HEADER HYDROLASE 06-NOV-06 2NSX
TITLE STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH PHARMACOLOGICAL CHAPERONE
TITLE 2 PROVIDES INSIGHT INTO GAUCHER DISEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL-
COMPND 5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;
COMPND 6 EC: 3.2.1.45;
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: GBA;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_ORGAN: OVARY
KEYWDS TIM-BARREL GLYCOSIDASE CEREZYME HYDROLYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.L.LIEBERMAN,G.A.PETSKO,D.RINGE
REVDAT 4 13-JUL-11 2NSX 1 VERSN
REVDAT 3 24-FEB-09 2NSX 1 VERSN
REVDAT 2 30-JAN-07 2NSX 1 JRNL
REVDAT 1 26-DEC-06 2NSX 0
JRNL AUTH R.L.LIEBERMAN,B.A.WUSTMAN,P.HUERTAS,A.C.POWE,C.W.PINE,
JRNL AUTH 2 R.KHANNA,M.G.SCHLOSSMACHER,D.RINGE,G.A.PETSKO
JRNL TITL STRUCTURE OF ACID BETA-GLUCOSIDASE WITH PHARMACOLOGICAL
JRNL TITL 2 CHAPERONE PROVIDES INSIGHT INTO GAUCHER DISEASE.
JRNL REF NAT.CHEM.BIOL. V. 3 101 2007
JRNL REFN ISSN 1552-4450
JRNL PMID 17187079
JRNL DOI 10.1038/NCHEMBIO850
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 141806
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7504
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7613
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 422
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15720
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 1006
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.93000
REMARK 3 B22 (A**2) : -3.00000
REMARK 3 B33 (A**2) : -2.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.71000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.201
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.902
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16449 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22485 ; 1.527 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1984 ; 6.878 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 720 ;37.210 ;23.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2516 ;16.335 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;21.739 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2422 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12536 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8228 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11015 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1161 ; 0.170 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 73 ; 0.184 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.110 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 10178 ; 0.887 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.450 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7136 ; 2.089 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6287 ; 3.175 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NSX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 149310
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1OGS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM SULFATE 0.17 M
REMARK 280 GUANIDINIUM HCL 0.02 M KCL 0.1 M ACETATE BUFFER PH 4.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.10800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -250.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 92.21600
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -249.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -127.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 8
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 9
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 92.21600
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 OE1 GLN C 73 O HOH C 655 1.70
REMARK 500 O ASN C 396 O HOH C 588 2.01
REMARK 500 O GLY C 389 O HOH C 588 2.16
REMARK 500 OE2 GLU C 254 O HOH C 756 2.18
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 LEU A 286 CA - CB - CG ANGL. DEV. = -24.3 DEGREES
