HEADER TRANSFERASE 25-NOV-05 2D7R
TITLE CRYSTAL STRUCTURE OF PP-GALNAC-T10 COMPLEXED WITH GALNAC-SER ON LECTIN
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 10;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 40-603;
COMPND 5 SYNONYM: PROTEIN-UDP ACETYLGALACTOSAMINYLTRANSFERASE 10, UDP-
COMPND 6 GALNAC:POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 10, POLYPEPTIDE
COMPND 7 GALNAC TRANSFERASE 10, GALNAC-T10, PP-GANTASE 10;
COMPND 8 EC: 2.4.1.41;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SMD1168;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS BETA TREFOIL, ROSSMANN FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KUBOTA,T.SHIBA,S.SUGIOKA,R.KATO,S.WAKATSUKI,H.NARIMATSU
REVDAT 6 25-OCT-23 2D7R 1 HETSYN
REVDAT 5 29-JUL-20 2D7R 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 01-JUL-20 2D7R 1 COMPND REMARK SEQADV HET
REVDAT 4 2 1 HETNAM FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 13-JUL-11 2D7R 1 VERSN
REVDAT 2 24-FEB-09 2D7R 1 VERSN
REVDAT 1 07-NOV-06 2D7R 0
JRNL AUTH T.KUBOTA,T.SHIBA,S.SUGIOKA,S.FURUKAWA,H.SAWAKI,R.KATO,
JRNL AUTH 2 S.WAKATSUKI,H.NARIMATSU
JRNL TITL STRUCTURAL BASIS OF CARBOHYDRATE TRANSFER ACTIVITY BY HUMAN
JRNL TITL 2 UDP-GALNAC: POLYPEPTIDE
JRNL TITL 3 ALPHA-N-ACETYLGALACTOSAMINYLTRANSFERASE (PP-GALNAC-T10)
JRNL REF J.MOL.BIOL. V. 359 708 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16650853
JRNL DOI 10.1016/J.JMB.2006.03.061
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 18437
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1814
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4357
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 118
REMARK 3 SOLVENT ATOMS : 74
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.301
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D7R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000025092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : 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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18964
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ID: 2D7I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 3350, 0.05M SODIUM THIOCYANATE,
REMARK 280 0.1M TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 69.47650
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 69.47650
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 40.09750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.40600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.09750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.40600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.47650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.09750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.40600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.47650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.09750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.40600
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 834 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 848 LIES ON A SPECIAL POSITION.
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 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 HIS A 38
REMARK 465 HIS A 39
REMARK 465 PRO A 40
REMARK 465 GLY A 41
REMARK 465 GLY A 42
REMARK 465 SER A 43
REMARK 465 GLY A 44
