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HEADER TRANSFERASE 15-AUG-11 3TEJ
TITLE CRYSTAL STRUCTURE OF A DOMAIN FRAGMENT INVOLVED IN PEPTIDE NATURAL
TITLE 2 PRODUCT BIOSYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROBACTIN SYNTHASE COMPONENT F;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ACYL CARRIER AND THIOESTERASE RESIDUES 965-1293;
COMPND 5 SYNONYM: ENTEROCHELIN SYNTHASE F, SERINE-ACTIVATING ENZYME, SERYL-AMP
COMPND 6 LIGASE;
COMPND 7 EC: 2.7.7.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: ENTF, B0586, JW0578;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS NONRIBOSOMAL PEPTIDE, THIOESTERASE, CARRIER DOMAIN, ATP- BINDING,
KEYWDS 2 ENTEROBACTIN BIOSYNTHESIS, ION TRANSPORT, IRON, IRON TRANSPORT,
KEYWDS 3 LIGASE, MULTIFUNCTIONAL ENZYME, NUCLEOTIDE- BINDING,
KEYWDS 4 PHOSPHOPANTETHEINE, TRANSFERASE, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,T.ZHENG,S.D.BRUNER
REVDAT 1 18-JAN-12 3TEJ 0
JRNL AUTH Y.LIU,T.ZHENG,S.D.BRUNER
JRNL TITL STRUCTURAL BASIS FOR PHOSPHOPANTETHEINYL CARRIER DOMAIN
JRNL TITL 2 INTERACTIONS IN THE TERMINAL MODULE OF NONRIBOSOMAL PEPTIDE
JRNL TITL 3 SYNTHETASES.
JRNL REF CHEM.BIOL. V. 18 1482 2011
JRNL REFN ISSN 1074-5521
JRNL PMID 22118682
JRNL DOI 10.1016/J.CHEMBIOL.2011.09.018
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 45590
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) : 0.206
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4590
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE : 0.2760
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 : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4562
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.18
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
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 3TEJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-11.
REMARK 100 THE RCSB ID CODE IS RCSB067383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE FLAT SI(111)
REMARK 200 OPTICS : PT-COATED TOROIDAL SI MIRROR FOR
REMARK 200 HORIZONTAL AND VERTICAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47257
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.50900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 42.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24.5% PEG 6000, 0.1M TRIS-HCL, 70MM
REMARK 280 MGCL2, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 34.70000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.76500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.18000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.76500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.18000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ALA A 965
REMARK 465 GLN A 966
REMARK 465 ALA A 967
REMARK 465 ASP A 991
REMARK 465 GLU A 1176
REMARK 465 LYS A 1177
REMARK 465 GLU A 1178
REMARK 465 ALA A 1179
REMARK 465 ASN A 1180
REMARK 465 ALA B 965
REMARK 465 GLN B 966
REMARK 465 ALA B 967
REMARK 465 PRO B 968
REMARK 465 GLU B 1045
