HEADER HYDROLASE 29-OCT-02 1O7A
TITLE HUMAN BETA-HEXOSAMINIDASE B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-HEXOSAMINIDASE BETA CHAIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: 42-556;
COMPND 5 SYNONYM: BETA-N-ACETYLHEXOSAMINIDASE, HEXOSAMINIDASE B, N-ACETYL-
COMPND 6 BETA-GLUCOSAMINIDASE;
COMPND 7 EC: 3.2.1.52;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: RECOMBINANTLY EXPRESSED FRAGMENT COMPOSED OF RESIDUES
COMPND 10 42-556, N-TERMINUS OF MATURE HUMAN ENZYME IS BETWEEN RESIDUE 48 - 50
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PACYM-1BETA
KEYWDS HYDROLASE, GLYCOSYL HYDROLASE, HEXOSAMINIDASE, LYSOSOMAL,
KEYWDS 2 SPHINGOLIPID DEGRADATION, SANDHOFF DISEASE, BA8-BARREL, GLYCOSIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.MAIER,N.STRATER,C.SCHUETTE,R.KLINGENSTEIN,K.SANDHOFF,W.SAENGER
REVDAT 8 18-NOV-20 1O7A 1 JRNL HETSYN
REVDAT 7 29-JUL-20 1O7A 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE ATOM
REVDAT 6 09-OCT-19 1O7A 1 REMARK
REVDAT 5 08-MAY-19 1O7A 1 REMARK
REVDAT 4 24-APR-19 1O7A 1 SOURCE LINK
REVDAT 3 25-APR-12 1O7A 1 REMARK VERSN HETSYN FORMUL
REVDAT 3 2 1 SITE
REVDAT 2 24-FEB-09 1O7A 1 VERSN
REVDAT 1 23-OCT-03 1O7A 0
JRNL AUTH T.MAIER,N.STRATER,C.SCHUETTE,R.KLINGENSTEIN,K.SANDHOFF,
JRNL AUTH 2 W.SAENGER
JRNL TITL THE X-RAY CRYSTAL STRUCTURE OF HUMAN BETA-HEXOSAMINIDASE B
JRNL TITL 2 PROVIDES NEW INSIGHTS INTO SANDHOFF DISEASE
JRNL REF J.MOL.BIOL. V. 328 669 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12706724
JRNL DOI 10.1016/S0022-2836(03)00311-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.G.SCHUETTE,J.WEISSGERBER,K.SANDHOFF
REMARK 1 TITL COMPLETE ANALYSIS OF THE GLYCOSYLATION AND DISULFIDE BOND
REMARK 1 TITL 2 PATTERN OF HUMAN BETA-HEXOSAMINIDASE B BY MALDI-MS
REMARK 1 REF GLYCOBIOLOGY V. 11 549 2001
REMARK 1 REFN ISSN 0959-6658
REMARK 1 PMID 11447134
REMARK 1 DOI 10.1093/GLYCOB/11.7.549
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.A.BOOSE,C.J.TIFFT,R.L.PROIA,R.MYEROWITZ
REMARK 1 TITL SYNTHESIS OF A HUMAN LYSOSOMAL ENZYME, BETA-HEXOSAMINIDASE
REMARK 1 TITL 2 B, USING THE BACULAOVIRUS EXPRESSION SYSTEM
REMARK 1 REF PROTEIN EXPR.PURIF. V. 1 111 1990
REMARK 1 REFN ISSN 1046-5928
REMARK 1 PMID 1967020
REMARK 1 DOI 10.1016/1046-5928(90)90003-H
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4883320.780
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 175064
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1708
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 17305
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 174
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23420
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 402
REMARK 3 SOLVENT ATOMS : 2326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.86000
REMARK 3 B22 (A**2) : 8.56000
REMARK 3 B33 (A**2) : -17.42000
REMARK 3 B12 (A**2) : 6.16000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.970
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.370 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.150 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.040 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 56.61
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : LIGANDS.PAR
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : LIGANDS.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1290011558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93400
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 180325
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.35600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOUR DIFFUSION PROTEIN
REMARK 280 SOLUTION: 10 MG/ML HEXB IN 10MM SODIUM CITRATE, 100 MM NACL,
REMARK 280 PH6.0 RESERVOIR SOLUTION: 100 MM SODIUM CITRATE, PH 5.6, 16% (V/
REMARK 280 V) ETHYLENE GLYCOL, 10%(V/V) POLYETHYLENE GLYCOL 8000, PH 5.60,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.57233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 163.14467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 163.14467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 81.57233
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I, 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K
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 BIOMT1 2 -0.500000 -0.866025 0.000000 245.89650
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 141.96841
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 81.57233
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 245.89650
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 141.96841
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 81.57233
REMARK 400
REMARK 400 COMPOUND
REMARK 400 BETA-HEXOSAMINIDASE IS RESPONSIBLE FOR THE DEGRADATION
REMARK 400 OF GM2 GANGLIOSIDES, AND A VARIETY OF OTHER MOLECULES CONTAINING
REMARK 400 TERMINAL N-ACETYL HEXOSAMINES, IN THE BRAIN AND OTHER TISSUES.
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 ALA A 42
REMARK 465 ALA A 43
REMARK 465 ARG A 44
REMARK 465 ALA A 45
REMARK 465 PRO A 46
REMARK 465 SER A 47
REMARK 465 VAL A 48
REMARK 465 SER A 49
REMARK 465 ALA A 50
REMARK 465 LYS A 51
REMARK 465 PRO A 52
REMARK 465 GLY A 53
REMARK 465 PHE A 108
REMARK 465 TYR A 109
REMARK 465 LYS A 110
REMARK 465 TRP A 111
REMARK 465 HIS A 112
REMARK 465 HIS A 113
REMARK 465 GLU A 114
REMARK 465 PRO A 115
REMARK 465 ALA A 116
REMARK 465 GLU A 117