REMARK 465 ALA A 45
REMARK 465 ALA A 46
REMARK 465 VAL A 47
REMARK 465 ALA A 48
REMARK 465 PRO A 49
REMARK 465 ALA A 50
REMARK 465 ALA A 51
REMARK 465 GLY A 52
REMARK 465 GLN A 53
REMARK 465 GLY A 54
REMARK 465 SER A 55
REMARK 465 HIS A 56
REMARK 465 SER A 57
REMARK 465 ARG A 58
REMARK 465 GLN A 59
REMARK 465 LYS A 60
REMARK 465 LYS A 61
REMARK 465 THR A 62
REMARK 465 PHE A 63
REMARK 465 PHE A 64
REMARK 465 LEU A 65
REMARK 465 GLY A 66
REMARK 465 ASP A 67
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 GLN A 69 47.64 -147.45
REMARK 500 LEU A 71 -165.18 -77.89
REMARK 500 LYS A 72 143.66 179.38
REMARK 500 GLU A 91 151.98 -49.81
REMARK 500 GLN A 92 16.79 57.65
REMARK 500 PRO A 97 81.91 -63.30
REMARK 500 ARG A 109 -33.91 -36.94
REMARK 500 ASN A 114 92.37 -55.61
REMARK 500 ILE A 130 32.59 -86.61
REMARK 500 ARG A 131 -161.22 -72.13
REMARK 500 PRO A 174 -39.02 -39.68
REMARK 500 LYS A 193 -111.67 -107.09
REMARK 500 HIS A 271 7.70 -64.43
REMARK 500 ASP A 272 -67.92 -124.62
REMARK 500 ASP A 282 -131.44 43.16
REMARK 500 ALA A 287 -160.07 -169.05
REMARK 500 PRO A 308 2.02 -59.86
REMARK 500 GLU A 340 -120.83 -79.08
REMARK 500 PRO A 381 152.06 -49.12
REMARK 500 ASP A 399 -126.26 47.12
REMARK 500 HIS A 414 51.97 -90.11
REMARK 500 ALA A 417 31.41 -91.24
REMARK 500 LYS A 475 35.63 -67.92
REMARK 500 ARG A 484 -162.91 -67.86
REMARK 500 ASN A 498 72.07 40.59
REMARK 500 LYS A 521 37.78 -72.27
REMARK 500 ILE A 527 -99.75 -84.57
REMARK 500 HIS A 529 30.93 -78.48
REMARK 500 THR A 530 -24.54 -151.52
REMARK 500 PRO A 532 -158.41 -69.97
REMARK 500 HIS A 539 128.93 166.91
REMARK 500 SER A 540 57.95 -69.74
REMARK 500 LYS A 542 83.98 -46.26
REMARK 500 LEU A 555 70.03 -117.08
REMARK 500 HIS A 571 -158.08 -129.37
REMARK 500 ARG A 572 -165.16 -77.58
REMARK 500 ASN A 579 84.61 -150.25
REMARK 500 SER A 582 -154.06 -143.19
REMARK 500 LEU A 583 -37.65 -151.85
REMARK 500 LYS A 599 -99.02 -78.20
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 706 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 237 OD2
REMARK 620 2 HIS A 239 NE2 101.8
REMARK 620 3 HIS A 370 NE2 88.0 93.5
REMARK 620 4 UDP A 707 O1A 94.8 84.5 176.8
REMARK 620 5 UDP A 707 O3B 92.4 163.1 96.1 85.2
REMARK 620 6 HOH A 816 O 177.2 75.7 90.8 86.3 90.3
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2D7I RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT GALNAC-SER
DBREF 2D7R A 40 603 UNP Q86SR1 GLT10_HUMAN 40 603
SEQADV 2D7R HIS A 34 UNP Q86SR1 EXPRESSION TAG
SEQADV 2D7R HIS A 35 UNP Q86SR1 EXPRESSION TAG
SEQADV 2D7R HIS A 36 UNP Q86SR1 EXPRESSION TAG
SEQADV 2D7R HIS A 37 UNP Q86SR1 EXPRESSION TAG
SEQADV 2D7R HIS A 38 UNP Q86SR1 EXPRESSION TAG
SEQADV 2D7R HIS A 39 UNP Q86SR1 EXPRESSION TAG
SEQRES 1 A 570 HIS HIS HIS HIS HIS HIS PRO GLY GLY SER GLY ALA ALA
SEQRES 2 A 570 VAL ALA PRO ALA ALA GLY GLN GLY SER HIS SER ARG GLN
SEQRES 3 A 570 LYS LYS THR PHE PHE LEU GLY ASP GLY GLN LYS LEU LYS
SEQRES 4 A 570 ASP TRP HIS ASP LYS GLU ALA ILE ARG ARG ASP ALA GLN
SEQRES 5 A 570 ARG VAL GLY ASN GLY GLU GLN GLY ARG PRO TYR PRO MET
SEQRES 6 A 570 THR ASP ALA GLU ARG VAL ASP GLN ALA TYR ARG GLU ASN
SEQRES 7 A 570 GLY PHE ASN ILE TYR VAL SER ASP LYS ILE SER LEU ASN
SEQRES 8 A 570 ARG SER LEU PRO ASP ILE ARG HIS PRO ASN CYS ASN SER
SEQRES 9 A 570 LYS ARG TYR LEU GLU THR LEU PRO ASN THR SER ILE ILE