REMARK 465 GLU B 1046
REMARK 465 ASN B 1173
REMARK 465 TRP B 1174
REMARK 465 GLN B 1175
REMARK 465 GLU B 1176
REMARK 465 LYS B 1177
REMARK 465 GLU B 1178
REMARK 465 ALA B 1179
REMARK 465 ASN B 1180
REMARK 465 GLY B 1181
REMARK 465 LEU B 1182
REMARK 465 ASP B 1183
REMARK 465 PRO B 1184
REMARK 465 GLU B 1185
REMARK 465 VAL B 1186
REMARK 465 LEU B 1187
REMARK 465 ALA B 1188
REMARK 465 GLU B 1189
REMARK 465 ILE B 1190
REMARK 465 ASN B 1191
REMARK 465 ARG B 1192
REMARK 465 GLU B 1193
REMARK 465 ARG B 1194
REMARK 465 GLU B 1195
REMARK 465 ALA B 1196
REMARK 465 PHE B 1197
REMARK 465 LEU B 1198
REMARK 465 ALA B 1199
REMARK 465 ALA B 1200
REMARK 465 GLN B 1201
REMARK 465 GLN B 1202
REMARK 465 GLY B 1203
REMARK 465 SER B 1204
REMARK 465 THR B 1205
REMARK 465 SER B 1206
REMARK 465 GLN B 1246
REMARK 465 GLU B 1247
REMARK 465 GLY B 1248
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO A 968 CG CD
REMARK 470 VAL A 992 CG1 CG2
REMARK 470 ASP A 996 CG OD1 OD2
REMARK 470 LYS A1011 CG CD CE NZ
REMARK 470 ARG A1022 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1047 CG OD1 OD2
REMARK 470 ARG A1050 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1086 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1125 CG CD OE1 OE2
REMARK 470 GLN A1157 CG CD OE1 NE2
REMARK 470 ASP A1183 CG OD1 OD2
REMARK 470 GLU A1185 CG CD OE1 OE2
REMARK 470 GLU A1189 CG CD OE1 OE2
REMARK 470 ASN A1191 CG OD1 ND2
REMARK 470 ARG A1192 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1193 CG CD OE1 OE2
REMARK 470 ARG A1194 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1197 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A1202 CG CD OE1 NE2
REMARK 470 GLU A1208 CG CD OE1 OE2
REMARK 470 GLN A1246 CG CD OE1 NE2
REMARK 470 GLU A1261 CG CD OE1 OE2
REMARK 470 LYS B1011 CG CD CE NZ
REMARK 470 ARG B1050 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1062 CG CD OE1 OE2
REMARK 470 GLU B1114 CG CD OE1 OE2
REMARK 470 THR B1207 OG1 CG2
REMARK 470 GLU B1208 CG CD OE1 OE2
REMARK 470 GLU B1214 CG CD OE1 OE2
REMARK 470 LYS B1235 CG CD CE NZ
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 ARG A 970 -164.68 -115.11
REMARK 500 GLU A1046 -1.79 -57.62
REMARK 500 SER A1138 -121.33 54.79
REMARK 500 LEU A1182 102.68 -57.54
REMARK 500 GLN A1202 72.59 50.70
REMARK 500 THR A1205 -7.72 67.36
REMARK 500 THR A1207 13.89 -140.93
REMARK 500 SER B1048 72.05 -102.45
REMARK 500 PRO B1073 -154.98 -85.12
REMARK 500 SER B1138 -121.82 47.67
REMARK 500 THR B1171 43.38 -89.91
REMARK 500 ASP B1233 41.80 -83.47
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3TEJ A 965 1293 UNP P11454 ENTF_ECOLI 965 1293
DBREF 3TEJ B 965 1293 UNP P11454 ENTF_ECOLI 965 1293
SEQRES 1 A 329 ALA GLN ALA PRO GLY ARG ALA PRO LYS ALA GLY SER GLU
SEQRES 2 A 329 THR ILE ILE ALA ALA ALA PHE SER SER LEU LEU GLY CYS
SEQRES 3 A 329 ASP VAL GLN ASP ALA ASP ALA ASP PHE PHE ALA LEU GLY
SEQRES 4 A 329 GLY HIS UF0 LEU LEU ALA MET LYS LEU ALA ALA GLN LEU