REMARK 500 GLY B 344 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 LEU C 286 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 LEU D 317 CA - CB - CG ANGL. DEV. = 14.0 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 PHE A 75 -135.06 -116.28
REMARK 500 ALA A 124 -154.23 62.65
REMARK 500 ASP A 141 78.80 -110.96
REMARK 500 LEU A 156 -64.03 -105.03
REMARK 500 ASN A 192 -158.48 -120.58
REMARK 500 LYS A 194 102.38 -51.51
REMARK 500 ASP A 203 -172.05 -69.12
REMARK 500 GLU A 233 142.36 167.98
REMARK 500 GLU A 235 69.83 27.48
REMARK 500 LEU A 281 -85.28 76.07
REMARK 500 PHE A 316 -152.63 -106.92
REMARK 500 LEU A 317 97.59 -167.59
REMARK 500 THR A 323 -71.17 -109.23
REMARK 500 LYS A 346 109.62 -43.79
REMARK 500 TRP A 381 -138.07 -79.36
REMARK 500 ARG A 395 136.30 175.91
REMARK 500 PHE A 397 -4.66 -145.75
REMARK 500 VAL A 477 -45.28 -132.21
REMARK 500 PHE B 75 -140.16 -109.40
REMARK 500 ALA B 124 -158.05 64.43
REMARK 500 PHE B 128 55.55 -92.09
REMARK 500 LEU B 156 -71.99 -111.01
REMARK 500 TRP B 179 -61.18 -95.41
REMARK 500 ASN B 192 -162.19 -114.90
REMARK 500 GLU B 233 130.83 168.30
REMARK 500 GLU B 235 67.09 38.59
REMARK 500 ASP B 263 -68.26 -122.46
REMARK 500 LEU B 281 -76.56 68.54
REMARK 500 PRO B 319 133.40 -39.45
REMARK 500 THR B 323 -74.68 -106.58
REMARK 500 SER B 345 -62.66 58.41
REMARK 500 HIS B 374 -3.77 82.28
REMARK 500 TRP B 381 -133.52 -76.11
REMARK 500 VAL B 477 -34.08 -132.03
REMARK 500 PHE C 75 -134.62 -119.98
REMARK 500 ALA C 124 -148.95 59.91
REMARK 500 ASP C 141 74.87 -106.63
REMARK 500 LEU C 156 -68.59 -101.07
REMARK 500 ASN C 192 -164.97 -122.99
REMARK 500 LYS C 194 108.44 -57.43
REMARK 500 GLU C 233 133.47 160.29
REMARK 500 GLU C 235 66.05 30.33
REMARK 500 ASP C 263 -62.85 -120.35
REMARK 500 LEU C 281 -81.81 73.29
REMARK 500 THR C 323 -69.70 -103.36
REMARK 500 TRP C 381 -138.34 -79.10
REMARK 500 ARG C 395 146.90 177.94
REMARK 500 PHE C 397 -26.12 22.92
REMARK 500 VAL C 477 -50.17 -133.10
REMARK 500 ASN D 19 -159.25 -153.87
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 344 SER B 345 38.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE A 161 19.5 L L OUTSIDE RANGE
REMARK 500 SER B 345 21.5 L L OUTSIDE RANGE
REMARK 500 PHE C 397 19.5 L L OUTSIDE RANGE
REMARK 500 ILE D 93 24.3 L L OUTSIDE RANGE
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 A 707 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH D 649 DISTANCE = 5.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG C 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFM B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFM D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 502
DBREF 2NSX A 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 2NSX B 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 2NSX C 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 2NSX D 1 497 UNP P04062 GLCM_HUMAN 40 536
SEQADV 2NSX HIS A 495 UNP P04062 ARG 534 CONFLICT
SEQADV 2NSX HIS B 495 UNP P04062 ARG 534 CONFLICT
SEQADV 2NSX HIS C 495 UNP P04062 ARG 534 CONFLICT
SEQADV 2NSX HIS D 495 UNP P04062 ARG 534 CONFLICT
SEQRES 1 A 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 A 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 A 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 A 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 A 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 A 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 A 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 A 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 A 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 A 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 A 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 A 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 A 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 A 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 A 