HEADER HYDROLASE 22-APR-11 3RN6
TITLE CRYSTAL STRUCTURE OF CYTOSINE DEAMINASE FROM ESCHERICHIA COLI
TITLE 2 COMPLEXED WITH ZINC AND ISOGUANINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOSINE DEAMINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOSINE AMINOHYDROLASE;
COMPND 5 EC: 3.5.4.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CODA, B0337, JW0328;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMIDOHYDROLASE FOLD, CYTOSINE DEAMINASE, ISOGUANINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,D.S.HITCHCOCK,F.M.RAUSHEL,S.C.ALMO
REVDAT 2 13-SEP-23 3RN6 1 REMARK LINK
REVDAT 1 24-AUG-11 3RN6 0
JRNL AUTH D.S.HITCHCOCK,A.A.FEDOROV,E.V.FEDOROV,L.J.DANGOTT,S.C.ALMO,
JRNL AUTH 2 F.M.RAUSHEL
JRNL TITL RESCUE OF THE ORPHAN ENZYME ISOGUANINE DEAMINASE.
JRNL REF BIOCHEMISTRY V. 50 5555 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21604715
JRNL DOI 10.1021/BI200680Y
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 36490
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1825
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 39.3134 - 5.2973 1.00 3020 146 0.1744 0.2132
REMARK 3 2 5.2973 - 4.2062 1.00 2905 163 0.1389 0.1726
REMARK 3 3 4.2062 - 3.6749 1.00 2864 177 0.1588 0.2017
REMARK 3 4 3.6749 - 3.3391 1.00 2870 157 0.1797 0.2464
REMARK 3 5 3.3391 - 3.0999 1.00 2885 139 0.2172 0.2363
REMARK 3 6 3.0999 - 2.9172 1.00 2880 136 0.2338 0.2607
REMARK 3 7 2.9172 - 2.7711 1.00 2831 166 0.2601 0.2786
REMARK 3 8 2.7711 - 2.6505 1.00 2882 157 0.2801 0.3036
REMARK 3 9 2.6505 - 2.5485 1.00 2822 154 0.3061 0.3549
REMARK 3 10 2.5485 - 2.4606 0.97 2761 146 0.3182 0.3379
REMARK 3 11 2.4606 - 2.3837 0.89 2548 128 0.3313 0.3616
REMARK 3 12 2.3837 - 2.3155 0.73 2093 93 0.3411 0.3878
REMARK 3 13 2.3155 - 2.2546 0.46 1304 63 0.3639 0.3986
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 37.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.63440
REMARK 3 B22 (A**2) : 3.63440
REMARK 3 B33 (A**2) : -7.26880
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 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 : 0.008 3424
REMARK 3 ANGLE : 1.091 4656
REMARK 3 CHIRALITY : 0.066 520
REMARK 3 PLANARITY : 0.005 605
REMARK 3 DIHEDRAL : 14.099 1256
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 3RN6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000065137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36490
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.255
REMARK 200 RESOLUTION RANGE LOW (A) : 39.307
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: BALBES
REMARK 200 STARTING MODEL: 3O7U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PENTAERYTHRITOL PROPOXYLATE, 0.05M
REMARK 280 HEPES, POTASSIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 73.59050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.48749
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 66.58233
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 73.59050
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 42.48749
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 66.58233
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 73.59050
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 42.48749
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.58233
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 73.59050
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 42.48749
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 66.58233
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 73.59050
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 42.48749
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 66.58233
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 73.59050
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 42.48749
