HEADER TRANSFERASE 19-JUL-05 2ACV
TITLE CRYSTAL STRUCTURE OF MEDICAGO TRUNCATULA UGT71G1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRITERPENE UDP-GLUCOSYL TRANSFERASE UGT71G1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MEDICAGO TRUNCATULA;
SOURCE 3 ORGANISM_COMMON: BARREL MEDIC;
SOURCE 4 ORGANISM_TAXID: 3880;
SOURCE 5 GENE: UGT71G1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS GLYCOSYLTRANSFERASE, UDP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SHAO,X.HE,L.ACHNINE,J.W.BLOUNT,R.A.DIXON,X.WANG
REVDAT 3 14-FEB-24 2ACV 1 REMARK
REVDAT 2 24-FEB-09 2ACV 1 VERSN
REVDAT 1 15-NOV-05 2ACV 0
JRNL AUTH H.SHAO,X.HE,L.ACHNINE,J.W.BLOUNT,R.A.DIXON,X.WANG
JRNL TITL CRYSTAL STRUCTURES OF A MULTIFUNCTIONAL TRITERPENE/FLAVONOID
JRNL TITL 2 GLYCOSYLTRANSFERASE FROM MEDICAGO TRUNCATULA.
JRNL REF PLANT CELL V. 17 3141 2005
JRNL REFN ISSN 1040-4651
JRNL PMID 16214900
JRNL DOI 10.1105/TPC.105.035055
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 60990
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) : 0.187
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4980
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 : 7204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 728
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.84
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) : 0.21
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.270
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 2ACV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033747.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JAN-05; 09-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 93; NULL
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; Y
REMARK 200 RADIATION SOURCE : ROTATING ANODE; CAMD
REMARK 200 BEAMLINE : NULL; GCPCC
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 0.9797, 0.97996, 0.9393
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL MAX-FLUX; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62825
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM ACETATE, SODIUM
REMARK 280 CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 45.29650
REMARK 290 SMTRY3 2 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: DIMERIC
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 MET A 1
REMARK 465 SER A 2
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 MET B 3
REMARK 465 SER B 4
REMARK 465 ASP B 5
REMARK 465 ILE B 6
REMARK 465 ASN B 7
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 413 NH2 ARG B 296 2.17
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 ASP A 37 101.47 -161.41
