HEADER ISOMERASE 09-SEP-15 5DN1
TITLE CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ISOMERASE A FROM STREPTOMYCES
TITLE 2 COELICOLOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYL ISOMERASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)
COMPND 5 METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE,N-(5'-
COMPND 6 PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE,PRAI,PHOSPHORIBOSYLFORMIMINO-5-
COMPND 7 AMINOIMIDAZOLE CARBOXAMIDE RIBOTIDE ISOMERASE;
COMPND 8 EC: 5.3.1.16,5.3.1.24;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 100226;
SOURCE 4 STRAIN: ATCC BAA-471 / A3(2) / M145;
SOURCE 5 GENE: PRIA, HISA, SCO2050, SC4G6.19C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, HISTIDINE BIOSYNTHESIS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,E.A.VERDUZCO-CASTRO,M.ENDRES,F.BARONA-GOMEZ,A.JOACHIMIAK,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 3 06-MAR-24 5DN1 1 REMARK
REVDAT 2 08-NOV-17 5DN1 1 JRNL REMARK
REVDAT 1 30-SEP-15 5DN1 0
JRNL AUTH E.A.VERDUZCO-CASTRO,K.MICHALSKA,M.ENDRES,A.L.JUAREZ-VAZQUEZ,
JRNL AUTH 2 L.NODA-GARCIA,C.CHANG,C.S.HENRY,G.BABNIGG,A.JOACHIMIAK,
JRNL AUTH 3 F.BARONA-GOMEZ
JRNL TITL CO-OCCURRENCE OF ANALOGOUS ENZYMES DETERMINES EVOLUTION OF A
JRNL TITL 2 NOVEL ( BETA ALPHA )8-ISOMERASE SUB-FAMILY AFTER
JRNL TITL 3 NON-CONSERVED MUTATIONS IN FLEXIBLE LOOP.
JRNL REF BIOCHEM. J. V. 473 1141 2016
JRNL REFN ESSN 1470-8728
JRNL PMID 26929404
JRNL DOI 10.1042/BJ20151271
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 19184
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 985
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 38.3670 - 3.7345 1.00 2766 132 0.1471 0.1763
REMARK 3 2 3.7345 - 2.9646 1.00 2622 142 0.1346 0.1600
REMARK 3 3 2.9646 - 2.5899 1.00 2607 143 0.1556 0.1850
REMARK 3 4 2.5899 - 2.3532 1.00 2570 144 0.1550 0.2111
REMARK 3 5 2.3532 - 2.1845 1.00 2556 154 0.1487 0.2132
REMARK 3 6 2.1845 - 2.0557 1.00 2554 145 0.1545 0.2043
REMARK 3 7 2.0557 - 1.9528 0.98 2524 125 0.1656 0.2182
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 1838
REMARK 3 ANGLE : 0.980 2503
REMARK 3 CHIRALITY : 0.051 295
REMARK 3 PLANARITY : 0.004 324
REMARK 3 DIHEDRAL : 14.642 1089
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5049 49.6855 12.5881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1455 T22: 0.1661
REMARK 3 T33: 0.1286 T12: 0.0033
REMARK 3 T13: 0.0023 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.5048 L22: 1.4457
REMARK 3 L33: 0.5525 L12: -0.2625
REMARK 3 L13: 0.1948 L23: -0.3184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0047 S12: 0.0409 S13: 0.0046
REMARK 3 S21: 0.0520 S22: 0.0034 S23: -0.0459
REMARK 3 S31: 0.0003 S32: 0.0284 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0608 39.5136 6.3187
REMARK 3 T TENSOR
REMARK 3 T11: 0.1631 T22: 0.1916
REMARK 3 T33: 0.1278 T12: 0.0277
