER GLY
SEQRES 28 C 526 ILE ILE SER GLU TYR ILE PRO ASP THR THR ARG TYR LYS
SEQRES 29 C 526 LEU VAL ASN LYS ASN SER GLY LYS VAL LEU ASP VAL LEU
SEQRES 30 C 526 ASP GLY SER VAL ASP ASN ALA ALA GLN ILE VAL GLN TRP
SEQRES 31 C 526 THR ASP ASN GLY SER LEU SER GLN GLN TRP TYR LEU VAL
SEQRES 32 C 526 ASP VAL GLY GLY GLY TYR LYS LYS ILE VAL ASN VAL LYS
SEQRES 33 C 526 SER GLY ARG ALA LEU ASP VAL LYS ASP GLU SER LYS GLU
SEQRES 34 C 526 ASP GLY GLY VAL LEU ILE GLN TYR THR SER ASN GLY GLY
SEQRES 35 C 526 TYR ASN GLN HIS TRP LYS PHE THR ASP ILE GLY ASP GLY
SEQRES 36 C 526 TYR TYR LYS ILE SER SER ARG HIS CYS GLY LYS LEU ILE
SEQRES 37 C 526 ASP VAL ARG LYS TRP SER THR GLU ASP GLY GLY ILE ILE
SEQRES 38 C 526 GLN GLN TRP SER ASP ALA GLY GLY THR ASN GLN HIS TRP
SEQRES 39 C 526 LYS LEU VAL LEU VAL SER SER PRO GLU PRO SER PRO SER
SEQRES 40 C 526 PRO SER PRO GLN VAL VAL LYS GLY ASP VAL ASN GLY ASP
SEQRES 41 C 526 LEU LYS VAL ASN SER THR
SEQRES 1 D 526 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 526 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 D 526 GLY GLN GLN MET GLY ARG GLY SER GLU PHE ALA ALA GLU
SEQRES 4 D 526 GLY VAL ILE VAL ASN GLY THR GLN PHE LYS ASP THR SER
SEQRES 5 D 526 GLY ASN VAL ILE HIS ALA HIS GLY GLY GLY MET LEU LYS
SEQRES 6 D 526 HIS GLY ASP TYR TYR TYR TRP TYR GLY GLU TYR ARG ASP
SEQRES 7 D 526 ASP SER ASN LEU PHE LEU GLY VAL SER CYS TYR ARG SER
SEQRES 8 D 526 LYS ASP LEU VAL ASN TRP GLU TYR ARG GLY GLU VAL LEU
SEQRES 9 D 526 SER ARG ASN SER ALA PRO GLU LEU ASN HIS CYS ASN ILE
SEQRES 10 D 526 GLU ARG PRO LYS VAL MET TYR ASN ALA SER THR GLY GLU
SEQRES 11 D 526 PHE VAL MET TRP MET HIS TRP GLU ASN GLY ILE ASN TYR
SEQRES 12 D 526 GLY GLN ALA ARG ALA ALA VAL ALA TYR SER LYS THR PRO
SEQRES 13 D 526 ASP GLY LYS PHE THR TYR ILE ARG SER PHE ARG PRO MET
SEQRES 14 D 526 GLN ASP THR GLY VAL MET ASP HIS GLY LEU PRO GLY TYR
SEQRES 15 D 526 MET SER ARG ASP CYS ASN VAL PHE VAL ASP THR ASP GLY
SEQRES 16 D 526 LYS GLY TYR PHE ILE SER ALA ALA ASN GLU ASN MET ASP
SEQRES 17 D 526 LEU HIS LEU TYR GLU LEU THR PRO ASP TYR LYS ASN ILE
SEQRES 18 D 526 ALA SER LEU LYS ALA LYS LEU PHE VAL GLY GLN GLN ARG
SEQRES 19 D 526 GLU ALA PRO CYS LEU ILE LYS ARG ASN GLY TYR TYR TYR
SEQRES 20 D 526 LEU ILE THR SER GLY CYS THR GLY TRP ASN PRO ASN GLN
SEQRES 21 D 526 ALA LYS TYR ALA TYR SER LYS ASP LEU ALA SER GLY TRP
SEQRES 22 D 526 SER GLN LEU TYR ASN LEU GLY ASN SER THR THR TYR ARG
SEQRES 23 D 526 SER GLN PRO THR PHE ILE ILE PRO VAL GLN GLY SER SER
SEQRES 24 D 526 GLY THR SER TYR LEU TYR MET GLY ASP ARG TRP ALA GLY
SEQRES 25 D 526 ALA TRP GLY GLY LYS VAL ASN ASP SER GLN TYR VAL TRP
SEQRES 26 D 526 LEU PRO LEU ASN PHE ILE SER ASP THR THR LEU GLU LEU
SEQRES 27 D 526 PRO TYR TYR ASP SER VAL LYS ILE ASP ALA SER SER GLY
SEQRES 28 D 526 ILE ILE SER GLU TYR ILE PRO ASP THR THR ARG TYR LYS
SEQRES 29 D 526 LEU VAL ASN LYS ASN SER GLY LYS VAL LEU ASP VAL LEU
SEQRES 30 D 526 ASP GLY SER VAL ASP ASN ALA ALA GLN ILE VAL GLN TRP
