HEADER TRANSFERASE 04-SEP-08 3EE5
TITLE CRYSTAL STRUCTURE OF HUMAN M340H-BETA1,4-GALACTOSYLTRANSFERASE-I
TITLE 2 (M340H-B4GAL-T1) IN COMPLEX WITH GLCNAC-BETA1,3-GAL-BETA-
TITLE 3 NAPHTHALENEMETHANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-1,4-GALACTOSYLTRANSFERASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN OF BETA-1,4-GALACTOSYLTRANSFERASE;
COMPND 5 SYNONYM: BETA-1,4-GALTASE 1, BETA4GAL-T1, B4GAL-T1, UDP-
COMPND 6 GALACTOSE:BETA-N-ACETYLGLUCOSAMINE BETA-1,4-GALACTOSYLTRANSFERASE 1,
COMPND 7 UDP-GAL:BETA-GLCNAC BETA-1,4-GALACTOSYLTRANSFERASE 1;
COMPND 8 EC: 2.4.1.38;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B4GALT1, GGTB2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS CLOSED CONFORMATION, CARBOHYDRATE ACCEPTOR BINDING, ALTERNATIVE
KEYWDS 2 INITIATION, CELL MEMBRANE, CONGENITAL DISORDER OF GLYCOSYLATION,
KEYWDS 3 GLYCOPROTEIN, GLYCOSYLTRANSFERASE, GOLGI APPARATUS, MANGANESE,
KEYWDS 4 MEMBRANE, METAL-BINDING, SECRETED, SIGNAL-ANCHOR, TRANSFERASE,
KEYWDS 5 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.RAMAKRISHNAN,P.K.QASBA
REVDAT 6 30-AUG-23 3EE5 1 REMARK
REVDAT 5 20-OCT-21 3EE5 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 3EE5 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 13-JUL-11 3EE5 1 VERSN
REVDAT 2 17-MAR-09 3EE5 1 JRNL
REVDAT 1 06-JAN-09 3EE5 0
JRNL AUTH J.R.BROWN,F.YANG,A.SINHA,B.RAMAKRISHNAN,Y.TOR,P.K.QASBA,
JRNL AUTH 2 J.D.ESKO
JRNL TITL DEOXYGENATED DISACCHARIDE ANALOGS AS SPECIFIC INHIBITORS OF
JRNL TITL 2 {BETA}1-4-GALACTOSYLTRANSFERASE 1 AND SELECTIN-MEDIATED
JRNL TITL 3 TUMOR METASTASIS
JRNL REF J.BIOL.CHEM. V. 284 4952 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19106107
JRNL DOI 10.1074/JBC.M805782200
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3004894.130
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 75540
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) : 0.206
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 7621
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10974
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1275
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 340
REMARK 3 SOLVENT ATOMS : 475
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.77000
REMARK 3 B22 (A**2) : 15.47000
REMARK 3 B33 (A**2) : -11.70000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.120
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) : 1.230 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.090 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 35.82
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : UDPH_CTB1.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : UDPH_CTB1.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85066
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.54600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: 2AEC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, AMMONIUM SULFATE, DIOXANE, PH