REMARK 465 PHE A 118
REMARK 465 GLN A 119
REMARK 465 ALA A 120
REMARK 465 LYS A 121
REMARK 465 ARG A 312
REMARK 465 GLN A 313
REMARK 465 ASN A 314
REMARK 465 ASN A 555
REMARK 465 MET A 556
REMARK 465 ALA B 42
REMARK 465 ALA B 43
REMARK 465 ARG B 44
REMARK 465 ALA B 45
REMARK 465 PRO B 46
REMARK 465 SER B 47
REMARK 465 VAL B 48
REMARK 465 SER B 49
REMARK 465 ALA B 50
REMARK 465 LYS B 51
REMARK 465 PRO B 52
REMARK 465 GLY B 53
REMARK 465 PHE B 108
REMARK 465 TYR B 109
REMARK 465 LYS B 110
REMARK 465 TRP B 111
REMARK 465 HIS B 112
REMARK 465 HIS B 113
REMARK 465 GLU B 114
REMARK 465 PRO B 115
REMARK 465 ALA B 116
REMARK 465 GLU B 117
REMARK 465 PHE B 118
REMARK 465 GLN B 119
REMARK 465 ALA B 120
REMARK 465 LYS B 121
REMARK 465 ARG B 312
REMARK 465 GLN B 313
REMARK 465 ASN B 314
REMARK 465 ASN B 555
REMARK 465 MET B 556
REMARK 465 ALA C 42
REMARK 465 ALA C 43
REMARK 465 ARG C 44
REMARK 465 ALA C 45
REMARK 465 PRO C 46
REMARK 465 SER C 47
REMARK 465 VAL C 48
REMARK 465 SER C 49
REMARK 465 ALA C 50
REMARK 465 LYS C 51
REMARK 465 PRO C 52
REMARK 465 GLY C 53
REMARK 465 PHE C 108
REMARK 465 TYR C 109
REMARK 465 LYS C 110
REMARK 465 TRP C 111
REMARK 465 HIS C 112
REMARK 465 HIS C 113
REMARK 465 GLU C 114
REMARK 465 PRO C 115
REMARK 465 ALA C 116
REMARK 465 GLU C 117
REMARK 465 PHE C 118
REMARK 465 GLN C 119
REMARK 465 ALA C 120
REMARK 465 LYS C 121
REMARK 465 ARG C 312
REMARK 465 GLN C 313
REMARK 465 ASN C 314
REMARK 465 ASN C 555
REMARK 465 MET C 556
REMARK 465 ALA D 42
REMARK 465 ALA D 43
REMARK 465 ARG D 44
REMARK 465 ALA D 45
REMARK 465 PRO D 46
REMARK 465 SER D 47
REMARK 465 VAL D 48
REMARK 465 SER D 49
REMARK 465 ALA D 50
REMARK 465 LYS D 51
REMARK 465 PRO D 52
REMARK 465 GLY D 53
REMARK 465 PHE D 108
REMARK 465 TYR D 109
REMARK 465 LYS D 110
REMARK 465 TRP D 111
REMARK 465 HIS D 112
REMARK 465 HIS D 113
REMARK 465 GLU D 114
REMARK 465 PRO D 115
REMARK 465 ALA D 116
REMARK 465 GLU D 117
REMARK 465 PHE D 118
REMARK 465 GLN D 119
REMARK 465 ALA D 120
REMARK 465 LYS D 121
REMARK 465 ARG D 312
REMARK 465 GLN D 313
REMARK 465 ASN D 314
REMARK 465 GLU D 554
REMARK 465 ASN D 555
REMARK 465 MET D 556
REMARK 465 ALA E 42
REMARK 465 ALA E 43
REMARK 465 ARG E 44
REMARK 465 ALA E 45
REMARK 465 PRO E 46
REMARK 465 SER E 47
REMARK 465 VAL E 48
REMARK 465 SER E 49
REMARK 465 ALA E 50
REMARK 465 LYS E 51
REMARK 465 PRO E 52
REMARK 465 GLY E 53
REMARK 465 PHE E 108
REMARK 465 TYR E 109
REMARK 465 LYS E 110
REMARK 465 TRP E 111
REMARK 465 HIS E 112
REMARK 465 HIS E 113
REMARK 465 GLU E 114
REMARK 465 PRO E 115
REMARK 465 ALA E 116
REMARK 465 GLU E 117
REMARK 465 PHE E 118
REMARK 465 GLN E 119
REMARK 465 ALA E 120
REMARK 465 LYS E 121
REMARK 465 ARG E 312
REMARK 465 GLN E 313
REMARK 465 ASN E 314
REMARK 465 ASN E 555
REMARK 465 MET E 556
REMARK 465 ALA F 42
REMARK 465 ALA F 43
REMARK 465 ARG F 44
REMARK 465 ALA F 45
REMARK 465 PRO F 46
REMARK 465 SER F 47
REMARK 465 VAL F 48
REMARK 465 SER F 49
REMARK 465 ALA F 50
REMARK 465 LYS F 51
REMARK 465 PRO F 52
REMARK 465 GLY F 53
REMARK 465 PHE F 108
REMARK 465 TYR F 109
REMARK 465 LYS F 110
REMARK 465 TRP F 111
REMARK 465 HIS F 112
REMARK 465 HIS F 113
REMARK 465 GLU F 114
REMARK 465 PRO F 115
REMARK 465 ALA F 116
REMARK 465 GLU F 117
REMARK 465 PHE F 118
REMARK 465 GLN F 119
REMARK 465 ALA F 120
REMARK 465 LYS F 121
REMARK 465 ARG F 312
REMARK 465 GLN F 313
REMARK 465 ASN F 314
REMARK 465 ASN F 555
REMARK 465 MET F 556
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 GLU A 554 CA C O CB CG CD OE1
REMARK 470 GLU A 554 OE2
REMARK 470 GLU B 554 CA C O CB CG CD OE1
REMARK 470 GLU B 554 OE2
REMARK 470 GLU C 554 CA C O CB CG CD OE1
REMARK 470 GLU C 554 OE2
REMARK 470 HIS D 553 CA C O CB CG ND1 CD2
REMARK 470 HIS D 553 CE1 NE2
REMARK 470 GLU E 554 CA C O CB CG CD OE1
REMARK 470 GLU E 554 OE2
REMARK 470 GLU F 554 CA C O CB CG CD OE1
REMARK 470 GLU F 554 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N LYS E 315 O HOH E 2243 2.11
REMARK 500 O HOH B 2070 O HOH B 2086 2.13
REMARK 500 N THR E 122 O HOH E 2057 2.15
REMARK 500 NH1 ARG F 99 O HOH F 2044 2.17
REMARK 500 O HOH A 2178 O HOH A 2214 2.17
REMARK 500 O HOH A 2288 O HOH A 2299 2.19
REMARK 500 O HOH C 2075 O HOH C 2093 2.19
REMARK 500 O HOH F 2083 O HOH F 2088 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN A 142 CG ASN A 142 ND2 0.318
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 142 OD1 - CG - ND2 ANGL. DEV. = -25.8 DEGREES
REMARK 500 ASN A 142 CB - CG - ND2 ANGL. DEV. = 16.8 DEGREES
REMARK 500 PRO E 156 C - N - CD ANGL. DEV. = -15.5 DEGREES
REMARK 500 LEU F 316 CA - CB - CG ANGL. DEV. = -15.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 76 48.14 -149.46
REMARK 500 ASP A 240 -158.67 -169.79
REMARK 500 HIS A 264 59.83 -119.23
REMARK 500 LEU A 316 163.77 171.80
REMARK 500 GLU A 355 53.87 39.40
REMARK 500 ARG A 520 -7.59 -141.42
REMARK 500 ALA A 548 150.46 -49.30
REMARK 500 ASP B 240 -162.20 -170.95
REMARK 500 HIS B 264 58.57 -118.85
REMARK 500 LEU B 316 131.49 142.12
REMARK 500 TYR B 547 -173.72 -173.23
REMARK 500 PHE C 106 42.91 -106.55
REMARK 500 ASP C 240 -160.51 -169.34
REMARK 500 HIS C 264 56.07 -111.95
REMARK 500 SER C 318 -179.04 141.75
REMARK 500 PRO C 321 171.95 -59.31
REMARK 500 ALA C 542 59.36 -67.46
REMARK 500 TRP D 57 119.85 -161.20
REMARK 500 ASP D 240 -158.20 -170.98
REMARK 500 HIS D 264 56.29 -119.81
REMARK 500 ASP D 304 13.39 58.00