SEQRES 31 D 526 THR ASP ASN GLY SER LEU SER GLN GLN TRP TYR LEU VAL
SEQRES 32 D 526 ASP VAL GLY GLY GLY TYR LYS LYS ILE VAL ASN VAL LYS
SEQRES 33 D 526 SER GLY ARG ALA LEU ASP VAL LYS ASP GLU SER LYS GLU
SEQRES 34 D 526 ASP GLY GLY VAL LEU ILE GLN TYR THR SER ASN GLY GLY
SEQRES 35 D 526 TYR ASN GLN HIS TRP LYS PHE THR ASP ILE GLY ASP GLY
SEQRES 36 D 526 TYR TYR LYS ILE SER SER ARG HIS CYS GLY LYS LEU ILE
SEQRES 37 D 526 ASP VAL ARG LYS TRP SER THR GLU ASP GLY GLY ILE ILE
SEQRES 38 D 526 GLN GLN TRP SER ASP ALA GLY GLY THR ASN GLN HIS TRP
SEQRES 39 D 526 LYS LEU VAL LEU VAL SER SER PRO GLU PRO SER PRO SER
SEQRES 40 D 526 PRO SER PRO GLN VAL VAL LYS GLY ASP VAL ASN GLY ASP
SEQRES 41 D 526 LEU LYS VAL ASN SER THR
SEQRES 1 E 526 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 526 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 E 526 GLY GLN GLN MET GLY ARG GLY SER GLU PHE ALA ALA GLU
SEQRES 4 E 526 GLY VAL ILE VAL ASN GLY THR GLN PHE LYS ASP THR SER
SEQRES 5 E 526 GLY ASN VAL ILE HIS ALA HIS GLY GLY GLY MET LEU LYS
SEQRES 6 E 526 HIS GLY ASP TYR TYR TYR TRP TYR GLY GLU TYR ARG ASP
SEQRES 7 E 526 ASP SER ASN LEU PHE LEU GLY VAL SER CYS TYR ARG SER
SEQRES 8 E 526 LYS ASP LEU VAL ASN TRP GLU TYR ARG GLY GLU VAL LEU
SEQRES 9 E 526 SER ARG ASN SER ALA PRO GLU LEU ASN HIS CYS ASN ILE
SEQRES 10 E 526 GLU ARG PRO LYS VAL MET TYR ASN ALA SER THR GLY GLU
SEQRES 11 E 526 PHE VAL MET TRP MET HIS TRP GLU ASN GLY ILE ASN TYR
SEQRES 12 E 526 GLY GLN ALA ARG ALA ALA VAL ALA TYR SER LYS THR PRO
SEQRES 13 E 526 ASP GLY LYS PHE THR TYR ILE ARG SER PHE ARG PRO MET
SEQRES 14 E 526 GLN ASP THR GLY VAL MET ASP HIS GLY LEU PRO GLY TYR
SEQRES 15 E 526 MET SER ARG ASP CYS ASN VAL PHE VAL ASP THR ASP GLY
SEQRES 16 E 526 LYS GLY TYR PHE ILE SER ALA ALA ASN GLU ASN MET ASP
SEQRES 17 E 526 LEU HIS LEU TYR GLU LEU THR PRO ASP TYR LYS ASN ILE
SEQRES 18 E 526 ALA SER LEU LYS ALA LYS LEU PHE VAL GLY GLN GLN ARG
SEQRES 19 E 526 GLU ALA PRO CYS LEU ILE LYS ARG ASN GLY TYR TYR TYR
SEQRES 20 E 526 LEU ILE THR SER GLY CYS THR GLY TRP ASN PRO ASN GLN
SEQRES 21 E 526 ALA LYS TYR ALA TYR SER LYS ASP LEU ALA SER GLY TRP
SEQRES 22 E 526 SER GLN LEU TYR ASN LEU GLY ASN SER THR THR TYR ARG
SEQRES 23 E 526 SER GLN PRO THR PHE ILE ILE PRO VAL GLN GLY SER SER
SEQRES 24 E 526 GLY THR SER TYR LEU TYR MET GLY ASP ARG TRP ALA GLY
SEQRES 25 E 526 ALA TRP GLY GLY LYS VAL ASN ASP SER GLN TYR VAL TRP
SEQRES 26 E 526 LEU PRO LEU ASN PHE ILE SER ASP THR THR LEU GLU LEU
SEQRES 27 E 526 PRO TYR TYR ASP SER VAL LYS ILE ASP ALA SER SER GLY
SEQRES 28 E 526 ILE ILE SER GLU TYR ILE PRO ASP THR THR ARG TYR LYS
SEQRES 29 E 526 LEU VAL ASN LYS ASN SER GLY LYS VAL LEU ASP VAL LEU
SEQRES 30 E 526 ASP GLY SER VAL ASP ASN ALA ALA GLN ILE VAL GLN TRP
SEQRES 31 E 526 THR ASP ASN GLY SER LEU SER GLN GLN TRP TYR LEU VAL
SEQRES 32 E 526 ASP VAL GLY GLY GLY TYR LYS LYS ILE VAL ASN VAL LYS
SEQRES 33 E 526 SER GLY ARG ALA LEU ASP VAL LYS ASP GLU SER LYS GLU
SEQRES 34 E 526 ASP GLY GLY VAL LEU ILE GLN TYR THR SER ASN GLY GLY
