HEADER TOXIN 27-AUG-03 1UKM
TITLE CRYSTAL STRUCTURE OF EMS16, AN ANTAGONIST OF COLLAGEN RECEPTOR
TITLE 2 INTEGRIN ALPHA2BETA1 (GPIA/IIA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EMS16 A CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-134;
COMPND 5 SYNONYM: EMS16 SUBUNIT A;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EMS16 B CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 1-128;
COMPND 10 SYNONYM: EMS16 SUBUNIT B;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ECHIS MULTISQUAMATUS;
SOURCE 3 ORGANISM_TAXID: 93050;
SOURCE 4 SECRETION: VENOM;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ECHIS MULTISQUAMATUS;
SOURCE 7 ORGANISM_TAXID: 93050;
SOURCE 8 SECRETION: VENOM
KEYWDS DOMAIN SWAPPING, C-TYPE LECTIN, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HORII,D.OKUDA,T.MORITA,H.MIZUNO
REVDAT 8 25-OCT-23 1UKM 1 HETSYN
REVDAT 7 29-JUL-20 1UKM 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE
REVDAT 6 25-JUL-18 1UKM 1 SEQADV
REVDAT 5 04-OCT-17 1UKM 1 REMARK
REVDAT 4 13-JUL-11 1UKM 1 VERSN
REVDAT 3 24-FEB-09 1UKM 1 VERSN
REVDAT 2 11-NOV-03 1UKM 1 TITLE
REVDAT 1 04-NOV-03 1UKM 0
JRNL AUTH K.HORII,D.OKUDA,T.MORITA,H.MIZUNO
JRNL TITL STRUCTURAL CHARACTERIZATION OF EMS16, AN ANTAGONIST OF
JRNL TITL 2 COLLAGEN RECEPTOR (GPIA/IIA) FROM THE VENOM OF ECHIS
JRNL TITL 3 MULTISQUAMATUS
JRNL REF BIOCHEMISTRY V. 42 12497 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14580195
JRNL DOI 10.1021/BI034890H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.OKUDA,K.HORII,H.MIZUNO,T.MORITA
REMARK 1 TITL CHARACTERIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF
REMARK 1 TITL 2 EMS16, AN ANTAGONIST OF COLLAGEN RECEPTOR (GPIA/IIA) FROM
REMARK 1 TITL 3 THE VENOM OF ECHIS MULTISQUAMATUS
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 134 19 2003
REMARK 1 REFN ISSN 0021-924X
REMARK 1 DOI 10.1093/JB/MVG108
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.MARCINKIEWICZ,R.R.LOBB,M.M.MARCINKIEWICZ,J.L.DANIEL,
REMARK 1 AUTH 2 J.B.SMITH,C.DANGELMAIER,P.H.WEINREB,D.A.BEACHAM,
REMARK 1 AUTH 3 S.NIEWIAROWSKI
REMARK 1 TITL ISOLATION AND CHARACTERIZATION OF EMS16, A C-LECTIN TYPE
REMARK 1 TITL 2 PROTEIN FROM ECHIS MULTISQUAMATUS VENOM, A POTENT AND
REMARK 1 TITL 3 SELECTIVE INHIBITOR OF THE ALPHA2BETA1 INTEGRIN
REMARK 1 REF BIOCHEMISTRY V. 39 9859 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI000428A
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1271064.400
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 26143
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 : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1303
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4092
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 209
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 : 2126
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.12000
REMARK 3 B22 (A**2) : -1.31000
REMARK 3 B33 (A**2) : -2.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 3.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.840 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.660 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.270 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 50.67
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 : HETERO.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBO_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : HETERO.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UKM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000005932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL
REMARK 200 OPTICS : OSMIC CONFOCAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26199
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.11600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1BJ3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, POTASSIUM DIHYDROGEN
REMARK 280 PHOSPHATE, GLYCEROL, PH 5.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.28500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.87150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.96650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.87150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.28500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.96650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 ASP A 1
REMARK 465 PHE A 2
REMARK 465 VAL A 134
REMARK 465 ASP B 125
REMARK 465 PRO B 126
REMARK 465 ALA B 127
REMARK 465 VAL B 128
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 SER A 6 -120.32 39.00
REMARK 500 ASP A 12 53.70 37.04
REMARK 500 ILE A 92 -72.42 -129.85
REMARK 500 ASN B 69 80.10 56.67
REMARK 500 ASP B 85 -74.29 -144.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE DATABASE UNP Q7T2Q0 REPORTS THERE IS A CONFLICT AS
REMARK 999 EXPERIMENTAL INFORMATION.
