HEADER TRANSFERASE 16-JUL-15 5CLW
TITLE CRYSTAL STRUCTURE OF HUMAN GLYCOGEN BRANCHING ENZYME (GBE1) IN COMPLEX
TITLE 2 WITH MALTOHEPTAOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,4-ALPHA-GLUCAN-BRANCHING ENZYME;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 38-700;
COMPND 5 SYNONYM: BRANCHER ENZYME,GLYCOGEN-BRANCHING ENZYME;
COMPND 6 EC: 2.4.1.18;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GBE1;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE
KEYWDS TRANSFERASE, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KROJER,D.S.FROESE,S.GOUBIN,C.STRAIN-DAMERELL,P.MAHAJAN,N.BURGESS-
AUTHOR 2 BROWN,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,W.YUE,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 10-JAN-24 5CLW 1 HETSYN LINK
REVDAT 2 29-JUL-20 5CLW 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 07-OCT-15 5CLW 0
JRNL AUTH T.KROJER,D.S.FROESE,S.GOUBIN,C.STRAIN-DAMERELL,P.MAHAJAN,
JRNL AUTH 2 N.BURGESS-BROWN,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,
JRNL AUTH 3 A.EDWARDS,W.YUE,STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF HUMAN GLYCOGEN BRANCHING ENZYME (GBE1)
JRNL TITL 2 IN COMPLEX WITH MALTOHEPTAOSE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 156.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 74138
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3710
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5406
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2534
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5139
REMARK 3 BIN R VALUE (WORKING SET) : 0.2514
REMARK 3 BIN FREE R VALUE : 0.2924
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.94
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 267
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15429
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 235
REMARK 3 SOLVENT ATOMS : 171
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.15050
REMARK 3 B22 (A**2) : 3.24520
REMARK 3 B33 (A**2) : -4.39570
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.364
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.608
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.290
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.665
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.299
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 16188 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 21993 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5418 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 346 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2374 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 16188 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 2038 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 18063 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.00
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.55
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211841.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 313.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.15300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.75800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 4BZY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 3350 , 0.2M SODIUM SUCCINATE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 156.60400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 156.60400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.34450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.26800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.34450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.26800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 156.60400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.34450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.26800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 156.60400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.34450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.26800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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 APPLY THE FOLLOWING TO CHAINS: C, F