SEQRES 35 E 526 TYR ASN GLN HIS TRP LYS PHE THR ASP ILE GLY ASP GLY
SEQRES 36 E 526 TYR TYR LYS ILE SER SER ARG HIS CYS GLY LYS LEU ILE
SEQRES 37 E 526 ASP VAL ARG LYS TRP SER THR GLU ASP GLY GLY ILE ILE
SEQRES 38 E 526 GLN GLN TRP SER ASP ALA GLY GLY THR ASN GLN HIS TRP
SEQRES 39 E 526 LYS LEU VAL LEU VAL SER SER PRO GLU PRO SER PRO SER
SEQRES 40 E 526 PRO SER PRO GLN VAL VAL LYS GLY ASP VAL ASN GLY ASP
SEQRES 41 E 526 LEU LYS VAL ASN SER THR
SEQRES 1 F 526 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 526 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 F 526 GLY GLN GLN MET GLY ARG GLY SER GLU PHE ALA ALA GLU
SEQRES 4 F 526 GLY VAL ILE VAL ASN GLY THR GLN PHE LYS ASP THR SER
SEQRES 5 F 526 GLY ASN VAL ILE HIS ALA HIS GLY GLY GLY MET LEU LYS
SEQRES 6 F 526 HIS GLY ASP TYR TYR TYR TRP TYR GLY GLU TYR ARG ASP
SEQRES 7 F 526 ASP SER ASN LEU PHE LEU GLY VAL SER CYS TYR ARG SER
SEQRES 8 F 526 LYS ASP LEU VAL ASN TRP GLU TYR ARG GLY GLU VAL LEU
SEQRES 9 F 526 SER ARG ASN SER ALA PRO GLU LEU ASN HIS CYS ASN ILE
SEQRES 10 F 526 GLU ARG PRO LYS VAL MET TYR ASN ALA SER THR GLY GLU
SEQRES 11 F 526 PHE VAL MET TRP MET HIS TRP GLU ASN GLY ILE ASN TYR
SEQRES 12 F 526 GLY GLN ALA ARG ALA ALA VAL ALA TYR SER LYS THR PRO
SEQRES 13 F 526 ASP GLY LYS PHE THR TYR ILE ARG SER PHE ARG PRO MET
SEQRES 14 F 526 GLN ASP THR GLY VAL MET ASP HIS GLY LEU PRO GLY TYR
SEQRES 15 F 526 MET SER ARG ASP CYS ASN VAL PHE VAL ASP THR ASP GLY
SEQRES 16 F 526 LYS GLY TYR PHE ILE SER ALA ALA ASN GLU ASN MET ASP
SEQRES 17 F 526 LEU HIS LEU TYR GLU LEU THR PRO ASP TYR LYS ASN ILE
SEQRES 18 F 526 ALA SER LEU LYS ALA LYS LEU PHE VAL GLY GLN GLN ARG
SEQRES 19 F 526 GLU ALA PRO CYS LEU ILE LYS ARG ASN GLY TYR TYR TYR
SEQRES 20 F 526 LEU ILE THR SER GLY CYS THR GLY TRP ASN PRO ASN GLN
SEQRES 21 F 526 ALA LYS TYR ALA TYR SER LYS ASP LEU ALA SER GLY TRP
SEQRES 22 F 526 SER GLN LEU TYR ASN LEU GLY ASN SER THR THR TYR ARG
SEQRES 23 F 526 SER GLN PRO THR PHE ILE ILE PRO VAL GLN GLY SER SER
SEQRES 24 F 526 GLY THR SER TYR LEU TYR MET GLY ASP ARG TRP ALA GLY
SEQRES 25 F 526 ALA TRP GLY GLY LYS VAL ASN ASP SER GLN TYR VAL TRP
SEQRES 26 F 526 LEU PRO LEU ASN PHE ILE SER ASP THR THR LEU GLU LEU
SEQRES 27 F 526 PRO TYR TYR ASP SER VAL LYS ILE ASP ALA SER SER GLY
SEQRES 28 F 526 ILE ILE SER GLU TYR ILE PRO ASP THR THR ARG TYR LYS
SEQRES 29 F 526 LEU VAL ASN LYS ASN SER GLY LYS VAL LEU ASP VAL LEU
SEQRES 30 F 526 ASP GLY SER VAL ASP ASN ALA ALA GLN ILE VAL GLN TRP
SEQRES 31 F 526 THR ASP ASN GLY SER LEU SER GLN GLN TRP TYR LEU VAL
SEQRES 32 F 526 ASP VAL GLY GLY GLY TYR LYS LYS ILE VAL ASN VAL LYS
SEQRES 33 F 526 SER GLY ARG ALA LEU ASP VAL LYS ASP GLU SER LYS GLU
SEQRES 34 F 526 ASP GLY GLY VAL LEU ILE GLN TYR THR SER ASN GLY GLY
SEQRES 35 F 526 TYR ASN GLN HIS TRP LYS PHE THR ASP ILE GLY ASP GLY
SEQRES 36 F 526 TYR TYR LYS ILE SER SER ARG HIS CYS GLY LYS LEU ILE
SEQRES 37 F 526 ASP VAL ARG LYS TRP SER THR GLU ASP GLY GLY ILE ILE