REMARK 3 T13: -0.0289 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 3.2426 L22: 3.2818
REMARK 3 L33: 3.2077 L12: 0.5433
REMARK 3 L13: -0.7665 L23: -1.2131
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: -0.2075 S13: 0.1481
REMARK 3 S21: 0.1317 S22: -0.1485 S23: -0.3167
REMARK 3 S31: -0.0826 S32: 0.3915 S33: 0.0848
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7085 49.8692 -2.9997
REMARK 3 T TENSOR
REMARK 3 T11: 0.1068 T22: 0.1267
REMARK 3 T33: 0.1116 T12: -0.0163
REMARK 3 T13: -0.0112 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.8179 L22: 3.0087
REMARK 3 L33: 1.3414 L12: -0.7429
REMARK 3 L13: -0.4697 L23: 0.3924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0286 S12: 0.0296 S13: 0.0832
REMARK 3 S21: 0.0473 S22: 0.0260 S23: -0.0926
REMARK 3 S31: -0.0781 S32: 0.0471 S33: 0.0110
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 5DN1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19264
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 : 6.500
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59100
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: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M SODIUM
REMARK 280 CACODYLATE, 2.0M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 34.84600
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 69.69200
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 69.69200
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 34.84600
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 OD2 ASP A 171 O HOH A 401 2.04
REMARK 500 O GLY A 23 N2 AMZ A 304 2.17
REMARK 500 O2 AMZ A 304 O HOH A 402 2.17
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 THR A 60 69.59 -106.37
REMARK 500 ARG A 162 145.38 -173.05
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMZ A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC111850 RELATED DB: TARGETTRACK
DBREF 5DN1 A 1 240 UNP P16250 HIS4_STRCO 1 240
SEQRES 1 A 240 MET SER LYS LEU GLU LEU LEU PRO ALA VAL ASP VAL ARG
SEQRES 2 A 240 ASP GLY GLN ALA VAL ARG LEU VAL HIS GLY GLU SER GLY
SEQRES 3 A 240 THR GLU THR SER TYR GLY SER PRO LEU GLU ALA ALA LEU
SEQRES 4 A 240 ALA TRP GLN ARG SER GLY ALA GLU TRP LEU HIS LEU VAL
SEQRES 5 A 240 ASP LEU ASP ALA ALA PHE GLY THR GLY ASP ASN ARG ALA
SEQRES 6 A 240 LEU ILE ALA GLU VAL ALA GLN ALA MET ASP ILE LYS VAL
SEQRES 7 A 240 GLU LEU SER GLY GLY ILE ARG ASP ASP ASP THR LEU ALA
SEQRES 8 A 240 ALA ALA LEU ALA THR GLY CYS THR ARG VAL ASN LEU GLY
SEQRES 9 A 240 THR ALA ALA LEU GLU THR PRO GLU TRP VAL ALA LYS VAL
SEQRES 10 A 240 ILE ALA GLU HIS GLY ASP LYS ILE ALA VAL GLY LEU ASP
SEQRES 11 A 240 VAL ARG GLY THR THR LEU ARG GLY ARG GLY TRP THR ARG
SEQRES 12 A 240 ASP GLY GLY ASP LEU TYR GLU THR LEU ASP ARG LEU ASN
SEQRES 13 A 240 LYS GLU GLY CYS ALA ARG TYR VAL VAL THR ASP ILE ALA
SEQRES 14 A 240 LYS ASP GLY THR LEU GLN GLY PRO ASN LEU GLU LEU LEU