REMARK 500 PRO A 53 -149.67 -81.73
REMARK 500 ALA A 55 -148.80 -89.04
REMARK 500 ALA A 64 57.81 39.34
REMARK 500 SER A 65 112.84 69.39
REMARK 500 LYS A 86 -8.02 -59.92
REMARK 500 SER A 144 -160.13 -101.84
REMARK 500 SER A 167 -100.68 -71.16
REMARK 500 HIS A 171 79.09 -155.10
REMARK 500 PHE A 283 50.14 -119.41
REMARK 500 ILE A 378 -56.19 -135.73
REMARK 500 ALA A 380 -132.24 53.76
REMARK 500 ASP B 37 99.14 -164.15
REMARK 500 PRO B 50 104.80 -43.07
REMARK 500 PRO B 53 -102.30 -66.96
REMARK 500 ALA B 55 -89.33 -38.50
REMARK 500 ILE B 59 -78.97 -56.20
REMARK 500 SER B 65 68.41 39.74
REMARK 500 SER B 144 -156.27 -100.50
REMARK 500 PHE B 164 80.18 36.28
REMARK 500 ASP B 165 24.30 40.46
REMARK 500 ASP B 168 45.60 -76.12
REMARK 500 ASP B 170 -46.22 -158.25
REMARK 500 GLN B 253 104.53 -54.93
REMARK 500 GLN B 260 67.28 64.32
REMARK 500 LYS B 276 18.36 59.72
REMARK 500 PHE B 283 50.84 -117.14
REMARK 500 ILE B 378 -55.32 -132.57
REMARK 500 ALA B 380 -136.67 53.48
REMARK 500
REMARK 500 REMARK: NULL
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 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 901
DBREF 2ACV A 1 463 UNP Q5IFH7 Q5IFH7_MEDTR 1 463
DBREF 2ACV B 1 463 UNP Q5IFH7 Q5IFH7_MEDTR 1 463
SEQRES 1 A 463 MET SER MET SER ASP ILE ASN LYS ASN SER GLU LEU ILE
SEQRES 2 A 463 PHE ILE PRO ALA PRO GLY ILE GLY HIS LEU ALA SER ALA
SEQRES 3 A 463 LEU GLU PHE ALA LYS LEU LEU THR ASN HIS ASP LYS ASN
SEQRES 4 A 463 LEU TYR ILE THR VAL PHE CYS ILE LYS PHE PRO GLY MET
SEQRES 5 A 463 PRO PHE ALA ASP SER TYR ILE LYS SER VAL LEU ALA SER
SEQRES 6 A 463 GLN PRO GLN ILE GLN LEU ILE ASP LEU PRO GLU VAL GLU
SEQRES 7 A 463 PRO PRO PRO GLN GLU LEU LEU LYS SER PRO GLU PHE TYR
SEQRES 8 A 463 ILE LEU THR PHE LEU GLU SER LEU ILE PRO HIS VAL LYS
SEQRES 9 A 463 ALA THR ILE LYS THR ILE LEU SER ASN LYS VAL VAL GLY
SEQRES 10 A 463 LEU VAL LEU ASP PHE PHE CYS VAL SER MET ILE ASP VAL
SEQRES 11 A 463 GLY ASN GLU PHE GLY ILE PRO SER TYR LEU PHE LEU THR
SEQRES 12 A 463 SER ASN VAL GLY PHE LEU SER LEU MET LEU SER LEU LYS
SEQRES 13 A 463 ASN ARG GLN ILE GLU GLU VAL PHE ASP ASP SER ASP ARG
SEQRES 14 A 463 ASP HIS GLN LEU LEU ASN ILE PRO GLY ILE SER ASN GLN
SEQRES 15 A 463 VAL PRO SER ASN VAL LEU PRO ASP ALA CYS PHE ASN LYS
SEQRES 16 A 463 ASP GLY GLY TYR ILE ALA TYR TYR LYS LEU ALA GLU ARG
SEQRES 17 A 463 PHE ARG ASP THR LYS GLY ILE ILE VAL ASN THR PHE SER
SEQRES 18 A 463 ASP LEU GLU GLN SER SER ILE ASP ALA LEU TYR ASP HIS
SEQRES 19 A 463 ASP GLU LYS ILE PRO PRO ILE TYR ALA VAL GLY PRO LEU
SEQRES 20 A 463 LEU ASP LEU LYS GLY GLN PRO ASN PRO LYS LEU ASP GLN
SEQRES 21 A 463 ALA GLN HIS ASP LEU ILE LEU LYS TRP LEU ASP GLU GLN
