HEADER TRANSFERASE 15-JAN-13 4IRP
TITLE CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN BETA1,4-
TITLE 2 GALACTOSYLTRANSFERASE-7 IN OPEN CONFORMATION WITH MANGANSES AND UDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-1,4-GALACTOSYLTRANSFERASE 7;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-1,4-GALTASE 7, BETA4GAL-T7, B4GAL-T7, UDP-GAL:BETA-
COMPND 5 GLCNAC BETA-1,4-GALACTOSYLTRANSFERASE 7, UDP-GALACTOSE:BETA-N-
COMPND 6 ACETYLGLUCOSAMINE BETA-1,4-GALACTOSYLTRANSFERASE 7, XYLOSYLPROTEIN 4-
COMPND 7 BETA-GALACTOSYLTRANSFERASE, PROTEOGLYCAN UDP-GALACTOSE:BETA-XYLOSE
COMPND 8 BETA1,4-GALACTOSYLTRANSFERASE I, UDP-GALACTOSE:BETA-XYLOSE BETA-1,4-
COMPND 9 GALACTOSYLTRANSFERASE, XGPT, XGALT-1, XYLOSYLPROTEIN BETA-1,4-
COMPND 10 GALACTOSYLTRANSFERASE;
COMPND 11 EC: 2.4.1.-, 2.4.1.133;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: 4GALACTOSYLTRANSFERASE, B4GALT7, BETA1, UNQ748/PRO1478,
SOURCE 6 XGALT1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS GT-A FOLD, OPEN CONFORMATION, MANGANESE AND UDP COMPLEX,
KEYWDS 2 GLYCOSYLTRANSFERASE, GOLGI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TSUTSUI,B.RAMAKRISHNAN,P.K.QASBA
REVDAT 3 20-SEP-23 4IRP 1 REMARK SEQADV LINK
REVDAT 2 27-NOV-13 4IRP 1 JRNL
REVDAT 1 25-SEP-13 4IRP 0
JRNL AUTH Y.TSUTSUI,B.RAMAKRISHNAN,P.K.QASBA
JRNL TITL CRYSTAL STRUCTURES OF BETA-1,4-GALACTOSYLTRANSFERASE 7
JRNL TITL 2 ENZYME REVEAL CONFORMATIONAL CHANGES AND SUBSTRATE BINDING.
JRNL REF J.BIOL.CHEM. V. 288 31963 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 24052259
JRNL DOI 10.1074/JBC.M113.509984
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.550
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 40726
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2081
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.2697 - 5.1766 0.98 2761 125 0.2825 0.3358
REMARK 3 2 5.1766 - 4.1097 0.99 2645 139 0.1981 0.2630
REMARK 3 3 4.1097 - 3.5905 0.99 2598 142 0.1940 0.2304
REMARK 3 4 3.5905 - 3.2623 0.99 2592 141 0.2027 0.2580
REMARK 3 5 3.2623 - 3.0286 0.99 2596 123 0.2162 0.2598
REMARK 3 6 3.0286 - 2.8500 1.00 2538 161 0.2232 0.2773
REMARK 3 7 2.8500 - 2.7073 0.99 2579 133 0.2111 0.2637
REMARK 3 8 2.7073 - 2.5895 1.00 2562 125 0.2201 0.2706
REMARK 3 9 2.5895 - 2.4898 1.00 2566 143 0.2175 0.3300
REMARK 3 10 2.4898 - 2.4039 1.00 2550 132 0.2080 0.2674
REMARK 3 11 2.4039 - 2.3287 0.99 2556 128 0.2087 0.2842
REMARK 3 12 2.3287 - 2.2622 0.99 2532 145 0.2102 0.3076
REMARK 3 13 2.2622 - 2.2026 0.99 2539 137 0.2103 0.2814
REMARK 3 14 2.2026 - 2.1489 0.99 2526 145 0.2300 0.2810
REMARK 3 15 2.1489 - 2.1000 0.99 2505 162 0.2383 0.3053
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.550
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.022 4144
REMARK 3 ANGLE : 1.930 5647
REMARK 3 CHIRALITY : 0.139 577
REMARK 3 PLANARITY : 0.010 730
REMARK 3 DIHEDRAL : 15.388 1541
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IRP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000077124.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-12
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
