HEADER TRANSPORT PROTEIN 17-APR-14 4PD8
TITLE STRUCTURE OF VCCNT-7C8C BOUND TO PYRROLO-CYTIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUPC FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: ATCC 39315 / EL TOR INABA N16961;
SOURCE 5 GENE: VC_2352;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET26
KEYWDS MEMBRANE PROTEIN, SODIUM-COUPLED TRANSPORTER, PYRROLO-CYTIDINE, DRUG
KEYWDS 2 TRANSPORTER, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.L.JOHNSON,S.-Y.LEE
REVDAT 5 27-SEP-23 4PD8 1 REMARK
REVDAT 4 25-DEC-19 4PD8 1 REMARK
REVDAT 3 20-SEP-17 4PD8 1 COMPND SOURCE REMARK
REVDAT 2 01-OCT-14 4PD8 1 JRNL
REVDAT 1 13-AUG-14 4PD8 0
JRNL AUTH Z.L.JOHNSON,J.H.LEE,K.LEE,M.LEE,D.Y.KWON,J.HONG,S.Y.LEE
JRNL TITL STRUCTURAL BASIS OF NUCLEOSIDE AND NUCLEOSIDE DRUG
JRNL TITL 2 SELECTIVITY BY CONCENTRATIVE NUCLEOSIDE TRANSPORTERS.
JRNL REF ELIFE V. 3 03604 2014
JRNL REFN ESSN 2050-084X
JRNL PMID 25082345
JRNL DOI 10.7554/ELIFE.03604
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 17698
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 896
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 39.1640 - 4.9940 1.00 2846 155 0.1959 0.2661
REMARK 3 2 4.9940 - 3.9651 1.00 2809 147 0.1941 0.2344
REMARK 3 3 3.9651 - 3.4642 1.00 2794 149 0.1890 0.2126
REMARK 3 4 3.4642 - 3.1476 1.00 2792 149 0.2071 0.2221
REMARK 3 5 3.1476 - 2.9221 1.00 2777 148 0.2310 0.2795
REMARK 3 6 2.9221 - 2.7499 1.00 2784 148 0.2583 0.2877
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.97
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 : 0.003 3042
REMARK 3 ANGLE : 0.646 4130
REMARK 3 CHIRALITY : 0.021 488
REMARK 3 PLANARITY : 0.003 509
REMARK 3 DIHEDRAL : 10.575 1028
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 4PD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000201080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-11
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 : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17711
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.65600
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: NULL
REMARK 200 STARTING MODEL: 3TIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 37-42% PEG 400, 100 MM CACL2, PH 8.5,
REMARK 280 LIQUID DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -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 0.00000
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 0.00000
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 41.53200
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 41.53200
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 41.53200
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: 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 119.63600
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 207.21563
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -119.63600
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 207.21563
REMARK 350 BIOMT3 3 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 GLY A -5
REMARK 465 PRO A -4
REMARK 465 ALA A -3
REMARK 465 VAL A -2
REMARK 465 PRO A -1
REMARK 465 ARG A 0
REMARK 465 MET A 1
REMARK 465 ASN A 230
REMARK 465 GLU A 231
REMARK 465 ASP A 232
REMARK 465 ILE A 233
REMARK 465 THR A 234