REMARK 500 LEU D 316 141.84 155.48
REMARK 500 GLU D 355 48.92 36.41
REMARK 500 SER D 427 105.52 -59.20
REMARK 500 ARG D 520 11.83 -146.43
REMARK 500 GLN E 126 145.24 -172.13
REMARK 500 ASP E 240 -159.76 -163.53
REMARK 500 HIS E 264 57.35 -112.66
REMARK 500 LEU E 316 138.68 171.98
REMARK 500 ASP E 317 37.38 -83.98
REMARK 500 GLU E 355 47.85 39.98
REMARK 500 ASN E 552 45.47 -56.62
REMARK 500 HIS E 553 -59.21 -125.21
REMARK 500 ASP F 182 -169.32 -75.69
REMARK 500 ASP F 240 -162.13 -165.70
REMARK 500 HIS F 264 62.44 -111.07
REMARK 500 LEU F 316 136.40 139.88
REMARK 500 GLU F 355 49.72 38.57
REMARK 500 LEU F 488 78.49 -117.13
REMARK 500 ARG F 520 25.47 -157.09
REMARK 500 TYR F 547 -176.40 -172.58
REMARK 500 ASN F 552 65.02 -68.49
REMARK 500 HIS F 553 -63.85 -163.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASN A 142 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E2072 DISTANCE = 6.05 ANGSTROMS
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QBD RELATED DB: PDB
REMARK 900 HEXOSAMINIDASE BETA CHAIN, GLYCOSYL HYDROLASE FAMILY 20,
REMARK 900 THEORETICAL MODEL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 EXPRESSED CONSTRUCT CONTAINS RESIDUES 42-TO 556 OF THE
REMARK 999 PRECURSOR PROTEIN
DBREF 1O7A A 42 556 UNP P07686 HEXB_HUMAN 42 556
DBREF 1O7A B 42 556 UNP P07686 HEXB_HUMAN 42 556
DBREF 1O7A C 42 556 UNP P07686 HEXB_HUMAN 42 556
DBREF 1O7A D 42 556 UNP P07686 HEXB_HUMAN 42 556
DBREF 1O7A E 42 556 UNP P07686 HEXB_HUMAN 42 556
DBREF 1O7A F 42 556 UNP P07686 HEXB_HUMAN 42 556
SEQRES 1 A 515 ALA ALA ARG ALA PRO SER VAL SER ALA LYS PRO GLY PRO
SEQRES 2 A 515 ALA LEU TRP PRO LEU PRO LEU SER VAL LYS MET THR PRO
SEQRES 3 A 515 ASN LEU LEU HIS LEU ALA PRO GLU ASN PHE TYR ILE SER
SEQRES 4 A 515 HIS SER PRO ASN SER THR ALA GLY PRO SER CYS THR LEU
SEQRES 5 A 515 LEU GLU GLU ALA PHE ARG ARG TYR HIS GLY TYR ILE PHE
SEQRES 6 A 515 GLY PHE TYR LYS TRP HIS HIS GLU PRO ALA GLU PHE GLN
SEQRES 7 A 515 ALA LYS THR GLN VAL GLN GLN LEU LEU VAL SER ILE THR
SEQRES 8 A 515 LEU GLN SER GLU CYS ASP ALA PHE PRO ASN ILE SER SER
SEQRES 9 A 515 ASP GLU SER TYR THR LEU LEU VAL LYS GLU PRO VAL ALA
SEQRES 10 A 515 VAL LEU LYS ALA ASN ARG VAL TRP GLY ALA LEU ARG GLY
SEQRES 11 A 515 LEU GLU THR PHE SER GLN LEU VAL TYR GLN ASP SER TYR
SEQRES 12 A 515 GLY THR PHE THR ILE ASN GLU SER THR ILE ILE ASP SER
SEQRES 13 A 515 PRO ARG PHE SER HIS ARG GLY ILE LEU ILE ASP THR SER
SEQRES 14 A 515 ARG HIS TYR LEU PRO VAL LYS ILE ILE LEU LYS THR LEU
SEQRES 15 A 515 ASP ALA MET ALA PHE ASN LYS PHE ASN VAL LEU HIS TRP
SEQRES 16 A 515 HIS ILE VAL ASP ASP GLN SER PHE PRO TYR GLN SER ILE
SEQRES 17 A 515 THR PHE PRO GLU LEU SER ASN LYS GLY SER TYR SER LEU
SEQRES 18 A 515 SER HIS VAL TYR THR PRO ASN ASP VAL ARG MET VAL ILE
SEQRES 19 A 515 GLU TYR ALA ARG LEU ARG GLY ILE ARG VAL LEU PRO GLU
SEQRES 20 A 515 PHE ASP THR PRO GLY HIS THR LEU SER TRP GLY LYS GLY
SEQRES 21 A 515 GLN LYS ASP LEU LEU THR PRO CYS TYR SER ARG GLN ASN
SEQRES 22 A 515 LYS LEU ASP SER PHE GLY PRO ILE ASN PRO THR LEU ASN
SEQRES 23 A 515 THR THR TYR SER PHE LEU THR THR PHE PHE LYS GLU ILE
SEQRES 24 A 515 SER GLU VAL PHE PRO ASP GLN PHE ILE HIS LEU GLY GLY
SEQRES 25 A 515 ASP GLU VAL GLU PHE LYS CYS TRP GLU SER ASN PRO LYS
SEQRES 26 A 515 ILE GLN ASP PHE MET ARG GLN LYS GLY PHE GLY THR ASP
SEQRES 27 A 515 PHE LYS LYS LEU GLU SER PHE TYR ILE GLN LYS VAL LEU
SEQRES 28 A 515 ASP ILE ILE ALA THR ILE ASN LYS GLY SER ILE VAL TRP
SEQRES 29 A 515 GLN GLU VAL PHE ASP ASP LYS ALA LYS LEU ALA PRO GLY
SEQRES 30 A 515 THR ILE VAL GLU VAL TRP LYS ASP SER ALA TYR PRO GLU
SEQRES 31 A 515 GLU LEU SER ARG VAL THR ALA SER GLY PHE PRO VAL ILE
SEQRES 32 A 515 LEU SER ALA PRO TRP TYR LEU ASP LEU ILE SER TYR GLY
SEQRES 33 A 515 GLN ASP TRP ARG LYS TYR TYR LYS VAL GLU PRO LEU ASP
SEQRES 34 A 515 PHE GLY GLY THR GLN LYS GLN LYS GLN LEU PHE ILE GLY
SEQRES 35 A 515 GLY GLU ALA CYS LEU TRP GLY GLU TYR VAL ASP ALA THR
SEQRES 36 A 515 ASN LEU THR PRO ARG LEU TRP PRO ARG ALA SER ALA VAL
SEQRES 37 A 515 GLY GLU ARG LEU TRP SER SER LYS ASP VAL ARG ASP MET
SEQRES 38 A 515 ASP ASP ALA TYR ASP ARG LEU THR ARG HIS ARG CYS ARG
SEQRES 39 A 515 MET VAL GLU ARG GLY ILE ALA ALA GLN PRO LEU TYR ALA
SEQRES 40 A 515 GLY TYR CYS ASN HIS GLU ASN MET
SEQRES 1 B 515 ALA ALA ARG ALA PRO SER VAL SER ALA LYS PRO GLY PRO
SEQRES 2 B 515 ALA LEU TRP PRO LEU PRO LEU SER VAL LYS MET THR PRO
SEQRES 3 B 515 ASN LEU LEU HIS LEU ALA PRO GLU ASN PHE TYR ILE SER
SEQRES 4 B 515 HIS SER PRO ASN SER THR ALA GLY PRO SER CYS THR LEU
SEQRES 5 B 515 LEU GLU GLU ALA PHE ARG ARG TYR HIS GLY TYR ILE PHE
SEQRES 6 B 515 GLY PHE TYR LYS TRP HIS HIS GLU PRO ALA GLU PHE GLN
SEQRES 7 B 515 ALA LYS THR GLN VAL GLN GLN LEU LEU VAL SER ILE THR
SEQRES 8 B 515 LEU GLN SER GLU CYS ASP ALA PHE PRO ASN ILE SER SER
SEQRES 9 B 515 ASP GLU SER TYR THR LEU LEU VAL LYS GLU PRO VAL ALA
SEQRES 10 B 515 VAL LEU LYS ALA ASN ARG VAL TRP GLY ALA LEU ARG GLY
SEQRES 11 B 515 LEU GLU THR PHE SER GLN LEU VAL TYR GLN ASP SER TYR
SEQRES 12 B 515 GLY THR PHE THR ILE ASN GLU SER THR ILE ILE ASP SER
SEQRES 13 B 515 PRO ARG PHE SER HIS ARG GLY ILE LEU ILE ASP THR SER
SEQRES 14 B 515 ARG HIS TYR LEU PRO VAL LYS ILE ILE LEU LYS THR LEU
SEQRES 15 B 515 ASP ALA MET ALA PHE ASN LYS PHE ASN VAL LEU HIS TRP
SEQRES 16 B 515 HIS ILE VAL ASP ASP GLN SER PHE PRO TYR GLN SER ILE
SEQRES 17 B 515 THR PHE PRO GLU LEU SER ASN LYS GLY SER TYR SER LEU