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 TYR A 33
REMARK 465 PHE A 34
REMARK 465 GLN A 35
REMARK 465 SER A 36
REMARK 465 MET A 37
REMARK 465 LEU A 38
REMARK 465 LYS A 39
REMARK 465 PRO A 40
REMARK 465 TYR A 41
REMARK 465 ALA A 42
REMARK 465 HIS A 366
REMARK 465 HIS A 367
REMARK 465 GLY A 368
REMARK 465 VAL A 369
REMARK 465 GLY A 370
REMARK 465 GLN A 371
REMARK 465 GLY A 372
REMARK 465 PHE A 373
REMARK 465 SER A 374
REMARK 465 GLY A 375
REMARK 465 ASP A 376
REMARK 465 TYR A 377
REMARK 465 SER A 378
REMARK 465 GLU A 379
REMARK 465 TYR A 380
REMARK 465 PHE A 381
REMARK 465 GLY A 382
REMARK 465 LEU A 383
REMARK 465 ARG A 468
REMARK 465 TYR A 469
REMARK 465 LEU A 470
REMARK 465 TYR B 33
REMARK 465 PHE B 34
REMARK 465 GLN B 35
REMARK 465 SER B 36
REMARK 465 MET B 37
REMARK 465 LEU B 38
REMARK 465 LYS B 39
REMARK 465 PRO B 40
REMARK 465 TYR B 41
REMARK 465 ALA B 42
REMARK 465 VAL B 43
REMARK 465 GLY B 368
REMARK 465 VAL B 369
REMARK 465 GLY B 370
REMARK 465 GLN B 371
REMARK 465 GLY B 372
REMARK 465 PHE B 373
REMARK 465 SER B 374
REMARK 465 GLY B 375
REMARK 465 ASP B 376
REMARK 465 TYR B 377
REMARK 465 SER B 378
REMARK 465 LEU B 700
REMARK 465 TYR C 33
REMARK 465 PHE C 34
REMARK 465 GLN C 35
REMARK 465 SER C 36
REMARK 465 MET C 37
REMARK 465 LEU C 38
REMARK 465 LYS C 39
REMARK 465 PRO C 40
REMARK 465 TYR C 41
REMARK 465 ALA C 42
REMARK 465 VAL C 43
REMARK 465 ASP C 44
REMARK 465 PHE C 45
REMARK 465 HIS C 366
REMARK 465 HIS C 367
REMARK 465 GLY C 368
REMARK 465 VAL C 369
REMARK 465 GLY C 370
REMARK 465 GLN C 371
REMARK 465 GLY C 372
REMARK 465 PHE C 373
REMARK 465 SER C 374
REMARK 465 GLY C 375
REMARK 465 ASP C 376
REMARK 465 TYR C 377
REMARK 465 SER C 378
REMARK 465 GLU C 379
REMARK 465 TYR C 380
REMARK 465 PHE C 381
REMARK 465 GLY C 382
REMARK 465 LEU C 700
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 50 CG CD CE NZ
REMARK 470 GLU A 96 CG CD OE1 OE2
REMARK 470 LYS A 116 CE NZ
REMARK 470 GLN A 130 CG CD OE1 NE2
REMARK 470 LYS A 149 CG CD CE NZ
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 LYS A 187 CE NZ
REMARK 470 LYS A 212 CE NZ
REMARK 470 LYS A 217 CE NZ
REMARK 470 ASP A 320 CG OD1 OD2
REMARK 470 HIS A 365 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 384 CG CD OE1 NE2
REMARK 470 LYS A 451 CD CE NZ
REMARK 470 MET A 499 CG SD CE
REMARK 470 LEU A 506 CG CD1 CD2
REMARK 470 LYS A 554 CG CD CE NZ
REMARK 470 ASN A 557 CG OD1 ND2
REMARK 470 GLU A 656 CG CD OE1 OE2
REMARK 470 ASP B 44 CG OD1 OD2
REMARK 470 GLN B 46 CG CD OE1 NE2
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 GLN B 130 CG CD OE1 NE2
REMARK 470 LYS B 149 CG CD CE NZ
REMARK 470 GLU B 185 CG CD OE1 OE2
REMARK 470 LYS B 192 CG CD CE NZ
REMARK 470 ARG B 195 NE CZ NH1 NH2
REMARK 470 LYS B 212 CE NZ
REMARK 470 LYS B 217 CE NZ
REMARK 470 GLU B 379 CG CD OE1 OE2
REMARK 470 LYS B 451 CE NZ
REMARK 470 LYS B 472 NZ
REMARK 470 LYS B 554 CG CD CE NZ
REMARK 470 GLU B 675 CG CD OE1 OE2
REMARK 470 GLN C 46 CG CD OE1 NE2
REMARK 470 ARG C 47 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 50 CG CD CE NZ
REMARK 470 GLU C 96 CG CD OE1 OE2
REMARK 470 GLN C 130 CG CD OE1 NE2
REMARK 470 VAL C 144 CG2
REMARK 470 LYS C 149 CG CD CE NZ
REMARK 470 LYS C 187 CE NZ
REMARK 470 LYS C 192 CG CD CE NZ
REMARK 470 ARG C 195 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 212 CE NZ
REMARK 470 LYS C 217 CE NZ
REMARK 470 LYS C 294 CG CD CE NZ
REMARK 470 HIS C 365 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 383 CG CD1 CD2
REMARK 470 GLN C 384 CG CD OE1 NE2
REMARK 470 GLU C 387 OE1 OE2
REMARK 470 LYS C 451 CD CE NZ
REMARK 470 LEU C 506 CG CD1 CD2
