HEADER HYDROLASE 21-NOV-08 3FCI
TITLE COMPLEX OF UNG2 AND A FRAGMENT-BASED DESIGNED INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URACIL-DNA GLYCOSYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UDG;
COMPND 5 EC: 3.2.2.-;
COMPND 6 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: UNG, DGU, UNG1, UNG15;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA REPAIR, URACIL, URACIL DNA GLYCOSYLASE, ALTERNATIVE SPLICING,
KEYWDS 2 DISEASE MUTATION, DNA DAMAGE, GLYCOSIDASE, HOST-VIRUS INTERACTION,
KEYWDS 3 HYDROLASE, MITOCHONDRION, NUCLEUS, PHOSPHOPROTEIN, TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.BIANCHET,S.CHUNG,J.B.PARKER,L.M.AMZEL,J.T.STIVERS
REVDAT 4 27-DEC-23 3FCI 1 REMARK SEQADV
REVDAT 3 01-NOV-17 3FCI 1 REMARK
REVDAT 2 02-JUN-09 3FCI 1 JRNL
REVDAT 1 28-APR-09 3FCI 0
JRNL AUTH S.CHUNG,J.B.PARKER,M.BIANCHET,L.M.AMZEL,J.T.STIVERS
JRNL TITL IMPACT OF LINKER STRAIN AND FLEXIBILITY IN THE DESIGN OF A
JRNL TITL 2 FRAGMENT-BASED INHIBITOR
JRNL REF NAT.CHEM.BIOL. V. 5 407 2009
JRNL REFN ISSN 1552-4450
JRNL PMID 19396178
JRNL DOI 10.1038/NCHEMBIO.163
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.L.JIANG,D.J.KROSKY,L.SEIPLE,J.T.STIVERS
REMARK 1 TITL URACIL-DIRECTED LIGAND TETHERING: AN EFFICIENT STRATEGY FOR
REMARK 1 TITL 2 URACIL DNA GLYCOSYLASE (UNG) INHIBITOR DEVELOPMENT
REMARK 1 REF J.AM.CHEM.SOC. V. 127 17412 2005
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.J.KROSKY,M.A.BIANCHET,L.SEIPLE,S.CHUNG,L.M.AMZEL,
REMARK 1 AUTH 2 J.T.STIVERS
REMARK 1 TITL MIMICKING DAMAGED DNA WITH A SMALL MOLECULE INHIBITOR OF
REMARK 1 TITL 2 HUMAN UNG2.
REMARK 1 REF NUCLEIC ACIDS RES. V. 34 5872 2006
REMARK 1 REFN ISSN 0305-1048
REMARK 2
REMARK 2 RESOLUTION. 1.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.9
REMARK 3 NUMBER OF REFLECTIONS : 45025
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2283
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 465
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 12.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3840
REMARK 3 BIN FREE R VALUE SET COUNT : 22
REMARK 3 BIN FREE R VALUE : 0.4940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1808
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 495
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.067
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.035
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.771
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1923 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2606 ; 1.441 ; 2.057
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 226 ; 5.686 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;38.289 ;23.736
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 310 ;12.718 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;21.581 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 259 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1504 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1003 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1267 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 380 ; 0.158 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.035 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 68 ; 0.204 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 74 ; 0.147 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1124 ; 0.651 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1818 ; 1.200 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 843 ; 1.885 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 788 ; 3.032 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3FCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45064
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
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 (%) : 81.0
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.05600
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) : 1.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 16.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.27500
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITER OF THE SOLUTION: 0.001 M
REMARK 280 UNG2 0.05 M TRIS-OAC PH 7.0 0.15 M NACL 0.001 M DTT 0.005 M
REMARK 280 INHIBITOR, WAS MIXED WITH EQUAL AMOUNT OF THE SOLUTION
REMARK 280 CONTAINING 0.16 M KSCN AND 22% PEG 3350 , VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K, PH 8.0
