HEADER MEMBRANE PROTEIN 30-OCT-18 6I1R
TITLE CRYSTAL STRUCTURE OF CMP BOUND CST IN AN OUTWARD FACING CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CMP-SIALIC ACID TRANSPORTER 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577;
SOURCE 5 GENE: 100274139, ZEAMMB73_ZM00001D046060;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS CMP-SIALIC ACID TRANSPORTER, SECONDARY ACTIVE TRANSPORTER, NUCLEOTIDE
KEYWDS 2 SUGAR TRANSPORTER, SLC35A1, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.NJI,A.GULATI,A.A.QURESHI,D.DREW
REVDAT 3 24-JAN-24 6I1R 1 REMARK
REVDAT 2 19-JUN-19 6I1R 1 JRNL
REVDAT 1 05-JUN-19 6I1R 0
JRNL AUTH E.NJI,A.GULATI,A.A.QURESHI,M.COINCON,D.DREW
JRNL TITL STRUCTURAL BASIS FOR THE DELIVERY OF ACTIVATED SIALIC ACID
JRNL TITL 2 INTO GOLGI FOR SIALYATION.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 26 415 2019
JRNL REFN ESSN 1545-9985
JRNL PMID 31133698
JRNL DOI 10.1038/S41594-019-0225-Y
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19661
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 + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1048
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4817
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 5.588
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.360
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.225
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.686
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6I1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012661.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20716
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.18500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.94400
REMARK 200 R SYM FOR SHELL (I) : 1.94400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
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: 5I20
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 400 MM AMMONIUM SULFATE, 100 MM
REMARK 280 LITHIUM SULFATE, 100 MM NACL, 100 MM SODIUM CITRATE, 30% PEG 300,
REMARK 280 TERT BUTANOL AND 1.2 MM CMP, PH 5, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.68950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.50450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.68950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 90.50450
REMARK 290 SMTRY3 4 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 ASN A 27
REMARK 465 GLY A 28
REMARK 465 LYS A 29
REMARK 465 TYR A 30
REMARK 465 PRO A 314
REMARK 465 GLN A 315
REMARK 465 THR A 316
REMARK 465 LEU A 317
REMARK 465 PRO A 318
REMARK 465 VAL A 319
REMARK 465 THR A 320
REMARK 465 SER A 321
REMARK 465 LYS A 322
REMARK 465 GLY B 28
REMARK 465 LYS B 29
REMARK 465 TYR B 30
