HEADER TRANSFERASE 20-DEC-05 2FFU
TITLE CRYSTAL STRUCTURE OF HUMAN PPGALNACT-2 COMPLEXED WITH UDP AND EA2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC AND LECTIN DOMAINS;
COMPND 5 SYNONYM: PPGALNACT-2; PROTEIN-UDP ACETYLGALACTOSAMINYLTRANSFERASE 2;
COMPND 6 UDP-GALNAC:POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2;
COMPND 7 POLYPEPTIDE GALNAC TRANSFERASE 2; GALNAC-T2; PP-GANTASE 2;
COMPND 8 EC: 2.4.1.41;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: 13-PEPTIDE EA2, PTTDSTTPAPTTK;
COMPND 12 CHAIN: P;
COMPND 13 FRAGMENT: RESIDUES 244-256 OF RAT SUBMANDIBULAR GLAND MUCIN;
COMPND 14 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: GALNT2;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SMD1168;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9;
SOURCE 11 OTHER_DETAILS: INVITROGEN PPIC9 VECTOR WITH TEV-PROTEASE-CLEAVABLE,
SOURCE 12 N-TERMINAL ENGINEERED 6HIS TAG;
SOURCE 13 MOL_ID: 2;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 OTHER_DETAILS: OCCURS NATURALLY IN RATTUS NORVEGICUS
KEYWDS PPGALNACT; MUCIN; GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.FRITZ
REVDAT 4 18-OCT-17 2FFU 1 REMARK
REVDAT 3 24-FEB-09 2FFU 1 VERSN
REVDAT 2 18-APR-06 2FFU 1 JRNL
REVDAT 1 31-JAN-06 2FFU 0
JRNL AUTH T.A.FRITZ,J.RAMAN,L.A.TABAK
JRNL TITL DYNAMIC ASSOCIATION BETWEEN THE CATALYTIC AND LECTIN DOMAINS
JRNL TITL 2 OF HUMAN UDP-GALNAC:POLYPEPTIDE
JRNL TITL 3 {ALPHA}-N-ACETYLGALACTOSAMINYLTRANSFERASE-2
JRNL REF J.BIOL.CHEM. V. 281 8613 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16434399
JRNL DOI 10.1074/JBC.M513590200
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2043107.150
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 55904
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) : 0.178
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2822
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8825
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 468
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4022
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 495
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : 0.37000
REMARK 3 B12 (A**2) : 0.84000
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) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
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) : 1.410 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.740 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.290 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 43.17
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_REP.PARAM
REMARK 3 PARAMETER FILE 4 : UDP.PARAM2
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : UDP.TOPO2
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035828.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55904