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 A 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 A 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 A 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 A 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 A 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 A 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 A 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 A 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 A 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 A 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 A 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 A 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 A 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 A 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 A 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 A 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 A 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 A 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 A 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 A 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 A 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 A 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 A 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 A 497 HIS ARG GLN
SEQRES 1 B 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 B 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 B 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 B 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 B 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 B 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 B 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 B 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 B 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 B 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 B 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 B 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 B 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 B 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 B 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 B 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 B 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 B 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 B 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 B 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 B 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 B 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 B 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 B 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 B 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 B 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 B 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 B 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 B 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 B 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 B 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 B 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 B 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 B 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 B 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 B 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 B 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 B 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 B 497 HIS ARG GLN
SEQRES 1 C 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 C 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 C 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 C 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 C 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 C 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 C 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 C 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 C 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 C 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 C 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 C 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 C 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 C 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 C 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 C 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 C 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 C 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 C 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 C 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 C 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 C 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 C 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 C 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 C 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 C 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 C 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 C 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 C 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 C 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 C 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 C 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 C 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 C 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 C 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 C 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 C 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 C 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 C 497 HIS ARG GLN
SEQRES 1 D 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 D 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 D 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 D 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 D 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 D 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 D 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 D 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 D 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 D 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 D 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 D 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 D 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 D 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 D 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 D 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 D 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 D 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 D 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 D 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 D 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 D 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 D 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 D 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 D 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 D 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 D 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 D 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 D 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 D 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 D 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 D 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 D 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 D 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 D 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 D 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 D 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 D 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 D 497 HIS ARG GLN