REMARK 465 LEU A 235
REMARK 465 ASP A 236
REMARK 465 GLY A 237
REMARK 465 GLY A 238
REMARK 465 ASP A 239
REMARK 465 ASP A 240
REMARK 465 SER A 417
REMARK 465 PHE A 418
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 LEU A 3 CG CD1 CD2
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 LYS A 167 CD CE NZ
REMARK 470 LYS A 226 CD CE NZ
REMARK 470 GLN A 228 CG CD OE1 NE2
REMARK 470 ASP A 229 CG OD1 OD2
REMARK 470 TRP A 314 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 314 CZ3 CH2
REMARK 470 GLU A 345 CG CD OE1 OE2
REMARK 470 LEU A 416 CG CD1 CD2
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 ASN A 23 98.97 -163.04
REMARK 500 TYR A 48 -55.35 -122.19
REMARK 500 ILE A 184 -144.41 -118.12
REMARK 500 ALA A 330 -97.90 -139.03
REMARK 500 ALA A 346 32.30 -94.67
REMARK 500 ALA A 367 92.35 -67.49
REMARK 500 ALA A 383 79.37 -153.84
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 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 149 O
REMARK 620 2 ASN A 149 OD1 104.9
REMARK 620 3 VAL A 152 O 82.1 98.2
REMARK 620 4 SER A 183 OG 79.4 83.4 161.1
REMARK 620 5 ILE A 184 O 89.2 164.4 76.8 106.1
REMARK 620 6 HOH A 601 O 160.6 92.1 105.1 93.6 75.2
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 P0C A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TIJ RELATED DB: PDB
REMARK 900 3TIJ CONTAINS WILDTYPE VCCNT BOUND TO URIDINE
REMARK 900 RELATED ID: 4PB1 RELATED DB: PDB
REMARK 900 RELATED ID: 4PD5 RELATED DB: PDB
REMARK 900 RELATED ID: 4PD7 RELATED DB: PDB
REMARK 900 RELATED ID: 4PB2 RELATED DB: PDB
REMARK 900 RELATED ID: 4PD9 RELATED DB: PDB
REMARK 900 RELATED ID: 4PDA RELATED DB: PDB
DBREF 4PD8 A 1 418 UNP Q9KPL5 Q9KPL5_VIBCH 1 418
SEQADV 4PD8 GLY A -5 UNP Q9KPL5 EXPRESSION TAG
SEQADV 4PD8 PRO A -4 UNP Q9KPL5 EXPRESSION TAG
SEQADV 4PD8 ALA A -3 UNP Q9KPL5 EXPRESSION TAG
SEQADV 4PD8 VAL A -2 UNP Q9KPL5 EXPRESSION TAG
SEQADV 4PD8 PRO A -1 UNP Q9KPL5 EXPRESSION TAG
SEQADV 4PD8 ARG A 0 UNP Q9KPL5 EXPRESSION TAG
SEQADV 4PD8 CYS A 7 UNP Q9KPL5 LEU 7 ENGINEERED MUTATION
SEQADV 4PD8 CYS A 8 UNP Q9KPL5 ILE 8 ENGINEERED MUTATION
SEQRES 1 A 424 GLY PRO ALA VAL PRO ARG MET SER LEU PHE MET SER CYS
SEQRES 2 A 424 CYS GLY MET ALA VAL LEU LEU GLY ILE ALA VAL LEU LEU
SEQRES 3 A 424 SER SER ASN ARG LYS ALA ILE ASN LEU ARG THR VAL GLY
SEQRES 4 A 424 GLY ALA PHE ALA ILE GLN PHE SER LEU GLY ALA PHE ILE
SEQRES 5 A 424 LEU TYR VAL PRO TRP GLY GLN GLU LEU LEU ARG GLY PHE
SEQRES 6 A 424 SER ASP ALA VAL SER ASN VAL ILE ASN TYR GLY ASN ASP
SEQRES 7 A 424 GLY THR SER PHE LEU PHE GLY GLY LEU VAL SER GLY LYS
SEQRES 8 A 424 MET PHE GLU VAL PHE GLY GLY GLY GLY PHE ILE PHE ALA
SEQRES 9 A 424 PHE ARG VAL LEU PRO THR LEU ILE PHE PHE SER ALA LEU
SEQRES 10 A 424 ILE SER VAL LEU TYR TYR LEU GLY VAL MET GLN TRP VAL
SEQRES 11 A 424 ILE ARG ILE LEU GLY GLY GLY LEU GLN LYS ALA LEU GLY
SEQRES 12 A 424 THR SER ARG ALA GLU SER MET SER ALA ALA ALA ASN ILE
SEQRES 13 A 424 PHE VAL GLY GLN THR GLU ALA PRO LEU VAL VAL ARG PRO
SEQRES 14 A 424 PHE VAL PRO LYS MET THR GLN SER GLU LEU PHE ALA VAL
SEQRES 15 A 424 MET CYS GLY GLY LEU ALA SER ILE ALA GLY GLY VAL LEU
SEQRES 16 A 424 ALA GLY TYR ALA SER MET GLY VAL LYS ILE GLU TYR LEU
SEQRES 17 A 424 VAL ALA ALA SER PHE MET ALA ALA PRO GLY GLY LEU LEU