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 : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 11.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3LW6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 TO 1.0 M SODIUM ACCETATE, 100 MM
REMARK 280 IMIDAZOLE.HCL PH 6.5 AS PRECIPATING AGENT, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 43.66300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.59300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.59300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.83150
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.59300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.59300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.49450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.59300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.59300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 21.83150
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.59300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.59300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.49450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 43.66300
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 260
REMARK 465 PRO A 261
REMARK 465 ALA A 262
REMARK 465 TRP A 263
REMARK 465 ARG A 264
REMARK 465 LYS A 265
REMARK 465 ARG A 266
REMARK 465 ASP A 267
REMARK 465 GLN A 268
REMARK 465 LYS A 269
REMARK 465 ARG A 270
REMARK 465 ILE A 271
REMARK 465 ALA A 272
REMARK 465 ALA A 273
REMARK 465 GLN A 274
REMARK 465 LYS A 275
REMARK 465 GLN A 276
REMARK 465 GLU A 277
REMARK 465 GLN A 278
REMARK 465 HIS B 259
REMARK 465 ASP B 260
REMARK 465 PRO B 261
REMARK 465 ALA B 262
REMARK 465 TRP B 263
REMARK 465 ARG B 264
REMARK 465 LYS B 265
REMARK 465 ARG B 266
REMARK 465 ASP B 267
REMARK 465 GLN B 268
REMARK 465 LYS B 269
REMARK 465 ARG B 270
REMARK 465 ILE B 271
REMARK 465 ALA B 272
REMARK 465 ALA B 273
REMARK 465 GLN B 274
REMARK 465 LYS B 275
REMARK 465 GLN B 276
REMARK 465 GLU B 277
REMARK 465 GLN B 278
REMARK 465 PHE B 279
REMARK 465 LYS B 280
REMARK 465 VAL B 281
REMARK 465 ASP B 282
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 92 C - N - CA ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG B 116 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 116 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP B 174 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 193 -71.09 -127.86
REMARK 500 HIS A 195 19.90 -141.23
REMARK 500 GLU B 103 62.40 37.75
REMARK 500 ASN B 140 79.40 -117.46
REMARK 500 ALA B 186 55.19 -90.98
REMARK 500 LEU B 193 -63.15 -129.89
REMARK 500 TRP B 323 0.60 -65.16
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 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 257 NE2
REMARK 620 2 UDP A 401 O1A 163.5
REMARK 620 3 HOH A 653 O 111.6 83.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 165 OD2
REMARK 620 2 HIS B 257 NE2 100.7
REMARK 620 3 UDP B 401 O1B 139.5 118.9
REMARK 620 4 UDP B 401 O1A 68.6 167.2 71.0
REMARK 620 5 HOH B 636 O 96.4 106.5 81.0 82.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IRQ RELATED DB: PDB
DBREF 4IRP A 81 327 UNP Q9UBV7 B4GT7_HUMAN 81 327
DBREF 4IRP B 81 327 UNP Q9UBV7 B4GT7_HUMAN 81 327