REMARK 470 LYS C 554 CG CD CE NZ
REMARK 470 ASN C 557 CG OD1 ND2
REMARK 470 LYS C 578 CG CD CE NZ
REMARK 470 ARG C 589 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 593 NE CZ NH1 NH2
REMARK 470 LYS C 631 CG CD CE NZ
REMARK 470 ASP C 635 CG OD1 OD2
REMARK 470 LYS C 647 CG CD CE NZ
REMARK 470 GLN C 661 CG CD OE1 NE2
REMARK 470 GLU C 672 CG CD OE1 OE2
REMARK 470 GLU C 675 CG CD OE1 OE2
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 GLU A 63 -167.76 -104.72
REMARK 500 SER A 308 71.56 -119.16
REMARK 500 CYS A 309 -81.82 -113.25
REMARK 500 ASP A 496 -129.46 51.64
REMARK 500 THR A 501 -62.17 -96.43
REMARK 500 ASN A 502 30.63 -99.20
REMARK 500 MET A 539 115.28 -30.63
REMARK 500 GLU A 547 -139.57 52.90
REMARK 500 ASN A 556 11.15 -142.23
REMARK 500 SER A 630 -40.40 -137.19
REMARK 500 GLU B 63 -167.11 -107.16
REMARK 500 ALA B 247 0.74 -69.48
REMARK 500 ARG B 262 -44.72 -28.09
REMARK 500 ASP B 307 31.55 -93.08
REMARK 500 SER B 308 54.60 -161.42
REMARK 500 CYS B 309 -76.28 -88.59
REMARK 500 ASP B 496 -129.21 49.71
REMARK 500 GLU B 547 -140.75 54.83
REMARK 500 ASN B 556 10.88 -142.98
REMARK 500 SER B 630 -39.29 -138.75
REMARK 500 ALA B 673 83.48 -61.71
REMARK 500 GLU C 63 -166.98 -105.86
REMARK 500 ARG C 262 -44.64 -28.05
REMARK 500 CYS C 309 -96.62 -101.39
REMARK 500 ASP C 496 -128.58 51.50
REMARK 500 GLU C 547 -141.90 54.17
REMARK 500 ASN C 556 11.00 -142.60
REMARK 500 SER C 630 -39.72 -138.72
REMARK 500 GLN C 661 63.37 15.19
REMARK 500 VAL C 698 33.66 -76.35
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5CLW A 38 700 UNP Q04446 GLGB_HUMAN 38 700
DBREF 5CLW B 38 700 UNP Q04446 GLGB_HUMAN 38 700
DBREF 5CLW C 38 700 UNP Q04446 GLGB_HUMAN 38 700
SEQADV 5CLW TYR A 33 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW PHE A 34 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW GLN A 35 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW SER A 36 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW MET A 37 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW SER A 265 UNP Q04446 THR 265 CONFLICT
SEQADV 5CLW VAL A 334 UNP Q04446 ILE 334 CONFLICT
SEQADV 5CLW TYR B 33 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW PHE B 34 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW GLN B 35 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW SER B 36 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW MET B 37 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW SER B 265 UNP Q04446 THR 265 CONFLICT
SEQADV 5CLW VAL B 334 UNP Q04446 ILE 334 CONFLICT
SEQADV 5CLW TYR C 33 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW PHE C 34 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW GLN C 35 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW SER C 36 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW MET C 37 UNP Q04446 EXPRESSION TAG
SEQADV 5CLW SER C 265 UNP Q04446 THR 265 CONFLICT
SEQADV 5CLW VAL C 334 UNP Q04446 ILE 334 CONFLICT
SEQRES 1 A 668 TYR PHE GLN SER MET LEU LYS PRO TYR ALA VAL ASP PHE
SEQRES 2 A 668 GLN ARG ARG TYR LYS GLN PHE SER GLN ILE LEU LYS ASN
SEQRES 3 A 668 ILE GLY GLU ASN GLU GLY GLY ILE ASP LYS PHE SER ARG
SEQRES 4 A 668 GLY TYR GLU SER PHE GLY VAL HIS ARG CYS ALA ASP GLY
SEQRES 5 A 668 GLY LEU TYR CYS LYS GLU TRP ALA PRO GLY ALA GLU GLY
SEQRES 6 A 668 VAL PHE LEU THR GLY ASP PHE ASN GLY TRP ASN PRO PHE
SEQRES 7 A 668 SER TYR PRO TYR LYS LYS LEU ASP TYR GLY LYS TRP GLU
SEQRES 8 A 668 LEU TYR ILE PRO PRO LYS GLN ASN LYS SER VAL LEU VAL
SEQRES 9 A 668 PRO HIS GLY SER LYS LEU LYS VAL VAL ILE THR SER LYS
SEQRES 10 A 668 SER GLY GLU ILE LEU TYR ARG ILE SER PRO TRP ALA LYS
SEQRES 11 A 668 TYR VAL VAL ARG GLU GLY ASP ASN VAL ASN TYR ASP TRP
SEQRES 12 A 668 ILE HIS TRP ASP PRO GLU HIS SER TYR GLU PHE LYS HIS
SEQRES 13 A 668 SER ARG PRO LYS LYS PRO ARG SER LEU ARG ILE TYR GLU
SEQRES 14 A 668 SER HIS VAL GLY ILE SER SER HIS GLU GLY LYS VAL ALA