SEQRES 5 A 329 SER ARG GLN VAL ALA ARG GLN VAL THR PRO GLY GLN VAL
SEQRES 6 A 329 MET VAL ALA SER THR VAL ALA LYS LEU ALA THR ILE ILE
SEQRES 7 A 329 ASP ALA GLU GLU ASP SER THR ARG ARG MET GLY PHE GLU
SEQRES 8 A 329 THR ILE LEU PRO LEU ARG GLU GLY ASN GLY PRO THR LEU
SEQRES 9 A 329 PHE CYS PHE HIS PRO ALA SER GLY PHE ALA TRP GLN PHE
SEQRES 10 A 329 SER VAL LEU SER ARG TYR LEU ASP PRO GLN TRP SER ILE
SEQRES 11 A 329 ILE GLY ILE GLN SER PRO ARG PRO ASN GLY PRO MET GLN
SEQRES 12 A 329 THR ALA ALA ASN LEU ASP GLU VAL CYS GLU ALA HIS LEU
SEQRES 13 A 329 ALA THR LEU LEU GLU GLN GLN PRO HIS GLY PRO TYR TYR
SEQRES 14 A 329 LEU LEU GLY TYR SER LEU GLY GLY THR LEU ALA GLN GLY
SEQRES 15 A 329 ILE ALA ALA ARG LEU ARG ALA ARG GLY GLU GLN VAL ALA
SEQRES 16 A 329 PHE LEU GLY LEU LEU ASP THR TRP PRO PRO GLU THR GLN
SEQRES 17 A 329 ASN TRP GLN GLU LYS GLU ALA ASN GLY LEU ASP PRO GLU
SEQRES 18 A 329 VAL LEU ALA GLU ILE ASN ARG GLU ARG GLU ALA PHE LEU
SEQRES 19 A 329 ALA ALA GLN GLN GLY SER THR SER THR GLU LEU PHE THR
SEQRES 20 A 329 THR ILE GLU GLY ASN TYR ALA ASP ALA VAL ARG LEU LEU
SEQRES 21 A 329 THR THR ALA HIS SER VAL PRO PHE ASP GLY LYS ALA THR
SEQRES 22 A 329 LEU PHE VAL ALA GLU ARG THR LEU GLN GLU GLY MET SER
SEQRES 23 A 329 PRO GLU ARG ALA TRP SER PRO TRP ILE ALA GLU LEU ASP
SEQRES 24 A 329 ILE TYR ARG GLN ASP CYS ALA HIS VAL ASP ILE ILE SER
SEQRES 25 A 329 PRO GLY THR PHE GLU LYS ILE GLY PRO ILE ILE ARG ALA
SEQRES 26 A 329 THR LEU ASN ARG
SEQRES 1 B 329 ALA GLN ALA PRO GLY ARG ALA PRO LYS ALA GLY SER GLU
SEQRES 2 B 329 THR ILE ILE ALA ALA ALA PHE SER SER LEU LEU GLY CYS
SEQRES 3 B 329 ASP VAL GLN ASP ALA ASP ALA ASP PHE PHE ALA LEU GLY
SEQRES 4 B 329 GLY HIS UF0 LEU LEU ALA MET LYS LEU ALA ALA GLN LEU
SEQRES 5 B 329 SER ARG GLN VAL ALA ARG GLN VAL THR PRO GLY GLN VAL
SEQRES 6 B 329 MET VAL ALA SER THR VAL ALA LYS LEU ALA THR ILE ILE
SEQRES 7 B 329 ASP ALA GLU GLU ASP SER THR ARG ARG MET GLY PHE GLU
SEQRES 8 B 329 THR ILE LEU PRO LEU ARG GLU GLY ASN GLY PRO THR LEU
SEQRES 9 B 329 PHE CYS PHE HIS PRO ALA SER GLY PHE ALA TRP GLN PHE
SEQRES 10 B 329 SER VAL LEU SER ARG TYR LEU ASP PRO GLN TRP SER ILE
SEQRES 11 B 329 ILE GLY ILE GLN SER PRO ARG PRO ASN GLY PRO MET GLN
SEQRES 12 B 329 THR ALA ALA ASN LEU ASP GLU VAL CYS GLU ALA HIS LEU
SEQRES 13 B 329 ALA THR LEU LEU GLU GLN GLN PRO HIS GLY PRO TYR TYR
SEQRES 14 B 329 LEU LEU GLY TYR SER LEU GLY GLY THR LEU ALA GLN GLY
SEQRES 15 B 329 ILE ALA ALA ARG LEU ARG ALA ARG GLY GLU GLN VAL ALA
SEQRES 16 B 329 PHE LEU GLY LEU LEU ASP THR TRP PRO PRO GLU THR GLN
SEQRES 17 B 329 ASN TRP GLN GLU LYS GLU ALA ASN GLY LEU ASP PRO GLU
SEQRES 18 B 329 VAL LEU ALA GLU ILE ASN ARG GLU ARG GLU ALA PHE LEU
SEQRES 19 B 329 ALA ALA GLN GLN GLY SER THR SER THR GLU LEU PHE THR
SEQRES 20 B 329 THR ILE GLU GLY ASN TYR ALA ASP ALA VAL ARG LEU LEU
SEQRES 21 B 329 THR THR ALA HIS SER VAL PRO PHE ASP GLY LYS ALA THR
SEQRES 22 B 329 LEU PHE VAL ALA GLU ARG THR LEU GLN GLU GLY MET SER
SEQRES 23 B 329 PRO GLU ARG ALA TRP SER PRO TRP ILE ALA GLU LEU ASP
