HEADER TRANSFERASE 13-SEP-10 3OTK
TITLE STRUCTURE AND MECHANISIM OF CORE 2 BETA1,6-N-
TITLE 2 ACETYLGLUCOSAMINYLTRANSFERASE: A METAL-ION INDEPENDENT GT-A
TITLE 3 GLYCOSYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-1,3-GALACTOSYL-O-GLYCOSYL-GLYCOPROTEIN BETA-1,6-N-
COMPND 3 ACETYLGLUCOSAMINYLTRANSFERASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: SOLUBLE CATALYTIC DOMAIN (UNP RESIDUES 38-428);
COMPND 6 SYNONYM: CORE 2-BRANCHING ENZYME, CORE2-GLCNAC-TRANSFERASE, C2GNT;
COMPND 7 EC: 2.4.1.102;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GCNT1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY (HEK) 293 CELLS
KEYWDS GLYCOSYLTRANSFERASE, GOLGI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.PAK,J.M.RINI
REVDAT 3 29-JUL-20 3OTK 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 02-OCT-13 3OTK 1 JRNL
REVDAT 1 14-SEP-11 3OTK 0
JRNL AUTH J.E.PAK,M.SATKUNARAJAH,J.SEETHARAMAN,J.M.RINI
JRNL TITL STRUCTURAL AND MECHANISTIC CHARACTERIZATION OF
JRNL TITL 2 LEUKOCYTE-TYPE CORE 2 BETA
JRNL TITL 3 1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE: A METAL-ION-INDEPENDENT
JRNL TITL 4 GT-A GLYCOSYLTRANSFERASE.
JRNL REF J.MOL.BIOL. V. 414 798 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 22056345
JRNL DOI 10.1016/J.JMB.2011.10.039
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 80656
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4289
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5713
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 291
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11832
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 254
REMARK 3 SOLVENT ATOMS : 533
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.54000
REMARK 3 B22 (A**2) : -1.80000
REMARK 3 B33 (A**2) : 3.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.206
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.961
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12463 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16941 ; 1.172 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1461 ; 5.258 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 581 ;33.334 ;23.959
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2125 ;14.852 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;17.594 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1845 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9348 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5627 ; 0.220 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8653 ; 0.323 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1115 ; 0.175 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.112 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 62 ; 0.181 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.188 ; 0.500
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): 7324 ; 1.020 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11920 ; 2.599 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5361 ;14.092 ;30.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5018 ;19.005 ;50.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 86 A 424
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2000 -34.2710 -70.6630
REMARK 3 T TENSOR
REMARK 3 T11: -0.0366 T22: -0.0192
REMARK 3 T33: -0.0664 T12: -0.0051
REMARK 3 T13: 0.0063 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.4387 L22: 0.9496
REMARK 3 L33: 0.2505 L12: 0.2176