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 24.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, HEPES, MERCAPTOETHANOL, UDP,
REMARK 280 EDTA, MNCL2, EA2, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.37467
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 112.74933
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 84.56200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 140.93667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.18733
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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 SER A 71
REMARK 465 ASP A 72
REMARK 465 ALA A 73
REMARK 465 LEU A 74
REMARK 465 LEU A 569
REMARK 465 GLN A 570
REMARK 465 GLN A 571
REMARK 465 PRO P 1
REMARK 465 THR P 2
REMARK 465 THR P 3
REMARK 465 ASP P 4
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 THR A 90 19.50 -148.29
REMARK 500 LYS A 192 -2.28 71.62
REMARK 500 HIS A 226 57.28 -149.33
REMARK 500 LYS A 323 -113.65 43.27
REMARK 500 VAL A 330 -79.53 55.14
REMARK 500 ASP A 390 -139.10 51.70
REMARK 500 ASN A 405 51.95 -99.81
REMARK 500 PHE A 463 -156.94 -125.95
REMARK 500 LYS A 488 32.01 70.85
REMARK 500 MET A 493 -119.06 60.81
REMARK 500 ASN A 516 39.04 -98.12
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 600 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 224 OD2
REMARK 620 2 HIS A 226 NE2 103.7
REMARK 620 3 HIS A 359 NE2 89.4 93.1
REMARK 620 4 UDP A 601 O1A 97.1 84.9 173.5
REMARK 620 5 UDP A 601 O1B 93.3 161.9 93.1 86.9
REMARK 620 6 HOH A1054 O 176.2 80.0 89.6 84.0 83.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 601
DBREF 2FFU A 75 571 UNP Q10471 GALT2_HUMAN 75 571
DBREF 2FFU P 1 13 GB 995765 AAA75589 244 256
SEQADV 2FFU SER A 71 UNP Q10471 CLONING ARTIFACT
SEQADV 2FFU ASP A 72 UNP Q10471 CLONING ARTIFACT
SEQADV 2FFU ALA A 73 UNP Q10471 CLONING ARTIFACT
SEQADV 2FFU LEU A 74 UNP Q10471 CLONING ARTIFACT
SEQRES 1 A 501 SER ASP ALA LEU LYS VAL ARG TRP PRO ASP PHE ASN GLN
SEQRES 2 A 501 GLU ALA TYR VAL GLY GLY THR MET VAL ARG SER GLY GLN
SEQRES 3 A 501 ASP PRO TYR ALA ARG ASN LYS PHE ASN GLN VAL GLU SER
SEQRES 4 A 501 ASP LYS LEU ARG MET ASP ARG ALA ILE PRO ASP THR ARG
SEQRES 5 A 501 HIS ASP GLN CYS GLN ARG LYS GLN TRP ARG VAL ASP LEU
SEQRES 6 A 501 PRO ALA THR SER VAL VAL ILE THR PHE HIS ASN GLU ALA
SEQRES 7 A 501 ARG SER ALA LEU LEU ARG THR VAL VAL SER VAL LEU LYS
SEQRES 8 A 501 LYS SER PRO PRO HIS LEU ILE LYS GLU ILE ILE LEU VAL
SEQRES 9 A 501 ASP ASP TYR SER ASN ASP PRO GLU ASP GLY ALA LEU LEU
SEQRES 10 A 501 GLY LYS ILE GLU LYS VAL ARG VAL LEU ARG ASN ASP ARG
SEQRES 11 A 501 ARG GLU GLY LEU MET ARG SER ARG VAL ARG GLY ALA ASP
SEQRES 12 A 501 ALA ALA GLN ALA LYS VAL LEU THR PHE LEU ASP SER HIS
