HEADER HYDROLASE/HYDROLASE INHIBITOR 16-DEC-15 5FDD
TITLE ENDONUCLEASE INHIBITOR 1 BOUND TO INFLUENZA STRAIN H1N1 POLYMERASE
TITLE 2 ACIDIC SUBUNIT N-TERMINAL REGION AT PH 7.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYMERASE ACIDIC PROTEIN,POLYMERASE ACIDIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENDONUCLEASE, RESIDUES 1-50, 73-196;
COMPND 5 SYNONYM: RNA-DIRECTED RNA POLYMERASE SUBUNIT P2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 211044;
SOURCE 4 STRAIN: A/PUERTO RICO/8/1934 H1N1;
SOURCE 5 GENE: PA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET50B(+)
KEYWDS HYDROLASE/INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.FUDO,N.YAMAMOTO,M.NUKAGA,T.ODAGIRI,M.TASHIRO,T.HOSHINO
REVDAT 4 08-NOV-23 5FDD 1 REMARK
REVDAT 3 19-FEB-20 5FDD 1 JRNL REMARK
REVDAT 2 25-MAY-16 5FDD 1 JRNL
REVDAT 1 30-DEC-15 5FDD 0
JRNL AUTH S.FUDO,N.YAMAMOTO,M.NUKAGA,T.ODAGIRI,M.TASHIRO,T.HOSHINO
JRNL TITL TWO DISTINCTIVE BINDING MODES OF ENDONUCLEASE INHIBITORS TO
JRNL TITL 2 THE N-TERMINAL REGION OF INFLUENZA VIRUS POLYMERASE ACIDIC
JRNL TITL 3 SUBUNIT
JRNL REF BIOCHEMISTRY V. 55 2646 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27088785
JRNL DOI 10.1021/ACS.BIOCHEM.5B01087
REMARK 2
REMARK 2 RESOLUTION. 2.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX PHENIX.REFINE: 1.8.1_1168
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) : 2.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 10350
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.310
REMARK 3 FREE R VALUE TEST SET COUNT : 550
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 37.7970 - 3.9766 1.00 2579 152 0.1858 0.1933
REMARK 3 2 3.9766 - 3.1569 1.00 2435 129 0.1939 0.2332
REMARK 3 3 3.1569 - 2.7579 1.00 2404 129 0.2361 0.3217
REMARK 3 4 2.7579 - 2.5058 1.00 2382 140 0.2459 0.3190
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.34
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 : 0.006 1548
REMARK 3 ANGLE : 0.794 2079
REMARK 3 CHIRALITY : 0.059 218
REMARK 3 PLANARITY : 0.003 265
REMARK 3 DIHEDRAL : 13.054 585
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 5FDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 LIQUID NITROGEN COOLED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10401
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 : 11.30
REMARK 200 R MERGE (I) : 0.15200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 1.19500
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: MOLREP
REMARK 200 STARTING MODEL: 4ZQQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN WITH THE RESERVOIR
REMARK 280 CONTAINING 100 MM MES, 1.1 M AMMONIUM SULFATE, 0.1 M POTASSIUM
REMARK 280 CHLORIDE AND 9 % TREHALOSE AT PH 5.8. CRYSTAL WAS THEN SOAKED
REMARK 280 WITH THE LIGAND SOLUTION AT PH 7.0., VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 63.69600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.19850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.19850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.84800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.19850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.19850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 95.54400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.19850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.19850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.84800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.19850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.19850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 95.54400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.69600
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 TOTAL BURIED SURFACE AREA: 180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 182
REMARK 465 ALA A 183
REMARK 465 ALA A 184
REMARK 465 GLU A 185
REMARK 465 LEU A 186
REMARK 465 ALA A 187
REMARK 465 LEU A 188
REMARK 465 VAL A 189
REMARK 465 PRO A 190
REMARK 465 ARG A 191
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 OAS 4P8 A 201 O HOH A 301 1.95
REMARK 500 OE2 GLU A 104 O HOH A 301 2.04
REMARK 500 NZ LYS A 122 O HOH A 302 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 SER A 57 82.46 -154.80
REMARK 500 HIS A 59 -0.35 74.87
REMARK 500 LYS A 124 5.01 57.36
REMARK 500 THR A 147 -58.44 64.83
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 4P8 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZHZ RELATED DB: PDB
REMARK 900 4ZHZ CONTAINS THE SAME PROTEIN AND LIGAND. THE DIFFERENCE IS THE PH
REMARK 900 UNDER WHICH CRYSTALS WERE SOAKED WITH THE LIGAND SOLUTION. 4ZHZ WAS
REMARK 900 PH 5.8 WHILE THIS ENTRY WAS PH 7.0.