SEQRES 18 B 515 SER HIS VAL TYR THR PRO ASN ASP VAL ARG MET VAL ILE
SEQRES 19 B 515 GLU TYR ALA ARG LEU ARG GLY ILE ARG VAL LEU PRO GLU
SEQRES 20 B 515 PHE ASP THR PRO GLY HIS THR LEU SER TRP GLY LYS GLY
SEQRES 21 B 515 GLN LYS ASP LEU LEU THR PRO CYS TYR SER ARG GLN ASN
SEQRES 22 B 515 LYS LEU ASP SER PHE GLY PRO ILE ASN PRO THR LEU ASN
SEQRES 23 B 515 THR THR TYR SER PHE LEU THR THR PHE PHE LYS GLU ILE
SEQRES 24 B 515 SER GLU VAL PHE PRO ASP GLN PHE ILE HIS LEU GLY GLY
SEQRES 25 B 515 ASP GLU VAL GLU PHE LYS CYS TRP GLU SER ASN PRO LYS
SEQRES 26 B 515 ILE GLN ASP PHE MET ARG GLN LYS GLY PHE GLY THR ASP
SEQRES 27 B 515 PHE LYS LYS LEU GLU SER PHE TYR ILE GLN LYS VAL LEU
SEQRES 28 B 515 ASP ILE ILE ALA THR ILE ASN LYS GLY SER ILE VAL TRP
SEQRES 29 B 515 GLN GLU VAL PHE ASP ASP LYS ALA LYS LEU ALA PRO GLY
SEQRES 30 B 515 THR ILE VAL GLU VAL TRP LYS ASP SER ALA TYR PRO GLU
SEQRES 31 B 515 GLU LEU SER ARG VAL THR ALA SER GLY PHE PRO VAL ILE
SEQRES 32 B 515 LEU SER ALA PRO TRP TYR LEU ASP LEU ILE SER TYR GLY
SEQRES 33 B 515 GLN ASP TRP ARG LYS TYR TYR LYS VAL GLU PRO LEU ASP
SEQRES 34 B 515 PHE GLY GLY THR GLN LYS GLN LYS GLN LEU PHE ILE GLY
SEQRES 35 B 515 GLY GLU ALA CYS LEU TRP GLY GLU TYR VAL ASP ALA THR
SEQRES 36 B 515 ASN LEU THR PRO ARG LEU TRP PRO ARG ALA SER ALA VAL
SEQRES 37 B 515 GLY GLU ARG LEU TRP SER SER LYS ASP VAL ARG ASP MET
SEQRES 38 B 515 ASP ASP ALA TYR ASP ARG LEU THR ARG HIS ARG CYS ARG
SEQRES 39 B 515 MET VAL GLU ARG GLY ILE ALA ALA GLN PRO LEU TYR ALA
SEQRES 40 B 515 GLY TYR CYS ASN HIS GLU ASN MET
SEQRES 1 C 515 ALA ALA ARG ALA PRO SER VAL SER ALA LYS PRO GLY PRO
SEQRES 2 C 515 ALA LEU TRP PRO LEU PRO LEU SER VAL LYS MET THR PRO
SEQRES 3 C 515 ASN LEU LEU HIS LEU ALA PRO GLU ASN PHE TYR ILE SER
SEQRES 4 C 515 HIS SER PRO ASN SER THR ALA GLY PRO SER CYS THR LEU
SEQRES 5 C 515 LEU GLU GLU ALA PHE ARG ARG TYR HIS GLY TYR ILE PHE
SEQRES 6 C 515 GLY PHE TYR LYS TRP HIS HIS GLU PRO ALA GLU PHE GLN
SEQRES 7 C 515 ALA LYS THR GLN VAL GLN GLN LEU LEU VAL SER ILE THR
SEQRES 8 C 515 LEU GLN SER GLU CYS ASP ALA PHE PRO ASN ILE SER SER
SEQRES 9 C 515 ASP GLU SER TYR THR LEU LEU VAL LYS GLU PRO VAL ALA
SEQRES 10 C 515 VAL LEU LYS ALA ASN ARG VAL TRP GLY ALA LEU ARG GLY
SEQRES 11 C 515 LEU GLU THR PHE SER GLN LEU VAL TYR GLN ASP SER TYR
SEQRES 12 C 515 GLY THR PHE THR ILE ASN GLU SER THR ILE ILE ASP SER
SEQRES 13 C 515 PRO ARG PHE SER HIS ARG GLY ILE LEU ILE ASP THR SER
SEQRES 14 C 515 ARG HIS TYR LEU PRO VAL LYS ILE ILE LEU LYS THR LEU
SEQRES 15 C 515 ASP ALA MET ALA PHE ASN LYS PHE ASN VAL LEU HIS TRP
SEQRES 16 C 515 HIS ILE VAL ASP ASP GLN SER PHE PRO TYR GLN SER ILE
SEQRES 17 C 515 THR PHE PRO GLU LEU SER ASN LYS GLY SER TYR SER LEU
SEQRES 18 C 515 SER HIS VAL TYR THR PRO ASN ASP VAL ARG MET VAL ILE
SEQRES 19 C 515 GLU TYR ALA ARG LEU ARG GLY ILE ARG VAL LEU PRO GLU
SEQRES 20 C 515 PHE ASP THR PRO GLY HIS THR LEU SER TRP GLY LYS GLY
SEQRES 21 C 515 GLN LYS ASP LEU LEU THR PRO CYS TYR SER ARG GLN ASN
SEQRES 22 C 515 LYS LEU ASP SER PHE GLY PRO ILE ASN PRO THR LEU ASN
SEQRES 23 C 515 THR THR TYR SER PHE LEU THR THR PHE PHE LYS GLU ILE
SEQRES 24 C 515 SER GLU VAL PHE PRO ASP GLN PHE ILE HIS LEU GLY GLY
SEQRES 25 C 515 ASP GLU VAL GLU PHE LYS CYS TRP GLU SER ASN PRO LYS
SEQRES 26 C 515 ILE GLN ASP PHE MET ARG GLN LYS GLY PHE GLY THR ASP
SEQRES 27 C 515 PHE LYS LYS LEU GLU SER PHE TYR ILE GLN LYS VAL LEU
SEQRES 28 C 515 ASP ILE ILE ALA THR ILE ASN LYS GLY SER ILE VAL TRP
SEQRES 29 C 515 GLN GLU VAL PHE ASP ASP LYS ALA LYS LEU ALA PRO GLY
SEQRES 30 C 515 THR ILE VAL GLU VAL TRP LYS ASP SER ALA TYR PRO GLU
SEQRES 31 C 515 GLU LEU SER ARG VAL THR ALA SER GLY PHE PRO VAL ILE
SEQRES 32 C 515 LEU SER ALA PRO TRP TYR LEU ASP LEU ILE SER TYR GLY
SEQRES 33 C 515 GLN ASP TRP ARG LYS TYR TYR LYS VAL GLU PRO LEU ASP
SEQRES 34 C 515 PHE GLY GLY THR GLN LYS GLN LYS GLN LEU PHE ILE GLY
SEQRES 35 C 515 GLY GLU ALA CYS LEU TRP GLY GLU TYR VAL ASP ALA THR
SEQRES 36 C 515 ASN LEU THR PRO ARG LEU TRP PRO ARG ALA SER ALA VAL
SEQRES 37 C 515 GLY GLU ARG LEU TRP SER SER LYS ASP VAL ARG ASP MET
SEQRES 38 C 515 ASP ASP ALA TYR ASP ARG LEU THR ARG HIS ARG CYS ARG
SEQRES 39 C 515 MET VAL GLU ARG GLY ILE ALA ALA GLN PRO LEU TYR ALA
SEQRES 40 C 515 GLY TYR CYS ASN HIS GLU ASN MET
SEQRES 1 D 515 ALA ALA ARG ALA PRO SER VAL SER ALA LYS PRO GLY PRO
SEQRES 2 D 515 ALA LEU TRP PRO LEU PRO LEU SER VAL LYS MET THR PRO
SEQRES 3 D 515 ASN LEU LEU HIS LEU ALA PRO GLU ASN PHE TYR ILE SER
SEQRES 4 D 515 HIS SER PRO ASN SER THR ALA GLY PRO SER CYS THR LEU
SEQRES 5 D 515 LEU GLU GLU ALA PHE ARG ARG TYR HIS GLY TYR ILE PHE
SEQRES 6 D 515 GLY PHE TYR LYS TRP HIS HIS GLU PRO ALA GLU PHE GLN
SEQRES 7 D 515 ALA LYS THR GLN VAL GLN GLN LEU LEU VAL SER ILE THR
SEQRES 8 D 515 LEU GLN SER GLU CYS ASP ALA PHE PRO ASN ILE SER SER
SEQRES 9 D 515 ASP GLU SER TYR THR LEU LEU VAL LYS GLU PRO VAL ALA
SEQRES 10 D 515 VAL LEU LYS ALA ASN ARG VAL TRP GLY ALA LEU ARG GLY
SEQRES 11 D 515 LEU GLU THR PHE SER GLN LEU VAL TYR GLN ASP SER TYR
SEQRES 12 D 515 GLY THR PHE THR ILE ASN GLU SER THR ILE ILE ASP SER
SEQRES 13 D 515 PRO ARG PHE SER HIS ARG GLY ILE LEU ILE ASP THR SER
SEQRES 14 D 515 ARG HIS TYR LEU PRO VAL LYS ILE ILE LEU LYS THR LEU
SEQRES 15 D 515 ASP ALA MET ALA PHE ASN LYS PHE ASN VAL LEU HIS TRP
SEQRES 16 D 515 HIS ILE VAL ASP ASP GLN SER PHE PRO TYR GLN SER ILE