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 66.58233
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 84.97499
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 133.16467
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 84.97499
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 133.16467
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 84.97499
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 133.16467
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 84.97499
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 133.16467
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 84.97499
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 133.16467
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 84.97499
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 133.16467
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A 429 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 ARG A 426
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 26 31.70 72.82
REMARK 500 ASN A 44 -15.35 81.28
REMARK 500 ASN A 76 89.53 -69.68
REMARK 500 ALA A 144 -32.51 -39.26
REMARK 500 ILE A 183 66.76 -152.50
REMARK 500 ILE A 218 140.82 -174.55
REMARK 500 HIS A 246 -74.68 77.22
REMARK 500 THR A 247 43.22 37.02
REMARK 500 THR A 288 -96.59 -100.22
REMARK 500 ASP A 313 -62.24 69.11
REMARK 500 LEU A 322 -168.38 -124.61
REMARK 500 THR A 354 -95.35 -124.14
REMARK 500 LEU A 416 -123.50 -87.00
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 ZN A 428 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 61 NE2
REMARK 620 2 HIS A 63 NE2 118.8
REMARK 620 3 HIS A 214 NE2 98.6 98.9
REMARK 620 4 HOH A 431 O 118.0 114.5 102.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 429 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 97 NE2
REMARK 620 2 GLU A 138 OE2 116.8
REMARK 620 3 GLU A 138 OE1 92.8 54.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PXN A 427
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 428
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 429
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IGA A 430
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O7U RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PHOSPHO-CYTOSINE
DBREF 3RN6 A 0 426 UNP P25524 CODA_ECOLI 1 427
SEQRES 1 A 427 MET SER ASN ASN ALA LEU GLN THR ILE ILE ASN ALA ARG
SEQRES 2 A 427 LEU PRO GLY GLU GLU GLY LEU TRP GLN ILE HIS LEU GLN
SEQRES 3 A 427 ASP GLY LYS ILE SER ALA ILE ASP ALA GLN SER GLY VAL
SEQRES 4 A 427 MET PRO ILE THR GLU ASN SER LEU ASP ALA GLU GLN GLY
SEQRES 5 A 427 LEU VAL ILE PRO PRO PHE VAL GLU PRO HIS ILE HIS LEU
SEQRES 6 A 427 ASP THR THR GLN THR ALA GLY GLN PRO ASN TRP ASN GLN
SEQRES 7 A 427 SER GLY THR LEU PHE GLU GLY ILE GLU ARG TRP ALA GLU
SEQRES 8 A 427 ARG LYS ALA LEU LEU THR HIS ASP ASP VAL LYS GLN ARG
SEQRES 9 A 427 ALA TRP GLN THR LEU LYS TRP GLN ILE ALA ASN GLY ILE
SEQRES 10 A 427 GLN HIS VAL ARG THR HIS VAL ASP VAL SER ASP ALA THR
SEQRES 11 A 427 LEU THR ALA LEU LYS ALA MET LEU GLU VAL LYS GLN GLU
SEQRES 12 A 427 VAL ALA PRO TRP ILE ASP LEU GLN ILE VAL ALA PHE PRO
SEQRES 13 A 427 GLN GLU GLY ILE LEU SER TYR PRO ASN GLY GLU ALA LEU
SEQRES 14 A 427 LEU GLU GLU ALA LEU ARG LEU GLY ALA ASP VAL VAL GLY
SEQRES 15 A 427 ALA ILE PRO HIS PHE GLU PHE THR ARG GLU TYR GLY VAL
SEQRES 16 A 427 GLU SER LEU HIS LYS THR PHE ALA LEU ALA GLN LYS TYR
SEQRES 17 A 427 ASP ARG LEU ILE ASP VAL HIS CYS ASP GLU ILE ASP ASP
SEQRES 18 A 427 GLU GLN SER ARG PHE VAL GLU THR VAL ALA ALA LEU ALA
SEQRES 19 A 427 HIS HIS GLU GLY MET GLY ALA ARG VAL THR ALA SER HIS
SEQRES 20 A 427 THR THR ALA MET HIS SER TYR ASN GLY ALA TYR THR SER
SEQRES 21 A 427 ARG LEU PHE ARG LEU LEU LYS MET SER GLY ILE ASN PHE