REMARK 280 6.5, EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.90050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.90050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 53.56350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 97.87100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.56350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 97.87100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.90050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.56350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 97.87100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.90050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.56350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 97.87100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 112
REMARK 465 SER A 113
REMARK 465 MET A 114
REMARK 465 THR A 115
REMARK 465 GLY A 116
REMARK 465 GLY A 117
REMARK 465 GLN A 118
REMARK 465 GLN A 119
REMARK 465 MET A 120
REMARK 465 GLY A 121
REMARK 465 ARG A 122
REMARK 465 GLY A 123
REMARK 465 SER A 124
REMARK 465 ALA A 125
REMARK 465 ALA B 112
REMARK 465 SER B 113
REMARK 465 MET B 114
REMARK 465 THR B 115
REMARK 465 GLY B 116
REMARK 465 GLY B 117
REMARK 465 GLN B 118
REMARK 465 GLN B 119
REMARK 465 MET B 120
REMARK 465 GLY B 121
REMARK 465 ARG B 122
REMARK 465 GLY B 123
REMARK 465 SER B 124
REMARK 465 ALA B 125
REMARK 465 ALA C 112
REMARK 465 SER C 113
REMARK 465 MET C 114
REMARK 465 THR C 115
REMARK 465 GLY C 116
REMARK 465 GLY C 117
REMARK 465 GLN C 118
REMARK 465 GLN C 119
REMARK 465 MET C 120
REMARK 465 GLY C 121
REMARK 465 ARG C 122
REMARK 465 GLY C 123
REMARK 465 SER C 124
REMARK 465 ALA C 125
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 ARG A 185 121.13 -173.52
REMARK 500 TYR A 260 58.97 -98.19
REMARK 500 ASN A 349 50.04 -147.76
REMARK 500 SER A 373 21.69 -140.19
REMARK 500 ARG B 185 122.15 -171.31
REMARK 500 ASN C 146 16.91 -156.99
REMARK 500 ASN C 158 59.56 -112.73
REMARK 500 ARG C 185 116.59 -176.96
REMARK 500 ASP C 256 9.29 -66.60
REMARK 500 TYR C 282 149.12 -174.80
REMARK 500 ASN C 349 44.80 -148.30
REMARK 500 SER C 373 10.65 -145.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 611 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 250 OD2
REMARK 620 2 UDH A 399 O1A 96.2
REMARK 620 3 UDH A 399 O3B 171.4 80.8
REMARK 620 4 HOH A3012 O 85.6 108.7 87.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 400 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 250 OD2
REMARK 620 2 UDH B1399 O1A 93.0
REMARK 620 3 UDH B1399 O3B 162.9 81.0
REMARK 620 4 HOH B3155 O 82.9 99.2 82.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 400 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 250 OD2
REMARK 620 2 UDH C2399 O1A 95.6
REMARK 620 3 UDH C2399 O3B 172.8 80.0
REMARK 620 4 HOH C3275 O 86.4 104.1 89.0
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AEC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN M340H-BETA1,4-GALACTOSYLTRANSFERASE-I
REMARK 900 (M340H-B4GAL-T1) IN COMPLEX WITH GLCNAC-BETA1,2-MAN-ALPHA1,6-MAN-
REMARK 900 BETA-OR
DBREF 3EE5 A 126 398 UNP P15291 B4GT1_HUMAN 126 398
DBREF 3EE5 B 126 398 UNP P15291 B4GT1_HUMAN 126 398
DBREF 3EE5 C 126 398 UNP P15291 B4GT1_HUMAN 126 398