SEQRES 38 F 526 GLN GLN TRP SER ASP ALA GLY GLY THR ASN GLN HIS TRP
SEQRES 39 F 526 LYS LEU VAL LEU VAL SER SER PRO GLU PRO SER PRO SER
SEQRES 40 F 526 PRO SER PRO GLN VAL VAL LYS GLY ASP VAL ASN GLY ASP
SEQRES 41 F 526 LEU LYS VAL ASN SER THR
HET BGC G 1 12
HET GAL G 2 11
HET BGC H 1 12
HET GAL H 2 11
HET BGC I 1 12
HET GAL I 2 11
HET BGC J 1 12
HET GAL J 2 11
HET BGC K 1 12
HET GAL K 2 11
HET BGC L 1 12
HET GAL L 2 11
HET GOL A 602 6
HET GOL C 602 6
HET GOL F 603 6
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 BGC 6(C6 H12 O6)
FORMUL 7 GAL 6(C6 H12 O6)
FORMUL 13 GOL 3(C3 H8 O3)
HELIX 1 1 ALA A 103 ASN A 107 5 5
HELIX 2 2 TRP A 304 GLY A 309 5 6
HELIX 3 3 LYS A 311 SER A 315 5 5
HELIX 4 4 ASP A 372 SER A 374 5 3
HELIX 5 5 SER A 389 GLN A 392 5 4
HELIX 6 6 ASP A 419 SER A 421 5 3
HELIX 7 7 GLY A 436 ASN A 438 5 3
HELIX 8 8 LYS A 466 SER A 468 5 3
HELIX 9 9 GLY A 483 GLN A 486 5 4
HELIX 10 10 TRP B 304 GLY B 309 5 6
HELIX 11 11 LYS B 311 SER B 315 5 5
HELIX 12 12 ASP B 372 SER B 374 5 3
HELIX 13 13 SER B 389 GLN B 392 5 4
HELIX 14 14 ASP B 419 SER B 421 5 3
HELIX 15 15 GLY B 436 ASN B 438 5 3
HELIX 16 16 LYS B 466 SER B 468 5 3
HELIX 17 17 GLY B 483 GLN B 486 5 4
HELIX 18 18 ALA C 103 ASN C 107 5 5
HELIX 19 19 MET C 163 GLY C 167 5 5
HELIX 20 20 TRP C 304 GLY C 309 5 6
HELIX 21 21 LYS C 311 SER C 315 5 5
HELIX 22 22 ASP C 372 SER C 374 5 3
HELIX 23 23 SER C 389 GLN C 392 5 4
HELIX 24 24 ASP C 419 SER C 421 5 3
HELIX 25 25 GLY C 436 GLN C 439 5 4
HELIX 26 26 LYS C 466 SER C 468 5 3
HELIX 27 27 GLY C 483 GLN C 486 5 4
HELIX 28 28 ALA D 103 ASN D 107 5 5
HELIX 29 29 MET D 163 GLY D 167 5 5
HELIX 30 30 TRP D 304 GLY D 309 5 6
HELIX 31 31 LYS D 311 SER D 315 5 5
HELIX 32 32 ASP D 372 SER D 374 5 3
HELIX 33 33 ASP D 419 SER D 421 5 3
HELIX 34 34 GLY D 436 HIS D 440 5 5
HELIX 35 35 LYS D 466 SER D 468 5 3
HELIX 36 36 ALA E 103 ASN E 107 5 5
HELIX 37 37 MET E 163 GLY E 167 5 5
HELIX 38 38 TRP E 304 GLY E 309 5 6
HELIX 39 39 LYS E 311 SER E 315 5 5
HELIX 40 40 ASP E 372 SER E 374 5 3
HELIX 41 41 SER E 389 GLN E 392 5 4
HELIX 42 42 ASP E 419 SER E 421 5 3
HELIX 43 43 GLY E 436 GLN E 439 5 4
HELIX 44 44 LYS E 466 SER E 468 5 3
HELIX 45 45 GLY E 483 GLN E 486 5 4
HELIX 46 46 ALA F 103 ASN F 107 5 5
HELIX 47 47 TRP F 304 GLY F 309 5 6
HELIX 48 48 LYS F 311 SER F 315 5 5
HELIX 49 49 ASP F 372 SER F 374 5 3
HELIX 50 50 SER F 389 GLN F 392 5 4
HELIX 51 51 ASP F 419 SER F 421 5 3
HELIX 52 52 GLY F 436 GLN F 439 5 4
HELIX 53 53 LYS F 466 SER F 468 5 3
SHEET 1 A 3 VAL A 35 VAL A 37 0
SHEET 2 A 3 SER A 343 ASP A 341 -1 O VAL A 338 N ILE A 36
SHEET 3 A 3 ILE A 346 GLU A 349 -1 O ILE A 346 N ASP A 341
SHEET 1 B 4 HIS A 53 HIS A 60 0
SHEET 2 B 4 TYR A 63 ARG A 71 -1 O TYR A 65 N LEU A 58
SHEET 3 B 4 PHE A 77 SER A 85 -1 O TYR A 83 N TRP A 66
SHEET 4 B 4 GLU A 92 SER A 99 -1 O LEU A 98 N VAL A 80
SHEET 1 C 4 ASN A 110 TYR A 118 0
SHEET 2 C 4 PHE A 125 GLU A 132 -1 O VAL A 126 N MET A 117
SHEET 3 C 4 ARG A 141 SER A 147 -1 O ALA A 145 N MET A 127