SEQRES 17 D 515 THR PHE PRO GLU LEU SER ASN LYS GLY SER TYR SER LEU
SEQRES 18 D 515 SER HIS VAL TYR THR PRO ASN ASP VAL ARG MET VAL ILE
SEQRES 19 D 515 GLU TYR ALA ARG LEU ARG GLY ILE ARG VAL LEU PRO GLU
SEQRES 20 D 515 PHE ASP THR PRO GLY HIS THR LEU SER TRP GLY LYS GLY
SEQRES 21 D 515 GLN LYS ASP LEU LEU THR PRO CYS TYR SER ARG GLN ASN
SEQRES 22 D 515 LYS LEU ASP SER PHE GLY PRO ILE ASN PRO THR LEU ASN
SEQRES 23 D 515 THR THR TYR SER PHE LEU THR THR PHE PHE LYS GLU ILE
SEQRES 24 D 515 SER GLU VAL PHE PRO ASP GLN PHE ILE HIS LEU GLY GLY
SEQRES 25 D 515 ASP GLU VAL GLU PHE LYS CYS TRP GLU SER ASN PRO LYS
SEQRES 26 D 515 ILE GLN ASP PHE MET ARG GLN LYS GLY PHE GLY THR ASP
SEQRES 27 D 515 PHE LYS LYS LEU GLU SER PHE TYR ILE GLN LYS VAL LEU
SEQRES 28 D 515 ASP ILE ILE ALA THR ILE ASN LYS GLY SER ILE VAL TRP
SEQRES 29 D 515 GLN GLU VAL PHE ASP ASP LYS ALA LYS LEU ALA PRO GLY
SEQRES 30 D 515 THR ILE VAL GLU VAL TRP LYS ASP SER ALA TYR PRO GLU
SEQRES 31 D 515 GLU LEU SER ARG VAL THR ALA SER GLY PHE PRO VAL ILE
SEQRES 32 D 515 LEU SER ALA PRO TRP TYR LEU ASP LEU ILE SER TYR GLY
SEQRES 33 D 515 GLN ASP TRP ARG LYS TYR TYR LYS VAL GLU PRO LEU ASP
SEQRES 34 D 515 PHE GLY GLY THR GLN LYS GLN LYS GLN LEU PHE ILE GLY
SEQRES 35 D 515 GLY GLU ALA CYS LEU TRP GLY GLU TYR VAL ASP ALA THR
SEQRES 36 D 515 ASN LEU THR PRO ARG LEU TRP PRO ARG ALA SER ALA VAL
SEQRES 37 D 515 GLY GLU ARG LEU TRP SER SER LYS ASP VAL ARG ASP MET
SEQRES 38 D 515 ASP ASP ALA TYR ASP ARG LEU THR ARG HIS ARG CYS ARG
SEQRES 39 D 515 MET VAL GLU ARG GLY ILE ALA ALA GLN PRO LEU TYR ALA
SEQRES 40 D 515 GLY TYR CYS ASN HIS GLU ASN MET
SEQRES 1 E 515 ALA ALA ARG ALA PRO SER VAL SER ALA LYS PRO GLY PRO
SEQRES 2 E 515 ALA LEU TRP PRO LEU PRO LEU SER VAL LYS MET THR PRO
SEQRES 3 E 515 ASN LEU LEU HIS LEU ALA PRO GLU ASN PHE TYR ILE SER
SEQRES 4 E 515 HIS SER PRO ASN SER THR ALA GLY PRO SER CYS THR LEU
SEQRES 5 E 515 LEU GLU GLU ALA PHE ARG ARG TYR HIS GLY TYR ILE PHE
SEQRES 6 E 515 GLY PHE TYR LYS TRP HIS HIS GLU PRO ALA GLU PHE GLN
SEQRES 7 E 515 ALA LYS THR GLN VAL GLN GLN LEU LEU VAL SER ILE THR
SEQRES 8 E 515 LEU GLN SER GLU CYS ASP ALA PHE PRO ASN ILE SER SER
SEQRES 9 E 515 ASP GLU SER TYR THR LEU LEU VAL LYS GLU PRO VAL ALA
SEQRES 10 E 515 VAL LEU LYS ALA ASN ARG VAL TRP GLY ALA LEU ARG GLY
SEQRES 11 E 515 LEU GLU THR PHE SER GLN LEU VAL TYR GLN ASP SER TYR
SEQRES 12 E 515 GLY THR PHE THR ILE ASN GLU SER THR ILE ILE ASP SER
SEQRES 13 E 515 PRO ARG PHE SER HIS ARG GLY ILE LEU ILE ASP THR SER
SEQRES 14 E 515 ARG HIS TYR LEU PRO VAL LYS ILE ILE LEU LYS THR LEU
SEQRES 15 E 515 ASP ALA MET ALA PHE ASN LYS PHE ASN VAL LEU HIS TRP
SEQRES 16 E 515 HIS ILE VAL ASP ASP GLN SER PHE PRO TYR GLN SER ILE
SEQRES 17 E 515 THR PHE PRO GLU LEU SER ASN LYS GLY SER TYR SER LEU
SEQRES 18 E 515 SER HIS VAL TYR THR PRO ASN ASP VAL ARG MET VAL ILE
SEQRES 19 E 515 GLU TYR ALA ARG LEU ARG GLY ILE ARG VAL LEU PRO GLU
SEQRES 20 E 515 PHE ASP THR PRO GLY HIS THR LEU SER TRP GLY LYS GLY
SEQRES 21 E 515 GLN LYS ASP LEU LEU THR PRO CYS TYR SER ARG GLN ASN
SEQRES 22 E 515 LYS LEU ASP SER PHE GLY PRO ILE ASN PRO THR LEU ASN
SEQRES 23 E 515 THR THR TYR SER PHE LEU THR THR PHE PHE LYS GLU ILE
SEQRES 24 E 515 SER GLU VAL PHE PRO ASP GLN PHE ILE HIS LEU GLY GLY
SEQRES 25 E 515 ASP GLU VAL GLU PHE LYS CYS TRP GLU SER ASN PRO LYS
SEQRES 26 E 515 ILE GLN ASP PHE MET ARG GLN LYS GLY PHE GLY THR ASP
SEQRES 27 E 515 PHE LYS LYS LEU GLU SER PHE TYR ILE GLN LYS VAL LEU
SEQRES 28 E 515 ASP ILE ILE ALA THR ILE ASN LYS GLY SER ILE VAL TRP
SEQRES 29 E 515 GLN GLU VAL PHE ASP ASP LYS ALA LYS LEU ALA PRO GLY
SEQRES 30 E 515 THR ILE VAL GLU VAL TRP LYS ASP SER ALA TYR PRO GLU
SEQRES 31 E 515 GLU LEU SER ARG VAL THR ALA SER GLY PHE PRO VAL ILE
SEQRES 32 E 515 LEU SER ALA PRO TRP TYR LEU ASP LEU ILE SER TYR GLY
SEQRES 33 E 515 GLN ASP TRP ARG LYS TYR TYR LYS VAL GLU PRO LEU ASP
SEQRES 34 E 515 PHE GLY GLY THR GLN LYS GLN LYS GLN LEU PHE ILE GLY
SEQRES 35 E 515 GLY GLU ALA CYS LEU TRP GLY GLU TYR VAL ASP ALA THR
SEQRES 36 E 515 ASN LEU THR PRO ARG LEU TRP PRO ARG ALA SER ALA VAL
SEQRES 37 E 515 GLY GLU ARG LEU TRP SER SER LYS ASP VAL ARG ASP MET
SEQRES 38 E 515 ASP ASP ALA TYR ASP ARG LEU THR ARG HIS ARG CYS ARG
SEQRES 39 E 515 MET VAL GLU ARG GLY ILE ALA ALA GLN PRO LEU TYR ALA
SEQRES 40 E 515 GLY TYR CYS ASN HIS GLU ASN MET
SEQRES 1 F 515 ALA ALA ARG ALA PRO SER VAL SER ALA LYS PRO GLY PRO
SEQRES 2 F 515 ALA LEU TRP PRO LEU PRO LEU SER VAL LYS MET THR PRO
SEQRES 3 F 515 ASN LEU LEU HIS LEU ALA PRO GLU ASN PHE TYR ILE SER
SEQRES 4 F 515 HIS SER PRO ASN SER THR ALA GLY PRO SER CYS THR LEU
SEQRES 5 F 515 LEU GLU GLU ALA PHE ARG ARG TYR HIS GLY TYR ILE PHE
SEQRES 6 F 515 GLY PHE TYR LYS TRP HIS HIS GLU PRO ALA GLU PHE GLN
SEQRES 7 F 515 ALA LYS THR GLN VAL GLN GLN LEU LEU VAL SER ILE THR
SEQRES 8 F 515 LEU GLN SER GLU CYS ASP ALA PHE PRO ASN ILE SER SER
SEQRES 9 F 515 ASP GLU SER TYR THR LEU LEU VAL LYS GLU PRO VAL ALA
SEQRES 10 F 515 VAL LEU LYS ALA ASN ARG VAL TRP GLY ALA LEU ARG GLY
SEQRES 11 F 515 LEU GLU THR PHE SER GLN LEU VAL TYR GLN ASP SER TYR
SEQRES 12 F 515 GLY THR PHE THR ILE ASN GLU SER THR ILE ILE ASP SER
SEQRES 13 F 515 PRO ARG PHE SER HIS ARG GLY ILE LEU ILE ASP THR SER
SEQRES 14 F 515 ARG HIS TYR LEU PRO VAL LYS ILE ILE LEU LYS THR LEU
SEQRES 15 F 515 ASP ALA MET ALA PHE ASN LYS PHE ASN VAL LEU HIS TRP
SEQRES 16 F 515 HIS ILE VAL ASP ASP GLN SER PHE PRO TYR GLN SER ILE