SEQADV 4IRP GLY A 77 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP SER A 78 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP ASP A 79 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP ILE A 80 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP GLY B 77 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP SER B 78 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP ASP B 79 UNP Q9UBV7 EXPRESSION TAG
SEQADV 4IRP ILE B 80 UNP Q9UBV7 EXPRESSION TAG
SEQRES 1 A 251 GLY SER ASP ILE PRO GLU HIS TRP GLU GLU ASP ALA SER
SEQRES 2 A 251 TRP GLY PRO HIS ARG LEU ALA VAL LEU VAL PRO PHE ARG
SEQRES 3 A 251 GLU ARG PHE GLU GLU LEU LEU VAL PHE VAL PRO HIS MET
SEQRES 4 A 251 ARG ARG PHE LEU SER ARG LYS LYS ILE ARG HIS HIS ILE
SEQRES 5 A 251 TYR VAL LEU ASN GLN VAL ASP HIS PHE ARG PHE ASN ARG
SEQRES 6 A 251 ALA ALA LEU ILE ASN VAL GLY PHE LEU GLU SER SER ASN
SEQRES 7 A 251 SER THR ASP TYR ILE ALA MET HIS ASP VAL ASP LEU LEU
SEQRES 8 A 251 PRO LEU ASN GLU GLU LEU ASP TYR GLY PHE PRO GLU ALA
SEQRES 9 A 251 GLY PRO PHE HIS VAL ALA SER PRO GLU LEU HIS PRO LEU
SEQRES 10 A 251 TYR HIS TYR LYS THR TYR VAL GLY GLY ILE LEU LEU LEU
SEQRES 11 A 251 SER LYS GLN HIS TYR ARG LEU CYS ASN GLY MET SER ASN
SEQRES 12 A 251 ARG PHE TRP GLY TRP GLY ARG GLU ASP ASP GLU PHE TYR
SEQRES 13 A 251 ARG ARG ILE LYS GLY ALA GLY LEU GLN LEU PHE ARG PRO
SEQRES 14 A 251 SER GLY ILE THR THR GLY TYR LYS THR PHE ARG HIS LEU
SEQRES 15 A 251 HIS ASP PRO ALA TRP ARG LYS ARG ASP GLN LYS ARG ILE
SEQRES 16 A 251 ALA ALA GLN LYS GLN GLU GLN PHE LYS VAL ASP ARG GLU
SEQRES 17 A 251 GLY GLY LEU ASN THR VAL LYS TYR HIS VAL ALA SER ARG
SEQRES 18 A 251 THR ALA LEU SER VAL GLY GLY ALA PRO CYS THR VAL LEU
SEQRES 19 A 251 ASN ILE MET LEU ASP CYS ASP LYS THR ALA THR PRO TRP
SEQRES 20 A 251 CYS THR PHE SER
SEQRES 1 B 251 GLY SER ASP ILE PRO GLU HIS TRP GLU GLU ASP ALA SER
SEQRES 2 B 251 TRP GLY PRO HIS ARG LEU ALA VAL LEU VAL PRO PHE ARG
SEQRES 3 B 251 GLU ARG PHE GLU GLU LEU LEU VAL PHE VAL PRO HIS MET
SEQRES 4 B 251 ARG ARG PHE LEU SER ARG LYS LYS ILE ARG HIS HIS ILE
SEQRES 5 B 251 TYR VAL LEU ASN GLN VAL ASP HIS PHE ARG PHE ASN ARG
SEQRES 6 B 251 ALA ALA LEU ILE ASN VAL GLY PHE LEU GLU SER SER ASN
SEQRES 7 B 251 SER THR ASP TYR ILE ALA MET HIS ASP VAL ASP LEU LEU
SEQRES 8 B 251 PRO LEU ASN GLU GLU LEU ASP TYR GLY PHE PRO GLU ALA
SEQRES 9 B 251 GLY PRO PHE HIS VAL ALA SER PRO GLU LEU HIS PRO LEU
SEQRES 10 B 251 TYR HIS TYR LYS THR TYR VAL GLY GLY ILE LEU LEU LEU
SEQRES 11 B 251 SER LYS GLN HIS TYR ARG LEU CYS ASN GLY MET SER ASN
SEQRES 12 B 251 ARG PHE TRP GLY TRP GLY ARG GLU ASP ASP GLU PHE TYR
SEQRES 13 B 251 ARG ARG ILE LYS GLY ALA GLY LEU GLN LEU PHE ARG PRO
SEQRES 14 B 251 SER GLY ILE THR THR GLY TYR LYS THR PHE ARG HIS LEU
SEQRES 15 B 251 HIS ASP PRO ALA TRP ARG LYS ARG ASP GLN LYS ARG ILE
SEQRES 16 B 251 ALA ALA GLN LYS GLN GLU GLN PHE LYS VAL ASP ARG GLU
SEQRES 17 B 251 GLY GLY LEU ASN THR VAL LYS TYR HIS VAL ALA SER ARG
SEQRES 18 B 251 THR ALA LEU SER VAL GLY GLY ALA PRO CYS THR VAL LEU
SEQRES 19 B 251 ASN ILE MET LEU ASP CYS ASP LYS THR ALA THR PRO TRP
SEQRES 20 B 251 CYS THR PHE SER
HET UDP A 401 25
HET MN A 402 1
HET ACT A 403 4
HET ACT A 404 4
HET ACT A 405 4
HET ACT A 406 4
HET IMD A 407 5
HET UDP B 401 25
HET MN B 402 1
HET ACT B 403 4