SHEET 4 C 4 THR A 155 PHE A 160 -1 O PHE A 160 N ALA A 142
SHEET 1 D 2 MET A 169 ASP A 170 0
SHEET 2 D 2 LEU A 173 PRO A 174 -1 O LEU A 173 N ASP A 170
SHEET 1 E 4 CYS A 181 VAL A 185 0
SHEET 2 E 4 GLY A 191 ALA A 197 -1 O ILE A 194 N ASN A 182
SHEET 3 E 4 ASP A 202 LEU A 208 -1 O TYR A 212 N PHE A 193
SHEET 4 E 4 ILE A 215 LEU A 222 -1 O LEU A 222 N LEU A 203
SHEET 1 F 3 GLU A 229 LYS A 235 0
SHEET 2 F 3 TYR A 240 SER A 245 -1 O SER A 245 N GLU A 229
SHEET 3 F 3 TYR A 259 SER A 260 -1 O SER A 260 N TYR A 240
SHEET 1 G 2 ALA A 255 TYR A 257 0
SHEET 2 G 2 TYR A 271 LEU A 273 -1 O LEU A 273 N ALA A 255
SHEET 1 H 4 GLN A 282 GLN A 290 0
SHEET 2 H 4 THR A 295 ARG A 303 -1 O LEU A 298 N ILE A 287
SHEET 3 H 4 GLN A 316 PHE A 324 -1 O LEU A 322 N TYR A 297
SHEET 4 H 4 LEU A 330 GLU A 331 -1 O GLU A 331 N ASN A 323
SHEET 1 I 7 TYR A 357 ASN A 361 0
SHEET 2 I 7 TRP A 394 ASP A 398 -1 O TRP A 394 N TYR A 357
SHEET 3 I 7 TYR A 403 ASN A 408 -1 O VAL A 407 N TYR A 395
SHEET 4 I 7 HIS A 440 GLY A 447 -1 O TRP A 441 N LYS A 410
SHEET 5 I 7 TYR A 450 SER A 455 -1 O SER A 454 N LYS A 442
SHEET 6 I 7 TRP A 488 LEU A 492 -1 O TRP A 488 N TYR A 451
SHEET 7 I 7 TYR A 357 ASN A 361 -1 N VAL A 360 O LYS A 489
SHEET 1 J 5 VAL A 367 VAL A 370 0
SHEET 2 J 5 ALA A 379 TRP A 384 -1 O TRP A 384 N VAL A 367
SHEET 3 J 5 GLY A 426 TYR A 437 -1 O LEU A 428 N ILE A 381
SHEET 4 J 5 GLY A 473 TRP A 478 -1 O ILE A 475 N LEU A 428
SHEET 5 J 5 LEU A 461 VAL A 464 -1 N ASP A 463 O GLN A 476
SHEET 1 K 5 VAL A 367 VAL A 370 0
SHEET 2 K 5 ALA A 379 TRP A 384 -1 O TRP A 384 N VAL A 367
SHEET 3 K 5 GLY A 473 TRP A 478 -1 O ILE A 475 N ILE A 381
SHEET 4 K 5 GLY A 426 TYR A 437 -1 N LEU A 428 O ILE A 475
SHEET 5 K 5 ALA A 414 VAL A 417 -1 N ASP A 416 O ILE A 429
SHEET 1 L 3 VAL B 35 VAL B 37 0
SHEET 2 L 3 SER B 343 ASP B 341 -1 O VAL B 338 N ILE B 36
SHEET 3 L 3 ILE B 346 GLU B 349 -1 O SER B 348 N LYS B 339
SHEET 1 M 4 MET B 57 HIS B 60 0
SHEET 2 M 4 TYR B 63 ARG B 71 -1 O TYR B 65 N LEU B 58
SHEET 3 M 4 PHE B 77 SER B 85 -1 O TYR B 83 N TRP B 66
SHEET 4 M 4 GLU B 92 SER B 99 -1 O LEU B 98 N VAL B 80
SHEET 1 N 4 ASN B 110 TYR B 118 0
SHEET 2 N 4 PHE B 125 GLU B 132 -1 O TRP B 128 N LYS B 115
SHEET 3 N 4 ARG B 141 SER B 147 -1 O ALA B 145 N MET B 127
SHEET 4 N 4 THR B 155 PHE B 160 -1 O ILE B 157 N VAL B 144
SHEET 1 O 4 CYS B 181 VAL B 185 0
SHEET 2 O 4 GLY B 191 ALA B 197 -1 O ILE B 194 N ASN B 182
SHEET 3 O 4 ASP B 202 LEU B 208 -1 O TYR B 212 N PHE B 193
SHEET 4 O 4 ILE B 215 LEU B 222 -1 O LYS B 219 N LEU B 205
SHEET 1 P 3 ARG B 228 ARG B 236 0
SHEET 2 P 3 TYR B 239 GLY B 246 -1 O SER B 245 N GLU B 229
SHEET 3 P 3 TYR B 259 SER B 260 -1 O SER B 260 N TYR B 240
SHEET 1 Q 2 ALA B 255 TYR B 257 0
SHEET 2 Q 2 TYR B 271 LEU B 273 -1 O LEU B 273 N ALA B 255
SHEET 1 R 4 GLN B 282 GLN B 290 0
SHEET 2 R 4 THR B 295 ARG B 303 -1 O LEU B 298 N ILE B 287
SHEET 3 R 4 GLN B 316 SER B 326 -1 O LEU B 320 N TYR B 299
SHEET 4 R 4 THR B 329 GLU B 331 -1 O GLU B 331 N ASN B 323