SEQRES 13 A 501 CYS GLU CYS ASN GLU HIS TRP LEU GLU PRO LEU LEU GLU
SEQRES 14 A 501 ARG VAL ALA GLU ASP ARG THR ARG VAL VAL SER PRO ILE
SEQRES 15 A 501 ILE ASP VAL ILE ASN MET ASP ASN PHE GLN TYR VAL GLY
SEQRES 16 A 501 ALA SER ALA ASP LEU LYS GLY GLY PHE ASP TRP ASN LEU
SEQRES 17 A 501 VAL PHE LYS TRP ASP TYR MET THR PRO GLU GLN ARG ARG
SEQRES 18 A 501 SER ARG GLN GLY ASN PRO VAL ALA PRO ILE LYS THR PRO
SEQRES 19 A 501 MET ILE ALA GLY GLY LEU PHE VAL MET ASP LYS PHE TYR
SEQRES 20 A 501 PHE GLU GLU LEU GLY LYS TYR ASP MET MET MET ASP VAL
SEQRES 21 A 501 TRP GLY GLY GLU ASN LEU GLU ILE SER PHE ARG VAL TRP
SEQRES 22 A 501 GLN CYS GLY GLY SER LEU GLU ILE ILE PRO CYS SER ARG
SEQRES 23 A 501 VAL GLY HIS VAL PHE ARG LYS GLN HIS PRO TYR THR PHE
SEQRES 24 A 501 PRO GLY GLY SER GLY THR VAL PHE ALA ARG ASN THR ARG
SEQRES 25 A 501 ARG ALA ALA GLU VAL TRP MET ASP GLU TYR LYS ASN PHE
SEQRES 26 A 501 TYR TYR ALA ALA VAL PRO SER ALA ARG ASN VAL PRO TYR
SEQRES 27 A 501 GLY ASN ILE GLN SER ARG LEU GLU LEU ARG LYS LYS LEU
SEQRES 28 A 501 SER CYS LYS PRO PHE LYS TRP TYR LEU GLU ASN VAL TYR
SEQRES 29 A 501 PRO GLU LEU ARG VAL PRO ASP HIS GLN ASP ILE ALA PHE
SEQRES 30 A 501 GLY ALA LEU GLN GLN GLY THR ASN CYS LEU ASP THR LEU
SEQRES 31 A 501 GLY HIS PHE ALA ASP GLY VAL VAL GLY VAL TYR GLU CYS
SEQRES 32 A 501 HIS ASN ALA GLY GLY ASN GLN GLU TRP ALA LEU THR LYS
SEQRES 33 A 501 GLU LYS SER VAL LYS HIS MET ASP LEU CYS LEU THR VAL
SEQRES 34 A 501 VAL ASP ARG ALA PRO GLY SER LEU ILE LYS LEU GLN GLY
SEQRES 35 A 501 CYS ARG GLU ASN ASP SER ARG GLN LYS TRP GLU GLN ILE
SEQRES 36 A 501 GLU GLY ASN SER LYS LEU ARG HIS VAL GLY SER ASN LEU
SEQRES 37 A 501 CYS LEU ASP SER ARG THR ALA LYS SER GLY GLY LEU SER
SEQRES 38 A 501 VAL GLU VAL CYS GLY PRO ALA LEU SER GLN GLN TRP LYS
SEQRES 39 A 501 PHE THR LEU ASN LEU GLN GLN
SEQRES 1 P 13 PRO THR THR ASP SER THR THR PRO ALA PRO THR THR LYS
HET MN A 600 1
HET UDP A 601 25
HETNAM MN MANGANESE (II) ION
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 3 MN MN 2+
FORMUL 4 UDP C9 H14 N2 O12 P2
FORMUL 5 HOH *495(H2 O)
HELIX 1 1 ARG A 77 PHE A 81 5 5
HELIX 2 2 ASN A 82 GLY A 89 1 8
HELIX 3 3 ASN A 105 LEU A 112 1 8
HELIX 4 4 HIS A 123 LYS A 129 5 7
HELIX 5 5 ALA A 148 SER A 163 1 16
HELIX 6 6 PRO A 164 HIS A 166 5 3
HELIX 7 7 PRO A 181 LEU A 186 1 6
HELIX 8 8 LEU A 187 ILE A 190 5 4
HELIX 9 9 GLU A 202 ALA A 215 1 14
HELIX 10 10 TRP A 233 ASP A 244 1 12
HELIX 11 11 THR A 286 ARG A 293 1 8
HELIX 12 12 LYS A 315 LEU A 321 1 7
HELIX 13 13 GLY A 333 CYS A 345 1 13
HELIX 14 14 GLY A 372 MET A 389 1 18
HELIX 15 15 TYR A 392 VAL A 400 1 9
HELIX 16 16 PRO A 401 VAL A 406 5 6
HELIX 17 17 ILE A 411 LEU A 421 1 11
HELIX 18 18 PRO A 425 VAL A 433 1 9
HELIX 19 19 GLY A 477 GLU A 481 5 5
HELIX 20 20 ASP A 517 GLN A 520 5 4