SEQADV 3EE5 ALA A 112 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 SER A 113 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 MET A 114 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 THR A 115 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY A 116 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY A 117 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLN A 118 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLN A 119 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 MET A 120 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY A 121 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 ARG A 122 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY A 123 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 SER A 124 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 ALA A 125 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 THR A 337 UNP P15291 ARG 337 ENGINEERED MUTATION
SEQADV 3EE5 THR A 338 UNP P15291 CYS 338 ENGINEERED MUTATION
SEQADV 3EE5 HIS A 340 UNP P15291 MET 340 ENGINEERED MUTATION
SEQADV 3EE5 ALA B 112 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 SER B 113 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 MET B 114 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 THR B 115 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY B 116 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY B 117 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLN B 118 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLN B 119 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 MET B 120 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY B 121 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 ARG B 122 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY B 123 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 SER B 124 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 ALA B 125 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 THR B 337 UNP P15291 ARG 337 ENGINEERED MUTATION
SEQADV 3EE5 THR B 338 UNP P15291 CYS 338 ENGINEERED MUTATION
SEQADV 3EE5 HIS B 340 UNP P15291 MET 340 ENGINEERED MUTATION
SEQADV 3EE5 ALA C 112 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 SER C 113 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 MET C 114 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 THR C 115 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY C 116 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY C 117 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLN C 118 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLN C 119 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 MET C 120 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY C 121 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 ARG C 122 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 GLY C 123 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 SER C 124 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 ALA C 125 UNP P15291 EXPRESSION TAG
SEQADV 3EE5 THR C 337 UNP P15291 ARG 337 ENGINEERED MUTATION
SEQADV 3EE5 THR C 338 UNP P15291 CYS 338 ENGINEERED MUTATION
SEQADV 3EE5 HIS C 340 UNP P15291 MET 340 ENGINEERED MUTATION
SEQRES 1 A 287 ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY SER
SEQRES 2 A 287 ALA SER LEU PRO ALA CYS PRO GLU GLU SER PRO LEU LEU
SEQRES 3 A 287 VAL GLY PRO MET LEU ILE GLU PHE ASN MET PRO VAL ASP
SEQRES 4 A 287 LEU GLU LEU VAL ALA LYS GLN ASN PRO ASN VAL LYS MET
SEQRES 5 A 287 GLY GLY ARG TYR ALA PRO ARG ASP CYS VAL SER PRO HIS