MODRES 2NSX ASN A 19 ASN GLYCOSYLATION SITE
MODRES 2NSX ASN B 19 ASN GLYCOSYLATION SITE
MODRES 2NSX ASN C 19 ASN GLYCOSYLATION SITE
MODRES 2NSX ASN D 19 ASN GLYCOSYLATION SITE
MODRES 2NSX ASN B 146 ASN GLYCOSYLATION SITE
HET NAG B 498 14
HET NDG A 498 14
HET NAG B 499 14
HET NDG C 498 14
HET NAG D 498 14
HET SO4 D 499 5
HET SO4 A 499 5
HET SO4 C 499 5
HET SO4 A 500 5
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 B 500 5
HET SO4 B 501 5
HET SO4 B 502 5
HET SO4 B 503 5
HET SO4 B 504 5
HET SO4 B 505 5
HET SO4 C 500 5
HET SO4 C 501 5
HET SO4 D 500 5
HET SO4 D 501 5
HET SO4 D 502 5
HET SO4 A 503 5
HET IFM B 506 10
HET IFM D 503 10
HET GOL A 504 6
HET GOL C 502 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM IFM 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE
HETNAM GOL GLYCEROL
HETSYN IFM (3R,4R,5R)-5-(HYDROXYMETHYL)PIPERIDINE-3,4-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NAG 3(C8 H15 N O6)
FORMUL 6 NDG 2(C8 H15 N O6)
FORMUL 10 SO4 18(O4 S 2-)
FORMUL 28 IFM 2(C6 H13 N O3)
FORMUL 30 GOL 2(C3 H8 O3)
FORMUL 32 HOH *1006(H2 O)
HELIX 1 1 THR A 86 LEU A 94 1 9
HELIX 2 2 SER A 97 SER A 110 1 14
HELIX 3 3 PRO A 150 LEU A 156 1 7
HELIX 4 4 LEU A 156 ALA A 168 1 13
HELIX 5 5 PRO A 182 LYS A 186 5 5
HELIX 6 6 ASP A 203 HIS A 223 1 21
HELIX 7 7 GLU A 235 LEU A 241 5 7
HELIX 8 8 THR A 252 ASP A 263 1 12
HELIX 9 9 ASP A 263 ASN A 270 1 8
HELIX 10 10 LEU A 286 LEU A 288 5 3
HELIX 11 11 PRO A 289 THR A 297 1 9
HELIX 12 12 ASP A 298 LYS A 303 1 6
HELIX 13 13 PRO A 319 PHE A 331 1 13
HELIX 14 14 SER A 356 TYR A 373 1 18
HELIX 15 15 ILE A 406 ASP A 409 5 4
HELIX 16 16 GLN A 414 LYS A 425 1 12
HELIX 17 17 THR B 86 ALA B 95 1 10
HELIX 18 18 SER B 97 SER B 110 1 14
HELIX 19 19 PRO B 150 LYS B 155 1 6
HELIX 20 20 LEU B 156 ALA B 168 1 13
HELIX 21 21 PRO B 182 LYS B 186 5 5
HELIX 22 22 ASP B 203 HIS B 223 1 21
HELIX 23 23 GLU B 235 LEU B 241 5 7
HELIX 24 24 THR B 252 ASP B 263 1 12
HELIX 25 25 ASP B 263 ASN B 270 1 8
HELIX 26 26 LEU B 286 LEU B 288 5 3
HELIX 27 27 PRO B 289 THR B 297 1 9
HELIX 28 28 ASP B 298 LYS B 303 1 6
HELIX 29 29 LEU B 314 ALA B 318 5 5
HELIX 30 30 PRO B 319 PHE B 331 1 13
HELIX 31 31 SER B 356 TYR B 373 1 18
HELIX 32 32 ILE B 406 ASP B 409 5 4
HELIX 33 33 GLN B 414 LYS B 425 1 12
HELIX 34 34 THR C 86 ALA C 95 1 10
HELIX 35 35 SER C 97 SER C 110 1 14
HELIX 36 36 PRO C 150 LYS C 155 1 6
HELIX 37 37 LEU C 156 ALA C 168 1 13
HELIX 38 38 PRO C 182 LYS C 186 5 5
HELIX 39 39 ASP C 203 HIS C 223 1 21
HELIX 40 40 SER C 237 LEU C 241 5 5
HELIX 41 41 THR C 252 ASP C 263 1 12
HELIX 42 42 ASP C 263 ASN C 270 1 8
HELIX 43 43 LEU C 286 LEU C 288 5 3
HELIX 44 44 PRO C 289 THR C 297 1 9
HELIX 45 45 ASP C 298 LYS C 303 1 6
HELIX 46 46 PRO C 319 PHE C 331 1 13
HELIX 47 47 SER C 356 TYR C 373 1 18
HELIX 48 48 ILE C 406 ASP C 409 5 4
HELIX 49 49 GLN C 414 LYS C 425 1 12
HELIX 50 50 THR D 86 ALA D 95 1 10
HELIX 51 51 SER D 97 SER D 110 1 14
HELIX 52 52 PRO D 150 LYS D 155 1 6
HELIX 53 53 LEU D 156 ALA D 168 1 13
HELIX 54 54 PRO D 182 LYS D 186 5 5
HELIX 55 55 ASP D 203 HIS D 223 1 21
HELIX 56 56 GLU D 235 LEU D 241 5 7
HELIX 57 57 THR D 252 ASP D 263 1 12
HELIX 58 58 ASP D 263 ASN D 270 1 8
HELIX 59 59 LEU D 286 LEU D 288 5 3
HELIX 60 60 PRO D 289 THR D 297 1 9
HELIX 61 61 ASP D 298 LYS D 303 1 6
HELIX 62 62 LEU D 314 ALA D 318 5 5
HELIX 63 63 PRO D 319 PHE D 331 1 13
HELIX 64 64 SER D 356 TYR D 373 1 18
HELIX 65 65 ILE D 406 ASP D 409 5 4
HELIX 66 66 GLN D 414 LYS D 425 1 12
SHEET 1 A 4 PRO A 6 LYS A 7 0
SHEET 2 A 4 VAL A 15 CYS A 18 -1 O VAL A 15 N LYS A 7
SHEET 3 A 4 THR A 410 LYS A 413 -1 O LYS A 413 N CYS A 16
SHEET 4 A 4 ILE A 402 ASP A 405 -1 N ILE A 403 O TYR A 412
SHEET 1 B 9 GLU A 50 PRO A 55 0
SHEET 2 B 9 THR A 36 THR A 43 -1 N ARG A 39 O SER A 52