REMARK 900 RELATED ID: 5FDE RELATED DB: PDB
REMARK 900 RELATED ID: 5FDG RELATED DB: PDB
DBREF 5FDD A 6 55 UNP P03433 PA_I34A1 1 50
DBREF 5FDD A 58 182 UNP P03433 PA_I34A1 73 197
SEQADV 5FDD GLY A 1 UNP P03433 EXPRESSION TAG
SEQADV 5FDD PRO A 2 UNP P03433 EXPRESSION TAG
SEQADV 5FDD LEU A 3 UNP P03433 EXPRESSION TAG
SEQADV 5FDD GLY A 4 UNP P03433 EXPRESSION TAG
SEQADV 5FDD SER A 5 UNP P03433 EXPRESSION TAG
SEQADV 5FDD ALA A 56 UNP P03433 LINKER
SEQADV 5FDD SER A 57 UNP P03433 LINKER
SEQADV 5FDD ALA A 183 UNP P03433 EXPRESSION TAG
SEQADV 5FDD ALA A 184 UNP P03433 EXPRESSION TAG
SEQADV 5FDD GLU A 185 UNP P03433 EXPRESSION TAG
SEQADV 5FDD LEU A 186 UNP P03433 EXPRESSION TAG
SEQADV 5FDD ALA A 187 UNP P03433 EXPRESSION TAG
SEQADV 5FDD LEU A 188 UNP P03433 EXPRESSION TAG
SEQADV 5FDD VAL A 189 UNP P03433 EXPRESSION TAG
SEQADV 5FDD PRO A 190 UNP P03433 EXPRESSION TAG
SEQADV 5FDD ARG A 191 UNP P03433 EXPRESSION TAG
SEQRES 1 A 191 GLY PRO LEU GLY SER MET GLU ASP PHE VAL ARG GLN CYS
SEQRES 2 A 191 PHE ASN PRO MET ILE VAL GLU LEU ALA GLU LYS THR MET
SEQRES 3 A 191 LYS GLU TYR GLY GLU ASP LEU LYS ILE GLU THR ASN LYS
SEQRES 4 A 191 PHE ALA ALA ILE CYS THR HIS LEU GLU VAL CYS PHE MET
SEQRES 5 A 191 TYR SER ASP ALA SER LYS HIS ARG PHE GLU ILE ILE GLU
SEQRES 6 A 191 GLY ARG ASP ARG THR MET ALA TRP THR VAL VAL ASN SER
SEQRES 7 A 191 ILE CYS ASN THR THR GLY ALA GLU LYS PRO LYS PHE LEU
SEQRES 8 A 191 PRO ASP LEU TYR ASP TYR LYS GLU ASN ARG PHE ILE GLU
SEQRES 9 A 191 ILE GLY VAL THR ARG ARG GLU VAL HIS ILE TYR TYR LEU
SEQRES 10 A 191 GLU LYS ALA ASN LYS ILE LYS SER GLU LYS THR HIS ILE
SEQRES 11 A 191 HIS ILE PHE SER PHE THR GLY GLU GLU MET ALA THR LYS
SEQRES 12 A 191 ALA ASP TYR THR LEU ASP GLU GLU SER ARG ALA ARG ILE
SEQRES 13 A 191 LYS THR ARG LEU PHE THR ILE ARG GLN GLU MET ALA SER
SEQRES 14 A 191 ARG GLY LEU TRP ASP SER PHE ARG GLN SER GLU ARG GLY
SEQRES 15 A 191 ALA ALA GLU LEU ALA LEU VAL PRO ARG
HET 4P8 A 201 20
HET MN A 202 1
HET SO4 A 203 5
HETNAM 4P8 5-(2-CHLOROBENZYL)-2-HYDROXY-3-NITROBENZALDEHYDE
HETNAM MN MANGANESE (II) ION
HETNAM SO4 SULFATE ION
FORMUL 2 4P8 C14 H10 CL N O4
FORMUL 3 MN MN 2+
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *23(H2 O)
HELIX 1 AA1 SER A 5 PHE A 14 1 10
HELIX 2 AA2 ASN A 15 TYR A 29 1 15
HELIX 3 AA3 GLU A 36 ALA A 56 1 21
HELIX 4 AA4 ASP A 68 GLY A 84 1 17
HELIX 5 AA5 GLU A 111 LYS A 124 1 14
HELIX 6 AA6 LYS A 143 ASP A 145 5 3
HELIX 7 AA7 ASP A 149 ARG A 170 1 22
HELIX 8 AA8 LEU A 172 SER A 179 1 8
SHEET 1 AA1 5 PHE A 61 ILE A 63 0
SHEET 2 AA1 5 LEU A 94 ASP A 96 -1 O TYR A 95 N GLU A 62
SHEET 3 AA1 5 ARG A 101 THR A 108 -1 O ILE A 103 N LEU A 94
SHEET 4 AA1 5 HIS A 129 SER A 134 1 O HIS A 129 N PHE A 102
SHEET 5 AA1 5 GLU A 139 ALA A 141 -1 O MET A 140 N ILE A 132
LINK OD1 ASP A 93 MN MN A 202 1555 1555 2.49
SITE 1 AC1 8 TYR A 29 HIS A 46 GLU A 65 GLU A 104
SITE 2 AC1 8 TYR A 115 LYS A 119 MN A 202 HOH A 301
SITE 1 AC2 4 GLU A 65 LEU A 91 ASP A 93 4P8 A 201
SITE 1 AC3 3 ARG A 164 TRP A 173 ARG A 177
CRYST1 66.397 66.397 127.392 90.00 90.00 90.00 P 41 21 2 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 0.015061 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015061 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007850 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