REMARK 465 PRO B 314
REMARK 465 GLN B 315
REMARK 465 THR B 316
REMARK 465 LEU B 317
REMARK 465 PRO B 318
REMARK 465 VAL B 319
REMARK 465 THR B 320
REMARK 465 SER B 321
REMARK 465 LYS B 322
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 MET A 1 CG SD CE
REMARK 470 GLN A 2 CG CD OE1 NE2
REMARK 470 ARG A 58 CG CD NE CZ NH1 NH2
REMARK 470 THR A 59 OG1 CG2
REMARK 470 SER A 60 OG
REMARK 470 LYS A 67 CG CD CE NZ
REMARK 470 GLN A 102 CG CD OE1 NE2
REMARK 470 VAL A 119 CG1 CG2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 SER A 150 OG
REMARK 470 ASP A 153 CG OD1 OD2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 TYR A 279 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 284 CG CD CE NZ
REMARK 470 PHE A 290 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 309 CG SD CE
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 LEU A 313 CG CD1 CD2
REMARK 470 MET B 1 CG SD CE
REMARK 470 GLN B 25 CG CD OE1 NE2
REMARK 470 ASN B 27 CG OD1 ND2
REMARK 470 THR B 59 OG1 CG2
REMARK 470 LYS B 67 CG CD CE NZ
REMARK 470 ARG B 70 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 102 CG CD OE1 NE2
REMARK 470 VAL B 119 CG1 CG2
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 LYS B 216 CG CD CE NZ
REMARK 470 TYR B 279 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE B 281 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 284 CG CD CE NZ
REMARK 470 LEU B 313 CG CD1 CD2
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 OE1 GLN B 2 CE1 TYR B 4 1.95
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 GLN A 25 47.82 -76.50
REMARK 500 SER A 154 106.87 -58.10
REMARK 500 PHE A 156 -2.04 71.51
REMARK 500 SER A 257 -134.81 -147.13
REMARK 500 LEU A 280 -63.91 -103.86
REMARK 500 GLN B 25 30.54 -72.64
REMARK 500 SER B 154 106.74 -58.14
REMARK 500 PHE B 156 -2.24 71.50
REMARK 500 SER B 257 -138.98 -147.47
REMARK 500 LEU B 280 -64.61 -104.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 73 0.16 SIDE CHAIN
REMARK 500 ARG A 117 0.26 SIDE CHAIN
REMARK 500 ARG B 58 0.21 SIDE CHAIN
REMARK 500 ARG B 73 0.09 SIDE CHAIN
REMARK 500 ARG B 117 0.22 SIDE CHAIN
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 C5P A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C5P B 401
DBREF 6I1R A 1 322 UNP B4FZ94 B4FZ94_MAIZE 1 322
DBREF 6I1R B 1 322 UNP B4FZ94 B4FZ94_MAIZE 1 322
SEQADV 6I1R ARG A 58 UNP B4FZ94 HIS 58 ENGINEERED MUTATION
SEQADV 6I1R THR A 59 UNP B4FZ94 SER 59 ENGINEERED MUTATION
SEQADV 6I1R PRO A 61 UNP B4FZ94 SER 61 ENGINEERED MUTATION
SEQADV 6I1R SER A 62 UNP B4FZ94 PRO 62 ENGINEERED MUTATION
SEQADV 6I1R VAL A 63 UNP B4FZ94 PRO 63 ENGINEERED MUTATION
SEQADV 6I1R ARG B 58 UNP B4FZ94 HIS 58 ENGINEERED MUTATION