SHEET 1 S 3 TYR B 357 ASN B 361 0
SHEET 2 S 3 TRP B 488 LEU B 492 -1 O LYS B 489 N VAL B 360
SHEET 3 S 3 TYR B 450 TYR B 451 -1 N TYR B 451 O TRP B 488
SHEET 1 T 5 ALA B 414 VAL B 417 0
SHEET 2 T 5 GLY B 426 TYR B 437 -1 O ILE B 429 N ASP B 416
SHEET 3 T 5 ALA B 379 TRP B 384 -1 N ILE B 381 O LEU B 428
SHEET 4 T 5 GLY B 473 TRP B 478 -1 O ILE B 475 N ILE B 381
SHEET 5 T 5 LEU B 461 VAL B 464 -1 N ASP B 463 O GLN B 476
SHEET 1 U 5 VAL B 367 VAL B 370 0
SHEET 2 U 5 ALA B 379 TRP B 384 -1 O TRP B 384 N VAL B 367
SHEET 3 U 5 GLY B 426 TYR B 437 -1 O LEU B 428 N ILE B 381
SHEET 4 U 5 GLY B 473 TRP B 478 -1 O ILE B 475 N LEU B 428
SHEET 5 U 5 LEU B 461 VAL B 464 -1 N ASP B 463 O GLN B 476
SHEET 1 V 4 TRP B 394 ASP B 398 0
SHEET 2 V 4 TYR B 403 ASN B 408 -1 O VAL B 407 N TYR B 395
SHEET 3 V 4 HIS B 440 LYS B 442 -1 O TRP B 441 N LYS B 410
SHEET 4 V 4 SER B 454 SER B 455 -1 O SER B 454 N LYS B 442
SHEET 1 W 3 VAL C 35 VAL C 37 0
SHEET 2 W 3 SER C 343 ASP C 341 -1 O VAL C 338 N ILE C 36
SHEET 3 W 3 ILE C 346 GLU C 349 -1 O SER C 348 N LYS C 339
SHEET 1 X 4 HIS C 53 HIS C 60 0
SHEET 2 X 4 TYR C 63 ARG C 71 -1 O TYR C 65 N LEU C 58
SHEET 3 X 4 PHE C 77 SER C 85 -1 O TYR C 83 N TRP C 66
SHEET 4 X 4 GLU C 92 SER C 99 -1 O ARG C 100 N CYS C 82
SHEET 1 Y 4 ASN C 110 TYR C 118 0
SHEET 2 Y 4 PHE C 125 GLU C 132 -1 O HIS C 130 N GLU C 112
SHEET 3 Y 4 ARG C 141 SER C 147 -1 O ALA C 145 N MET C 127
SHEET 4 Y 4 THR C 155 PHE C 160 -1 O THR C 155 N TYR C 146
SHEET 1 Z 4 CYS C 181 VAL C 185 0
SHEET 2 Z 4 GLY C 191 ALA C 197 -1 O ILE C 194 N ASN C 182
SHEET 3 Z 4 ASP C 202 LEU C 208 -1 O HIS C 204 N SER C 195
SHEET 4 Z 4 ILE C 215 LEU C 222 -1 O ALA C 216 N GLU C 207
SHEET 1 AA 4 GLU C 229 LYS C 235 0
SHEET 2 AA 4 TYR C 240 SER C 245 -1 O SER C 245 N GLU C 229
SHEET 3 AA 4 ALA C 255 SER C 260 -1 O SER C 260 N TYR C 240
SHEET 4 AA 4 TYR C 271 LEU C 273 -1 O LEU C 273 N ALA C 255
SHEET 1 AB 4 GLN C 282 GLN C 290 0
SHEET 2 AB 4 THR C 295 ARG C 303 -1 O SER C 296 N VAL C 289
SHEET 3 AB 4 GLN C 316 PHE C 324 -1 O LEU C 320 N TYR C 299
SHEET 4 AB 4 LEU C 330 GLU C 331 -1 O GLU C 331 N ASN C 323
SHEET 1 AC 4 TYR C 357 ASN C 361 0
SHEET 2 AC 4 TRP C 488 LEU C 492 -1 O LYS C 489 N VAL C 360
SHEET 3 AC 4 TYR C 450 SER C 455 -1 N TYR C 451 O TRP C 488
SHEET 4 AC 4 TRP C 441 ASP C 445 -1 N LYS C 442 O SER C 454
SHEET 1 AD 4 VAL C 367 VAL C 370 0
SHEET 2 AD 4 ALA C 379 TRP C 384 -1 O TRP C 384 N VAL C 367
SHEET 3 AD 4 LEU C 428 TYR C 437 -1 O LEU C 428 N ILE C 381
SHEET 4 AD 4 ALA C 414 VAL C 417 -1 N ASP C 416 O ILE C 429
SHEET 1 AE 2 TRP C 394 GLY C 400 0
SHEET 2 AE 2 TYR C 403 ASN C 408 -1 O VAL C 407 N TYR C 395
SHEET 1 AF 2 LEU C 461 VAL C 464 0
SHEET 2 AF 2 ILE C 475 TRP C 478 -1 O GLN C 476 N ASP C 463
SHEET 1 AG 3 VAL D 35 VAL D 37 0
SHEET 2 AG 3 SER D 343 ASP D 341 -1 O VAL D 338 N ILE D 36
SHEET 3 AG 3 ILE D 346 GLU D 349 -1 O SER D 348 N LYS D 339
SHEET 1 AH 4 HIS D 53 HIS D 60 0
SHEET 2 AH 4 TYR D 63 ARG D 71 -1 O TYR D 65 N LEU D 58