SEQRES 24 B 329 ILE TYR ARG GLN ASP CYS ALA HIS VAL ASP ILE ILE SER
SEQRES 25 B 329 PRO GLY THR PHE GLU LYS ILE GLY PRO ILE ILE ARG ALA
SEQRES 26 B 329 THR LEU ASN ARG
MODRES 3TEJ UF0 A 1006 SER
MODRES 3TEJ UF0 B 1006 SER
HET UF0 A1006 31
HET UF0 B1006 31
HETNAM UF0 O-[(R)-HYDROXY{[(3R)-3-HYDROXY-4-{[3-({2-
HETNAM 2 UF0 [(HYDROXYACETYL)AMINO]ETHYL}AMINO)-3-OXOPROPYL]AMINO}-
HETNAM 3 UF0 2,2-DIMETHYL-4-OXOBUTYL]OXY}PHOSPHORYL]-L-SERINE
FORMUL 1 UF0 2(C16 H31 N4 O11 P)
FORMUL 3 HOH *293(H2 O)
HELIX 1 1 GLY A 975 GLY A 989 1 15
HELIX 2 2 HIS A 1005 ALA A 1021 1 17
HELIX 3 3 THR A 1025 ALA A 1032 1 8
HELIX 4 4 THR A 1034 ALA A 1044 1 11
HELIX 5 5 ALA A 1078 TYR A 1087 5 10
HELIX 6 6 GLY A 1104 ALA A 1109 1 6
HELIX 7 7 ASN A 1111 GLN A 1127 1 17
HELIX 8 8 SER A 1138 ARG A 1154 1 17
HELIX 9 9 PRO A 1169 TRP A 1174 1 6
HELIX 10 10 GLU A 1185 ALA A 1200 1 16
HELIX 11 11 THR A 1207 THR A 1225 1 19
HELIX 12 12 ARG A 1243 LEU A 1245 5 3
HELIX 13 13 SER A 1250 SER A 1256 1 7
HELIX 14 14 ALA A 1270 SER A 1276 5 7
HELIX 15 15 THR A 1279 ASN A 1292 1 14
HELIX 16 16 GLY B 975 GLY B 989 1 15
HELIX 17 17 HIS B 1005 VAL B 1020 1 16
HELIX 18 18 THR B 1025 ALA B 1032 1 8
HELIX 19 19 THR B 1034 ALA B 1044 1 11
HELIX 20 20 ALA B 1078 TYR B 1087 5 10
HELIX 21 21 GLY B 1104 ALA B 1109 1 6
HELIX 22 22 ASN B 1111 GLN B 1127 1 17
HELIX 23 23 SER B 1138 ARG B 1154 1 17
HELIX 24 24 GLU B 1208 THR B 1225 1 18
HELIX 25 25 ARG B 1243 LEU B 1245 5 3
HELIX 26 26 SER B 1250 SER B 1256 1 7
HELIX 27 27 ALA B 1270 ILE B 1274 5 5
HELIX 28 28 SER B 1276 ASN B 1292 1 17
SHEET 1 A 7 ILE A1057 ARG A1061 0
SHEET 2 A 7 SER A1093 ILE A1097 -1 O GLY A1096 N LEU A1058
SHEET 3 A 7 THR A1067 PHE A1071 1 N CYS A1070 O ILE A1097
SHEET 4 A 7 TYR A1132 TYR A1137 1 O LEU A1135 N PHE A1071
SHEET 5 A 7 VAL A1158 LEU A1164 1 O GLY A1162 N LEU A1134
SHEET 6 A 7 PHE A1232 ALA A1241 1 O THR A1237 N LEU A1161
SHEET 7 A 7 ILE A1259 GLN A1267 1 O GLN A1267 N VAL A1240
SHEET 1 B 7 ILE B1057 ARG B1061 0
SHEET 2 B 7 SER B1093 ILE B1097 -1 O GLY B1096 N LEU B1058
SHEET 3 B 7 THR B1067 PHE B1071 1 N CYS B1070 O ILE B1097
SHEET 4 B 7 TYR B1132 TYR B1137 1 O LEU B1135 N PHE B1071
SHEET 5 B 7 VAL B1158 LEU B1164 1 O PHE B1160 N LEU B1134
SHEET 6 B 7 PHE B1232 ALA B1241 1 O THR B1237 N LEU B1163
SHEET 7 B 7 ILE B1259 GLN B1267 1 O GLN B1267 N VAL B1240
LINK C HIS A1005 N UF0 A1006 1555 1555 1.33
LINK C UF0 A1006 N LEU A1007 1555 1555 1.33
LINK C HIS B1005 N UF0 B1006 1555 1555 1.33
LINK C UF0 B1006 N LEU B1007 1555 1555 1.33
CISPEP 1 ARG A 1101 PRO A 1102 0 0.00
CISPEP 2 GLY A 1130 PRO A 1131 0 0.03
CISPEP 3 ASP A 1183 PRO A 1184 0 -0.06
CISPEP 4 ARG B 1101 PRO B 1102 0 -0.08
CISPEP 5 GLY B 1130 PRO B 1131 0 0.16
CRYST1 69.400 90.360 97.530 90.00 90.00 90.00 P 21 21 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 0.014409 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010253 0.00000
TER 2385 ARG A1293
TER 4564 ARG B1293
MASTER 345 0 2 28 14 0 0 6 4855 2 66 52
END |