REMARK 3 L13: 0.0516 L23: 0.2148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0388 S12: 0.0063 S13: -0.0420
REMARK 3 S21: -0.0322 S22: 0.0172 S23: 0.0261
REMARK 3 S31: 0.0011 S32: -0.0043 S33: 0.0216
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 86 B 424
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2670 -14.2920 -56.6470
REMARK 3 T TENSOR
REMARK 3 T11: -0.0485 T22: -0.0257
REMARK 3 T33: -0.0654 T12: 0.0151
REMARK 3 T13: -0.0172 T23: -0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 1.1643 L22: 0.7441
REMARK 3 L33: 0.4267 L12: -0.0433
REMARK 3 L13: -0.2176 L23: -0.0753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0720 S12: -0.1442 S13: 0.0565
REMARK 3 S21: 0.0655 S22: 0.0554 S23: -0.1288
REMARK 3 S31: 0.0039 S32: 0.0243 S33: 0.0166
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 86 C 424
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6890 -0.0130 -2.5630
REMARK 3 T TENSOR
REMARK 3 T11: -0.0368 T22: -0.0384
REMARK 3 T33: -0.0544 T12: -0.0084
REMARK 3 T13: -0.0048 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.4101 L22: 1.2733
REMARK 3 L33: 0.2020 L12: 0.3354
REMARK 3 L13: -0.1609 L23: -0.2876
REMARK 3 S TENSOR
REMARK 3 S11: -0.0641 S12: 0.0092 S13: 0.0556
REMARK 3 S21: -0.0762 S22: 0.0557 S23: -0.0137
REMARK 3 S31: 0.0077 S32: 0.0106 S33: 0.0085
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 86 D 424
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1230 -19.7810 11.6130
REMARK 3 T TENSOR
REMARK 3 T11: -0.0415 T22: -0.0436
REMARK 3 T33: -0.0527 T12: 0.0127
REMARK 3 T13: 0.0159 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.8491 L22: 0.7464
REMARK 3 L33: 0.4406 L12: -0.0174
REMARK 3 L13: 0.0495 L23: 0.0343
REMARK 3 S TENSOR
REMARK 3 S11: -0.0631 S12: -0.0587 S13: -0.0267
REMARK 3 S21: 0.0630 S22: 0.0392 S23: 0.1326
REMARK 3 S31: 0.0119 S32: -0.0081 S33: 0.0239
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OTK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061555.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9771
REMARK 200 MONOCHROMATOR : HORIZONTAL FOCUSING 5.05
REMARK 200 ASYMMETRIC CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : 0.11600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
REMARK 200 R SYM FOR SHELL (I) : 0.67600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% POLYETHYLENE GLYCOL 4000, 0.15 M
REMARK 280 GLYCINE PH 9.0, 0.6 M LICL, 1.5% 1,2,3 HEPTANETRIOL, 25 MM UDP-
REMARK 280 GLCNAC, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
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 50.51000
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
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, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 PRO A 38
REMARK 465 GLU A 39
REMARK 465 PHE A 40
REMARK 465 PHE A 41
REMARK 465 SER A 42
REMARK 465 VAL A 43
REMARK 465 ARG A 44
REMARK 465 HIS A 45
REMARK 465 LEU A 46
REMARK 465 GLU A 47
REMARK 465 LEU A 48
REMARK 465 ALA A 49
REMARK 465 GLY A 50
REMARK 465 ASP A 51
REMARK 465 ASP A 52
REMARK 465 PRO A 53
REMARK 465 TYR A 54
REMARK 465 SER A 55
REMARK 465 ASN A 425
REMARK 465 LEU A 426
REMARK 465 GLU A 427
REMARK 465 HIS A 428
REMARK 465 PRO B 38
REMARK 465 GLU B 39
REMARK 465 PHE B 40
REMARK 465 PHE B 41
REMARK 465 SER B 42
REMARK 465 VAL B 43
REMARK 465 ARG B 44
REMARK 465 HIS B 45
REMARK 465 LEU B 46
REMARK 465 GLU B 47
REMARK 465 LEU B 48
REMARK 465 ALA B 49
REMARK 465 GLY B 50