SHEET 3 AH 4 PHE D 77 SER D 85 -1 O TYR D 83 N TRP D 66
SHEET 4 AH 4 GLU D 92 SER D 99 -1 O LEU D 98 N VAL D 80
SHEET 1 AI 4 ASN D 110 TYR D 118 0
SHEET 2 AI 4 PHE D 125 GLU D 132 -1 O TRP D 128 N LYS D 115
SHEET 3 AI 4 ARG D 141 SER D 147 -1 O ALA D 145 N MET D 127
SHEET 4 AI 4 THR D 155 PHE D 160 -1 O PHE D 160 N ALA D 142
SHEET 1 AJ 2 MET D 169 ASP D 170 0
SHEET 2 AJ 2 LEU D 173 PRO D 174 -1 O LEU D 173 N ASP D 170
SHEET 1 AK 4 CYS D 181 VAL D 185 0
SHEET 2 AK 4 GLY D 191 ALA D 197 -1 O ILE D 194 N ASN D 182
SHEET 3 AK 4 ASP D 202 LEU D 208 -1 O HIS D 204 N SER D 195
SHEET 4 AK 4 ILE D 215 LEU D 222 -1 O LEU D 222 N LEU D 203
SHEET 1 AL 4 ARG D 228 LYS D 235 0
SHEET 2 AL 4 TYR D 240 GLY D 246 -1 O SER D 245 N GLU D 229
SHEET 3 AL 4 ALA D 255 SER D 260 -1 O LYS D 256 N THR D 244
SHEET 4 AL 4 TYR D 271 LEU D 273 -1 O LEU D 273 N ALA D 255
SHEET 1 AM 3 GLN D 282 VAL D 289 0
SHEET 2 AM 3 SER D 296 ARG D 303 -1 O LEU D 298 N ILE D 287
SHEET 3 AM 3 GLN D 316 PRO D 321 -1 O GLN D 316 N ARG D 303
SHEET 1 AN 2 ASN D 323 PHE D 324 0
SHEET 2 AN 2 LEU D 330 GLU D 331 -1 O GLU D 331 N ASN D 323
SHEET 1 AO 2 TYR D 357 ASN D 361 0
SHEET 2 AO 2 TRP D 488 LEU D 492 -1 O VAL D 491 N LYS D 358
SHEET 1 AP 2 ASP D 369 VAL D 370 0
SHEET 2 AP 2 ILE D 381 VAL D 382 -1 O VAL D 382 N ASP D 369
SHEET 1 AQ 2 TRP D 394 ASP D 398 0
SHEET 2 AQ 2 LYS D 410 ASN D 408 -1 O LYS D 405 N VAL D 397
SHEET 1 AR 2 ALA D 414 VAL D 417 0
SHEET 2 AR 2 LEU D 428 TYR D 437 -1 O ILE D 429 N ASP D 416
SHEET 1 AS 2 LEU D 461 VAL D 464 0
SHEET 2 AS 2 ILE D 475 TRP D 478 -1 O TRP D 478 N LEU D 461
SHEET 1 AT 3 VAL E 35 VAL E 37 0
SHEET 2 AT 3 SER E 343 ASP E 341 -1 O VAL E 338 N ILE E 36
SHEET 3 AT 3 ILE E 346 GLU E 349 -1 O ILE E 346 N ASP E 341
SHEET 1 AU 4 MET E 57 HIS E 60 0
SHEET 2 AU 4 TYR E 63 GLY E 68 -1 O TYR E 65 N LEU E 58
SHEET 3 AU 4 GLY E 79 SER E 85 -1 O TYR E 83 N TRP E 66
SHEET 4 AU 4 GLU E 92 SER E 99 -1 O GLU E 92 N ARG E 84
SHEET 1 AV 4 ASN E 110 TYR E 118 0
SHEET 2 AV 4 PHE E 125 GLU E 132 -1 O TRP E 128 N LYS E 115
SHEET 3 AV 4 ARG E 141 SER E 147 -1 O ALA E 145 N MET E 127
SHEET 4 AV 4 THR E 155 PHE E 160 -1 O THR E 155 N TYR E 146
SHEET 1 AW 4 CYS E 181 VAL E 185 0
SHEET 2 AW 4 GLY E 191 ALA E 197 -1 O ILE E 194 N ASN E 182
SHEET 3 AW 4 ASP E 202 LEU E 208 -1 O TYR E 212 N PHE E 193
SHEET 4 AW 4 ILE E 215 LEU E 222 -1 O LEU E 222 N LEU E 203
SHEET 1 AX 4 GLU E 229 LYS E 235 0
SHEET 2 AX 4 TYR E 240 SER E 245 -1 O SER E 245 N GLU E 229
SHEET 3 AX 4 LYS E 256 SER E 260 -1 O SER E 260 N TYR E 240
SHEET 4 AX 4 TYR E 271 ASN E 272 -1 O TYR E 271 N TYR E 257
SHEET 1 AY 4 GLN E 282 GLN E 290 0
SHEET 2 AY 4 THR E 295 ARG E 303 -1 O LEU E 298 N ILE E 287
SHEET 3 AY 4 GLN E 316 PHE E 324 -1 O LEU E 320 N TYR E 299
SHEET 4 AY 4 LEU E 330 GLU E 331 -1 O GLU E 331 N ASN E 323
SHEET 1 AZ 4 TYR E 357 ASN E 361 0
SHEET 2 AZ 4 TRP E 488 LEU E 492 -1 O LYS E 489 N VAL E 360
SHEET 3 AZ 4 TYR E 450 SER E 455 -1 N TYR E 451 O TRP E 488
SHEET 4 AZ 4 TRP E 441 GLY E 447 -1 N LYS E 442 O SER E 454