SHEET 3 B 9 SER A 488 TRP A 494 -1 O LEU A 493 N SER A 38
SHEET 4 B 9 ALA A 456 ASN A 462 -1 N VAL A 458 O TYR A 492
SHEET 5 B 9 ASP A 445 MET A 450 -1 N ASP A 445 O LEU A 461
SHEET 6 B 9 GLN A 432 ALA A 438 -1 N GLN A 432 O MET A 450
SHEET 7 B 9 LEU A 65 LYS A 77 -1 N PHE A 75 O ARG A 433
SHEET 8 B 9 VAL A 468 ASP A 474 1 O THR A 471 N LEU A 67
SHEET 9 B 9 GLY A 478 SER A 484 -1 O SER A 484 N VAL A 468
SHEET 1 C 9 GLY A 80 ALA A 84 0
SHEET 2 C 9 ILE A 118 MET A 123 1 O ARG A 120 N GLY A 83
SHEET 3 C 9 SER A 173 PRO A 178 1 O LEU A 175 N VAL A 121
SHEET 4 C 9 ALA A 229 THR A 231 1 O THR A 231 N ALA A 176
SHEET 5 C 9 ARG A 277 GLN A 284 1 O LEU A 279 N VAL A 230
SHEET 6 C 9 GLY A 307 TYR A 313 1 O ALA A 309 N MET A 280
SHEET 7 C 9 MET A 335 CYS A 342 1 O MET A 335 N ILE A 308
SHEET 8 C 9 VAL A 375 ASN A 382 1 O GLY A 377 N ALA A 338
SHEET 9 C 9 GLY A 80 ALA A 84 1 N ALA A 84 O TRP A 381
SHEET 1 D 4 PRO B 6 LYS B 7 0
SHEET 2 D 4 VAL B 15 CYS B 18 -1 O VAL B 15 N LYS B 7
SHEET 3 D 4 THR B 410 LYS B 413 -1 O LYS B 413 N CYS B 16
SHEET 4 D 4 ILE B 402 ASP B 405 -1 N ASP B 405 O THR B 410
SHEET 1 E 9 GLU B 50 PRO B 55 0
SHEET 2 E 9 THR B 36 THR B 43 -1 N ARG B 39 O SER B 52
SHEET 3 E 9 SER B 488 TRP B 494 -1 O LEU B 493 N SER B 38
SHEET 4 E 9 ALA B 456 ASN B 462 -1 N ASN B 462 O SER B 488
SHEET 5 E 9 LEU B 444 MET B 450 -1 N ASP B 445 O LEU B 461
SHEET 6 E 9 GLN B 432 ALA B 438 -1 N GLN B 432 O MET B 450
SHEET 7 E 9 LEU B 65 LYS B 77 -1 N THR B 68 O VAL B 437
SHEET 8 E 9 VAL B 468 ASP B 474 1 O LYS B 473 N LEU B 69
SHEET 9 E 9 GLY B 478 SER B 484 -1 O SER B 484 N VAL B 468
SHEET 1 F 9 GLY B 80 ALA B 84 0
SHEET 2 F 9 ILE B 118 MET B 123 1 O ARG B 120 N GLY B 83
SHEET 3 F 9 SER B 173 PRO B 178 1 O LEU B 175 N VAL B 121
SHEET 4 F 9 ALA B 229 THR B 231 1 O THR B 231 N ALA B 176
SHEET 5 F 9 ARG B 277 GLN B 284 1 O ARG B 277 N VAL B 230
SHEET 6 F 9 GLY B 307 HIS B 311 1 O ALA B 309 N MET B 280
SHEET 7 F 9 MET B 335 GLU B 340 1 O PHE B 337 N ILE B 308
SHEET 8 F 9 VAL B 375 ASN B 382 1 O VAL B 376 N LEU B 336
SHEET 9 F 9 GLY B 80 ALA B 84 1 N GLY B 82 O ASP B 380
SHEET 1 G 4 PRO C 6 LYS C 7 0
SHEET 2 G 4 VAL C 15 CYS C 18 -1 O VAL C 15 N LYS C 7
SHEET 3 G 4 THR C 410 LYS C 413 -1 O PHE C 411 N CYS C 18
SHEET 4 G 4 ILE C 402 ASP C 405 -1 N ASP C 405 O THR C 410
SHEET 1 H 9 GLU C 50 PRO C 55 0
SHEET 2 H 9 THR C 36 THR C 43 -1 N GLU C 41 O GLU C 50
SHEET 3 H 9 SER C 488 TRP C 494 -1 O LEU C 493 N SER C 38
SHEET 4 H 9 ALA C 456 ASN C 462 -1 N VAL C 458 O TYR C 492
SHEET 5 H 9 ASP C 445 MET C 450 -1 N ASP C 445 O LEU C 461
SHEET 6 H 9 GLN C 432 ALA C 438 -1 N GLN C 432 O MET C 450
SHEET 7 H 9 LEU C 65 LYS C 77 -1 N PHE C 75 O ARG C 433
SHEET 8 H 9 VAL C 468 ASP C 474 1 O THR C 471 N LEU C 67
SHEET 9 H 9 GLY C 478 SER C 484 -1 O LEU C 480 N ILE C 472
SHEET 1 I 9 GLY C 80 ALA C 84 0
SHEET 2 I 9 ILE C 118 MET C 123 1 O ARG C 120 N GLY C 83
SHEET 3 I 9 SER C 173 PRO C 178 1 O LEU C 175 N VAL C 121
SHEET 4 I 9 ALA C 229 THR C 231 1 O THR C 231 N ALA C 176
SHEET 5 I 9 ARG C 277 GLN C 284 1 O LEU C 279 N VAL C 230
SHEET 6 I 9 GLY C 307 TYR C 313 1 O ALA C 309 N MET C 280
SHEET 7 I 9 MET C 335 CYS C 342 1 O MET C 335 N ILE C 308
SHEET 8 I 9 VAL C 375 ASN C 382 1 O VAL C 376 N LEU C 336
SHEET 9 I 9 GLY C 80 ALA C 84 1 N GLY C 82 O ASP C 380
SHEET 1 J 4 PRO D 6 LYS D 7 0
SHEET 2 J 4 VAL D 15 CYS D 18 -1 O VAL D 15 N LYS D 7
SHEET 3 J 4 THR D 410 LYS D 413 -1 O LYS D 413 N CYS D 16
SHEET 4 J 4 ILE D 402 ASP D 405 -1 N ASP D 405 O THR D 410
SHEET 1 K 9 GLU D 50 PRO D 55 0
SHEET 2 K 9 THR D 36 THR D 43 -1 N ARG D 39 O SER D 52
SHEET 3 K 9 SER D 488 TRP D 494 -1 O LEU D 493 N SER D 38
SHEET 4 K 9 ALA D 456 ASN D 462 -1 N VAL D 460 O HIS D 490
SHEET 5 K 9 LEU D 444 MET D 450 -1 N ASP D 445 O LEU D 461
SHEET 6 K 9 GLN D 432 ALA D 438 -1 N VAL D 434 O ALA D 448
SHEET 7 K 9 LEU D 65 LYS D 77 -1 N THR D 68 O VAL D 437
SHEET 8 K 9 VAL D 468 ASP D 474 1 O LYS D 473 N LEU D 69