SEQRES 17 F 515 THR PHE PRO GLU LEU SER ASN LYS GLY SER TYR SER LEU
SEQRES 18 F 515 SER HIS VAL TYR THR PRO ASN ASP VAL ARG MET VAL ILE
SEQRES 19 F 515 GLU TYR ALA ARG LEU ARG GLY ILE ARG VAL LEU PRO GLU
SEQRES 20 F 515 PHE ASP THR PRO GLY HIS THR LEU SER TRP GLY LYS GLY
SEQRES 21 F 515 GLN LYS ASP LEU LEU THR PRO CYS TYR SER ARG GLN ASN
SEQRES 22 F 515 LYS LEU ASP SER PHE GLY PRO ILE ASN PRO THR LEU ASN
SEQRES 23 F 515 THR THR TYR SER PHE LEU THR THR PHE PHE LYS GLU ILE
SEQRES 24 F 515 SER GLU VAL PHE PRO ASP GLN PHE ILE HIS LEU GLY GLY
SEQRES 25 F 515 ASP GLU VAL GLU PHE LYS CYS TRP GLU SER ASN PRO LYS
SEQRES 26 F 515 ILE GLN ASP PHE MET ARG GLN LYS GLY PHE GLY THR ASP
SEQRES 27 F 515 PHE LYS LYS LEU GLU SER PHE TYR ILE GLN LYS VAL LEU
SEQRES 28 F 515 ASP ILE ILE ALA THR ILE ASN LYS GLY SER ILE VAL TRP
SEQRES 29 F 515 GLN GLU VAL PHE ASP ASP LYS ALA LYS LEU ALA PRO GLY
SEQRES 30 F 515 THR ILE VAL GLU VAL TRP LYS ASP SER ALA TYR PRO GLU
SEQRES 31 F 515 GLU LEU SER ARG VAL THR ALA SER GLY PHE PRO VAL ILE
SEQRES 32 F 515 LEU SER ALA PRO TRP TYR LEU ASP LEU ILE SER TYR GLY
SEQRES 33 F 515 GLN ASP TRP ARG LYS TYR TYR LYS VAL GLU PRO LEU ASP
SEQRES 34 F 515 PHE GLY GLY THR GLN LYS GLN LYS GLN LEU PHE ILE GLY
SEQRES 35 F 515 GLY GLU ALA CYS LEU TRP GLY GLU TYR VAL ASP ALA THR
SEQRES 36 F 515 ASN LEU THR PRO ARG LEU TRP PRO ARG ALA SER ALA VAL
SEQRES 37 F 515 GLY GLU ARG LEU TRP SER SER LYS ASP VAL ARG ASP MET
SEQRES 38 F 515 ASP ASP ALA TYR ASP ARG LEU THR ARG HIS ARG CYS ARG
SEQRES 39 F 515 MET VAL GLU ARG GLY ILE ALA ALA GLN PRO LEU TYR ALA
SEQRES 40 F 515 GLY TYR CYS ASN HIS GLU ASN MET
MODRES 1O7A ASN A 84 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN A 190 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN B 84 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN B 190 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN C 190 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN C 327 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN D 190 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN E 84 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN E 190 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN F 84 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN F 190 ASN GLYCOSYLATION SITE
MODRES 1O7A ASN F 327 ASN GLYCOSYLATION SITE
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET GDL A 600 15
HET NAG A 702 14
HET EDO A 800 4
HET EDO A 801 4
HET EDO A 802 4
HET GDL B 600 15
HET NAG B 702 14
HET EDO B 800 4
HET EDO B 801 4
HET EDO B 802 4
HET GDL C 600 15
HET NAG C 703 14
HET EDO C 800 4
HET EDO C 801 4
HET EDO C 802 4
HET GDL D 600 15
HET GDL E 600 15
HET NAG E 702 14
HET EDO E 800 4
HET EDO E 801 4
HET EDO E 802 4
HET GDL F 600 15
HET NAG F 702 14
HET NAG F 703 14
HET EDO F 800 4
HET EDO F 801 4
HET EDO F 802 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GDL 2-(ACETYLAMIDO)-2-DEOXY-D-GLUCONO-1,5-LACTONE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GDL 2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 NAG 18(C8 H15 N O6)
FORMUL 13 GDL 6(C8 H13 N O6)
FORMUL 15 EDO 15(C2 H6 O2)
FORMUL 40 HOH *2326(H2 O)
HELIX 1 1 ALA A 73 PHE A 77 5 5
HELIX 2 2 CYS A 91 GLY A 107 1 17
HELIX 3 3 ARG A 164 VAL A 179 1 16
HELIX 4 4 PRO A 215 ASN A 229 1 15
HELIX 5 5 PRO A 252 SER A 259 1 8
HELIX 6 6 THR A 267 LEU A 280 1 14
HELIX 7 7 THR A 295 LYS A 300 5 6
HELIX 8 8 LEU A 326 PHE A 344 1 19
HELIX 9 9 PHE A 358 ASN A 364 1 7
HELIX 10 10 PRO A 365 LYS A 374 1 10
HELIX 11 11 ASP A 379 THR A 397 1 19
HELIX 12 12 GLN A 406 ASP A 411 1 6
HELIX 13 13 ALA A 428 SER A 439 1 12
HELIX 14 14 ASP A 459 VAL A 466 1 8
HELIX 15 15 THR A 474 GLN A 479 1 6
HELIX 16 16 ASN A 497 TRP A 503 1 7
HELIX 17 17 PRO A 504 SER A 515 1 12
HELIX 18 18 ASP A 521 ARG A 539 1 19
HELIX 19 19 ALA B 73 PHE B 77 5 5
HELIX 20 20 CYS B 91 GLY B 107 1 17
HELIX 21 21 ARG B 164 VAL B 179 1 16
HELIX 22 22 PRO B 215 ASN B 229 1 15
HELIX 23 23 PRO B 252 SER B 259 1 8
HELIX 24 24 THR B 267 LEU B 280 1 14
HELIX 25 25 THR B 295 LYS B 300 5 6
HELIX 26 26 LEU B 326 PHE B 344 1 19
HELIX 27 27 PHE B 358 ASN B 364 1 7
HELIX 28 28 PRO B 365 LYS B 374 1 10
HELIX 29 29 ASP B 379 THR B 397 1 19
HELIX 30 30 GLN B 406 ASP B 411 1 6
HELIX 31 31 ALA B 428 SER B 439 1 12
HELIX 32 32 ASP B 459 VAL B 466 1 8
HELIX 33 33 THR B 474 GLN B 479 1 6
HELIX 34 34 ASN B 497 TRP B 503 1 7
HELIX 35 35 PRO B 504 SER B 515 1 12
HELIX 36 36 ASP B 521 ARG B 539 1 19
HELIX 37 37 ALA C 73 PHE C 77 5 5
HELIX 38 38 CYS C 91 GLY C 107 1 17
HELIX 39 39 ARG C 164 VAL C 179 1 16
HELIX 40 40 PRO C 215 ASN C 229 1 15
HELIX 41 41 PRO C 252 SER C 259 1 8
HELIX 42 42 THR C 267 LEU C 280 1 14
HELIX 43 43 THR C 295 LYS C 300 5 6
HELIX 44 44 LEU C 326 PHE C 344 1 19
HELIX 45 45 PHE C 358 SER C 363 1 6
HELIX 46 46 PRO C 365 LYS C 374 1 10
HELIX 47 47 ASP C 379 THR C 397 1 19
HELIX 48 48 GLN C 406 ASP C 411 1 6
HELIX 49 49 ALA C 428 SER C 439 1 12
HELIX 50 50 ASP C 459 VAL C 466 1 8
HELIX 51 51 THR C 474 GLN C 479 1 6
HELIX 52 52 ASN C 497 TRP C 503 1 7
HELIX 53 53 PRO C 504 SER C 515 1 12
HELIX 54 54 ASP C 521 ARG C 539 1 19
HELIX 55 55 ALA D 73 PHE D 77 5 5
HELIX 56 56 CYS D 91 GLY D 107 1 17
HELIX 57 57 ARG D 164 VAL D 179 1 16
HELIX 58 58 PRO D 215 ASN D 229 1 15
HELIX 59 59 PRO D 252 SER D 259 1 8
HELIX 60 60 THR D 267 LEU D 280 1 14
HELIX 61 61 THR D 295 LYS D 300 5 6