SEQRES 22 A 463 PRO ASP LYS SER VAL VAL PHE LEU CYS PHE GLY SER MET
SEQRES 23 A 463 GLY VAL SER PHE GLY PRO SER GLN ILE ARG GLU ILE ALA
SEQRES 24 A 463 LEU GLY LEU LYS HIS SER GLY VAL ARG PHE LEU TRP SER
SEQRES 25 A 463 ASN SER ALA GLU LYS LYS VAL PHE PRO GLU GLY PHE LEU
SEQRES 26 A 463 GLU TRP MET GLU LEU GLU GLY LYS GLY MET ILE CYS GLY
SEQRES 27 A 463 TRP ALA PRO GLN VAL GLU VAL LEU ALA HIS LYS ALA ILE
SEQRES 28 A 463 GLY GLY PHE VAL SER HIS CYS GLY TRP ASN SER ILE LEU
SEQRES 29 A 463 GLU SER MET TRP PHE GLY VAL PRO ILE LEU THR TRP PRO
SEQRES 30 A 463 ILE TYR ALA GLU GLN GLN LEU ASN ALA PHE ARG LEU VAL
SEQRES 31 A 463 LYS GLU TRP GLY VAL GLY LEU GLY LEU ARG VAL ASP TYR
SEQRES 32 A 463 ARG LYS GLY SER ASP VAL VAL ALA ALA GLU GLU ILE GLU
SEQRES 33 A 463 LYS GLY LEU LYS ASP LEU MET ASP LYS ASP SER ILE VAL
SEQRES 34 A 463 HIS LYS LYS VAL GLN GLU MET LYS GLU MET SER ARG ASN
SEQRES 35 A 463 ALA VAL VAL ASP GLY GLY SER SER LEU ILE SER VAL GLY
SEQRES 36 A 463 LYS LEU ILE ASP ASP ILE THR GLY
SEQRES 1 B 463 MET SER MET SER ASP ILE ASN LYS ASN SER GLU LEU ILE
SEQRES 2 B 463 PHE ILE PRO ALA PRO GLY ILE GLY HIS LEU ALA SER ALA
SEQRES 3 B 463 LEU GLU PHE ALA LYS LEU LEU THR ASN HIS ASP LYS ASN
SEQRES 4 B 463 LEU TYR ILE THR VAL PHE CYS ILE LYS PHE PRO GLY MET
SEQRES 5 B 463 PRO PHE ALA ASP SER TYR ILE LYS SER VAL LEU ALA SER
SEQRES 6 B 463 GLN PRO GLN ILE GLN LEU ILE ASP LEU PRO GLU VAL GLU
SEQRES 7 B 463 PRO PRO PRO GLN GLU LEU LEU LYS SER PRO GLU PHE TYR
SEQRES 8 B 463 ILE LEU THR PHE LEU GLU SER LEU ILE PRO HIS VAL LYS
SEQRES 9 B 463 ALA THR ILE LYS THR ILE LEU SER ASN LYS VAL VAL GLY
SEQRES 10 B 463 LEU VAL LEU ASP PHE PHE CYS VAL SER MET ILE ASP VAL
SEQRES 11 B 463 GLY ASN GLU PHE GLY ILE PRO SER TYR LEU PHE LEU THR
SEQRES 12 B 463 SER ASN VAL GLY PHE LEU SER LEU MET LEU SER LEU LYS
SEQRES 13 B 463 ASN ARG GLN ILE GLU GLU VAL PHE ASP ASP SER ASP ARG
SEQRES 14 B 463 ASP HIS GLN LEU LEU ASN ILE PRO GLY ILE SER ASN GLN
SEQRES 15 B 463 VAL PRO SER ASN VAL LEU PRO ASP ALA CYS PHE ASN LYS
SEQRES 16 B 463 ASP GLY GLY TYR ILE ALA TYR TYR LYS LEU ALA GLU ARG
SEQRES 17 B 463 PHE ARG ASP THR LYS GLY ILE ILE VAL ASN THR PHE SER
SEQRES 18 B 463 ASP LEU GLU GLN SER SER ILE ASP ALA LEU TYR ASP HIS
SEQRES 19 B 463 ASP GLU LYS ILE PRO PRO ILE TYR ALA VAL GLY PRO LEU
SEQRES 20 B 463 LEU ASP LEU LYS GLY GLN PRO ASN PRO LYS LEU ASP GLN
SEQRES 21 B 463 ALA GLN HIS ASP LEU ILE LEU LYS TRP LEU ASP GLU GLN
SEQRES 22 B 463 PRO ASP LYS SER VAL VAL PHE LEU CYS PHE GLY SER MET
SEQRES 23 B 463 GLY VAL SER PHE GLY PRO SER GLN ILE ARG GLU ILE ALA