SHEET 9 K 9 GLY D 478 SER D 484 -1 O GLY D 478 N ASP D 474
SHEET 1 L 9 GLY D 80 ALA D 84 0
SHEET 2 L 9 ILE D 118 MET D 123 1 O ARG D 120 N GLY D 83
SHEET 3 L 9 SER D 173 PRO D 178 1 O LEU D 175 N VAL D 121
SHEET 4 L 9 ALA D 229 THR D 231 1 O THR D 231 N ALA D 176
SHEET 5 L 9 ARG D 277 GLN D 284 1 O LEU D 279 N VAL D 230
SHEET 6 L 9 GLY D 307 HIS D 311 1 O ALA D 309 N MET D 280
SHEET 7 L 9 MET D 335 GLU D 340 1 O MET D 335 N ILE D 308
SHEET 8 L 9 VAL D 375 ASN D 382 1 O VAL D 376 N LEU D 336
SHEET 9 L 9 GLY D 80 ALA D 84 1 N ALA D 84 O TRP D 381
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.04
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.04
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.04
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.05
SSBOND 5 CYS C 4 CYS C 16 1555 1555 2.04
SSBOND 6 CYS C 18 CYS C 23 1555 1555 2.04
SSBOND 7 CYS D 4 CYS D 16 1555 1555 2.60
SSBOND 8 CYS D 18 CYS D 23 1555 1555 2.05
LINK ND2 ASN A 19 C1 NDG A 498 1555 1555 1.44
LINK ND2 ASN B 19 C1 NAG B 499 1555 1555 1.45
LINK ND2 ASN C 19 C1 NDG C 498 1555 1555 1.43
LINK ND2 ASN D 19 C1 NAG D 498 1555 1555 2.08
LINK OD1 ASN B 146 C1 NAG B 498 1555 1555 2.04
CISPEP 1 LEU A 288 PRO A 289 0 -0.56
CISPEP 2 GLY A 390 PRO A 391 0 0.37
CISPEP 3 GLY B 62 THR B 63 0 -6.04
CISPEP 4 LEU B 288 PRO B 289 0 -3.05
CISPEP 5 GLY B 390 PRO B 391 0 2.66
CISPEP 6 LEU C 288 PRO C 289 0 4.89
CISPEP 7 GLY C 390 PRO C 391 0 -1.03
CISPEP 8 LEU D 288 PRO D 289 0 0.57
CISPEP 9 GLY D 390 PRO D 391 0 1.16
SITE 1 AC1 2 ASN B 146 PRO C 98
SITE 1 AC2 6 ASN A 19 TYR A 22 HOH A 667 HOH A 683
SITE 2 AC2 6 HOH A 724 HOH A 759
SITE 1 AC3 5 ILE B 5 ASN B 19 HOH B 596 HOH B 616
SITE 2 AC3 5 HOH B 662
SITE 1 AC4 7 ILE C 5 ASN C 19 THR C 21 TYR C 22
SITE 2 AC4 7 HOH C 627 HOH C 678 HOH C 751
SITE 1 AC5 6 ILE D 5 ASN D 19 THR D 21 TYR D 22
SITE 2 AC5 6 HOH D 590 HOH D 738
SITE 1 AC6 6 SER C 242 TYR D 11 SER D 12 ARG D 353
SITE 2 AC6 6 SER D 356 ASP D 358
SITE 1 AC7 6 TYR A 11 SER A 12 ARG A 353 SER A 356
SITE 2 AC7 6 TRP A 357 ASP A 358
SITE 1 AC8 6 LYS C 79 TRP C 228 ARG C 277 HIS C 306
SITE 2 AC8 6 HOH C 632 HOH C 759
SITE 1 AC9 3 ARG A 44 SER A 45 HOH A 547
SITE 1 BC1 5 THR A 63 GLY A 64 GLN A 440 HOH A 762
SITE 2 BC1 5 LYS C 473
SITE 1 BC2 5 LYS A 79 TRP A 228 ARG A 277 HIS A 306
SITE 2 BC2 5 HOH A 755
SITE 1 BC3 7 SER A 242 TYR B 11 SER B 12 ARG B 353
SITE 2 BC3 7 SER B 356 TRP B 357 ASP B 358
SITE 1 BC4 3 ARG B 44 SER B 45 HOH B 533
SITE 1 BC5 5 LYS B 79 TRP B 228 ARG B 277 HIS B 306
SITE 2 BC5 5 HOH B 576
SITE 1 BC6 6 GLY B 193 LYS B 194 SER B 242 GLY B 243
SITE 2 BC6 6 HOH B 600 HOH B 687
SITE 1 BC7 4 LYS B 321 ARG B 329 ARG C 329 LEU C 330
SITE 1 BC8 2 ARG B 44 TYR B 487
SITE 1 BC9 6 TYR C 11 SER C 12 ARG C 353 SER C 356
SITE 2 BC9 6 TRP C 357 ASP C 358
SITE 1 CC1 3 ARG C 44 SER C 45 HOH C 613
SITE 1 CC2 3 ARG D 44 SER D 45 HOH D 562
SITE 1 CC3 5 LYS D 79 TRP D 228 ARG D 277 HIS D 306
SITE 2 CC3 5 HOH D 733
SITE 1 CC4 6 GLY D 193 LYS D 194 SER D 242 GLY D 243
SITE 2 CC4 6 HOH D 594 HOH D 689
SITE 1 CC5 6 LYS A 473 HOH A 653 HOH A 710 THR C 63
SITE 2 CC5 6 GLY C 64 GLN C 440
SITE 1 CC6 9 ASP B 127 PHE B 128 TRP B 179 GLU B 235
SITE 2 CC6 9 PHE B 246 TYR B 313 GLU B 340 TRP B 381
SITE 3 CC6 9 ASN B 396
SITE 1 CC7 9 ASP D 127 PHE D 128 TRP D 179 GLU D 235
SITE 2 CC7 9 PHE D 246 TYR D 313 GLU D 340 TRP D 381
SITE 3 CC7 9 ASN D 396
SITE 1 CC8 7 ASP A 127 PHE A 128 TRP A 179 GLU A 235
SITE 2 CC8 7 GLU A 340 TRP A 381 PHE A 397
SITE 1 CC9 7 ASP C 127 PHE C 128 TRP C 179 GLU C 235
SITE 2 CC9 7 GLU C 340 TRP C 381 PHE C 397
CRYST1 108.967 92.216 152.670 90.00 110.94 90.00 P 1 21 1 8
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 0.009177 0.000000 0.003512 0.00000
SCALE2 0.000000 0.010844 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007013 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