SEQRES 18 A 424 PHE ALA LYS LEU MET MET PRO GLU THR GLU LYS PRO GLN
SEQRES 19 A 424 ASP ASN GLU ASP ILE THR LEU ASP GLY GLY ASP ASP LYS
SEQRES 20 A 424 PRO ALA ASN VAL ILE ASP ALA ALA ALA GLY GLY ALA SER
SEQRES 21 A 424 ALA GLY LEU GLN LEU ALA LEU ASN VAL GLY ALA MET LEU
SEQRES 22 A 424 ILE ALA PHE ILE GLY LEU ILE ALA LEU ILE ASN GLY MET
SEQRES 23 A 424 LEU GLY GLY ILE GLY GLY TRP PHE GLY MET PRO GLU LEU
SEQRES 24 A 424 LYS LEU GLU MET LEU LEU GLY TRP LEU PHE ALA PRO LEU
SEQRES 25 A 424 ALA PHE LEU ILE GLY VAL PRO TRP ASN GLU ALA THR VAL
SEQRES 26 A 424 ALA GLY GLU PHE ILE GLY LEU LYS THR VAL ALA ASN GLU
SEQRES 27 A 424 PHE VAL ALA TYR SER GLN PHE ALA PRO TYR LEU THR GLU
SEQRES 28 A 424 ALA ALA PRO VAL VAL LEU SER GLU LYS THR LYS ALA ILE
SEQRES 29 A 424 ILE SER PHE ALA LEU CYS GLY PHE ALA ASN LEU SER SER
SEQRES 30 A 424 ILE ALA ILE LEU LEU GLY GLY LEU GLY SER LEU ALA PRO
SEQRES 31 A 424 LYS ARG ARG GLY ASP ILE ALA ARG MET GLY VAL LYS ALA
SEQRES 32 A 424 VAL ILE ALA GLY THR LEU SER ASN LEU MET ALA ALA THR
SEQRES 33 A 424 ILE ALA GLY PHE PHE LEU SER PHE
HET P0C A 501 20
HET NA A 502 1
HET DMU A 503 33
HETNAM P0C 6-METHYL-3-(BETA-D-RIBOFURANOSYL)-3,7-DIHYDRO-2H-
HETNAM 2 P0C PYRROLO[2,3-D]PYRIMIDIN-2-ONE
HETNAM NA SODIUM ION
HETNAM DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETSYN P0C 6-METHYL-3-(BETA-D-2-RIBOFURANOSYL)PYRROLO[2,3-D]
HETSYN 2 P0C PYRIMIDIN-2-ONE
HETSYN DMU DECYLMALTOSIDE
FORMUL 2 P0C C12 H15 N3 O5
FORMUL 3 NA NA 1+
FORMUL 4 DMU C22 H42 O11
FORMUL 5 HOH *3(H2 O)
HELIX 1 AA1 LEU A 3 LEU A 20 1 18
HELIX 2 AA2 ASN A 23 ILE A 27 5 5
HELIX 3 AA3 ASN A 28 TYR A 48 1 21
HELIX 4 AA4 VAL A 49 GLY A 79 1 31
HELIX 5 AA5 GLY A 80 SER A 83 5 4
HELIX 6 AA6 GLY A 84 GLY A 91 1 8
HELIX 7 AA7 GLY A 92 PHE A 95 5 4
HELIX 8 AA8 ILE A 96 VAL A 101 1 6
HELIX 9 AA9 VAL A 101 LEU A 118 1 18
HELIX 10 AB1 GLY A 119 GLY A 137 1 19
HELIX 11 AB2 SER A 139 ASN A 149 1 11
HELIX 12 AB3 GLU A 156 VAL A 165 5 10
HELIX 13 AB4 THR A 169 ALA A 182 1 14
HELIX 14 AB5 ALA A 185 SER A 194 1 10
HELIX 15 AB6 LYS A 198 MET A 208 1 11
HELIX 16 AB7 MET A 208 MET A 221 1 14
HELIX 17 AB8 ASN A 244 TRP A 287 1 44
HELIX 18 AB9 LYS A 294 ILE A 310 1 17
HELIX 19 AC1 PRO A 313 ASN A 315 5 3
HELIX 20 AC2 GLU A 316 ALA A 330 1 15
HELIX 21 AC3 ASN A 331 ALA A 340 1 10
HELIX 22 AC4 PRO A 341 THR A 344 5 4
HELIX 23 AC5 SER A 352 CYS A 364 1 13
HELIX 24 AC6 LEU A 369 ALA A 383 1 15
HELIX 25 AC7 ARG A 386 PHE A 415 1 30
LINK O ASN A 149 NA NA A 502 1555 1555 2.50
LINK OD1 ASN A 149 NA NA A 502 1555 1555 2.50
LINK O VAL A 152 NA NA A 502 1555 1555 2.44
LINK OG SER A 183 NA NA A 502 1555 1555 2.41
LINK O ILE A 184 NA NA A 502 1555 1555 2.34
LINK NA NA A 502 O HOH A 601 1555 1555 2.40
SITE 1 AC1 13 GLN A 154 ALA A 185 VAL A 188 TYR A 192
SITE 2 AC1 13 LEU A 259 GLU A 332 PHE A 333 PHE A 366
SITE 3 AC1 13 ASN A 368 SER A 371 ILE A 374 HOH A 602
SITE 4 AC1 13 HOH A 603
SITE 1 AC2 5 ASN A 149 VAL A 152 SER A 183 ILE A 184
SITE 2 AC2 5 HOH A 601
SITE 1 AC3 4 ALA A 243 ASN A 244 ILE A 372 ALA A 391
CRYST1 119.636 119.636 83.064 90.00 90.00 120.00 P 63 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 0.008359 0.004826 0.000000 0.00000
SCALE2 0.000000 0.009652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