SEQRES 24 B 463 LEU GLY LEU LYS HIS SER GLY VAL ARG PHE LEU TRP SER
SEQRES 25 B 463 ASN SER ALA GLU LYS LYS VAL PHE PRO GLU GLY PHE LEU
SEQRES 26 B 463 GLU TRP MET GLU LEU GLU GLY LYS GLY MET ILE CYS GLY
SEQRES 27 B 463 TRP ALA PRO GLN VAL GLU VAL LEU ALA HIS LYS ALA ILE
SEQRES 28 B 463 GLY GLY PHE VAL SER HIS CYS GLY TRP ASN SER ILE LEU
SEQRES 29 B 463 GLU SER MET TRP PHE GLY VAL PRO ILE LEU THR TRP PRO
SEQRES 30 B 463 ILE TYR ALA GLU GLN GLN LEU ASN ALA PHE ARG LEU VAL
SEQRES 31 B 463 LYS GLU TRP GLY VAL GLY LEU GLY LEU ARG VAL ASP TYR
SEQRES 32 B 463 ARG LYS GLY SER ASP VAL VAL ALA ALA GLU GLU ILE GLU
SEQRES 33 B 463 LYS GLY LEU LYS ASP LEU MET ASP LYS ASP SER ILE VAL
SEQRES 34 B 463 HIS LYS LYS VAL GLN GLU MET LYS GLU MET SER ARG ASN
SEQRES 35 B 463 ALA VAL VAL ASP GLY GLY SER SER LEU ILE SER VAL GLY
SEQRES 36 B 463 LYS LEU ILE ASP ASP ILE THR GLY
HET UDP A 900 25
HET UDP B 901 25
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 3 UDP 2(C9 H14 N2 O12 P2)
FORMUL 5 HOH *728(H2 O)
HELIX 1 1 MET A 3 ASN A 9 1 7
HELIX 2 2 HIS A 22 HIS A 36 1 15
HELIX 3 3 ALA A 55 ALA A 64 1 10
HELIX 4 4 PRO A 81 LYS A 86 5 6
HELIX 5 5 SER A 87 LEU A 99 1 13
HELIX 6 6 LEU A 99 LEU A 111 1 13
HELIX 7 7 PHE A 123 SER A 126 5 4
HELIX 8 8 MET A 127 PHE A 134 1 8
HELIX 9 9 ASN A 145 LEU A 155 1 11
HELIX 10 10 LYS A 156 ARG A 158 5 3
HELIX 11 11 ASP A 168 HIS A 171 5 4
HELIX 12 12 ASN A 186 LEU A 188 5 3
HELIX 13 13 PRO A 189 ASN A 194 1 6
HELIX 14 14 GLY A 197 GLU A 207 1 11
HELIX 15 15 ARG A 208 THR A 212 5 5
HELIX 16 16 PHE A 220 ASP A 235 1 16
HELIX 17 17 ASP A 259 GLU A 272 1 14
HELIX 18 18 GLY A 291 GLY A 306 1 16
HELIX 19 19 GLU A 316 PHE A 320 5 5
HELIX 20 20 GLY A 323 GLY A 332 1 10
HELIX 21 21 PRO A 341 HIS A 348 1 8
HELIX 22 22 GLY A 359 PHE A 369 1 11
HELIX 23 23 GLU A 381 GLU A 392 1 12
HELIX 24 24 ALA A 411 MET A 423 1 13
HELIX 25 25 ILE A 428 VAL A 444 1 17
HELIX 26 26 GLY A 448 GLY A 463 1 16
HELIX 27 27 GLY B 19 HIS B 36 1 18
HELIX 28 28 ASP B 56 VAL B 62 1 7
HELIX 29 29 PRO B 81 LYS B 86 5 6
HELIX 30 30 SER B 87 SER B 98 1 12
HELIX 31 31 LEU B 99 LEU B 111 1 13
HELIX 32 32 PHE B 123 SER B 126 5 4
HELIX 33 33 MET B 127 PHE B 134 1 8
HELIX 34 34 ASN B 145 LEU B 155 1 11
HELIX 35 35 LYS B 156 ARG B 158 5 3
HELIX 36 36 VAL B 163 ASP B 168 1 6
HELIX 37 37 ASN B 186 LEU B 188 5 3
HELIX 38 38 PRO B 189 ASN B 194 1 6
HELIX 39 39 GLY B 197 GLU B 207 1 11
HELIX 40 40 ARG B 208 THR B 212 5 5
HELIX 41 41 PHE B 220 ASP B 235 1 16
HELIX 42 42 GLN B 260 GLN B 273 1 14
HELIX 43 43 GLY B 291 GLY B 306 1 16
HELIX 44 44 GLU B 316 PHE B 320 5 5
HELIX 45 45 GLY B 323 GLY B 332 1 10