SEQRES 10 A 570 ILE PRO PHE HIS ASN GLU GLY TRP SER SER LEU LEU ARG
SEQRES 11 A 570 THR VAL HIS SER VAL LEU ASN ARG SER PRO PRO GLU LEU
SEQRES 12 A 570 VAL ALA GLU ILE VAL LEU VAL ASP ASP PHE SER ASP ARG
SEQRES 13 A 570 GLU HIS LEU LYS LYS PRO LEU GLU ASP TYR MET ALA LEU
SEQRES 14 A 570 PHE PRO SER VAL ARG ILE LEU ARG THR LYS LYS ARG GLU
SEQRES 15 A 570 GLY LEU ILE ARG THR ARG MET LEU GLY ALA SER VAL ALA
SEQRES 16 A 570 THR GLY ASP VAL ILE THR PHE LEU ASP SER HIS CYS GLU
SEQRES 17 A 570 ALA ASN VAL ASN TRP LEU PRO PRO LEU LEU ASP ARG ILE
SEQRES 18 A 570 ALA ARG ASN ARG LYS THR ILE VAL CYS PRO MET ILE ASP
SEQRES 19 A 570 VAL ILE ASP HIS ASP ASP PHE ARG TYR GLU THR GLN ALA
SEQRES 20 A 570 GLY ASP ALA MET ARG GLY ALA PHE ASP TRP GLU MET TYR
SEQRES 21 A 570 TYR LYS ARG ILE PRO ILE PRO PRO GLU LEU GLN LYS ALA
SEQRES 22 A 570 ASP PRO SER ASP PRO PHE GLU SER PRO VAL MET ALA GLY
SEQRES 23 A 570 GLY LEU PHE ALA VAL ASP ARG LYS TRP PHE TRP GLU LEU
SEQRES 24 A 570 GLY GLY TYR ASP PRO GLY LEU GLU ILE TRP GLY GLY GLU
SEQRES 25 A 570 GLN TYR GLU ILE SER PHE LYS VAL TRP MET CYS GLY GLY
SEQRES 26 A 570 ARG MET GLU ASP ILE PRO CYS SER ARG VAL GLY HIS ILE
SEQRES 27 A 570 TYR ARG LYS TYR VAL PRO TYR LYS VAL PRO ALA GLY VAL
SEQRES 28 A 570 SER LEU ALA ARG ASN LEU LYS ARG VAL ALA GLU VAL TRP
SEQRES 29 A 570 MET ASP GLU TYR ALA GLU TYR ILE TYR GLN ARG ARG PRO
SEQRES 30 A 570 GLU TYR ARG HIS LEU SER ALA GLY ASP VAL ALA VAL GLN
SEQRES 31 A 570 LYS LYS LEU ARG SER SER LEU ASN CYS LYS SER PHE LYS
SEQRES 32 A 570 TRP PHE MET THR LYS ILE ALA TRP ASP LEU PRO LYS PHE
SEQRES 33 A 570 TYR PRO PRO VAL GLU PRO PRO ALA ALA ALA TRP GLY GLU
SEQRES 34 A 570 ILE ARG ASN VAL GLY THR GLY LEU CYS ALA ASP THR LYS
SEQRES 35 A 570 HIS GLY ALA LEU GLY SER PRO LEU ARG LEU GLU GLY CYS
SEQRES 36 A 570 VAL ARG GLY ARG GLY GLU ALA ALA TRP ASN ASN MET GLN
SEQRES 37 A 570 VAL PHE THR PHE THR TRP ARG GLU ASP ILE ARG PRO GLY
SEQRES 38 A 570 ASP PRO GLN HIS THR LYS LYS PHE CYS PHE ASP ALA ILE
SEQRES 39 A 570 SER HIS THR SER PRO VAL THR LEU TYR ASP CYS HIS SER
SEQRES 40 A 570 MET LYS GLY ASN GLN LEU TRP LYS TYR ARG LYS ASP LYS
SEQRES 41 A 570 THR LEU TYR HIS PRO VAL SER GLY SER CYS MET ASP CYS
SEQRES 42 A 570 SER GLU SER ASP HIS ARG ILE PHE MET ASN THR CYS ASN
SEQRES 43 A 570 PRO SER SER LEU THR GLN GLN TRP LEU PHE GLU HIS THR
SEQRES 44 A 570 ASN SER THR VAL LEU GLU LYS PHE ASN ARG ASN
MODRES 2D7R ASN A 124 ASN GLYCOSYLATION SITE
MODRES 2D7R ASN A 146 ASN GLYCOSYLATION SITE
MODRES 2D7R ASN A 593 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG A 703 14
HET NGA A 704 15
HET NAG A 705 14
HET MN A 706 1
HET UDP A 707 25
HET SER A 708 7
HET A2G A 709 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NGA 2-ACETAMIDO-2-DEOXY-BETA-D-GALACTOPYRANOSE
HETNAM MN MANGANESE (II) ION
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM SER SERINE
HETNAM A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE
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 NGA N-ACETYL-BETA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 NGA BETA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2-
HETSYN 3 NGA ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-D-GALACTOSAMINE
HETSYN A2G N-ACETYL-ALPHA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 A2G ALPHA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2-