SEQRES 6 A 287 LYS VAL ALA ILE ILE ILE PRO PHE ARG ASN ARG GLN GLU
SEQRES 7 A 287 HIS LEU LYS TYR TRP LEU TYR TYR LEU HIS PRO VAL LEU
SEQRES 8 A 287 GLN ARG GLN GLN LEU ASP TYR GLY ILE TYR VAL ILE ASN
SEQRES 9 A 287 GLN ALA GLY ASP THR ILE PHE ASN ARG ALA LYS LEU LEU
SEQRES 10 A 287 ASN VAL GLY PHE GLN GLU ALA LEU LYS ASP TYR ASP TYR
SEQRES 11 A 287 THR CYS PHE VAL PHE SER ASP VAL ASP LEU ILE PRO MET
SEQRES 12 A 287 ASN ASP HIS ASN ALA TYR ARG CYS PHE SER GLN PRO ARG
SEQRES 13 A 287 HIS ILE SER VAL ALA MET ASP LYS PHE GLY PHE SER LEU
SEQRES 14 A 287 PRO TYR VAL GLN TYR PHE GLY GLY VAL SER ALA LEU SER
SEQRES 15 A 287 LYS GLN GLN PHE LEU THR ILE ASN GLY PHE PRO ASN ASN
SEQRES 16 A 287 TYR TRP GLY TRP GLY GLY GLU ASP ASP ASP ILE PHE ASN
SEQRES 17 A 287 ARG LEU VAL PHE ARG GLY MET SER ILE SER ARG PRO ASN
SEQRES 18 A 287 ALA VAL VAL GLY THR THR ARG HIS ILE ARG HIS SER ARG
SEQRES 19 A 287 ASP LYS LYS ASN GLU PRO ASN PRO GLN ARG PHE ASP ARG
SEQRES 20 A 287 ILE ALA HIS THR LYS GLU THR MET LEU SER ASP GLY LEU
SEQRES 21 A 287 ASN SER LEU THR TYR GLN VAL LEU ASP VAL GLN ARG TYR
SEQRES 22 A 287 PRO LEU TYR THR GLN ILE THR VAL ASP ILE GLY THR PRO
SEQRES 23 A 287 SER
SEQRES 1 B 287 ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY SER
SEQRES 2 B 287 ALA SER LEU PRO ALA CYS PRO GLU GLU SER PRO LEU LEU
SEQRES 3 B 287 VAL GLY PRO MET LEU ILE GLU PHE ASN MET PRO VAL ASP
SEQRES 4 B 287 LEU GLU LEU VAL ALA LYS GLN ASN PRO ASN VAL LYS MET
SEQRES 5 B 287 GLY GLY ARG TYR ALA PRO ARG ASP CYS VAL SER PRO HIS
SEQRES 6 B 287 LYS VAL ALA ILE ILE ILE PRO PHE ARG ASN ARG GLN GLU
SEQRES 7 B 287 HIS LEU LYS TYR TRP LEU TYR TYR LEU HIS PRO VAL LEU
SEQRES 8 B 287 GLN ARG GLN GLN LEU ASP TYR GLY ILE TYR VAL ILE ASN
SEQRES 9 B 287 GLN ALA GLY ASP THR ILE PHE ASN ARG ALA LYS LEU LEU
SEQRES 10 B 287 ASN VAL GLY PHE GLN GLU ALA LEU LYS ASP TYR ASP TYR
SEQRES 11 B 287 THR CYS PHE VAL PHE SER ASP VAL ASP LEU ILE PRO MET
SEQRES 12 B 287 ASN ASP HIS ASN ALA TYR ARG CYS PHE SER GLN PRO ARG
SEQRES 13 B 287 HIS ILE SER VAL ALA MET ASP LYS PHE GLY PHE SER LEU
SEQRES 14 B 287 PRO TYR VAL GLN TYR PHE GLY GLY VAL SER ALA LEU SER
SEQRES 15 B 287 LYS GLN GLN PHE LEU THR ILE ASN GLY PHE PRO ASN ASN
SEQRES 16 B 287 TYR TRP GLY TRP GLY GLY GLU ASP ASP ASP ILE PHE ASN
SEQRES 17 B 287 ARG LEU VAL PHE ARG GLY MET SER ILE SER ARG PRO ASN
SEQRES 18 B 287 ALA VAL VAL GLY THR THR ARG HIS ILE ARG HIS SER ARG
SEQRES 19 B 287 ASP LYS LYS ASN GLU PRO ASN PRO GLN ARG PHE ASP ARG
SEQRES 20 B 287 ILE ALA HIS THR LYS GLU THR MET LEU SER ASP GLY LEU
SEQRES 21 B 287 ASN SER LEU THR TYR GLN VAL LEU ASP VAL GLN ARG TYR
SEQRES 22 B 287 PRO LEU TYR THR GLN ILE THR VAL ASP ILE GLY THR PRO
SEQRES 23 B 287 SER
SEQRES 1 C 287 ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY SER
SEQRES 2 C 287 ALA SER LEU PRO ALA CYS PRO GLU GLU SER PRO LEU LEU
SEQRES 3 C 287 VAL GLY PRO MET LEU ILE GLU PHE ASN MET PRO VAL ASP
SEQRES 4 C 287 LEU GLU LEU VAL ALA LYS GLN ASN PRO ASN VAL LYS MET
SEQRES 5 C 287 GLY GLY ARG TYR ALA PRO ARG ASP CYS VAL SER PRO HIS
SEQRES 6 C 287 LYS VAL ALA ILE ILE ILE PRO PHE ARG ASN ARG GLN GLU
SEQRES 7 C 287 HIS LEU LYS TYR TRP LEU TYR TYR LEU HIS PRO VAL LEU
SEQRES 8 C 287 GLN ARG GLN GLN LEU ASP TYR GLY ILE TYR VAL ILE ASN