SEQRES 15 A 668 SER TYR LYS HIS PHE THR CYS ASN VAL LEU PRO ARG ILE
SEQRES 16 A 668 LYS GLY LEU GLY TYR ASN CYS ILE GLN LEU MET ALA ILE
SEQRES 17 A 668 MET GLU HIS ALA TYR TYR ALA SER PHE GLY TYR GLN ILE
SEQRES 18 A 668 THR SER PHE PHE ALA ALA SER SER ARG TYR GLY SER PRO
SEQRES 19 A 668 GLU GLU LEU GLN GLU LEU VAL ASP THR ALA HIS SER MET
SEQRES 20 A 668 GLY ILE ILE VAL LEU LEU ASP VAL VAL HIS SER HIS ALA
SEQRES 21 A 668 SER LYS ASN SER ALA ASP GLY LEU ASN MET PHE ASP GLY
SEQRES 22 A 668 THR ASP SER CYS TYR PHE HIS SER GLY PRO ARG GLY THR
SEQRES 23 A 668 HIS ASP LEU TRP ASP SER ARG LEU PHE ALA TYR SER SER
SEQRES 24 A 668 TRP GLU VAL LEU ARG PHE LEU LEU SER ASN ILE ARG TRP
SEQRES 25 A 668 TRP LEU GLU GLU TYR ARG PHE ASP GLY PHE ARG PHE ASP
SEQRES 26 A 668 GLY VAL THR SER MET LEU TYR HIS HIS HIS GLY VAL GLY
SEQRES 27 A 668 GLN GLY PHE SER GLY ASP TYR SER GLU TYR PHE GLY LEU
SEQRES 28 A 668 GLN VAL ASP GLU ASP ALA LEU THR TYR LEU MET LEU ALA
SEQRES 29 A 668 ASN HIS LEU VAL HIS THR LEU CYS PRO ASP SER ILE THR
SEQRES 30 A 668 ILE ALA GLU ASP VAL SER GLY MET PRO ALA LEU CYS SER
SEQRES 31 A 668 PRO ILE SER GLN GLY GLY GLY GLY PHE ASP TYR ARG LEU
SEQRES 32 A 668 ALA MET ALA ILE PRO ASP LYS TRP ILE GLN LEU LEU LYS
SEQRES 33 A 668 GLU PHE LYS ASP GLU ASP TRP ASN MET GLY ASP ILE VAL
SEQRES 34 A 668 TYR THR LEU THR ASN ARG ARG TYR LEU GLU LYS CYS ILE
SEQRES 35 A 668 ALA TYR ALA GLU SER HIS ASP GLN ALA LEU VAL GLY ASP
SEQRES 36 A 668 LYS SER LEU ALA PHE TRP LEU MET ASP ALA GLU MET TYR
SEQRES 37 A 668 THR ASN MET SER VAL LEU THR PRO PHE THR PRO VAL ILE
SEQRES 38 A 668 ASP ARG GLY ILE GLN LEU HIS LYS MET ILE ARG LEU ILE
SEQRES 39 A 668 THR HIS GLY LEU GLY GLY GLU GLY TYR LEU ASN PHE MET
SEQRES 40 A 668 GLY ASN GLU PHE GLY HIS PRO GLU TRP LEU ASP PHE PRO
SEQRES 41 A 668 ARG LYS GLY ASN ASN GLU SER TYR HIS TYR ALA ARG ARG
SEQRES 42 A 668 GLN PHE HIS LEU THR ASP ASP ASP LEU LEU ARG TYR LYS
SEQRES 43 A 668 PHE LEU ASN ASN PHE ASP ARG ASP MET ASN ARG LEU GLU
SEQRES 44 A 668 GLU ARG TYR GLY TRP LEU ALA ALA PRO GLN ALA TYR VAL
SEQRES 45 A 668 SER GLU LYS HIS GLU GLY ASN LYS ILE ILE ALA PHE GLU
SEQRES 46 A 668 ARG ALA GLY LEU LEU PHE ILE PHE ASN PHE HIS PRO SER
SEQRES 47 A 668 LYS SER TYR THR ASP TYR ARG VAL GLY THR ALA LEU PRO
SEQRES 48 A 668 GLY LYS PHE LYS ILE VAL LEU ASP SER ASP ALA ALA GLU
SEQRES 49 A 668 TYR GLY GLY HIS GLN ARG LEU ASP HIS SER THR ASP PHE
SEQRES 50 A 668 PHE SER GLU ALA PHE GLU HIS ASN GLY ARG PRO TYR SER
SEQRES 51 A 668 LEU LEU VAL TYR ILE PRO SER ARG VAL ALA LEU ILE LEU
SEQRES 52 A 668 GLN ASN VAL ASP LEU
SEQRES 1 B 668 TYR PHE GLN SER MET LEU LYS PRO TYR ALA VAL ASP PHE
SEQRES 2 B 668 GLN ARG ARG TYR LYS GLN PHE SER GLN ILE LEU LYS ASN
SEQRES 3 B 668 ILE GLY GLU ASN GLU GLY GLY ILE ASP LYS PHE SER ARG
SEQRES 4 B 668 GLY TYR GLU SER PHE GLY VAL HIS ARG CYS ALA ASP GLY
SEQRES 5 B 668 GLY LEU TYR CYS LYS GLU TRP ALA PRO GLY ALA GLU GLY
SEQRES 6 B 668 VAL PHE LEU THR GLY ASP PHE ASN GLY TRP ASN PRO PHE
SEQRES 7 B 668 SER TYR PRO TYR LYS LYS LEU ASP TYR GLY LYS TRP GLU
SEQRES 8 B 668 LEU TYR ILE PRO PRO LYS GLN ASN LYS SER VAL LEU VAL
SEQRES 9 B 668 PRO HIS GLY SER LYS LEU LYS VAL VAL ILE THR SER LYS
SEQRES 10 B 668 SER GLY GLU ILE LEU TYR ARG ILE SER PRO TRP ALA LYS
SEQRES 11 B 668 TYR VAL VAL ARG GLU GLY ASP ASN VAL ASN TYR ASP TRP
SEQRES 12 B 668 ILE HIS TRP ASP PRO GLU HIS SER TYR GLU PHE LYS HIS
SEQRES 13 B 668 SER ARG PRO LYS LYS PRO ARG SER LEU ARG ILE TYR GLU
SEQRES 14 B 668 SER HIS VAL GLY ILE SER SER HIS GLU GLY LYS VAL ALA
SEQRES 15 B 668 SER TYR LYS HIS PHE THR CYS ASN VAL LEU PRO ARG ILE
SEQRES 16 B 668 LYS GLY LEU GLY TYR ASN CYS ILE GLN LEU MET ALA ILE
SEQRES 17 B 668 MET GLU HIS ALA TYR TYR ALA SER PHE GLY TYR GLN ILE
SEQRES 18 B 668 THR SER PHE PHE ALA ALA SER SER ARG TYR GLY SER PRO
SEQRES 19 B 668 GLU GLU LEU GLN GLU LEU VAL ASP THR ALA HIS SER MET