SEQADV 6I1R THR B 59 UNP B4FZ94 SER 59 ENGINEERED MUTATION
SEQADV 6I1R PRO B 61 UNP B4FZ94 SER 61 ENGINEERED MUTATION
SEQADV 6I1R SER B 62 UNP B4FZ94 PRO 62 ENGINEERED MUTATION
SEQADV 6I1R VAL B 63 UNP B4FZ94 PRO 63 ENGINEERED MUTATION
SEQRES 1 A 322 MET GLN TRP TYR LEU VAL ALA ALA LEU LEU THR ILE LEU
SEQRES 2 A 322 THR SER SER GLN GLY ILE LEU THR THR LEU SER GLN SER
SEQRES 3 A 322 ASN GLY LYS TYR ASN TYR ASP TYR ALA THR ILE PRO PHE
SEQRES 4 A 322 LEU ALA GLU LEU PHE LYS LEU SER VAL SER GLY PHE PHE
SEQRES 5 A 322 LEU TRP LYS GLU CYS ARG THR SER PRO SER VAL ARG MET
SEQRES 6 A 322 THR LYS GLU TRP ARG SER VAL ARG LEU TYR VAL VAL PRO
SEQRES 7 A 322 SER VAL ILE TYR LEU ILE HIS ASN ASN VAL GLN PHE ALA
SEQRES 8 A 322 THR LEU THR TYR VAL ASP PRO SER THR TYR GLN ILE MET
SEQRES 9 A 322 GLY ASN LEU LYS ILE VAL THR THR GLY ILE LEU PHE ARG
SEQRES 10 A 322 LEU VAL LEU LYS ARG LYS LEU SER ASN ILE GLN TRP MET
SEQRES 11 A 322 ALA ILE VAL LEU LEU ALA VAL GLY THR THR THR SER GLN
SEQRES 12 A 322 VAL LYS GLY CYS GLY ASP SER PRO CYS ASP SER LEU PHE
SEQRES 13 A 322 SER ALA PRO LEU GLU GLY TYR LEU LEU GLY ILE LEU SER
SEQRES 14 A 322 ALA CYS LEU SER ALA LEU ALA GLY VAL TYR THR GLU TYR
SEQRES 15 A 322 LEU MET LYS LYS ASN ASN ASP SER LEU TYR TRP GLN ASN
SEQRES 16 A 322 VAL GLN LEU TYR THR PHE GLY VAL ILE PHE ASN MET GLY
SEQRES 17 A 322 TRP LEU ILE TYR GLY ASP PHE LYS ALA GLY PHE GLU LEU
SEQRES 18 A 322 GLY PRO TRP TRP GLN ARG LEU PHE ASN GLY TYR SER ILE
SEQRES 19 A 322 THR THR TRP MET VAL VAL PHE ASN LEU GLY SER THR GLY
SEQRES 20 A 322 LEU LEU VAL SER TRP LEU MET LYS TYR SER ASP ASN ILE
SEQRES 21 A 322 VAL LYS VAL TYR SER THR SER MET ALA MET LEU LEU THR
SEQRES 22 A 322 MET VAL LEU SER ILE TYR LEU PHE SER VAL LYS ALA THR
SEQRES 23 A 322 ILE GLN LEU PHE LEU GLY ILE ILE ILE CYS ILE ILE SER
SEQRES 24 A 322 LEU GLN MET TYR PHE MET PRO VAL HIS MET LEU ILE GLU
SEQRES 25 A 322 LEU PRO GLN THR LEU PRO VAL THR SER LYS
SEQRES 1 B 322 MET GLN TRP TYR LEU VAL ALA ALA LEU LEU THR ILE LEU
SEQRES 2 B 322 THR SER SER GLN GLY ILE LEU THR THR LEU SER GLN SER
SEQRES 3 B 322 ASN GLY LYS TYR ASN TYR ASP TYR ALA THR ILE PRO PHE
SEQRES 4 B 322 LEU ALA GLU LEU PHE LYS LEU SER VAL SER GLY PHE PHE
SEQRES 5 B 322 LEU TRP LYS GLU CYS ARG THR SER PRO SER VAL ARG MET
SEQRES 6 B 322 THR LYS GLU TRP ARG SER VAL ARG LEU TYR VAL VAL PRO
SEQRES 7 B 322 SER VAL ILE TYR LEU ILE HIS ASN ASN VAL GLN PHE ALA
SEQRES 8 B 322 THR LEU THR TYR VAL ASP PRO SER THR TYR GLN ILE MET
SEQRES 9 B 322 GLY ASN LEU LYS ILE VAL THR THR GLY ILE LEU PHE ARG
SEQRES 10 B 322 LEU VAL LEU LYS ARG LYS LEU SER ASN ILE GLN TRP MET
SEQRES 11 B 322 ALA ILE VAL LEU LEU ALA VAL GLY THR THR THR SER GLN
SEQRES 12 B 322 VAL LYS GLY CYS GLY ASP SER PRO CYS ASP SER LEU PHE