HELIX 62 62 LEU D 326 PHE D 344 1 19
HELIX 63 63 PHE D 358 SER D 363 1 6
HELIX 64 64 PRO D 365 LYS D 374 1 10
HELIX 65 65 ASP D 379 THR D 397 1 19
HELIX 66 66 GLN D 406 ASP D 411 1 6
HELIX 67 67 ALA D 428 SER D 439 1 12
HELIX 68 68 ASP D 459 VAL D 466 1 8
HELIX 69 69 THR D 474 GLN D 479 1 6
HELIX 70 70 ASN D 497 TRP D 503 1 7
HELIX 71 71 PRO D 504 SER D 515 1 12
HELIX 72 72 ASP D 521 ARG D 539 1 19
HELIX 73 73 ALA E 73 PHE E 77 5 5
HELIX 74 74 CYS E 91 GLY E 107 1 17
HELIX 75 75 ARG E 164 VAL E 179 1 16
HELIX 76 76 PRO E 215 ASN E 229 1 15
HELIX 77 77 PRO E 252 SER E 259 1 8
HELIX 78 78 THR E 267 LEU E 280 1 14
HELIX 79 79 THR E 295 LYS E 300 1 6
HELIX 80 80 LEU E 326 PHE E 344 1 19
HELIX 81 81 PHE E 358 SER E 363 1 6
HELIX 82 82 PRO E 365 LYS E 374 1 10
HELIX 83 83 ASP E 379 THR E 397 1 19
HELIX 84 84 GLN E 406 ASP E 411 1 6
HELIX 85 85 ALA E 428 SER E 439 1 12
HELIX 86 86 ASP E 459 VAL E 466 1 8
HELIX 87 87 THR E 474 GLN E 479 1 6
HELIX 88 88 ASN E 497 TRP E 503 1 7
HELIX 89 89 PRO E 504 SER E 515 1 12
HELIX 90 90 ASP E 521 ARG E 539 1 19
HELIX 91 91 ALA F 73 PHE F 77 5 5
HELIX 92 92 CYS F 91 GLY F 107 1 17
HELIX 93 93 ARG F 164 VAL F 179 1 16
HELIX 94 94 PRO F 215 ASN F 229 1 15
HELIX 95 95 PRO F 252 SER F 259 1 8
HELIX 96 96 THR F 267 LEU F 280 1 14
HELIX 97 97 THR F 295 LYS F 300 5 6
HELIX 98 98 LEU F 326 PHE F 344 1 19
HELIX 99 99 PHE F 358 SER F 363 1 6
HELIX 100 100 PRO F 365 LYS F 374 1 10
HELIX 101 101 ASP F 379 THR F 397 1 19
HELIX 102 102 GLN F 406 ASP F 411 1 6
HELIX 103 103 ALA F 428 SER F 439 1 12
HELIX 104 104 ASP F 459 VAL F 466 1 8
HELIX 105 105 THR F 474 GLN F 479 1 6
HELIX 106 106 ASN F 497 TRP F 503 1 7
HELIX 107 107 PRO F 504 SER F 515 1 12
HELIX 108 108 ASP F 521 ARG F 539 1 19
SHEET 1 AA 6 SER A 62 MET A 65 0
SHEET 2 AA 6 SER A 192 ASP A 196 -1 O THR A 193 N LYS A 64
SHEET 3 AA 6 TYR A 149 VAL A 153 -1 O TYR A 149 N ASP A 196
SHEET 4 AA 6 PRO A 156 ALA A 162 -1 O VAL A 159 N LEU A 152
SHEET 5 AA 6 GLN A 125 THR A 132 1 O GLN A 125 N PRO A 156
SHEET 6 AA 6 TYR A 78 SER A 82 1 O TYR A 78 N GLN A 125
SHEET 1 AB 2 LEU A 69 HIS A 71 0
SHEET 2 AB 2 PHE A 187 ASN A 190 -1 O PHE A 187 N LEU A 72
SHEET 1 AC 9 HIS A 202 THR A 209 0
SHEET 2 AC 9 LEU A 480 LEU A 488 1 O ILE A 482 N HIS A 202
SHEET 3 AC 9 PRO A 442 SER A 446 1 O VAL A 443 N LEU A 480
SHEET 4 AC 9 ILE A 420 VAL A 423 1 O VAL A 421 N PRO A 442
SHEET 5 AC 9 GLY A 401 TRP A 405 1 O SER A 402 N ILE A 420
SHEET 6 AC 9 GLN A 347 GLY A 352 1 O GLN A 347 N GLY A 401
SHEET 7 AC 9 ARG A 284 GLU A 288 1 O PRO A 287 N HIS A 350
SHEET 8 AC 9 ASN A 232 ILE A 238 1 O ASN A 232 N ARG A 284
SHEET 9 AC 9 HIS A 202 THR A 209 1 O ARG A 203 N ASN A 232
SHEET 1 AD 2 LEU A 305 CYS A 309 0
SHEET 2 AD 2 SER A 318 ASN A 323 -1 N SER A 318 O CYS A 309
SHEET 1 BA 6 SER B 62 MET B 65 0
SHEET 2 BA 6 SER B 192 ASP B 196 -1 O THR B 193 N LYS B 64
SHEET 3 BA 6 TYR B 149 VAL B 153 -1 O TYR B 149 N ASP B 196
SHEET 4 BA 6 PRO B 156 ALA B 162 -1 O VAL B 159 N LEU B 152
SHEET 5 BA 6 GLN B 125 THR B 132 1 O GLN B 125 N PRO B 156
SHEET 6 BA 6 TYR B 78 SER B 82 1 O TYR B 78 N GLN B 125
SHEET 1 BB 2 LEU B 69 HIS B 71 0
SHEET 2 BB 2 PHE B 187 ASN B 190 -1 O PHE B 187 N LEU B 72
SHEET 1 BC 9 HIS B 202 THR B 209 0
SHEET 2 BC 9 LEU B 480 LEU B 488 1 O ILE B 482 N HIS B 202
SHEET 3 BC 9 PRO B 442 SER B 446 1 O VAL B 443 N LEU B 480
SHEET 4 BC 9 ILE B 420 VAL B 423 1 O VAL B 421 N PRO B 442
SHEET 5 BC 9 GLY B 401 TRP B 405 1 O SER B 402 N ILE B 420
SHEET 6 BC 9 GLN B 347 GLY B 352 1 O GLN B 347 N GLY B 401
SHEET 7 BC 9 ARG B 284 GLU B 288 1 O PRO B 287 N HIS B 350
SHEET 8 BC 9 ASN B 232 ILE B 238 1 O ASN B 232 N ARG B 284
SHEET 9 BC 9 HIS B 202 THR B 209 1 O ARG B 203 N ASN B 232
SHEET 1 BD 2 LEU B 305 CYS B 309 0
SHEET 2 BD 2 SER B 318 ASN B 323 -1 N SER B 318 O CYS B 309
SHEET 1 CA 6 SER C 62 MET C 65 0
SHEET 2 CA 6 SER C 192 ASP C 196 -1 O THR C 193 N LYS C 64
SHEET 3 CA 6 TYR C 149 VAL C 153 -1 O TYR C 149 N ASP C 196
SHEET 4 CA 6 PRO C 156 ALA C 162 -1 O VAL C 159 N LEU C 152
SHEET 5 CA 6 GLN C 125 THR C 132 1 O GLN C 125 N PRO C 156
SHEET 6 CA 6 TYR C 78 SER C 82 1 O TYR C 78 N GLN C 125
SHEET 1 CB 2 LEU C 69 HIS C 71 0
SHEET 2 CB 2 PHE C 187 ASN C 190 -1 O PHE C 187 N LEU C 72
SHEET 1 CC 9 HIS C 202 THR C 209 0
SHEET 2 CC 9 LEU C 480 LEU C 488 1 O ILE C 482 N HIS C 202
SHEET 3 CC 9 PRO C 442 SER C 446 1 O VAL C 443 N LEU C 480
SHEET 4 CC 9 ILE C 420 VAL C 423 1 O VAL C 421 N PRO C 442
SHEET 5 CC 9 GLY C 401 TRP C 405 1 O SER C 402 N ILE C 420
SHEET 6 CC 9 GLN C 347 GLY C 352 1 O GLN C 347 N GLY C 401
SHEET 7 CC 9 ARG C 284 GLU C 288 1 O PRO C 287 N HIS C 350
SHEET 8 CC 9 ASN C 232 ILE C 238 1 O ASN C 232 N ARG C 284
SHEET 9 CC 9 HIS C 202 THR C 209 1 O ARG C 203 N ASN C 232
SHEET 1 CD 2 LEU C 305 CYS C 309 0
SHEET 2 CD 2 SER C 318 ASN C 323 -1 N SER C 318 O CYS C 309
SHEET 1 DA 6 SER D 62 MET D 65 0
SHEET 2 DA 6 SER D 192 ASP D 196 -1 O THR D 193 N LYS D 64
SHEET 3 DA 6 TYR D 149 VAL D 153 -1 O TYR D 149 N ASP D 196
SHEET 4 DA 6 PRO D 156 ALA D 162 -1 O VAL D 159 N LEU D 152
SHEET 5 DA 6 GLN D 125 THR D 132 1 O GLN D 125 N PRO D 156
SHEET 6 DA 6 TYR D 78 SER D 82 1 O TYR D 78 N GLN D 125
SHEET 1 DB 2 LEU D 69 HIS D 71 0
SHEET 2 DB 2 PHE D 187 ASN D 190 -1 O PHE D 187 N LEU D 72
SHEET 1 DC 9 HIS D 202 THR D 209 0
SHEET 2 DC 9 LEU D 480 LEU D 488 1 O ILE D 482 N HIS D 202
SHEET 3 DC 9 PRO D 442 SER D 446 1 O VAL D 443 N LEU D 480