DBREF 1UKM A 1 134 UNP Q7T2Q1 Q7T2Q1_ECHML 24 157
DBREF 1UKM B 1 128 UNP Q7T2Q0 Q7T2Q0_ECHML 27 154
SEQADV 1UKM SER B 43 UNP Q7T2Q0 GLY 69 SEE REMARK 999
SEQRES 1 A 134 ASP PHE ASP CYS PRO SER ASP TRP THR ALA TYR ASP GLN
SEQRES 2 A 134 HIS CYS TYR LEU ALA ILE GLY GLU PRO GLN ASN TRP TYR
SEQRES 3 A 134 GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ASP GLY
SEQRES 4 A 134 HIS LEU VAL SER ILE GLN SER ARG GLU GLU GLY ASN PHE
SEQRES 5 A 134 VAL ALA GLN LEU VAL SER GLY PHE MET HIS ARG SER GLU
SEQRES 6 A 134 ILE TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG GLU GLU
SEQRES 7 A 134 GLN GLN CYS ASN PRO GLU TRP ASN ASP GLY SER LYS ILE
SEQRES 8 A 134 ILE TYR VAL ASN TRP LYS GLU GLY GLU SER LYS MET CYS
SEQRES 9 A 134 GLN GLY LEU THR LYS TRP THR ASN PHE HIS ASP TRP ASN
SEQRES 10 A 134 ASN ILE ASN CYS GLU ASP LEU TYR PRO PHE VAL CYS LYS
SEQRES 11 A 134 PHE SER ALA VAL
SEQRES 1 B 128 CYS PRO LEU GLY TRP SER SER PHE ASP GLN HIS CYS TYR
SEQRES 2 B 128 LYS VAL PHE GLU PRO VAL LYS ASN TRP THR GLU ALA GLU
SEQRES 3 B 128 GLU ILE CYS MET GLN GLN HIS LYS GLY SER ARG LEU ALA
SEQRES 4 B 128 SER ILE HIS SER SER GLU GLU GLU ALA PHE VAL SER LYS
SEQRES 5 B 128 LEU ALA SER LYS ALA LEU LYS PHE THR SER MET TRP ILE
SEQRES 6 B 128 GLY LEU ASN ASN PRO TRP LYS ASP CYS LYS TRP GLU TRP
SEQRES 7 B 128 SER ASP ASN ALA ARG PHE ASP TYR LYS ALA TRP LYS ARG
SEQRES 8 B 128 ARG PRO TYR CYS THR VAL MET VAL VAL LYS PRO ASP ARG
SEQRES 9 B 128 ILE PHE TRP PHE THR ARG GLY CYS GLU LYS SER VAL SER
SEQRES 10 B 128 PHE VAL CYS LYS PHE LEU THR ASP PRO ALA VAL
MODRES 1UKM ASN B 21 ASN GLYCOSYLATION SITE
HET CL A1304 1
HET GOL A1300 6
HET GOL A1301 6
HET GOL A1302 6
HET NAG B1022 14
HET GOL B1303 6
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
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
FORMUL 3 CL CL 1-
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 7 NAG C8 H15 N O6
FORMUL 9 HOH *250(H2 O)
HELIX 1 1 ASN A 24 ALA A 36 1 13
HELIX 2 2 SER A 46 VAL A 57 1 12
HELIX 3 3 SER A 58 ARG A 63 5 6
HELIX 4 4 TRP A 110 ASN A 112 5 3
HELIX 5 5 ASN B 21 HIS B 33 1 13
HELIX 6 6 SER B 43 LEU B 58 1 16
SHEET 1 A 4 THR A 9 TYR A 11 0
SHEET 2 A 4 HIS A 14 GLN A 23 -1 O TYR A 16 N THR A 9
SHEET 3 A 4 TYR A 125 SER A 132 -1 O PHE A 127 N ILE A 19
SHEET 4 A 4 HIS A 40 LEU A 41 -1 N HIS A 40 O LYS A 130
SHEET 1 B 4 TRP A 116 ILE A 119 0
SHEET 2 B 4 CYS A 104 THR A 108 -1 N CYS A 104 O ILE A 119
SHEET 3 B 4 TYR A 67 ASP A 74 -1 N VAL A 68 O LEU A 107
SHEET 4 B 4 TRP B 76 TRP B 78 -1 O GLU B 77 N ARG A 73
SHEET 1 C 4 SER B 6 PHE B 8 0
SHEET 2 C 4 HIS B 11 LYS B 20 -1 O TYR B 13 N SER B 6
SHEET 3 C 4 VAL B 116 LEU B 123 -1 O PHE B 118 N PHE B 16
SHEET 4 C 4 ARG B 37 LEU B 38 -1 N ARG B 37 O LYS B 121
SHEET 1 D 6 SER B 6 PHE B 8 0
SHEET 2 D 6 HIS B 11 LYS B 20 -1 O TYR B 13 N SER B 6
SHEET 3 D 6 VAL B 116 LEU B 123 -1 O PHE B 118 N PHE B 16
SHEET 4 D 6 SER B 62 ASN B 68 1 N TRP B 64 O SER B 117
SHEET 5 D 6 TYR B 94 VAL B 100 -1 O MET B 98 N MET B 63
SHEET 6 D 6 ILE B 105 GLY B 111 -1 O ARG B 110 N CYS B 95
SSBOND 1 CYS A 4 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 32 CYS A 129 1555 1555 2.04
SSBOND 3 CYS A 81 CYS B 74 1555 1555 2.03
SSBOND 4 CYS A 104 CYS A 121 1555 1555 2.03
SSBOND 5 CYS B 1 CYS B 12 1555 1555 2.04
SSBOND 6 CYS B 29 CYS B 120 1555 1555 2.04
SSBOND 7 CYS B 95 CYS B 112 1555 1555 2.05
LINK ND2 ASN B 21 C1 NAG B1022 1555 1555 1.46
CRYST1 46.570 59.933 115.743 90.00 90.00 90.00 P 21 21 21 4
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 0.021473 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