REMARK 465 ASP B 51
REMARK 465 ASP B 52
REMARK 465 PRO B 53
REMARK 465 TYR B 54
REMARK 465 SER B 55
REMARK 465 VAL B 80
REMARK 465 GLN B 81
REMARK 465 PHE B 82
REMARK 465 LYS B 83
REMARK 465 LYS B 84
REMARK 465 ARG B 85
REMARK 465 ASN B 425
REMARK 465 LEU B 426
REMARK 465 GLU B 427
REMARK 465 HIS B 428
REMARK 465 PRO C 38
REMARK 465 GLU C 39
REMARK 465 PHE C 40
REMARK 465 PHE C 41
REMARK 465 SER C 42
REMARK 465 VAL C 43
REMARK 465 ARG C 44
REMARK 465 HIS C 45
REMARK 465 LEU C 46
REMARK 465 GLU C 47
REMARK 465 LEU C 48
REMARK 465 ALA C 49
REMARK 465 GLY C 50
REMARK 465 ASP C 51
REMARK 465 ASP C 52
REMARK 465 PRO C 53
REMARK 465 TYR C 54
REMARK 465 SER C 55
REMARK 465 ILE C 77
REMARK 465 LEU C 78
REMARK 465 THR C 79
REMARK 465 VAL C 80
REMARK 465 GLN C 81
REMARK 465 PHE C 82
REMARK 465 LYS C 83
REMARK 465 LYS C 84
REMARK 465 ARG C 85
REMARK 465 ASN C 425
REMARK 465 LEU C 426
REMARK 465 GLU C 427
REMARK 465 HIS C 428
REMARK 465 PRO D 38
REMARK 465 GLU D 39
REMARK 465 PHE D 40
REMARK 465 PHE D 41
REMARK 465 SER D 42
REMARK 465 VAL D 43
REMARK 465 ARG D 44
REMARK 465 HIS D 45
REMARK 465 LEU D 46
REMARK 465 GLU D 47
REMARK 465 LEU D 48
REMARK 465 ALA D 49
REMARK 465 GLY D 50
REMARK 465 ASP D 51
REMARK 465 ASP D 52
REMARK 465 PRO D 53
REMARK 465 TYR D 54
REMARK 465 SER D 55
REMARK 465 GLN D 81
REMARK 465 PHE D 82
REMARK 465 LYS D 83
REMARK 465 LYS D 84
REMARK 465 ARG D 85
REMARK 465 ASN D 425
REMARK 465 LEU D 426
REMARK 465 GLU D 427
REMARK 465 HIS D 428
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 HIS A 130 -16.08 -149.99
REMARK 500 LYS A 132 73.30 56.90
REMARK 500 THR A 244 102.36 -162.00
REMARK 500 ASP A 263 62.55 63.60
REMARK 500 SER A 317 60.89 39.48
REMARK 500 GLU A 331 -22.70 88.19
REMARK 500 SER A 379 -5.44 76.83
REMARK 500 ASP A 403 113.06 -162.31
REMARK 500 LEU A 423 19.82 -69.54
REMARK 500 LYS B 108 41.32 70.17
REMARK 500 HIS B 130 -16.37 -150.93
REMARK 500 LYS B 132 74.57 55.00
REMARK 500 GLU B 331 -16.95 86.98
REMARK 500 SER B 379 -4.62 75.24
REMARK 500 LEU C 75 -88.32 -89.01
REMARK 500 HIS C 130 -12.05 -150.14
REMARK 500 LYS C 132 72.76 58.50
REMARK 500 THR C 244 100.87 -160.13
REMARK 500 GLU C 331 -12.82 85.92
REMARK 500 SER C 379 -3.92 74.04
REMARK 500 VAL C 406 -62.01 -94.16
REMARK 500 LYS D 108 40.29 72.98
REMARK 500 HIS D 130 -13.86 -152.62
REMARK 500 LYS D 132 68.45 60.85
REMARK 500 GLU D 331 -9.54 82.79
REMARK 500 SER D 379 -1.84 73.49
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 NA A 586 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 170 O
REMARK 620 2 PHE A 173 O 73.2
REMARK 620 3 VAL A 176 O 86.1 80.6
REMARK 620 4 HOH A 438 O 96.4 169.0 102.6
REMARK 620 5 HOH A 484 O 170.3 97.5 89.8 93.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 587 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 29 O
REMARK 620 2 ALA C 170 O 171.1
REMARK 620 3 PHE C 173 O 109.4 79.6
REMARK 620 4 VAL C 176 O 95.9 84.9 87.0
REMARK 620 N 1 2 3
DBREF 3OTK A 38 428 UNP Q09324 GCNT1_MOUSE 38 428
DBREF 3OTK B 38 428 UNP Q09324 GCNT1_MOUSE 38 428
DBREF 3OTK C 38 428 UNP Q09324 GCNT1_MOUSE 38 428
DBREF 3OTK D 38 428 UNP Q09324 GCNT1_MOUSE 38 428
SEQADV 3OTK SER A 217 UNP Q09324 CYS 217 ENGINEERED MUTATION
SEQADV 3OTK SER B 217 UNP Q09324 CYS 217 ENGINEERED MUTATION
SEQADV 3OTK SER C 217 UNP Q09324 CYS 217 ENGINEERED MUTATION
SEQADV 3OTK SER D 217 UNP Q09324 CYS 217 ENGINEERED MUTATION
SEQRES 1 A 391 PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY
SEQRES 2 A 391 ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU
SEQRES 3 A 391 GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU
SEQRES 4 A 391 ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR
SEQRES 5 A 391 PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER
SEQRES 6 A 391 PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR
SEQRES 7 A 391 LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL
SEQRES 8 A 391 VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG
SEQRES 9 A 391 ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL
SEQRES 10 A 391 ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN
SEQRES 11 A 391 GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER
SEQRES 12 A 391 GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL
SEQRES 13 A 391 LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET
SEQRES 14 A 391 ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET
SEQRES 15 A 391 ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS
SEQRES 16 A 391 LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU
SEQRES 17 A 391 LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG
SEQRES 18 A 391 TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE
SEQRES 19 A 391 VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER
SEQRES 20 A 391 GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY
SEQRES 21 A 391 TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU
SEQRES 22 A 391 TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP
SEQRES 23 A 391 ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE
SEQRES 24 A 391 PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA
SEQRES 25 A 391 ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP
SEQRES 26 A 391 VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL
SEQRES 27 A 391 HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU
SEQRES 28 A 391 SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS
SEQRES 29 A 391 PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU
SEQRES 30 A 391 ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU
SEQRES 31 A 391 HIS
SEQRES 1 B 391 PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY
SEQRES 2 B 391 ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU
SEQRES 3 B 391 GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU
SEQRES 4 B 391 ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR
SEQRES 5 B 391 PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER
SEQRES 6 B 391 PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR
SEQRES 7 B 391 LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL
SEQRES 8 B 391 VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG
SEQRES 9 B 391 ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL
SEQRES 10 B 391 ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN
SEQRES 11 B 391 GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER
SEQRES 12 B 391 GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL
SEQRES 13 B 391 LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET
SEQRES 14 B 391 ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET
SEQRES 15 B 391 ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS
SEQRES 16 B 391 LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU
SEQRES 17 B 391 LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG
SEQRES 18 B 391 TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE
SEQRES 19 B 391 VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER
SEQRES 20 B 391 GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY
SEQRES 21 B 391 TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU
SEQRES 22 B 391 TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP
SEQRES 23 B 391 ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE
SEQRES 24 B 391 PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA
SEQRES 25 B 391 ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP
SEQRES 26 B 391 VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL
SEQRES 27 B 391 HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU
SEQRES 28 B 391 SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS
SEQRES 29 B 391 PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU
SEQRES 30 B 391 ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU
SEQRES 31 B 391 HIS
SEQRES 1 C 391 PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY
SEQRES 2 C 391 ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU
SEQRES 3 C 391 GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU
SEQRES 4 C 391 ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR
SEQRES 5 C 391 PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER
SEQRES 6 C 391 PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR
SEQRES 7 C 391 LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL
SEQRES 8 C 391 VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG
SEQRES 9 C 391 ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL
SEQRES 10 C 391 ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN
SEQRES 11 C 391 GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER
SEQRES 12 C 391 GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL
SEQRES 13 C 391 LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET
SEQRES 14 C 391 ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET
SEQRES 15 C 391 ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS
SEQRES 16 C 391 LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU
SEQRES 17 C 391 LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG
SEQRES 18 C 391 TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE
SEQRES 19 C 391 VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER
SEQRES 20 C 391 GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY
SEQRES 21 C 391 TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU
SEQRES 22 C 391 TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP
SEQRES 23 C 391 ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE
SEQRES 24 C 391 PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA
SEQRES 25 C 391 ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP
SEQRES 26 C 391 VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL
SEQRES 27 C 391 HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU
SEQRES 28 C 391 SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS
SEQRES 29 C 391 PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU
SEQRES 30 C 391 ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU
SEQRES 31 C 391 HIS
SEQRES 1 D 391 PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY
SEQRES 2 D 391 ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU
SEQRES 3 D 391 GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU
SEQRES 4 D 391 ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR
SEQRES 5 D 391 PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER
SEQRES 6 D 391 PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR
SEQRES 7 D 391 LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL
SEQRES 8 D 391 VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG
SEQRES 9 D 391 ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL
SEQRES 10 D 391 ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN
SEQRES 11 D 391 GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER
SEQRES 12 D 391 GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL
SEQRES 13 D 391 LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET
SEQRES 14 D 391 ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET
SEQRES 15 D 391 ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS
SEQRES 16 D 391 LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU
SEQRES 17 D 391 LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG
SEQRES 18 D 391 TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE
SEQRES 19 D 391 VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER
SEQRES 20 D 391 GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY
SEQRES 21 D 391 TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU
SEQRES 22 D 391 TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP
SEQRES 23 D 391 ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE
SEQRES 24 D 391 PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA
SEQRES 25 D 391 ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP
SEQRES 26 D 391 VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL
SEQRES 27 D 391 HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU
SEQRES 28 D 391 SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS
SEQRES 29 D 391 PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU
SEQRES 30 D 391 ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU
SEQRES 31 D 391 HIS
MODRES 3OTK ASN C 95 ASN GLYCOSYLATION SITE
MODRES 3OTK ASN A 95 ASN GLYCOSYLATION SITE
MODRES 3OTK ASN D 58 ASN GLYCOSYLATION SITE
MODRES 3OTK ASN A 58 ASN GLYCOSYLATION SITE
MODRES 3OTK ASN B 58 ASN GLYCOSYLATION SITE
MODRES 3OTK ASN C 58 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET FUC E 3 10
HET NAG F 1 14
HET NAG F 2 14
HET FUC F 3 10
HET HTO A 584 10
HET HTO A 585 10
HET NA A 586 1
HET NAG A 588 14
HET UDP A 598 25
HET NAG B 592 14
HET UDP B 599 25
HET NA C 587 1
HET NAG C 593 14
HET UDP C 600 25
HET NAG D 597 14
HET UDP D 601 25
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM HTO HEPTANE-1,2,3-TRIOL
HETNAM NA SODIUM ION
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 5 NAG 8(C8 H15 N O6)
FORMUL 5 FUC 2(C6 H12 O5)
FORMUL 7 HTO 2(C7 H16 O3)
FORMUL 9 NA 2(NA 1+)
FORMUL 11 UDP 4(C9 H14 N2 O12 P2)
FORMUL 19 HOH *533(H2 O)
HELIX 1 1 ASN A 58 GLY A 65 1 8
HELIX 2 2 ASP A 66 THR A 79 1 14
HELIX 3 3 THR A 79 LYS A 84 1 6
HELIX 4 4 THR A 89 THR A 97 1 9
HELIX 5 5 ASP A 99 LYS A 108 1 10
HELIX 6 6 THR A 115 GLY A 120 1 6
HELIX 7 7 LYS A 132 TYR A 144 1 13
HELIX 8 8 GLU A 159 CYS A 172 1 14
HELIX 9 9 SER A 189 ASN A 207 1 19
HELIX 10 10 THR A 225 THR A 237 1 13
HELIX 11 11 PRO A 248 LYS A 251 5 4
HELIX 12 12 GLU A 252 LYS A 256 1 5
HELIX 13 13 ARG A 293 ASN A 302 1 10
HELIX 14 14 ASN A 302 GLN A 313 1 12
HELIX 15 15 SER A 317 GLU A 320 5 4
HELIX 16 16 PHE A 321 GLN A 327 1 7
HELIX 17 17 SER A 339 ASP A 343 5 5
HELIX 18 18 TRP A 356 GLU A 360 5 5
HELIX 19 19 ASP A 362 GLY A 366 5 5
HELIX 20 20 GLY A 384 GLY A 386 5 3
HELIX 21 21 ASP A 387 LEU A 392 1 6
HELIX 22 22 ASP A 407 LEU A 423 1 17
HELIX 23 23 ASN B 58 GLY B 65 1 8