SEQRES 20 B 668 GLY ILE ILE VAL LEU LEU ASP VAL VAL HIS SER HIS ALA
SEQRES 21 B 668 SER LYS ASN SER ALA ASP GLY LEU ASN MET PHE ASP GLY
SEQRES 22 B 668 THR ASP SER CYS TYR PHE HIS SER GLY PRO ARG GLY THR
SEQRES 23 B 668 HIS ASP LEU TRP ASP SER ARG LEU PHE ALA TYR SER SER
SEQRES 24 B 668 TRP GLU VAL LEU ARG PHE LEU LEU SER ASN ILE ARG TRP
SEQRES 25 B 668 TRP LEU GLU GLU TYR ARG PHE ASP GLY PHE ARG PHE ASP
SEQRES 26 B 668 GLY VAL THR SER MET LEU TYR HIS HIS HIS GLY VAL GLY
SEQRES 27 B 668 GLN GLY PHE SER GLY ASP TYR SER GLU TYR PHE GLY LEU
SEQRES 28 B 668 GLN VAL ASP GLU ASP ALA LEU THR TYR LEU MET LEU ALA
SEQRES 29 B 668 ASN HIS LEU VAL HIS THR LEU CYS PRO ASP SER ILE THR
SEQRES 30 B 668 ILE ALA GLU ASP VAL SER GLY MET PRO ALA LEU CYS SER
SEQRES 31 B 668 PRO ILE SER GLN GLY GLY GLY GLY PHE ASP TYR ARG LEU
SEQRES 32 B 668 ALA MET ALA ILE PRO ASP LYS TRP ILE GLN LEU LEU LYS
SEQRES 33 B 668 GLU PHE LYS ASP GLU ASP TRP ASN MET GLY ASP ILE VAL
SEQRES 34 B 668 TYR THR LEU THR ASN ARG ARG TYR LEU GLU LYS CYS ILE
SEQRES 35 B 668 ALA TYR ALA GLU SER HIS ASP GLN ALA LEU VAL GLY ASP
SEQRES 36 B 668 LYS SER LEU ALA PHE TRP LEU MET ASP ALA GLU MET TYR
SEQRES 37 B 668 THR ASN MET SER VAL LEU THR PRO PHE THR PRO VAL ILE
SEQRES 38 B 668 ASP ARG GLY ILE GLN LEU HIS LYS MET ILE ARG LEU ILE
SEQRES 39 B 668 THR HIS GLY LEU GLY GLY GLU GLY TYR LEU ASN PHE MET
SEQRES 40 B 668 GLY ASN GLU PHE GLY HIS PRO GLU TRP LEU ASP PHE PRO
SEQRES 41 B 668 ARG LYS GLY ASN ASN GLU SER TYR HIS TYR ALA ARG ARG
SEQRES 42 B 668 GLN PHE HIS LEU THR ASP ASP ASP LEU LEU ARG TYR LYS
SEQRES 43 B 668 PHE LEU ASN ASN PHE ASP ARG ASP MET ASN ARG LEU GLU
SEQRES 44 B 668 GLU ARG TYR GLY TRP LEU ALA ALA PRO GLN ALA TYR VAL
SEQRES 45 B 668 SER GLU LYS HIS GLU GLY ASN LYS ILE ILE ALA PHE GLU
SEQRES 46 B 668 ARG ALA GLY LEU LEU PHE ILE PHE ASN PHE HIS PRO SER
SEQRES 47 B 668 LYS SER TYR THR ASP TYR ARG VAL GLY THR ALA LEU PRO
SEQRES 48 B 668 GLY LYS PHE LYS ILE VAL LEU ASP SER ASP ALA ALA GLU
SEQRES 49 B 668 TYR GLY GLY HIS GLN ARG LEU ASP HIS SER THR ASP PHE
SEQRES 50 B 668 PHE SER GLU ALA PHE GLU HIS ASN GLY ARG PRO TYR SER
SEQRES 51 B 668 LEU LEU VAL TYR ILE PRO SER ARG VAL ALA LEU ILE LEU
SEQRES 52 B 668 GLN ASN VAL ASP LEU
SEQRES 1 C 668 TYR PHE GLN SER MET LEU LYS PRO TYR ALA VAL ASP PHE
SEQRES 2 C 668 GLN ARG ARG TYR LYS GLN PHE SER GLN ILE LEU LYS ASN
SEQRES 3 C 668 ILE GLY GLU ASN GLU GLY GLY ILE ASP LYS PHE SER ARG
SEQRES 4 C 668 GLY TYR GLU SER PHE GLY VAL HIS ARG CYS ALA ASP GLY
SEQRES 5 C 668 GLY LEU TYR CYS LYS GLU TRP ALA PRO GLY ALA GLU GLY
SEQRES 6 C 668 VAL PHE LEU THR GLY ASP PHE ASN GLY TRP ASN PRO PHE
SEQRES 7 C 668 SER TYR PRO TYR LYS LYS LEU ASP TYR GLY LYS TRP GLU
SEQRES 8 C 668 LEU TYR ILE PRO PRO LYS GLN ASN LYS SER VAL LEU VAL
SEQRES 9 C 668 PRO HIS GLY SER LYS LEU LYS VAL VAL ILE THR SER LYS
SEQRES 10 C 668 SER GLY GLU ILE LEU TYR ARG ILE SER PRO TRP ALA LYS
SEQRES 11 C 668 TYR VAL VAL ARG GLU GLY ASP ASN VAL ASN TYR ASP TRP
SEQRES 12 C 668 ILE HIS TRP ASP PRO GLU HIS SER TYR GLU PHE LYS HIS
SEQRES 13 C 668 SER ARG PRO LYS LYS PRO ARG SER LEU ARG ILE TYR GLU
SEQRES 14 C 668 SER HIS VAL GLY ILE SER SER HIS GLU GLY LYS VAL ALA
SEQRES 15 C 668 SER TYR LYS HIS PHE THR CYS ASN VAL LEU PRO ARG ILE
SEQRES 16 C 668 LYS GLY LEU GLY TYR ASN CYS ILE GLN LEU MET ALA ILE
SEQRES 17 C 668 MET GLU HIS ALA TYR TYR ALA SER PHE GLY TYR GLN ILE
SEQRES 18 C 668 THR SER PHE PHE ALA ALA SER SER ARG TYR GLY SER PRO
SEQRES 19 C 668 GLU GLU LEU GLN GLU LEU VAL ASP THR ALA HIS SER MET
SEQRES 20 C 668 GLY ILE ILE VAL LEU LEU ASP VAL VAL HIS SER HIS ALA
SEQRES 21 C 668 SER LYS ASN SER ALA ASP GLY LEU ASN MET PHE ASP GLY
SEQRES 22 C 668 THR ASP SER CYS TYR PHE HIS SER GLY PRO ARG GLY THR
SEQRES 23 C 668 HIS ASP LEU TRP ASP SER ARG LEU PHE ALA TYR SER SER
SEQRES 24 C 668 TRP GLU VAL LEU ARG PHE LEU LEU SER ASN ILE ARG TRP