SHEET 4 DC 9 ILE D 420 VAL D 423 1 O VAL D 421 N PRO D 442
SHEET 5 DC 9 GLY D 401 TRP D 405 1 O SER D 402 N ILE D 420
SHEET 6 DC 9 GLN D 347 GLY D 352 1 O GLN D 347 N GLY D 401
SHEET 7 DC 9 ARG D 284 GLU D 288 1 O PRO D 287 N HIS D 350
SHEET 8 DC 9 ASN D 232 ILE D 238 1 O ASN D 232 N ARG D 284
SHEET 9 DC 9 HIS D 202 THR D 209 1 O ARG D 203 N ASN D 232
SHEET 1 DD 2 LEU D 305 CYS D 309 0
SHEET 2 DD 2 SER D 318 ASN D 323 -1 N SER D 318 O CYS D 309
SHEET 1 EA 6 SER E 62 MET E 65 0
SHEET 2 EA 6 SER E 192 ASP E 196 -1 O THR E 193 N LYS E 64
SHEET 3 EA 6 TYR E 149 VAL E 153 -1 O TYR E 149 N ASP E 196
SHEET 4 EA 6 PRO E 156 ALA E 162 -1 O VAL E 159 N LEU E 152
SHEET 5 EA 6 GLN E 125 THR E 132 1 O GLN E 125 N PRO E 156
SHEET 6 EA 6 TYR E 78 SER E 82 1 O TYR E 78 N GLN E 125
SHEET 1 EB 2 LEU E 69 HIS E 71 0
SHEET 2 EB 2 PHE E 187 ASN E 190 -1 O PHE E 187 N LEU E 72
SHEET 1 EC 9 HIS E 202 THR E 209 0
SHEET 2 EC 9 LEU E 480 LEU E 488 1 O ILE E 482 N HIS E 202
SHEET 3 EC 9 PRO E 442 SER E 446 1 O VAL E 443 N LEU E 480
SHEET 4 EC 9 ILE E 420 VAL E 423 1 O VAL E 421 N PRO E 442
SHEET 5 EC 9 GLY E 401 TRP E 405 1 O SER E 402 N ILE E 420
SHEET 6 EC 9 GLN E 347 GLY E 352 1 O GLN E 347 N GLY E 401
SHEET 7 EC 9 ARG E 284 GLU E 288 1 O PRO E 287 N HIS E 350
SHEET 8 EC 9 ASN E 232 ILE E 238 1 O ASN E 232 N ARG E 284
SHEET 9 EC 9 HIS E 202 THR E 209 1 O ARG E 203 N ASN E 232
SHEET 1 ED 2 LEU E 305 CYS E 309 0
SHEET 2 ED 2 SER E 318 ASN E 323 -1 N SER E 318 O CYS E 309
SHEET 1 FA 6 SER F 62 MET F 65 0
SHEET 2 FA 6 SER F 192 ASP F 196 -1 O THR F 193 N LYS F 64
SHEET 3 FA 6 TYR F 149 VAL F 153 -1 O TYR F 149 N ASP F 196
SHEET 4 FA 6 PRO F 156 ALA F 162 -1 O VAL F 159 N LEU F 152
SHEET 5 FA 6 GLN F 125 THR F 132 1 O GLN F 125 N PRO F 156
SHEET 6 FA 6 TYR F 78 SER F 82 1 O TYR F 78 N GLN F 125
SHEET 1 FB 2 LEU F 69 HIS F 71 0
SHEET 2 FB 2 PHE F 187 ASN F 190 -1 O PHE F 187 N LEU F 72
SHEET 1 FC 9 HIS F 202 THR F 209 0
SHEET 2 FC 9 LEU F 480 LEU F 488 1 O ILE F 482 N HIS F 202
SHEET 3 FC 9 PRO F 442 SER F 446 1 O VAL F 443 N LEU F 480
SHEET 4 FC 9 ILE F 420 VAL F 423 1 O VAL F 421 N PRO F 442
SHEET 5 FC 9 GLY F 401 TRP F 405 1 O SER F 402 N ILE F 420
SHEET 6 FC 9 GLN F 347 GLY F 352 1 O GLN F 347 N GLY F 401
SHEET 7 FC 9 ARG F 284 GLU F 288 1 O PRO F 287 N HIS F 350
SHEET 8 FC 9 ASN F 232 ILE F 238 1 O ASN F 232 N ARG F 284
SHEET 9 FC 9 HIS F 202 THR F 209 1 O ARG F 203 N ASN F 232
SHEET 1 FD 2 LEU F 305 CYS F 309 0
SHEET 2 FD 2 SER F 318 ASN F 323 -1 N SER F 318 O CYS F 309
SSBOND 1 CYS A 91 CYS A 137 1555 1555 2.04
SSBOND 2 CYS A 309 CYS A 360 1555 1555 2.03
SSBOND 3 CYS A 534 CYS A 551 1555 1555 2.06
SSBOND 4 CYS B 91 CYS B 137 1555 1555 2.04
SSBOND 5 CYS B 309 CYS B 360 1555 1555 2.05
SSBOND 6 CYS B 534 CYS B 551 1555 1555 2.05
SSBOND 7 CYS C 91 CYS C 137 1555 1555 2.04
SSBOND 8 CYS C 309 CYS C 360 1555 1555 2.04
SSBOND 9 CYS C 534 CYS C 551 1555 1555 2.06
SSBOND 10 CYS D 91 CYS D 137 1555 1555 2.03
SSBOND 11 CYS D 309 CYS D 360 1555 1555 2.03
SSBOND 12 CYS D 534 CYS D 551 1555 1555 2.05
SSBOND 13 CYS E 91 CYS E 137 1555 1555 2.04
SSBOND 14 CYS E 309 CYS E 360 1555 1555 2.03
SSBOND 15 CYS E 534 CYS E 551 1555 1555 2.05
SSBOND 16 CYS F 91 CYS F 137 1555 1555 2.03
SSBOND 17 CYS F 309 CYS F 360 1555 1555 2.03
SSBOND 18 CYS F 534 CYS F 551 1555 1555 2.05
LINK ND2 ASN A 84 C1 NAG A 702 1555 1555 1.46
LINK ND2 ASN A 190 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 84 C1 NAG B 702 1555 1555 1.45
LINK ND2 ASN B 190 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN C 190 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN C 327 C1 NAG C 703 1555 1555 1.45
LINK ND2 ASN D 190 C1 NAG J 1 1555 1555 1.46
LINK ND2 ASN E 84 C1 NAG E 702 1555 1555 1.45
LINK ND2 ASN E 190 C1 NAG K 1 1555 1555 1.45
LINK ND2 ASN F 84 C1 NAG F 702 1555 1555 1.46
LINK ND2 ASN F 190 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN F 327 C1 NAG F 703 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.39
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.38
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.38
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.38
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.39
CISPEP 1 TRP A 57 PRO A 58 0 0.31
CISPEP 2 GLU A 155 PRO A 156 0 0.23
CISPEP 3 THR A 291 PRO A 292 0 -0.92
CISPEP 4 TRP A 503 PRO A 504 0 1.19
CISPEP 5 TRP B 57 PRO B 58 0 -0.70
CISPEP 6 GLU B 155 PRO B 156 0 -3.16
CISPEP 7 THR B 291 PRO B 292 0 -0.88
CISPEP 8 TRP B 503 PRO B 504 0 1.84
CISPEP 9 TRP C 57 PRO C 58 0 -1.41
CISPEP 10 GLU C 155 PRO C 156 0 0.42
CISPEP 11 THR C 291 PRO C 292 0 0.10
CISPEP 12 TRP C 503 PRO C 504 0 1.46
CISPEP 13 TRP D 57 PRO D 58 0 -1.78
CISPEP 14 GLU D 155 PRO D 156 0 -0.07
CISPEP 15 THR D 291 PRO D 292 0 -0.10
CISPEP 16 TRP D 503 PRO D 504 0 1.12
CISPEP 17 TRP E 57 PRO E 58 0 -0.82
CISPEP 18 GLU E 155 PRO E 156 0 0.24
CISPEP 19 THR E 291 PRO E 292 0 -0.45
CISPEP 20 TRP E 503 PRO E 504 0 2.15
CISPEP 21 TRP F 57 PRO F 58 0 -1.39
CISPEP 22 GLU F 155 PRO F 156 0 1.49
CISPEP 23 THR F 291 PRO F 292 0 0.28
CISPEP 24 TRP F 503 PRO F 504 0 1.30
CRYST1 163.931 163.931 244.717 90.00 90.00 120.00 P 31 2 1 36
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 0.006100 0.003522 0.000000 0.00000
SCALE2 0.000000 0.007044 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004086 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