HELIX 24 24 ASP B 66 THR B 79 1 14
HELIX 25 25 THR B 89 THR B 97 1 9
HELIX 26 26 ASP B 99 LYS B 108 1 10
HELIX 27 27 THR B 115 GLY B 120 1 6
HELIX 28 28 LYS B 132 TYR B 144 1 13
HELIX 29 29 GLU B 159 SER B 171 1 13
HELIX 30 30 SER B 189 ASN B 207 1 19
HELIX 31 31 THR B 225 SER B 236 1 12
HELIX 32 32 GLU B 252 LYS B 256 1 5
HELIX 33 33 ARG B 293 ASN B 302 1 10
HELIX 34 34 ASN B 302 GLN B 313 1 12
HELIX 35 35 SER B 317 GLU B 320 5 4
HELIX 36 36 PHE B 321 GLN B 327 1 7
HELIX 37 37 SER B 339 ASP B 343 5 5
HELIX 38 38 ASP B 362 GLY B 366 5 5
HELIX 39 39 GLY B 384 GLY B 386 5 3
HELIX 40 40 ASP B 387 LEU B 392 1 6
HELIX 41 41 ASP B 407 LEU B 423 1 17
HELIX 42 42 ASN C 58 GLY C 65 1 8
HELIX 43 43 ASP C 66 GLU C 76 1 11
HELIX 44 44 THR C 89 THR C 97 1 9
HELIX 45 45 ASP C 99 LYS C 108 1 10
HELIX 46 46 THR C 115 GLY C 120 1 6
HELIX 47 47 LYS C 132 TYR C 144 1 13
HELIX 48 48 GLU C 159 SER C 171 1 13
HELIX 49 49 SER C 189 ASN C 207 1 19
HELIX 50 50 THR C 225 THR C 237 1 13
HELIX 51 51 PRO C 248 LYS C 251 5 4
HELIX 52 52 GLU C 252 LYS C 256 1 5
HELIX 53 53 ARG C 293 ASN C 302 1 10
HELIX 54 54 ASN C 302 GLN C 313 1 12
HELIX 55 55 SER C 317 GLU C 320 5 4
HELIX 56 56 PHE C 321 GLN C 327 1 7
HELIX 57 57 SER C 339 ASP C 343 5 5
HELIX 58 58 TRP C 356 GLU C 360 5 5
HELIX 59 59 ASP C 362 GLY C 366 5 5
HELIX 60 60 GLY C 384 GLY C 386 5 3
HELIX 61 61 ASP C 387 LEU C 392 1 6
HELIX 62 62 ASP C 407 GLU C 424 1 18
HELIX 63 63 ASN D 58 GLY D 65 1 8
HELIX 64 64 ASP D 66 ILE D 77 1 12
HELIX 65 65 THR D 89 THR D 97 1 9
HELIX 66 66 ASP D 99 LYS D 108 1 10
HELIX 67 67 THR D 115 GLY D 120 1 6
HELIX 68 68 LYS D 132 TYR D 144 1 13
HELIX 69 69 GLU D 159 CYS D 172 1 14
HELIX 70 70 SER D 189 ASN D 207 1 19
HELIX 71 71 THR D 225 SER D 236 1 12
HELIX 72 72 GLU D 252 LYS D 256 1 5
HELIX 73 73 ARG D 293 ASN D 302 1 10
HELIX 74 74 ASN D 302 GLN D 313 1 12
HELIX 75 75 SER D 317 GLU D 320 5 4
HELIX 76 76 PHE D 321 GLN D 327 1 7
HELIX 77 77 SER D 339 ASP D 343 5 5
HELIX 78 78 ASP D 362 GLY D 366 5 5
HELIX 79 79 GLY D 384 GLY D 386 5 3
HELIX 80 80 ASP D 387 ARG D 393 1 7
HELIX 81 81 ASP D 407 GLU D 424 1 18
SHEET 1 A 5 VAL A 176 VAL A 178 0
SHEET 2 A 5 PHE A 149 VAL A 154 1 N ILE A 152 O PHE A 177
SHEET 3 A 5 ILE A 123 VAL A 129 1 N ILE A 127 O HIS A 153
SHEET 4 A 5 TYR A 212 SER A 217 1 O LEU A 216 N SER A 126
SHEET 5 A 5 VAL A 290 THR A 292 -1 O VAL A 291 N LEU A 213
SHEET 1 B 3 ASP A 220 PRO A 222 0
SHEET 2 B 3 PHE A 398 ASN A 400 -1 O ALA A 399 N PHE A 221
SHEET 3 B 3 ARG A 352 PHE A 353 1 N PHE A 353 O PHE A 398
SHEET 1 C 2 GLU A 245 LYS A 246 0
SHEET 2 C 2 PHE A 283 SER A 284 -1 O SER A 284 N GLU A 245
SHEET 1 D 2 LYS A 257 VAL A 261 0
SHEET 2 D 2 LEU A 266 VAL A 272 -1 O THR A 267 N ALA A 260
SHEET 1 E 2 VAL A 375 VAL A 377 0
SHEET 2 E 2 VAL A 380 VAL A 382 -1 O VAL A 382 N VAL A 375
SHEET 1 F 5 VAL B 176 VAL B 178 0
SHEET 2 F 5 PHE B 149 VAL B 154 1 N ILE B 152 O PHE B 177
SHEET 3 F 5 ILE B 123 VAL B 129 1 N TYR B 125 O PHE B 149
SHEET 4 F 5 TYR B 212 SER B 217 1 O LEU B 216 N SER B 126
SHEET 5 F 5 VAL B 290 THR B 292 -1 O VAL B 291 N LEU B 213
SHEET 1 G 3 ASP B 220 PRO B 222 0
SHEET 2 G 3 PHE B 398 ASN B 400 -1 O ALA B 399 N PHE B 221
SHEET 3 G 3 ARG B 352 PHE B 353 1 N PHE B 353 O PHE B 398
SHEET 1 H 2 GLU B 245 LYS B 246 0
SHEET 2 H 2 PHE B 283 SER B 284 -1 O SER B 284 N GLU B 245
SHEET 1 I 2 LYS B 257 VAL B 262 0
SHEET 2 I 2 LYS B 265 VAL B 272 -1 O LYS B 265 N VAL B 262
SHEET 1 J 2 VAL B 375 VAL B 377 0