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 21.50700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.83700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.23800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.83700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.50700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.23800
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: 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 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 OH TYR A 248 O HOH A 65 1.72
REMARK 500 CZ TYR A 248 O HOH A 65 1.79
REMARK 500 O HOH A 479 O HOH A 572 2.19
REMARK 500 O HOH A 481 O HOH A 537 2.19
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 144 -77.53 -111.06
REMARK 500 HIS A 154 17.98 -140.06
REMARK 500 PHE A 158 -13.49 75.73
REMARK 500 LEU A 202 77.64 -105.24
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 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 111 OE2
REMARK 620 2 HOH A 513 O 113.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FI A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FCF RELATED DB: PDB
REMARK 900 RELATED ID: 3FCK RELATED DB: PDB
REMARK 900 RELATED ID: 3FCL RELATED DB: PDB
DBREF 3FCI A 85 304 UNP P13051 UNG_HUMAN 94 313
SEQADV 3FCI MET A 82 UNP P13051 INSERTION
SEQADV 3FCI GLU A 83 UNP P13051 INSERTION
SEQADV 3FCI PHE A 84 UNP P13051 INSERTION
SEQRES 1 A 223 MET GLU PHE PHE GLY GLU SER TRP LYS LYS HIS LEU SER
SEQRES 2 A 223 GLY GLU PHE GLY LYS PRO TYR PHE ILE LYS LEU MET GLY
SEQRES 3 A 223 PHE VAL ALA GLU GLU ARG LYS HIS TYR THR VAL TYR PRO
SEQRES 4 A 223 PRO PRO HIS GLN VAL PHE THR TRP THR GLN MET CYS ASP
SEQRES 5 A 223 ILE LYS ASP VAL LYS VAL VAL ILE LEU GLY GLN ASP PRO
SEQRES 6 A 223 TYR HIS GLY PRO ASN GLN ALA HIS GLY LEU CYS PHE SER
SEQRES 7 A 223 VAL GLN ARG PRO VAL PRO PRO PRO PRO SER LEU GLU ASN
SEQRES 8 A 223 ILE TYR LYS GLU LEU SER THR ASP ILE GLU ASP PHE VAL
SEQRES 9 A 223 HIS PRO GLY HIS GLY ASP LEU SER GLY TRP ALA LYS GLN
SEQRES 10 A 223 GLY VAL LEU LEU LEU ASN ALA VAL LEU THR VAL ARG ALA
SEQRES 11 A 223 HIS GLN ALA ASN SER HIS LYS GLU ARG GLY TRP GLU GLN
SEQRES 12 A 223 PHE THR ASP ALA VAL VAL SER TRP LEU ASN GLN ASN SER
SEQRES 13 A 223 ASN GLY LEU VAL PHE LEU LEU TRP GLY SER TYR ALA GLN
SEQRES 14 A 223 LYS LYS GLY SER ALA ILE ASP ARG LYS ARG HIS HIS VAL
SEQRES 15 A 223 LEU GLN THR ALA HIS PRO SER PRO LEU SER VAL TYR ARG
SEQRES 16 A 223 GLY PHE PHE GLY CYS ARG HIS PHE SER LYS THR ASN GLU
SEQRES 17 A 223 LEU LEU GLN LYS SER GLY LYS LYS PRO ILE ASP TRP LYS
SEQRES 18 A 223 GLU LEU
HET 3FI A 1 25
HET NA A 305 1
HET SCN A 2 3
HET SCN A 3 3
HETNAM 3FI 3-{(E)-[(3-{[(2,6-DIOXO-1,2,3,6-TETRAHYDROPYRIMIDIN-4-
HETNAM 2 3FI YL)METHYL]AMINO}PROPOXY)IMINO]METHYL}BENZOIC ACID
HETNAM NA SODIUM ION
HETNAM SCN THIOCYANATE ION
FORMUL 2 3FI C16 H18 N4 O5
FORMUL 3 NA NA 1+
FORMUL 4 SCN 2(C N S 1-)
FORMUL 6 HOH *495(H2 O)
HELIX 1 1 GLY A 86 SER A 94 1 9
HELIX 2 2 GLY A 95 PHE A 97 5 3
HELIX 3 3 LYS A 99 TYR A 116 1 18
HELIX 4 4 PRO A 121 VAL A 125 5 5
HELIX 5 5 PHE A 126 GLN A 130 5 5
HELIX 6 6 ASP A 133 VAL A 137 5 5
HELIX 7 7 PRO A 167 ILE A 181 1 15
HELIX 8 8 LEU A 192 LYS A 197 1 6
HELIX 9 9 GLY A 221 SER A 237 1 17
HELIX 10 10 GLY A 246 GLY A 253 1 8
HELIX 11 11 SER A 273 GLY A 277 5 5
HELIX 12 12 ARG A 282 SER A 294 1 13
SHEET 1 A 2 VAL A 118 TYR A 119 0
SHEET 2 A 2 VAL A 209 ARG A 210 -1 O VAL A 209 N TYR A 119
SHEET 1 B 4 VAL A 200 ASN A 204 0
SHEET 2 B 4 VAL A 139 GLY A 143 1 N VAL A 139 O LEU A 201
SHEET 3 B 4 VAL A 241 TRP A 245 1 O LEU A 243 N VAL A 140
SHEET 4 B 4 HIS A 262 THR A 266 1 O LEU A 264 N PHE A 242
LINK OE2 GLU A 111 NA NA A 305 1555 1555 2.37
LINK NA NA A 305 O HOH A 513 1555 1555 2.66
CISPEP 1 TYR A 119 PRO A 120 0 -11.50
CISPEP 2 ARG A 162 PRO A 163 0 1.96
SITE 1 AC1 19 HOH A 75 HOH A 79 GLY A 143 GLN A 144
SITE 2 AC1 19 ASP A 145 TYR A 147 CYS A 157 PHE A 158
SITE 3 AC1 19 ASN A 204 GLY A 246 SER A 247 TYR A 248
SITE 4 AC1 19 HIS A 268 SER A 273 LYS A 293 HOH A 497
SITE 5 AC1 19 HOH A 598 HOH A 648 HOH A 704
SITE 1 AC2 4 GLU A 111 LYS A 114 HOH A 513 HOH A 583
SITE 1 AC3 3 VAL A 109 ARG A 113 HOH A 563
SITE 1 AC4 6 PRO A 100 TYR A 101 GLN A 224 LYS A 297
SITE 2 AC4 6 HOH A 494 HOH A 561
CRYST1 43.014 68.476 69.674 90.00 90.00 90.00 P 21 21 21 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 0.023248 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014604 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