SEQRES 9 C 287 GLN ALA GLY ASP THR ILE PHE ASN ARG ALA LYS LEU LEU
SEQRES 10 C 287 ASN VAL GLY PHE GLN GLU ALA LEU LYS ASP TYR ASP TYR
SEQRES 11 C 287 THR CYS PHE VAL PHE SER ASP VAL ASP LEU ILE PRO MET
SEQRES 12 C 287 ASN ASP HIS ASN ALA TYR ARG CYS PHE SER GLN PRO ARG
SEQRES 13 C 287 HIS ILE SER VAL ALA MET ASP LYS PHE GLY PHE SER LEU
SEQRES 14 C 287 PRO TYR VAL GLN TYR PHE GLY GLY VAL SER ALA LEU SER
SEQRES 15 C 287 LYS GLN GLN PHE LEU THR ILE ASN GLY PHE PRO ASN ASN
SEQRES 16 C 287 TYR TRP GLY TRP GLY GLY GLU ASP ASP ASP ILE PHE ASN
SEQRES 17 C 287 ARG LEU VAL PHE ARG GLY MET SER ILE SER ARG PRO ASN
SEQRES 18 C 287 ALA VAL VAL GLY THR THR ARG HIS ILE ARG HIS SER ARG
SEQRES 19 C 287 ASP LYS LYS ASN GLU PRO ASN PRO GLN ARG PHE ASP ARG
SEQRES 20 C 287 ILE ALA HIS THR LYS GLU THR MET LEU SER ASP GLY LEU
SEQRES 21 C 287 ASN SER LEU THR TYR GLN VAL LEU ASP VAL GLN ARG TYR
SEQRES 22 C 287 PRO LEU TYR THR GLN ILE THR VAL ASP ILE GLY THR PRO
SEQRES 23 C 287 SER
HET GAL D 1 11
HET NAG D 2 14
HET GAL E 1 11
HET NAG E 2 14
HET GAL F 1 11
HET NAG F 2 14
HET UDH A 399 32
HET 2NA A 100 12
HET SO4 A 602 5
HET SO4 A 604 5
HET SO4 A 607 5
HET SO4 A 609 5
HET SO4 A 610 5
HET MN A 611 1
HET GOL A 417 6
HET GOL A 420 6
HET UDH B1399 32
HET 2NA B 101 12
HET GOL B 414 6
HET GOL B 415 6
HET GOL B 416 6
HET GOL B 419 6
HET SO4 B 601 5
HET SO4 B 603 5
HET SO4 B 605 5
HET SO4 B 606 5
HET SO4 B 611 5
HET SO4 B 613 5
HET SO4 B 614 5
HET MN B 400 1
HET UDH C2399 32
HET 2NA C 102 12
HET GOL C 418 6
HET DIO C 435 6
HET MES C 436 12
HET SO4 C 608 5
HET SO4 C 612 5
HET MN C 400 1
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM UDH 6-AMINOHEXYL-URIDINE-C1,5'-DIPHOSPHATE
HETNAM 2NA NAPHTHALEN-2-YLMETHANOL
HETNAM SO4 SULFATE ION
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
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 2NA NAPHTHALENEMETHANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GAL 3(C6 H12 O6)
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 7 UDH 3(C15 H27 N3 O12 P2)
FORMUL 8 2NA 3(C11 H10 O)
FORMUL 9 SO4 14(O4 S 2-)
FORMUL 14 MN 3(MN 2+)
FORMUL 15 GOL 7(C3 H8 O3)
FORMUL 34 DIO C4 H8 O2
FORMUL 35 MES C6 H13 N O4 S
FORMUL 39 HOH *475(H2 O)
HELIX 1 1 ASP A 150 ASN A 158 1 9
HELIX 2 2 ARG A 187 GLN A 205 1 19
HELIX 3 3 ASN A 223 TYR A 239 1 17
HELIX 4 4 LYS A 275 GLY A 277 5 3
HELIX 5 5 LYS A 294 ILE A 300 1 7
HELIX 6 6 GLY A 312 ARG A 324 1 13
HELIX 7 7 GLN A 354 ALA A 360 1 7
HELIX 8 8 HIS A 361 MET A 366 1 6
HELIX 9 9 GLY A 370 LEU A 374 5 5
HELIX 10 10 ASP B 150 ASN B 158 1 9
HELIX 11 11 ARG B 187 GLN B 205 1 19
HELIX 12 12 ASN B 223 LYS B 237 1 15
HELIX 13 13 LYS B 275 GLY B 277 5 3
HELIX 14 14 LYS B 294 ILE B 300 1 7
HELIX 15 15 GLY B 312 ARG B 324 1 13
HELIX 16 16 GLN B 354 ALA B 360 1 7
HELIX 17 17 HIS B 361 MET B 366 1 6
HELIX 18 18 GLY B 370 LEU B 374 5 5
HELIX 19 19 ASP C 150 ASN C 158 1 9
HELIX 20 20 ARG C 187 GLN C 205 1 19
HELIX 21 21 ASN C 223 LEU C 236 1 14
HELIX 22 22 LYS C 275 GLY C 277 5 3
HELIX 23 23 LYS C 294 ILE C 300 1 7
HELIX 24 24 GLY C 312 ARG C 324 1 13
HELIX 25 25 GLN C 354 HIS C 361 1 8
HELIX 26 26 HIS C 361 ASP C 369 1 9
HELIX 27 27 GLY C 370 LEU C 374 5 5
SHEET 1 A 6 ARG A 166 TYR A 167 0
SHEET 2 A 6 ASP A 208 GLN A 216 -1 O TYR A 209 N TYR A 167