SEQRES 25 C 668 TRP LEU GLU GLU TYR ARG PHE ASP GLY PHE ARG PHE ASP
SEQRES 26 C 668 GLY VAL THR SER MET LEU TYR HIS HIS HIS GLY VAL GLY
SEQRES 27 C 668 GLN GLY PHE SER GLY ASP TYR SER GLU TYR PHE GLY LEU
SEQRES 28 C 668 GLN VAL ASP GLU ASP ALA LEU THR TYR LEU MET LEU ALA
SEQRES 29 C 668 ASN HIS LEU VAL HIS THR LEU CYS PRO ASP SER ILE THR
SEQRES 30 C 668 ILE ALA GLU ASP VAL SER GLY MET PRO ALA LEU CYS SER
SEQRES 31 C 668 PRO ILE SER GLN GLY GLY GLY GLY PHE ASP TYR ARG LEU
SEQRES 32 C 668 ALA MET ALA ILE PRO ASP LYS TRP ILE GLN LEU LEU LYS
SEQRES 33 C 668 GLU PHE LYS ASP GLU ASP TRP ASN MET GLY ASP ILE VAL
SEQRES 34 C 668 TYR THR LEU THR ASN ARG ARG TYR LEU GLU LYS CYS ILE
SEQRES 35 C 668 ALA TYR ALA GLU SER HIS ASP GLN ALA LEU VAL GLY ASP
SEQRES 36 C 668 LYS SER LEU ALA PHE TRP LEU MET ASP ALA GLU MET TYR
SEQRES 37 C 668 THR ASN MET SER VAL LEU THR PRO PHE THR PRO VAL ILE
SEQRES 38 C 668 ASP ARG GLY ILE GLN LEU HIS LYS MET ILE ARG LEU ILE
SEQRES 39 C 668 THR HIS GLY LEU GLY GLY GLU GLY TYR LEU ASN PHE MET
SEQRES 40 C 668 GLY ASN GLU PHE GLY HIS PRO GLU TRP LEU ASP PHE PRO
SEQRES 41 C 668 ARG LYS GLY ASN ASN GLU SER TYR HIS TYR ALA ARG ARG
SEQRES 42 C 668 GLN PHE HIS LEU THR ASP ASP ASP LEU LEU ARG TYR LYS
SEQRES 43 C 668 PHE LEU ASN ASN PHE ASP ARG ASP MET ASN ARG LEU GLU
SEQRES 44 C 668 GLU ARG TYR GLY TRP LEU ALA ALA PRO GLN ALA TYR VAL
SEQRES 45 C 668 SER GLU LYS HIS GLU GLY ASN LYS ILE ILE ALA PHE GLU
SEQRES 46 C 668 ARG ALA GLY LEU LEU PHE ILE PHE ASN PHE HIS PRO SER
SEQRES 47 C 668 LYS SER TYR THR ASP TYR ARG VAL GLY THR ALA LEU PRO
SEQRES 48 C 668 GLY LYS PHE LYS ILE VAL LEU ASP SER ASP ALA ALA GLU
SEQRES 49 C 668 TYR GLY GLY HIS GLN ARG LEU ASP HIS SER THR ASP PHE
SEQRES 50 C 668 PHE SER GLU ALA PHE GLU HIS ASN GLY ARG PRO TYR SER
SEQRES 51 C 668 LEU LEU VAL TYR ILE PRO SER ARG VAL ALA LEU ILE LEU
SEQRES 52 C 668 GLN ASN VAL ASP LEU
HET GLC D 1 12
HET GLC D 2 11
HET GLC D 3 11
HET GLC D 4 11
HET GLC D 5 11
HET GLC D 6 11
HET GLC D 7 11
HET GLC E 1 12
HET GLC E 2 11
HET GLC E 3 11
HET GLC E 4 11
HET GLC E 5 11
HET GLC E 6 11
HET GLC E 7 11
HET GLC F 1 12
HET GLC F 2 11
HET GLC F 3 11
HET GLC F 4 11
HET GLC F 5 11
HET GLC F 6 11
HET GLC F 7 11
HET NA B1008 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM NA SODIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 4 GLC 21(C6 H12 O6)
FORMUL 7 NA NA 1+
FORMUL 8 HOH *171(H2 O)
HELIX 1 AA1 ASP A 44 GLU A 63 1 20
HELIX 2 AA2 GLY A 65 SER A 70 1 6
HELIX 3 AA3 ARG A 71 SER A 75 5 5
HELIX 4 AA4 PHE A 104 GLY A 106 5 3
HELIX 5 AA5 SER A 215 LEU A 230 1 16
HELIX 6 AA6 TYR A 245 PHE A 249 5 5
HELIX 7 AA7 SER A 261 GLY A 264 5 4
HELIX 8 AA8 SER A 265 MET A 279 1 15
HELIX 9 AA9 SER A 313 ARG A 316 5 4
HELIX 10 AB1 SER A 331 GLU A 348 1 18
HELIX 11 AB2 GLY A 358 TYR A 364 1 7
HELIX 12 AB3 ASP A 386 CYS A 404 1 19
HELIX 13 AB4 PRO A 423 GLY A 427 5 5
HELIX 14 AB5 MET A 437 PHE A 450 1 14
HELIX 15 AB6 LYS A 451 TRP A 455 5 5
HELIX 16 AB7 ASN A 456 ASN A 466 1 11
HELIX 17 AB8 HIS A 480 LEU A 484 5 5
HELIX 18 AB9 SER A 489 ASP A 496 1 8
HELIX 19 AC1 ALA A 497 ASN A 502 1 6
HELIX 20 AC2 THR A 510 GLY A 531 1 22
HELIX 21 AC3 ARG A 553 ASN A 557 5 5
HELIX 22 AC4 GLN A 566 ASP A 571 5 6
HELIX 23 AC5 ARG A 576 GLY A 595 1 20
HELIX 24 AC6 ALA A 654 GLY A 658 5 5
HELIX 25 AC7 PHE B 45 GLU B 63 1 19
HELIX 26 AC8 GLY B 65 SER B 70 1 6
HELIX 27 AC9 ARG B 71 SER B 75 5 5
HELIX 28 AD1 PHE B 104 GLY B 106 5 3
HELIX 29 AD2 SER B 215 LEU B 230 1 16
HELIX 30 AD3 TYR B 245 PHE B 249 5 5
HELIX 31 AD4 SER B 261 GLY B 264 5 4
HELIX 32 AD5 SER B 265 MET B 279 1 15
HELIX 33 AD6 GLY B 314 ARG B 316 5 3
HELIX 34 AD7 SER B 331 GLU B 348 1 18
HELIX 35 AD8 GLY B 358 HIS B 365 1 8
HELIX 36 AD9 ASP B 386 CYS B 404 1 19
HELIX 37 AE1 PRO B 423 GLY B 427 5 5
HELIX 38 AE2 MET B 437 PHE B 450 1 14
HELIX 39 AE3 LYS B 451 TRP B 455 5 5
HELIX 40 AE4 ASN B 456 ASN B 466 1 11