SEQRES 22 A 427 VAL ALA ASN PRO LEU VAL ASN ILE HIS LEU GLN GLY ARG
SEQRES 23 A 427 PHE ASP THR TYR PRO LYS ARG ARG GLY ILE THR ARG VAL
SEQRES 24 A 427 LYS GLU MET LEU GLU SER GLY ILE ASN VAL CYS PHE GLY
SEQRES 25 A 427 HIS ASP ASP VAL PHE ASP PRO TRP TYR PRO LEU GLY THR
SEQRES 26 A 427 ALA ASN MET LEU GLN VAL LEU HIS MET GLY LEU HIS VAL
SEQRES 27 A 427 CYS GLN LEU MET GLY TYR GLY GLN ILE ASN ASP GLY LEU
SEQRES 28 A 427 ASN LEU ILE THR HIS HIS SER ALA ARG THR LEU ASN LEU
SEQRES 29 A 427 GLN ASP TYR GLY ILE ALA ALA GLY ASN SER ALA ASN LEU
SEQRES 30 A 427 ILE ILE LEU PRO ALA GLU ASN GLY PHE ASP ALA LEU ARG
SEQRES 31 A 427 ARG GLN VAL PRO VAL ARG TYR SER VAL ARG GLY GLY LYS
SEQRES 32 A 427 VAL ILE ALA SER THR GLN PRO ALA GLN THR THR VAL TYR
SEQRES 33 A 427 LEU GLU GLN PRO GLU ALA ILE ASP TYR LYS ARG
HET PXN A 427 25
HET ZN A 428 1
HET ZN A 429 1
HET IGA A 430 11
HETNAM PXN (2S)-1-[3-{[(2R)-2-HYDROXYPROPYL]OXY}-2,2-BIS({[(2R)-2-
HETNAM 2 PXN HYDROXYPROPYL]OXY}METHYL)PROPOXY]PROPAN-2-OL
HETNAM ZN ZINC ION
HETNAM IGA 6-AMINO-3,7-DIHYDRO-2H-PURIN-2-ONE
HETSYN PXN PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH)
HETSYN IGA ISOGUANINE
FORMUL 2 PXN C17 H36 O8
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 IGA C5 H5 N5 O
FORMUL 6 HOH *78(H2 O)
HELIX 1 1 THR A 80 ALA A 93 1 14
HELIX 2 2 THR A 96 ASN A 114 1 19
HELIX 3 3 LEU A 130 ALA A 144 1 15
HELIX 4 4 ASN A 164 GLY A 176 1 13
HELIX 5 5 ILE A 183 GLU A 187 5 5
HELIX 6 6 THR A 189 TYR A 207 1 19
HELIX 7 7 PHE A 225 GLU A 236 1 12
HELIX 8 8 MET A 238 ALA A 240 5 3
HELIX 9 9 THR A 248 TYR A 253 5 6
HELIX 10 10 ASN A 254 GLY A 269 1 16
HELIX 11 11 ASN A 275 GLN A 283 1 9
HELIX 12 12 ARG A 297 GLY A 305 1 9
HELIX 13 13 ASN A 326 CYS A 338 1 13
HELIX 14 14 GLY A 342 ASP A 348 1 7
HELIX 15 15 GLY A 349 ILE A 353 5 5
HELIX 16 16 THR A 354 ASN A 362 1 9
HELIX 17 17 ASN A 383 GLN A 391 1 9
SHEET 1 A 7 ILE A 29 ALA A 34 0
SHEET 2 A 7 TRP A 20 LEU A 24 -1 N HIS A 23 O ALA A 31
SHEET 3 A 7 THR A 7 ARG A 12 -1 N ILE A 8 O ILE A 22
SHEET 4 A 7 SER A 45 ILE A 54 1 O ALA A 48 N ILE A 9
SHEET 5 A 7 LEU A 376 LEU A 379 -1 O LEU A 379 N LEU A 52
SHEET 6 A 7 TYR A 396 ARG A 399 -1 O VAL A 398 N LEU A 376
SHEET 7 A 7 LYS A 402 SER A 406 -1 O LYS A 402 N ARG A 399
SHEET 1 B 8 PHE A 57 ILE A 62 0
SHEET 2 B 8 ILE A 116 ASP A 124 1 O HIS A 122 N ILE A 62
SHEET 3 B 8 ASP A 148 PHE A 154 1 O GLN A 150 N VAL A 119
SHEET 4 B 8 VAL A 179 ALA A 182 1 O VAL A 179 N ALA A 153
SHEET 5 B 8 LEU A 210 CYS A 215 1 O ASP A 212 N VAL A 180
SHEET 6 B 8 VAL A 242 HIS A 246 1 O SER A 245 N VAL A 213
SHEET 7 B 8 ASN A 271 ALA A 274 1 O ASN A 271 N ALA A 244
SHEET 8 B 8 VAL A 308 PHE A 310 1 O CYS A 309 N ALA A 274
SHEET 1 C 2 THR A 412 TYR A 415 0
SHEET 2 C 2 PRO A 419 ILE A 422 -1 O GLU A 420 N VAL A 414
LINK NE2 HIS A 61 ZN ZN A 428 1555 1555 2.05
LINK NE2 HIS A 63 ZN ZN A 428 1555 1555 2.13
LINK NE2 HIS A 97 ZN ZN A 429 1555 1555 2.13
LINK OE2 GLU A 138 ZN ZN A 429 1555 1555 2.39
LINK OE1 GLU A 138 ZN ZN A 429 1555 1555 2.45
LINK NE2 HIS A 214 ZN ZN A 428 1555 1555 2.19
LINK ZN ZN A 428 O HOH A 431 1555 1555 2.13
CISPEP 1 GLN A 72 PRO A 73 0 -4.48
CISPEP 2 TYR A 289 PRO A 290 0 0.53
SITE 1 AC1 5 GLN A 102 TRP A 105 LYS A 109 GLU A 417
SITE 2 AC1 5 GLU A 420
SITE 1 AC2 6 HIS A 61 HIS A 63 HIS A 214 HIS A 246
SITE 2 AC2 6 ASP A 313 HOH A 431
SITE 1 AC3 2 HIS A 97 GLU A 138
SITE 1 AC4 8 HIS A 63 LEU A 81 GLN A 156 GLU A 217
SITE 2 AC4 8 ASP A 313 ASP A 314 TRP A 319 HOH A 431
CRYST1 147.181 147.181 199.747 90.00 90.00 120.00 H 3 2 18
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 0.006794 0.003923 0.000000 0.00000
SCALE2 0.000000 0.007845 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005006 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