SHEET 3 A 6 LYS A 177 PHE A 184 1 N ILE A 180 O TYR A 212
SHEET 4 A 6 CYS A 243 SER A 247 1 O VAL A 245 N ILE A 181
SHEET 5 A 6 VAL A 289 SER A 293 -1 O SER A 290 N PHE A 246
SHEET 6 A 6 ARG A 267 HIS A 268 -1 N ARG A 267 O ALA A 291
SHEET 1 B 4 ARG A 166 TYR A 167 0
SHEET 2 B 4 ASP A 208 GLN A 216 -1 O TYR A 209 N TYR A 167
SHEET 3 B 4 THR A 388 ASP A 393 1 O ILE A 390 N VAL A 213
SHEET 4 B 4 GLN A 377 ARG A 383 -1 N GLN A 377 O ASP A 393
SHEET 1 C 3 LEU A 251 PRO A 253 0
SHEET 2 C 3 THR A 337 HIS A 340 -1 O ARG A 339 N ILE A 252
SHEET 3 C 3 ALA A 272 MET A 273 1 N ALA A 272 O THR A 338
SHEET 1 D 6 ARG B 166 TYR B 167 0
SHEET 2 D 6 ASP B 208 GLN B 216 -1 O TYR B 209 N TYR B 167
SHEET 3 D 6 LYS B 177 PHE B 184 1 N ILE B 180 O TYR B 212
SHEET 4 D 6 CYS B 243 SER B 247 1 O VAL B 245 N ILE B 181
SHEET 5 D 6 VAL B 289 SER B 293 -1 O SER B 290 N PHE B 246
SHEET 6 D 6 ARG B 267 HIS B 268 -1 N ARG B 267 O ALA B 291
SHEET 1 E 4 ARG B 166 TYR B 167 0
SHEET 2 E 4 ASP B 208 GLN B 216 -1 O TYR B 209 N TYR B 167
SHEET 3 E 4 THR B 388 ASP B 393 1 O THR B 388 N VAL B 213
SHEET 4 E 4 GLN B 377 ARG B 383 -1 N GLN B 377 O ASP B 393
SHEET 1 F 3 LEU B 251 PRO B 253 0
SHEET 2 F 3 THR B 337 HIS B 340 -1 O ARG B 339 N ILE B 252
SHEET 3 F 3 ALA B 272 MET B 273 1 N ALA B 272 O THR B 338
SHEET 1 G 6 ARG C 166 TYR C 167 0
SHEET 2 G 6 ASP C 208 GLN C 216 -1 O TYR C 209 N TYR C 167
SHEET 3 G 6 LYS C 177 PHE C 184 1 N PHE C 184 O GLN C 216
SHEET 4 G 6 CYS C 243 SER C 247 1 O VAL C 245 N ILE C 181
SHEET 5 G 6 VAL C 289 SER C 293 -1 O SER C 290 N PHE C 246
SHEET 6 G 6 ARG C 267 HIS C 268 -1 N ARG C 267 O ALA C 291
SHEET 1 H 4 ARG C 166 TYR C 167 0
SHEET 2 H 4 ASP C 208 GLN C 216 -1 O TYR C 209 N TYR C 167
SHEET 3 H 4 THR C 388 ASP C 393 1 O THR C 388 N VAL C 213
SHEET 4 H 4 GLN C 377 ARG C 383 -1 N LEU C 379 O THR C 391
SHEET 1 I 3 LEU C 251 PRO C 253 0
SHEET 2 I 3 THR C 337 HIS C 340 -1 O ARG C 339 N ILE C 252
SHEET 3 I 3 ALA C 272 MET C 273 1 N ALA C 272 O THR C 338
SSBOND 1 CYS A 130 CYS A 172 1555 1555 2.06
SSBOND 2 CYS A 243 CYS A 262 1555 1555 2.06
SSBOND 3 CYS B 130 CYS B 172 1555 1555 2.04
SSBOND 4 CYS B 243 CYS B 262 1555 1555 2.04
SSBOND 5 CYS C 130 CYS C 172 1555 1555 2.04
SSBOND 6 CYS C 243 CYS C 262 1555 1555 2.04
LINK O31 2NA A 100 C1 GAL D 1 1555 1555 1.38
LINK O31 2NA B 101 C1 GAL E 1 1555 1555 1.41
LINK O31 2NA C 102 C1 GAL F 1 1555 1555 1.41
LINK O3 GAL D 1 C1 NAG D 2 1555 1555 1.40
LINK O3 GAL E 1 C1 NAG E 2 1555 1555 1.40
LINK O3 GAL F 1 C1 NAG F 2 1555 1555 1.41
LINK OD2 ASP A 250 MN MN A 611 1555 1555 2.19
LINK O1A UDH A 399 MN MN A 611 1555 1555 2.07
LINK O3B UDH A 399 MN MN A 611 1555 1555 2.14
LINK MN MN A 611 O HOH A3012 1555 1555 2.18
LINK OD2 ASP B 250 MN MN B 400 1555 1555 2.30
LINK MN MN B 400 O1A UDH B1399 1555 1555 2.08
LINK MN MN B 400 O3B UDH B1399 1555 1555 2.17
LINK MN MN B 400 O HOH B3155 1555 1555 2.40
LINK OD2 ASP C 250 MN MN C 400 1555 1555 2.19
LINK MN MN C 400 O1A UDH C2399 1555 1555 2.12
LINK MN MN C 400 O3B UDH C2399 1555 1555 2.03
LINK MN MN C 400 O HOH C3275 1555 1555 2.17
CRYST1 107.127 195.742 143.801 90.00 90.00 90.00 C 2 2 21 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005109 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