SHEET 2 J 2 VAL B 380 VAL B 382 -1 O VAL B 382 N VAL B 375
SHEET 1 K 5 VAL C 176 VAL C 178 0
SHEET 2 K 5 PHE C 149 VAL C 154 1 N ILE C 152 O PHE C 177
SHEET 3 K 5 ILE C 123 VAL C 129 1 N ILE C 127 O HIS C 153
SHEET 4 K 5 TYR C 212 SER C 217 1 O LEU C 216 N SER C 126
SHEET 5 K 5 VAL C 290 THR C 292 -1 O VAL C 291 N LEU C 213
SHEET 1 L 3 ASP C 220 PRO C 222 0
SHEET 2 L 3 PHE C 398 ASN C 400 -1 O ALA C 399 N PHE C 221
SHEET 3 L 3 ARG C 352 PHE C 353 1 N PHE C 353 O PHE C 398
SHEET 1 M 2 GLU C 245 LYS C 246 0
SHEET 2 M 2 PHE C 283 SER C 284 -1 O SER C 284 N GLU C 245
SHEET 1 N 2 LYS C 257 VAL C 261 0
SHEET 2 N 2 LEU C 266 VAL C 272 -1 O THR C 267 N ALA C 260
SHEET 1 O 2 VAL C 375 VAL C 377 0
SHEET 2 O 2 VAL C 380 VAL C 382 -1 O VAL C 382 N VAL C 375
SHEET 1 P 5 VAL D 176 VAL D 178 0
SHEET 2 P 5 PHE D 149 VAL D 154 1 N ILE D 152 O PHE D 177
SHEET 3 P 5 ILE D 123 VAL D 129 1 N ILE D 127 O CYS D 151
SHEET 4 P 5 TYR D 212 SER D 217 1 O LEU D 216 N SER D 126
SHEET 5 P 5 VAL D 290 THR D 292 -1 O VAL D 291 N LEU D 213
SHEET 1 Q 3 ASP D 220 PRO D 222 0
SHEET 2 Q 3 PHE D 398 ASN D 400 -1 O ALA D 399 N PHE D 221
SHEET 3 Q 3 ARG D 352 PHE D 353 1 N PHE D 353 O PHE D 398
SHEET 1 R 2 THR D 244 LYS D 246 0
SHEET 2 R 2 PHE D 283 GLY D 285 -1 O SER D 284 N GLU D 245
SHEET 1 S 2 LYS D 257 VAL D 261 0
SHEET 2 S 2 LEU D 266 VAL D 272 -1 O ILE D 271 N ARG D 258
SHEET 1 T 2 VAL D 375 VAL D 377 0
SHEET 2 T 2 VAL D 380 VAL D 382 -1 O VAL D 382 N VAL D 375
SSBOND 1 CYS A 59 CYS A 413 1555 1555 2.07
SSBOND 2 CYS A 100 CYS A 172 1555 1555 2.11
SSBOND 3 CYS A 151 CYS A 199 1555 1555 2.14
SSBOND 4 CYS A 235 CYS B 235 1555 1555 2.03
SSBOND 5 CYS A 372 CYS A 381 1555 1555 2.09
SSBOND 6 CYS B 100 CYS B 172 1555 1555 2.07
SSBOND 7 CYS B 151 CYS B 199 1555 1555 2.12
SSBOND 8 CYS B 372 CYS B 381 1555 1555 2.08
SSBOND 9 CYS C 59 CYS C 413 1555 1555 2.07
SSBOND 10 CYS C 100 CYS C 172 1555 1555 2.10
SSBOND 11 CYS C 151 CYS C 199 1555 1555 2.14
SSBOND 12 CYS C 235 CYS D 235 1555 1555 2.02
SSBOND 13 CYS C 372 CYS C 381 1555 1555 2.06
SSBOND 14 CYS D 100 CYS D 172 1555 1555 2.08
SSBOND 15 CYS D 151 CYS D 199 1555 1555 2.12
SSBOND 16 CYS D 372 CYS D 381 1555 1555 2.11
LINK ND2 ASN A 58 C1 NAG A 588 1555 1555 1.45
LINK ND2 ASN A 95 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 58 C1 NAG B 592 1555 1555 1.45
LINK ND2 ASN C 58 C1 NAG C 593 1555 1555 1.45
LINK ND2 ASN C 95 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN D 58 C1 NAG D 597 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O6 NAG E 1 C1 FUC E 3 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O6 NAG F 1 C1 FUC F 3 1555 1555 1.45
LINK O ALA A 170 NA NA A 586 1555 1555 2.42
LINK O PHE A 173 NA NA A 586 1555 1555 2.44
LINK O VAL A 176 NA NA A 586 1555 1555 2.41
LINK O HOH A 438 NA NA A 586 1555 1555 2.40
LINK O HOH A 484 NA NA A 586 1555 1555 2.32
LINK O HOH C 29 NA NA C 587 1555 1555 2.21
LINK O ALA C 170 NA NA C 587 1555 1555 2.41
LINK O PHE C 173 NA NA C 587 1555 1555 2.44
LINK O VAL C 176 NA NA C 587 1555 1555 2.42
CISPEP 1 ASN A 400 LYS A 401 0 4.80
CISPEP 2 ASN B 400 LYS B 401 0 -1.10
CISPEP 3 ASN C 400 LYS C 401 0 5.25
CISPEP 4 ASN D 400 LYS D 401 0 -1.58
CRYST1 73.874 101.020 136.612 90.00 93.42 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 0.013537 0.000000 0.000808 0.00000
SCALE2 0.000000 0.009899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007333 0.00000
(ATOM LINES ARE NOT SHOWN.)
END