HELIX 46 46 PRO B 341 HIS B 348 1 8
HELIX 47 47 GLY B 359 PHE B 369 1 11
HELIX 48 48 GLU B 381 GLU B 392 1 12
HELIX 49 49 ALA B 411 MET B 423 1 13
HELIX 50 50 ILE B 428 VAL B 444 1 17
HELIX 51 51 GLY B 448 GLY B 463 1 16
SHEET 1 A 7 ILE A 69 ASP A 73 0
SHEET 2 A 7 LEU A 40 CYS A 46 1 N CYS A 46 O ILE A 72
SHEET 3 A 7 SER A 10 ILE A 15 1 N PHE A 14 O PHE A 45
SHEET 4 A 7 VAL A 115 ASP A 121 1 O VAL A 119 N ILE A 15
SHEET 5 A 7 SER A 138 LEU A 142 1 O PHE A 141 N LEU A 120
SHEET 6 A 7 GLY A 214 VAL A 217 1 O ILE A 216 N LEU A 142
SHEET 7 A 7 ILE A 241 ALA A 243 1 O TYR A 242 N ILE A 215
SHEET 1 B 2 LEU A 173 LEU A 174 0
SHEET 2 B 2 VAL A 183 PRO A 184 -1 O VAL A 183 N LEU A 174
SHEET 1 C 6 GLY A 334 CYS A 337 0
SHEET 2 C 6 ARG A 308 SER A 312 1 N TRP A 311 O MET A 335
SHEET 3 C 6 VAL A 278 CYS A 282 1 N LEU A 281 O SER A 312
SHEET 4 C 6 ILE A 351 SER A 356 1 O VAL A 355 N PHE A 280
SHEET 5 C 6 ILE A 373 THR A 375 1 O LEU A 374 N PHE A 354
SHEET 6 C 6 GLY A 396 GLY A 398 1 O LEU A 397 N ILE A 373
SHEET 1 D 7 ILE B 69 ASP B 73 0
SHEET 2 D 7 LEU B 40 CYS B 46 1 N CYS B 46 O ILE B 72
SHEET 3 D 7 SER B 10 ILE B 15 1 N PHE B 14 O THR B 43
SHEET 4 D 7 VAL B 115 ASP B 121 1 O VAL B 116 N GLU B 11
SHEET 5 D 7 SER B 138 LEU B 142 1 O PHE B 141 N LEU B 120
SHEET 6 D 7 GLY B 214 VAL B 217 1 O ILE B 216 N LEU B 140
SHEET 7 D 7 ILE B 241 ALA B 243 1 O TYR B 242 N VAL B 217
SHEET 1 E 2 LEU B 173 LEU B 174 0
SHEET 2 E 2 VAL B 183 PRO B 184 -1 O VAL B 183 N LEU B 174
SHEET 1 F 6 GLY B 334 CYS B 337 0
SHEET 2 F 6 ARG B 308 SER B 312 1 N TRP B 311 O MET B 335
SHEET 3 F 6 VAL B 278 CYS B 282 1 N LEU B 281 O SER B 312
SHEET 4 F 6 ILE B 351 SER B 356 1 O VAL B 355 N PHE B 280
SHEET 5 F 6 ILE B 373 THR B 375 1 O LEU B 374 N PHE B 354
SHEET 6 F 6 GLY B 396 GLY B 398 1 O LEU B 397 N ILE B 373
CISPEP 1 GLY A 245 PRO A 246 0 0.09
CISPEP 2 GLY B 245 PRO B 246 0 0.23
CISPEP 3 ASN B 255 PRO B 256 0 -0.02
SITE 1 AC1 20 ILE A 20 GLY A 21 CYS A 282 GLY A 284
SITE 2 AC1 20 SER A 285 TRP A 339 ALA A 340 GLN A 342
SITE 3 AC1 20 HIS A 357 GLY A 359 TRP A 360 ASN A 361
SITE 4 AC1 20 SER A 362 GLU A 365 TYR A 379 HOH A 925
SITE 5 AC1 20 HOH A 952 HOH A 977 HOH A1195 HOH A1216
SITE 1 AC2 16 CYS B 282 GLY B 284 SER B 285 TRP B 339
SITE 2 AC2 16 ALA B 340 GLN B 342 HIS B 357 GLY B 359
SITE 3 AC2 16 TRP B 360 ASN B 361 SER B 362 GLU B 365
SITE 4 AC2 16 TYR B 379 HOH B 989 HOH B1014 HOH B1024
CRYST1 53.713 90.593 101.788 90.00 102.57 90.00 P 1 21 1 4
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 0.018617 0.000000 0.004150 0.00000
SCALE2 0.000000 0.011038 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