HET ACT B 404 4
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM MN MANGANESE (II) ION
HETNAM ACT ACETATE ION
HETNAM IMD IMIDAZOLE
FORMUL 3 UDP 2(C9 H14 N2 O12 P2)
FORMUL 4 MN 2(MN 2+)
FORMUL 5 ACT 6(C2 H3 O2 1-)
FORMUL 9 IMD C3 H5 N2 1+
FORMUL 14 HOH *294(H2 O)
HELIX 1 1 PRO A 81 GLU A 85 5 5
HELIX 2 2 ASP A 87 GLY A 91 5 5
HELIX 3 3 ARG A 104 LYS A 122 1 19
HELIX 4 4 ASN A 140 SER A 152 1 13
HELIX 5 5 LYS A 208 CYS A 214 1 7
HELIX 6 6 ARG A 226 ALA A 238 1 13
HELIX 7 7 THR A 321 PHE A 326 5 6
HELIX 8 8 PRO B 81 GLU B 85 5 5
HELIX 9 9 ASP B 87 GLY B 91 5 5
HELIX 10 10 ARG B 104 LYS B 122 1 19
HELIX 11 11 ASN B 140 SER B 152 1 13
HELIX 12 12 LYS B 208 CYS B 214 1 7
HELIX 13 13 ARG B 226 ALA B 238 1 13
HELIX 14 14 THR B 321 THR B 325 5 5
SHEET 1 A14 PHE A 183 HIS A 184 0
SHEET 2 A14 ILE A 203 SER A 207 -1 O LEU A 205 N PHE A 183
SHEET 3 A14 TYR A 158 HIS A 162 -1 N ILE A 159 O LEU A 206
SHEET 4 A14 LEU A 95 PHE A 101 1 N LEU A 98 O ALA A 160
SHEET 5 A14 HIS A 126 GLN A 133 1 O TYR A 129 N VAL A 99
SHEET 6 A14 ALA A 305 LEU A 314 1 O LEU A 310 N ASN A 132
SHEET 7 A14 TYR A 292 VAL A 302 -1 N LEU A 300 O CYS A 307
SHEET 8 A14 TYR B 292 VAL B 302 -1 O SER B 301 N SER A 301
SHEET 9 A14 ALA B 305 LEU B 314 -1 O VAL B 309 N THR B 298
SHEET 10 A14 ARG B 125 GLN B 133 1 N VAL B 130 O LEU B 310
SHEET 11 A14 ARG B 94 PHE B 101 1 N VAL B 99 O LEU B 131
SHEET 12 A14 TYR B 158 HIS B 162 1 O ALA B 160 N LEU B 98
SHEET 13 A14 ILE B 203 SER B 207 -1 O LEU B 206 N ILE B 159
SHEET 14 A14 PHE B 183 HIS B 184 -1 N PHE B 183 O LEU B 205
SHEET 1 B 2 LEU A 166 PRO A 168 0
SHEET 2 B 2 PHE A 255 HIS A 257 -1 O ARG A 256 N LEU A 167
SHEET 1 C 2 LEU B 166 PRO B 168 0
SHEET 2 C 2 PHE B 255 HIS B 257 -1 O ARG B 256 N LEU B 167
SSBOND 1 CYS A 316 CYS A 324 1555 1555 2.02
SSBOND 2 CYS B 316 CYS B 324 1555 1555 2.05
LINK NE2 HIS A 257 MN MN A 402 1555 1555 2.43
LINK O1A UDP A 401 MN MN A 402 1555 1555 2.58
LINK MN MN A 402 O HOH A 653 1555 1555 2.39
LINK OD2 ASP B 165 MN MN B 402 1555 1555 2.66
LINK NE2 HIS B 257 MN MN B 402 1555 1555 2.35
LINK O1B UDP B 401 MN MN B 402 1555 1555 2.37
LINK O1A UDP B 401 MN MN B 402 1555 1555 2.50
LINK MN MN B 402 O HOH B 636 1555 1555 2.47
SITE 1 AC1 12 PRO A 100 PHE A 101 ARG A 102 ARG A 104
SITE 2 AC1 12 PHE A 139 ASP A 163 VAL A 164 ASP A 165
SITE 3 AC1 12 TYR A 194 MN A 402 HOH A 579 HOH A 617
SITE 1 AC2 4 ASP A 165 HIS A 257 UDP A 401 HOH A 653
SITE 1 AC3 3 ARG A 138 PHE A 139 GLY A 223
SITE 1 AC4 4 ASP A 79 PRO A 81 ARG A 117 ARG A 297
SITE 1 AC5 7 GLY A 91 PRO A 92 HOH A 650 ALA B 88
SITE 2 AC5 7 GLY B 91 PRO B 92 HOH B 637
SITE 1 AC6 3 ASP A 174 GLY A 176 PHE A 177
SITE 1 AC7 4 PHE A 243 HOH A 605 HOH A 608 HOH B 578
SITE 1 AC8 11 PRO B 100 PHE B 101 ARG B 102 ARG B 104
SITE 2 AC8 11 PHE B 139 ASP B 163 VAL B 164 ASP B 165
SITE 3 AC8 11 TYR B 194 MN B 402 HOH B 501
SITE 1 AC9 4 ASP B 165 HIS B 257 UDP B 401 HOH B 636
SITE 1 BC1 2 PRO B 92 SER B 155
SITE 1 BC2 2 TRP B 84 GLU B 85
CRYST1 125.186 125.186 87.326 90.00 90.00 90.00 P 41 21 2 16
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 0.007988 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011451 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