SHEET 1 BA 4 VAL E 367 VAL E 370 0
SHEET 2 BA 4 ALA E 379 TRP E 384 -1 O TRP E 384 N VAL E 367
SHEET 3 BA 4 LEU E 428 TYR E 437 -1 O GLN E 430 N ALA E 379
SHEET 4 BA 4 ALA E 414 VAL E 417 -1 N ALA E 414 O TYR E 437
SHEET 1 BB 4 VAL E 367 VAL E 370 0
SHEET 2 BB 4 ALA E 379 TRP E 384 -1 O TRP E 384 N VAL E 367
SHEET 3 BB 4 GLY E 473 TRP E 478 -1 O GLY E 473 N GLN E 383
SHEET 4 BB 4 LEU E 461 VAL E 464 -1 N ASP E 463 O GLN E 476
SHEET 1 BC 2 TRP E 394 ASP E 398 0
SHEET 2 BC 2 LYS E 410 ASN E 408 -1 O VAL E 407 N TYR E 395
SHEET 1 BD 3 VAL F 35 VAL F 37 0
SHEET 2 BD 3 SER F 343 ASP F 341 -1 O VAL F 338 N ILE F 36
SHEET 3 BD 3 ILE F 346 GLU F 349 -1 O SER F 348 N LYS F 339
SHEET 1 BE 4 HIS F 53 HIS F 60 0
SHEET 2 BE 4 TYR F 63 ARG F 71 -1 O TYR F 65 N LEU F 58
SHEET 3 BE 4 PHE F 77 SER F 85 -1 O TYR F 83 N TRP F 66
SHEET 4 BE 4 GLU F 92 SER F 99 -1 O GLU F 92 N ARG F 84
SHEET 1 BF 4 CYS F 109 TYR F 118 0
SHEET 2 BF 4 PHE F 125 ASN F 133 -1 O TRP F 128 N LYS F 115
SHEET 3 BF 4 ARG F 141 SER F 147 -1 O ALA F 145 N MET F 127
SHEET 4 BF 4 THR F 155 PHE F 160 -1 O PHE F 160 N ALA F 142
SHEET 1 BG 4 CYS F 181 VAL F 185 0
SHEET 2 BG 4 GLY F 191 ALA F 197 -1 O ILE F 194 N ASN F 182
SHEET 3 BG 4 ASP F 202 LEU F 208 -1 O HIS F 204 N SER F 195
SHEET 4 BG 4 ILE F 215 LEU F 222 -1 O ALA F 216 N GLU F 207
SHEET 1 BH 4 GLU F 229 ARG F 236 0
SHEET 2 BH 4 TYR F 239 SER F 245 -1 O TYR F 241 N ILE F 234
SHEET 3 BH 4 ALA F 255 SER F 260 -1 O SER F 260 N TYR F 240
SHEET 4 BH 4 TYR F 271 LEU F 273 -1 O LEU F 273 N ALA F 255
SHEET 1 BI 4 GLN F 282 GLN F 290 0
SHEET 2 BI 4 THR F 295 ARG F 303 -1 O SER F 296 N VAL F 289
SHEET 3 BI 4 GLN F 316 PHE F 324 -1 O LEU F 320 N TYR F 299
SHEET 4 BI 4 LEU F 330 GLU F 331 -1 O GLU F 331 N ASN F 323
SHEET 1 BJ 4 TYR F 357 ASN F 361 0
SHEET 2 BJ 4 TRP F 488 LEU F 492 -1 O LYS F 489 N VAL F 360
SHEET 3 BJ 4 TYR F 450 TYR F 451 -1 N TYR F 451 O TRP F 488
SHEET 4 BJ 4 ASP F 445 GLY F 447 -1 N ILE F 446 O TYR F 450
SHEET 1 BK 4 VAL F 367 VAL F 370 0
SHEET 2 BK 4 ALA F 379 TRP F 384 -1 O TRP F 384 N VAL F 367
SHEET 3 BK 4 LEU F 428 TYR F 437 -1 O LEU F 428 N ILE F 381
SHEET 4 BK 4 ALA F 414 VAL F 417 -1 N ASP F 416 O ILE F 429
SHEET 1 BL 2 TRP F 394 ASP F 398 0
SHEET 2 BL 2 LYS F 410 ASN F 408 -1 O VAL F 407 N TYR F 395
SHEET 1 BM 2 TRP F 441 LYS F 442 0
SHEET 2 BM 2 SER F 454 SER F 455 -1 O SER F 454 N LYS F 442
SHEET 1 BN 2 LEU F 461 VAL F 464 0
SHEET 2 BN 2 ILE F 475 TRP F 478 -1 O GLN F 476 N ASP F 463
LINK O4 BGC G 1 C1 GAL G 2 1555 1555 1.38
LINK O4 BGC H 1 C1 GAL H 2 1555 1555 1.38
LINK O4 BGC I 1 C1 GAL I 2 1555 1555 1.38
LINK O4 BGC J 1 C1 GAL J 2 1555 1555 1.39
LINK O4 BGC K 1 C1 GAL K 2 1555 1555 1.43
LINK O4 BGC L 1 C1 GAL L 2 1555 1555 1.43
CRYST1 107.694 122.376 404.656 90.00 90.00 90.00 P 21 21 21 24
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 0.009286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002471 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