SEQRES 13 B 322 SER ALA PRO LEU GLU GLY TYR LEU LEU GLY ILE LEU SER
SEQRES 14 B 322 ALA CYS LEU SER ALA LEU ALA GLY VAL TYR THR GLU TYR
SEQRES 15 B 322 LEU MET LYS LYS ASN ASN ASP SER LEU TYR TRP GLN ASN
SEQRES 16 B 322 VAL GLN LEU TYR THR PHE GLY VAL ILE PHE ASN MET GLY
SEQRES 17 B 322 TRP LEU ILE TYR GLY ASP PHE LYS ALA GLY PHE GLU LEU
SEQRES 18 B 322 GLY PRO TRP TRP GLN ARG LEU PHE ASN GLY TYR SER ILE
SEQRES 19 B 322 THR THR TRP MET VAL VAL PHE ASN LEU GLY SER THR GLY
SEQRES 20 B 322 LEU LEU VAL SER TRP LEU MET LYS TYR SER ASP ASN ILE
SEQRES 21 B 322 VAL LYS VAL TYR SER THR SER MET ALA MET LEU LEU THR
SEQRES 22 B 322 MET VAL LEU SER ILE TYR LEU PHE SER VAL LYS ALA THR
SEQRES 23 B 322 ILE GLN LEU PHE LEU GLY ILE ILE ILE CYS ILE ILE SER
SEQRES 24 B 322 LEU GLN MET TYR PHE MET PRO VAL HIS MET LEU ILE GLU
SEQRES 25 B 322 LEU PRO GLN THR LEU PRO VAL THR SER LYS
HET C5P A 401 21
HET C5P B 401 21
HETNAM C5P CYTIDINE-5'-MONOPHOSPHATE
FORMUL 3 C5P 2(C9 H14 N3 O8 P)
FORMUL 5 HOH *38(H2 O)
HELIX 1 AA1 GLN A 2 GLN A 25 1 24
HELIX 2 AA2 THR A 36 SER A 60 1 25
HELIX 3 AA3 GLU A 68 ARG A 73 1 6
HELIX 4 AA4 TYR A 75 LEU A 93 1 19
HELIX 5 AA5 ASP A 97 GLY A 105 1 9
HELIX 6 AA6 LEU A 107 VAL A 119 1 13
HELIX 7 AA7 SER A 125 VAL A 144 1 20
HELIX 8 AA8 PRO A 159 LYS A 186 1 28
HELIX 9 AA9 SER A 190 ALA A 217 1 28
HELIX 10 AB1 PRO A 223 LEU A 228 1 6
HELIX 11 AB2 SER A 233 SER A 257 1 25
HELIX 12 AB3 ASP A 258 LEU A 280 1 23
HELIX 13 AB4 THR A 286 MET A 305 1 20
HELIX 14 AB5 GLN B 2 GLN B 25 1 24
HELIX 15 AB6 THR B 36 SER B 60 1 25
HELIX 16 AB7 GLU B 68 ARG B 73 1 6
HELIX 17 AB8 TYR B 75 LEU B 93 1 19
HELIX 18 AB9 ASP B 97 GLY B 105 1 9
HELIX 19 AC1 LEU B 107 VAL B 119 1 13
HELIX 20 AC2 SER B 125 VAL B 144 1 20
HELIX 21 AC3 PRO B 159 ASN B 187 1 29
HELIX 22 AC4 SER B 190 ALA B 217 1 28
HELIX 23 AC5 PRO B 223 LEU B 228 1 6
HELIX 24 AC6 SER B 233 SER B 257 1 25
HELIX 25 AC7 ASP B 258 LEU B 280 1 23
HELIX 26 AC8 THR B 286 MET B 305 1 20
SITE 1 AC1 10 PRO A 38 GLU A 42 SER A 79 TYR A 82
SITE 2 AC1 10 LEU A 83 ASN A 86 PHE A 205 ASN A 206
SITE 3 AC1 10 TRP A 209 HOH A 508
SITE 1 AC2 11 PRO B 38 GLU B 42 SER B 79 TYR B 82
SITE 2 AC2 11 LEU B 83 ASN B 86 PHE B 205 ASN B 206
SITE 3 AC2 11 TRP B 209 HOH B 502 HOH B 507
CRYST1 89.379 181.009 53.081 90.00 90.00 90.00 C 1 2 1 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 0.011188 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005525 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018839 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.999959 -0.000490 0.009094 -45.02789 1
MTRIX2 2 0.000581 -0.999950 0.010026 -89.76479 1
MTRIX3 2 0.009089 0.010031 0.999908 0.61438 1
(ATOM LINES ARE NOT SHOWN.)
END