HELIX 21 21 THR A 544 GLY A 548 5 5
HELIX 22 22 ALA A 558 GLN A 562 5 5
SHEET 1 A 5 VAL A 193 ARG A 197 0
SHEET 2 A 5 ILE A 168 ASP A 175 1 N LEU A 173 O ARG A 194
SHEET 3 A 5 THR A 138 PHE A 144 1 N VAL A 140 O ILE A 172
SHEET 4 A 5 VAL A 219 PHE A 222 1 O THR A 221 N VAL A 141
SHEET 5 A 5 PHE A 311 ASP A 314 -1 O MET A 313 N LEU A 220
SHEET 1 B 4 CYS A 227 CYS A 229 0
SHEET 2 B 4 SER A 348 HIS A 359 -1 O GLY A 358 N GLU A 228
SHEET 3 B 4 ARG A 247 ILE A 256 1 N SER A 250 O ILE A 352
SHEET 4 B 4 TYR A 263 VAL A 264 -1 O VAL A 264 N VAL A 255
SHEET 1 C 3 CYS A 227 CYS A 229 0
SHEET 2 C 3 SER A 348 HIS A 359 -1 O GLY A 358 N GLU A 228
SHEET 3 C 3 ILE A 301 LYS A 302 -1 N ILE A 301 O ILE A 351
SHEET 1 D 2 LEU A 270 PHE A 274 0
SHEET 2 D 2 PHE A 280 TYR A 284 -1 O ASP A 283 N LYS A 271
SHEET 1 E 7 GLY A 469 GLU A 472 0
SHEET 2 E 7 ASN A 455 ASP A 458 -1 N ASP A 458 O GLY A 469
SHEET 3 E 7 PHE A 447 GLN A 452 -1 N GLN A 452 O ASN A 455
SHEET 4 E 7 TRP A 482 LEU A 484 -1 O TRP A 482 N GLY A 448
SHEET 5 E 7 VAL A 490 HIS A 492 -1 O LYS A 491 N ALA A 483
SHEET 6 E 7 LEU A 495 THR A 498 -1 O LEU A 495 N HIS A 492
SHEET 7 E 7 LYS A 509 GLY A 512 -1 O LYS A 509 N THR A 498
SHEET 1 F 4 GLY A 469 GLU A 472 0
SHEET 2 F 4 ASN A 455 ASP A 458 -1 N ASP A 458 O GLY A 469
SHEET 3 F 4 PHE A 447 GLN A 452 -1 N GLN A 452 O ASN A 455
SHEET 4 F 4 LYS A 564 LEU A 567 -1 O LYS A 564 N GLN A 451
SHEET 1 G 2 TRP A 522 ILE A 525 0
SHEET 2 G 2 LYS A 530 HIS A 533 -1 O ARG A 532 N GLU A 523
SHEET 1 H 2 LEU A 538 ASP A 541 0
SHEET 2 H 2 SER A 551 VAL A 554 -1 O GLU A 553 N CYS A 539
SSBOND 1 CYS A 126 CYS A 354 1555 1555 2.04
SSBOND 2 CYS A 345 CYS A 423 1555 1555 2.03
SSBOND 3 CYS A 456 CYS A 473 1555 1555 2.04
SSBOND 4 CYS A 496 CYS A 513 1555 1555 2.04
SSBOND 5 CYS A 539 CYS A 555 1555 1555 2.04
LINK MN MN A 600 OD2 ASP A 224 1555 1555 2.19
LINK MN MN A 600 NE2 HIS A 226 1555 1555 2.23
LINK MN MN A 600 NE2 HIS A 359 1555 1555 2.23
LINK MN MN A 600 O1A UDP A 601 1555 1555 2.21
LINK MN MN A 600 O1B UDP A 601 1555 1555 2.10
LINK MN MN A 600 O HOH A1054 1555 1555 2.45
SITE 1 AC1 5 ASP A 224 HIS A 226 HIS A 359 UDP A 601
SITE 2 AC1 5 HOH A1054
SITE 1 AC2 24 THR A 143 PHE A 144 HIS A 145 ASP A 176
SITE 2 AC2 24 ARG A 201 GLY A 203 ASP A 224 SER A 225
SITE 3 AC2 24 HIS A 226 VAL A 330 TRP A 331 HIS A 359
SITE 4 AC2 24 ARG A 362 HIS A 365 TYR A 367 MN A 600
SITE 5 AC2 24 HOH A 711 HOH A 733 HOH A 756 HOH A 779
SITE 6 AC2 24 HOH A 822 HOH A1054 THR P 6 THR P 7
CRYST1 69.344 69.344 169.124 90.00 90.00 120.00 P 61 6
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 0.014421 0.008326 0.000000 0.00000
SCALE2 0.000000 0.016652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005913 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