SEQRES 15 A 240 LYS ASN VAL CYS ALA ALA THR ASP ARG PRO VAL VAL ALA
SEQRES 16 A 240 SER GLY GLY VAL SER SER LEU ASP ASP LEU ARG ALA ILE
SEQRES 17 A 240 ALA GLY LEU VAL PRO ALA GLY VAL GLU GLY ALA ILE VAL
SEQRES 18 A 240 GLY LYS ALA LEU TYR ALA LYS ALA PHE THR LEU GLU GLU
SEQRES 19 A 240 ALA LEU GLU ALA THR SER
HET SO4 A 301 5
HET SO4 A 302 5
HET GOL A 303 6
HET AMZ A 304 22
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM AMZ AMINOIMIDAZOLE 4-CARBOXAMIDE RIBONUCLEOTIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN AMZ AICAR
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 AMZ C9 H15 N4 O8 P
FORMUL 6 HOH *254(H2 O)
HELIX 1 AA1 SER A 33 SER A 44 1 12
HELIX 2 AA2 LEU A 54 GLY A 59 1 6
HELIX 3 AA3 ASN A 63 MET A 74 1 12
HELIX 4 AA4 ASP A 86 THR A 96 1 11
HELIX 5 AA5 GLY A 104 THR A 110 1 7
HELIX 6 AA6 THR A 110 GLY A 122 1 13
HELIX 7 AA7 LEU A 148 GLU A 158 1 11
HELIX 8 AA8 ASN A 178 ALA A 188 1 11
HELIX 9 AA9 SER A 201 GLY A 210 1 10
HELIX 10 AB1 GLY A 222 ALA A 227 1 6
HELIX 11 AB2 THR A 231 THR A 239 1 9
SHEET 1 AA1 9 THR A 29 SER A 30 0
SHEET 2 AA1 9 GLN A 16 ARG A 19 -1 N ARG A 19 O THR A 29
SHEET 3 AA1 9 GLU A 5 ARG A 13 -1 N ASP A 11 O VAL A 18
SHEET 4 AA1 9 TRP A 48 ASP A 53 1 O HIS A 50 N VAL A 10
SHEET 5 AA1 9 LYS A 77 SER A 81 1 O GLU A 79 N LEU A 51
SHEET 6 AA1 9 ARG A 100 LEU A 103 1 O ASN A 102 N LEU A 80
SHEET 7 AA1 9 ILE A 125 ARG A 132 1 O GLY A 128 N LEU A 103
SHEET 8 AA1 9 THR A 135 GLY A 138 -1 O THR A 135 N ARG A 132
SHEET 9 AA1 9 ARG A 143 ASP A 147 -1 O ARG A 143 N GLY A 138
SHEET 1 AA2 9 THR A 29 SER A 30 0
SHEET 2 AA2 9 GLN A 16 ARG A 19 -1 N ARG A 19 O THR A 29
SHEET 3 AA2 9 GLU A 5 ARG A 13 -1 N ASP A 11 O VAL A 18
SHEET 4 AA2 9 VAL A 216 VAL A 221 1 O ALA A 219 N LEU A 7
SHEET 5 AA2 9 VAL A 193 SER A 196 1 N ALA A 195 O ILE A 220
SHEET 6 AA2 9 TYR A 163 ASP A 167 1 N TYR A 163 O VAL A 194
SHEET 7 AA2 9 ILE A 125 ARG A 132 1 N LEU A 129 O VAL A 164
SHEET 8 AA2 9 THR A 135 GLY A 138 -1 O THR A 135 N ARG A 132
SHEET 9 AA2 9 ARG A 143 ASP A 147 -1 O ARG A 143 N GLY A 138
SITE 1 AC1 10 ARG A 19 ASP A 171 GLY A 172 GLY A 197
SITE 2 AC1 10 GLY A 198 GLY A 222 LYS A 223 HOH A 419
SITE 3 AC1 10 HOH A 481 HOH A 496
SITE 1 AC2 6 LEU A 66 GLU A 69 TYR A 149 GLU A 150
SITE 2 AC2 6 ASP A 153 HOH A 525
SITE 1 AC3 9 VAL A 165 ASP A 167 PRO A 177 ASN A 178
SITE 2 AC3 9 LEU A 181 LEU A 182 SER A 196 GLY A 197
SITE 3 AC3 9 HOH A 487
SITE 1 AC4 16 LEU A 20 GLY A 23 LEU A 54 PHE A 58
SITE 2 AC4 16 SER A 81 GLY A 83 ARG A 85 GLY A 104
SITE 3 AC4 16 THR A 105 ASP A 130 GLY A 140 HOH A 402
SITE 4 AC4 16 HOH A 405 HOH A 410 HOH A 425 HOH A 453
CRYST1 65.208 65.208 104.538 90.00 90.00 120.00 P 31 2 1 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 0.015336 0.008854 0.000000 0.00000
SCALE2 0.000000 0.017708 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009566 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