HELIX 41 AE5 HIS B 480 LEU B 484 5 5
HELIX 42 AE6 SER B 489 ASP B 496 1 8
HELIX 43 AE7 ALA B 497 TYR B 500 5 4
HELIX 44 AE8 THR B 510 GLY B 531 1 22
HELIX 45 AE9 ARG B 553 ASN B 557 5 5
HELIX 46 AF1 GLN B 566 ASP B 571 5 6
HELIX 47 AF2 ARG B 576 GLY B 595 1 20
HELIX 48 AF3 ALA B 654 GLY B 658 5 5
HELIX 49 AF4 ARG C 47 GLU C 63 1 17
HELIX 50 AF5 GLY C 65 SER C 70 1 6
HELIX 51 AF6 ARG C 71 SER C 75 5 5
HELIX 52 AF7 PHE C 104 GLY C 106 5 3
HELIX 53 AF8 SER C 215 VAL C 223 1 9
HELIX 54 AF9 VAL C 223 LEU C 230 1 8
HELIX 55 AG1 TYR C 245 PHE C 249 5 5
HELIX 56 AG2 SER C 261 GLY C 264 5 4
HELIX 57 AG3 SER C 265 MET C 279 1 15
HELIX 58 AG4 GLY C 314 ARG C 316 5 3
HELIX 59 AG5 SER C 331 GLU C 348 1 18
HELIX 60 AG6 GLY C 358 TYR C 364 1 7
HELIX 61 AG7 ASP C 386 CYS C 404 1 19
HELIX 62 AG8 PRO C 423 GLY C 427 5 5
HELIX 63 AG9 MET C 437 PHE C 450 1 14
HELIX 64 AH1 LYS C 451 TRP C 455 5 5
HELIX 65 AH2 ASN C 456 ASN C 466 1 11
HELIX 66 AH3 HIS C 480 LEU C 484 5 5
HELIX 67 AH4 SER C 489 ASP C 496 1 8
HELIX 68 AH5 ALA C 497 TYR C 500 5 4
HELIX 69 AH6 THR C 510 GLY C 531 1 22
HELIX 70 AH7 GLY C 540 GLY C 544 5 5
HELIX 71 AH8 ARG C 553 ASN C 557 5 5
HELIX 72 AH9 GLN C 566 ASP C 571 5 6
HELIX 73 AI1 ARG C 576 GLY C 595 1 20
HELIX 74 AI2 ALA C 654 GLY C 658 5 5
SHEET 1 AA1 4 GLY A 77 ARG A 80 0
SHEET 2 AA1 4 LEU A 86 TRP A 91 -1 O LYS A 89 N GLY A 77
SHEET 3 AA1 4 LYS A 121 ILE A 126 -1 O LEU A 124 N CYS A 88
SHEET 4 AA1 4 LYS A 115 LYS A 116 -1 N LYS A 115 O GLU A 123
SHEET 1 AA2 3 GLY A 97 GLY A 102 0
SHEET 2 AA2 3 LYS A 141 THR A 147 -1 O VAL A 145 N PHE A 99
SHEET 3 AA2 3 ILE A 153 ARG A 156 -1 O LEU A 154 N ILE A 146
SHEET 1 AA3 4 GLY A 97 GLY A 102 0
SHEET 2 AA3 4 LYS A 141 THR A 147 -1 O VAL A 145 N PHE A 99
SHEET 3 AA3 4 ASP A 174 ILE A 176 -1 O TRP A 175 N LEU A 142
SHEET 4 AA3 4 VAL A 164 VAL A 165 -1 N VAL A 165 O ASP A 174
SHEET 1 AA4 9 LEU A 197 HIS A 203 0
SHEET 2 AA4 9 CYS A 234 MET A 238 1 O MET A 238 N SER A 202
SHEET 3 AA4 9 ILE A 282 VAL A 288 1 O LEU A 284 N LEU A 237
SHEET 4 AA4 9 GLY A 353 ASP A 357 1 O ARG A 355 N VAL A 287
SHEET 5 AA4 9 ILE A 408 ALA A 411 1 O ILE A 410 N PHE A 356
SHEET 6 AA4 9 TYR A 433 LEU A 435 1 N TYR A 433 O THR A 409
SHEET 7 AA4 9 CYS A 473 ALA A 475 1 O ILE A 474 N ARG A 434
SHEET 8 AA4 9 GLY A 534 PHE A 538 1 O GLY A 534 N ALA A 475
SHEET 9 AA4 9 LEU A 197 HIS A 203 1 N ILE A 199 O TYR A 535
SHEET 1 AA5 2 MET A 241 HIS A 243 0
SHEET 2 AA5 2 ILE A 253 ALA A 259 -1 O ALA A 258 N GLU A 242
SHEET 1 AA6 3 ALA A 292 SER A 293 0
SHEET 2 AA6 3 SER A 324 ARG A 325 -1 O ARG A 325 N ALA A 292
SHEET 3 AA6 3 THR A 318 HIS A 319 -1 N HIS A 319 O SER A 324
SHEET 1 AA7 6 TYR A 603 HIS A 608 0
SHEET 2 AA7 6 ILE A 613 ARG A 618 -1 O ALA A 615 N GLU A 606
SHEET 3 AA7 6 LEU A 621 ASN A 626 -1 O PHE A 623 N PHE A 616
SHEET 4 AA7 6 VAL A 691 VAL A 698 -1 O LEU A 693 N ILE A 624
SHEET 5 AA7 6 GLY A 644 ASP A 651 -1 N LEU A 650 O ILE A 694
SHEET 6 AA7 6 PHE A 669 SER A 671 -1 O SER A 671 N GLY A 644
SHEET 1 AA8 2 TYR A 633 THR A 640 0
SHEET 2 AA8 2 TYR A 681 ILE A 687 -1 O LEU A 683 N VAL A 638
SHEET 1 AA9 4 GLY B 77 ARG B 80 0
SHEET 2 AA9 4 LEU B 86 TRP B 91 -1 O LYS B 89 N GLY B 77
SHEET 3 AA9 4 LYS B 121 ILE B 126 -1 O LEU B 124 N CYS B 88
SHEET 4 AA9 4 LYS B 115 LYS B 116 -1 N LYS B 115 O GLU B 123
SHEET 1 AB1 3 GLY B 97 GLY B 102 0
SHEET 2 AB1 3 LYS B 141 THR B 147 -1 O VAL B 145 N PHE B 99
SHEET 3 AB1 3 ILE B 153 ARG B 156 -1 O LEU B 154 N ILE B 146
SHEET 1 AB2 4 GLY B 97 GLY B 102 0
SHEET 2 AB2 4 LYS B 141 THR B 147 -1 O VAL B 145 N PHE B 99
SHEET 3 AB2 4 ASP B 174 ILE B 176 -1 O TRP B 175 N LEU B 142
SHEET 4 AB2 4 VAL B 164 VAL B 165 -1 N VAL B 165 O ASP B 174
SHEET 1 AB3 9 LEU B 197 HIS B 203 0
SHEET 2 AB3 9 CYS B 234 MET B 238 1 O GLN B 236 N SER B 202
SHEET 3 AB3 9 ILE B 282 VAL B 288 1 O LEU B 284 N LEU B 237
SHEET 4 AB3 9 GLY B 353 ASP B 357 1 O ARG B 355 N VAL B 287