HETSYN 3 A2G ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-2-DEOXY-2-AMINO-
HETSYN 4 A2G GALACTOSE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 4 NGA C8 H15 N O6
FORMUL 6 MN MN 2+
FORMUL 7 UDP C9 H14 N2 O12 P2
FORMUL 8 SER C3 H7 N O3
FORMUL 9 A2G C8 H15 N O6
FORMUL 10 HOH *74(H2 O)
HELIX 1 1 ASP A 76 GLN A 85 1 10
HELIX 2 2 GLY A 90 ARG A 94 5 5
HELIX 3 3 VAL A 104 TYR A 108 5 5
HELIX 4 4 ASN A 114 LYS A 120 1 7
HELIX 5 5 ASN A 134 LYS A 138 5 5
HELIX 6 6 GLY A 157 SER A 172 1 16
HELIX 7 7 PRO A 173 GLU A 175 5 3
HELIX 8 8 ARG A 189 LEU A 192 5 4
HELIX 9 9 LYS A 193 LEU A 202 1 10
HELIX 10 10 GLY A 216 ALA A 228 1 13
HELIX 11 11 LEU A 247 ASN A 257 1 11
HELIX 12 12 ARG A 326 LEU A 332 1 7
HELIX 13 13 GLY A 344 CYS A 356 1 13
HELIX 14 14 SER A 385 MET A 398 1 14
HELIX 15 15 ASP A 399 TYR A 401 5 3
HELIX 16 16 ALA A 402 GLN A 407 1 6
HELIX 17 17 ARG A 409 ARG A 413 5 5
HELIX 18 18 VAL A 420 SER A 429 1 10
HELIX 19 19 SER A 434 ILE A 442 1 9
HELIX 20 20 ASP A 445 TYR A 450 1 6
HELIX 21 21 ASN A 593 GLU A 598 1 6
SHEET 1 A 5 VAL A 206 ARG A 210 0
SHEET 2 A 5 VAL A 177 ASP A 184 1 N LEU A 182 O ARG A 207
SHEET 3 A 5 THR A 147 PHE A 153 1 N ILE A 151 O VAL A 183
SHEET 4 A 5 VAL A 232 PHE A 235 1 O THR A 234 N ILE A 150
SHEET 5 A 5 PHE A 322 ASP A 325 -1 O VAL A 324 N ILE A 233
SHEET 1 B 4 CYS A 240 ALA A 242 0
SHEET 2 B 4 ARG A 359 HIS A 370 -1 O GLY A 369 N GLU A 241
SHEET 3 B 4 THR A 260 ILE A 269 1 N ILE A 261 O ARG A 359
SHEET 4 B 4 TYR A 276 GLU A 277 -1 O GLU A 277 N VAL A 268
SHEET 1 C 3 CYS A 240 ALA A 242 0
SHEET 2 C 3 ARG A 359 HIS A 370 -1 O GLY A 369 N GLU A 241
SHEET 3 C 3 PHE A 312 GLU A 313 -1 N PHE A 312 O ASP A 362
SHEET 1 D 2 ARG A 285 PHE A 288 0
SHEET 2 D 2 TYR A 294 ILE A 297 -1 O LYS A 295 N ALA A 287
SHEET 1 E 4 ASP A 510 PRO A 513 0
SHEET 2 E 4 PHE A 503 THR A 506 -1 N THR A 504 O ARG A 512
SHEET 3 E 4 ALA A 459 GLY A 461 -1 N ALA A 459 O PHE A 505
SHEET 4 E 4 HIS A 591 THR A 592 -1 O HIS A 591 N TRP A 460
SHEET 1 F 2 ARG A 464 ASN A 465 0
SHEET 2 F 2 TRP A 587 LEU A 588 -1 O LEU A 588 N ARG A 464
SHEET 1 G 2 CYS A 471 ALA A 472 0
SHEET 2 G 2 LEU A 485 GLU A 486 -1 O GLU A 486 N CYS A 471
SHEET 1 H 2 PHE A 522 ASP A 525 0
SHEET 2 H 2 THR A 534 ASP A 537 -1 O THR A 534 N ASP A 525
SHEET 1 I 2 LYS A 548 ARG A 550 0
SHEET 2 I 2 THR A 554 TYR A 556 -1 O THR A 554 N ARG A 550
SHEET 1 J 2 CYS A 563 CYS A 566 0
SHEET 2 J 2 ILE A 573 ASN A 576 -1 O PHE A 574 N ASP A 565
SSBOND 1 CYS A 135 CYS A 365 1555 1555 2.05
SSBOND 2 CYS A 356 CYS A 432 1555 1555 2.04
SSBOND 3 CYS A 471 CYS A 488 1555 1555 2.04
SSBOND 4 CYS A 523 CYS A 538 1555 1555 2.03
SSBOND 5 CYS A 563 CYS A 578 1555 1555 2.04
LINK ND2 ASN A 124 C1 NAG B 1 1555 1555 1.46
LINK ND2 ASN A 146 C1 NAG A 705 1555 1555 1.46
LINK ND2 ASN A 593 C1 NAG A 703 1555 1555 1.45
LINK OG SER A 708 C1 A2G A 709 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.40
LINK OD2 ASP A 237 MN MN A 706 1555 1555 2.14
LINK NE2 HIS A 239 MN MN A 706 1555 1555 2.30
LINK NE2 HIS A 370 MN MN A 706 1555 1555 2.27
LINK MN MN A 706 O1A UDP A 707 1555 1555 2.28
LINK MN MN A 706 O3B UDP A 707 1555 1555 2.20
LINK MN MN A 706 O HOH A 816 1555 1555 2.12
CRYST1 80.195 132.812 138.953 90.00 90.00 90.00 C 2 2 21 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 0.012470 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