SHEET 5 AB3 9 ILE B 408 ALA B 411 1 O ILE B 410 N PHE B 356
SHEET 6 AB3 9 TYR B 433 LEU B 435 1 O TYR B 433 N ALA B 411
SHEET 7 AB3 9 LYS B 472 ALA B 475 1 O ILE B 474 N ARG B 434
SHEET 8 AB3 9 GLY B 534 PHE B 538 1 O GLY B 534 N ALA B 475
SHEET 9 AB3 9 LEU B 197 HIS B 203 1 N ILE B 199 O TYR B 535
SHEET 1 AB4 2 MET B 241 HIS B 243 0
SHEET 2 AB4 2 ILE B 253 ALA B 259 -1 O ALA B 258 N GLU B 242
SHEET 1 AB5 3 ALA B 292 SER B 293 0
SHEET 2 AB5 3 SER B 324 ARG B 325 -1 O ARG B 325 N ALA B 292
SHEET 3 AB5 3 THR B 318 HIS B 319 -1 N HIS B 319 O SER B 324
SHEET 1 AB6 6 TYR B 603 HIS B 608 0
SHEET 2 AB6 6 ILE B 613 ARG B 618 -1 O ALA B 615 N GLU B 606
SHEET 3 AB6 6 LEU B 621 ASN B 626 -1 O PHE B 623 N PHE B 616
SHEET 4 AB6 6 VAL B 691 ASN B 697 -1 O LEU B 693 N ILE B 624
SHEET 5 AB6 6 GLY B 644 ASP B 651 -1 N LEU B 650 O ILE B 694
SHEET 6 AB6 6 PHE B 669 SER B 671 -1 O PHE B 669 N PHE B 646
SHEET 1 AB7 2 TYR B 633 THR B 640 0
SHEET 2 AB7 2 TYR B 681 ILE B 687 -1 O VAL B 685 N TYR B 636
SHEET 1 AB8 4 GLY C 77 ARG C 80 0
SHEET 2 AB8 4 LEU C 86 TRP C 91 -1 O LYS C 89 N GLY C 77
SHEET 3 AB8 4 LYS C 121 ILE C 126 -1 O LEU C 124 N CYS C 88
SHEET 4 AB8 4 LYS C 115 LYS C 116 -1 N LYS C 115 O GLU C 123
SHEET 1 AB9 3 GLY C 97 GLY C 102 0
SHEET 2 AB9 3 LYS C 141 THR C 147 -1 O VAL C 145 N PHE C 99
SHEET 3 AB9 3 ILE C 153 ARG C 156 -1 O LEU C 154 N ILE C 146
SHEET 1 AC1 4 GLY C 97 GLY C 102 0
SHEET 2 AC1 4 LYS C 141 THR C 147 -1 O VAL C 145 N PHE C 99
SHEET 3 AC1 4 ASP C 174 ILE C 176 -1 O TRP C 175 N LEU C 142
SHEET 4 AC1 4 VAL C 164 VAL C 165 -1 N VAL C 165 O ASP C 174
SHEET 1 AC2 9 LEU C 197 HIS C 203 0
SHEET 2 AC2 9 CYS C 234 MET C 238 1 O MET C 238 N SER C 202
SHEET 3 AC2 9 ILE C 282 VAL C 288 1 O LEU C 284 N LEU C 237
SHEET 4 AC2 9 GLY C 353 ASP C 357 1 O ARG C 355 N VAL C 287
SHEET 5 AC2 9 ILE C 408 ALA C 411 1 O ILE C 410 N PHE C 356
SHEET 6 AC2 9 TYR C 433 LEU C 435 1 O TYR C 433 N ALA C 411
SHEET 7 AC2 9 LYS C 472 ALA C 475 1 O ILE C 474 N ARG C 434
SHEET 8 AC2 9 GLY C 534 PHE C 538 1 O GLY C 534 N ALA C 475
SHEET 9 AC2 9 LEU C 197 HIS C 203 1 N ILE C 199 O TYR C 535
SHEET 1 AC3 2 MET C 241 HIS C 243 0
SHEET 2 AC3 2 ILE C 253 ALA C 259 -1 O ALA C 258 N GLU C 242
SHEET 1 AC4 3 ALA C 292 SER C 293 0
SHEET 2 AC4 3 SER C 324 ARG C 325 -1 O ARG C 325 N ALA C 292
SHEET 3 AC4 3 THR C 318 HIS C 319 -1 N HIS C 319 O SER C 324
SHEET 1 AC5 6 TYR C 603 HIS C 608 0
SHEET 2 AC5 6 ILE C 613 ARG C 618 -1 O ALA C 615 N GLU C 606
SHEET 3 AC5 6 LEU C 621 ASN C 626 -1 O PHE C 623 N PHE C 616
SHEET 4 AC5 6 VAL C 691 ASN C 697 -1 O LEU C 693 N ILE C 624
SHEET 5 AC5 6 GLY C 644 ASP C 651 -1 N LEU C 650 O ILE C 694
SHEET 6 AC5 6 PHE C 669 SER C 671 -1 O PHE C 669 N PHE C 646
SHEET 1 AC6 2 TYR C 633 THR C 640 0
SHEET 2 AC6 2 TYR C 681 ILE C 687 -1 O LEU C 683 N VAL C 638
LINK O4 GLC D 1 C1 GLC D 2 1555 1555 1.42
LINK O4 GLC D 2 C1 GLC D 3 1555 1555 1.39
LINK O4 GLC D 3 C1 GLC D 4 1555 1555 1.42
LINK O4 GLC D 4 C1 GLC D 5 1555 1555 1.43
LINK O4 GLC D 5 C1 GLC D 6 1555 1555 1.45
LINK O4 GLC D 6 C1 GLC D 7 1555 1555 1.45
LINK O4 GLC E 1 C1 GLC E 2 1555 1555 1.41
LINK O4 GLC E 2 C1 GLC E 3 1555 1555 1.37
LINK O4 GLC E 3 C1 GLC E 4 1555 1555 1.41
LINK O4 GLC E 4 C1 GLC E 5 1555 1555 1.44
LINK O4 GLC E 5 C1 GLC E 6 1555 1555 1.46
LINK O4 GLC E 6 C1 GLC E 7 1555 1555 1.45
LINK O4 GLC F 1 C1 GLC F 2 1555 1555 1.42
LINK O4 GLC F 2 C1 GLC F 3 1555 1555 1.33
LINK O4 GLC F 3 C1 GLC F 4 1555 1555 1.41
LINK O4 GLC F 4 C1 GLC F 5 1555 1555 1.44
LINK O4 GLC F 5 C1 GLC F 6 1555 1555 1.45
LINK O4 GLC F 6 C1 GLC F 7 1555 1555 1.45
CRYST1 116.689 164.536 313.208 90.00 90.00 90.00 C 2 2 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 0.008570 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006078 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003193 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
