HEADER HYDROLASE 27-APR-13 4KFU
TITLE STRUCTURE OF THE GENOME PACKAGING NTPASE B204 FROM SULFOLOBUS TURRETED
TITLE 2 ICOSAHEDRAL VIRUS 2 IN COMPLEX WITH AMPPCP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME PACKAGING NTPASE B204;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS TURRETED ICOSAHEDRAL VIRUS 2;
SOURCE 3 ORGANISM_COMMON: STIV2;
SOURCE 4 ORGANISM_TAXID: 754004;
SOURCE 5 GENE: B204, STIV2_B204;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ER2566/PTF16;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS FTSK-HERA SUPERFAMILY, P-LOOP ATPASE, GENOME PACKAGING NTPASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.HAPPONEN,E.OKSANEN,T.KAJANDER,A.GOLDMAN,S.BUTCHER
REVDAT 4 20-SEP-23 4KFU 1 REMARK SEQADV LINK
REVDAT 3 24-JUL-13 4KFU 1 JRNL
REVDAT 2 05-JUN-13 4KFU 1 JRNL
REVDAT 1 22-MAY-13 4KFU 0
JRNL AUTH L.J.HAPPONEN,E.OKSANEN,L.LILJEROOS,A.GOLDMAN,T.KAJANDER,
JRNL AUTH 2 S.J.BUTCHER
JRNL TITL THE STRUCTURE OF THE NTPASE THAT POWERS DNA PACKAGING INTO
JRNL TITL 2 SULFOLOBUS TURRETED ICOSAHEDRAL VIRUS 2.
JRNL REF J.VIROL. V. 87 8388 2013
JRNL REFN ISSN 0022-538X
JRNL PMID 23698307
JRNL DOI 10.1128/JVI.00831-13
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 65852
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3296
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 48.7334 - 5.4537 0.99 2638 139 0.1977 0.2259
REMARK 3 2 5.4537 - 4.3296 0.99 2672 139 0.1498 0.1668
REMARK 3 3 4.3296 - 3.7825 0.99 2649 141 0.1521 0.1740
REMARK 3 4 3.7825 - 3.4368 0.99 2637 139 0.1614 0.2078
REMARK 3 5 3.4368 - 3.1905 0.99 2690 141 0.1768 0.2164
REMARK 3 6 3.1905 - 3.0024 0.99 2627 137 0.1920 0.2367
REMARK 3 7 3.0024 - 2.8521 0.99 2649 141 0.1949 0.2430
REMARK 3 8 2.8521 - 2.7280 0.98 2595 138 0.1982 0.2492
REMARK 3 9 2.7280 - 2.6229 0.99 2661 140 0.2064 0.2747
REMARK 3 10 2.6229 - 2.5324 0.98 2639 138 0.2033 0.2722
REMARK 3 11 2.5324 - 2.4533 0.98 2621 139 0.2047 0.2776
REMARK 3 12 2.4533 - 2.3831 0.98 2619 137 0.1934 0.2716
REMARK 3 13 2.3831 - 2.3204 0.98 2614 136 0.1880 0.2504
REMARK 3 14 2.3204 - 2.2638 0.98 2665 141 0.1878 0.2036
REMARK 3 15 2.2638 - 2.2123 0.98 2594 138 0.1888 0.2382
REMARK 3 16 2.2123 - 2.1652 0.98 2670 140 0.1980 0.2751
REMARK 3 17 2.1652 - 2.1219 0.98 2545 135 0.2103 0.2823
REMARK 3 18 2.1219 - 2.0819 0.98 2646 140 0.2212 0.2684
REMARK 3 19 2.0819 - 2.0447 0.97 2592 137 0.2283 0.3213
REMARK 3 20 2.0447 - 2.0100 0.97 2625 137 0.2326 0.3027
REMARK 3 21 2.0100 - 1.9776 0.98 2613 137 0.2288 0.2870
REMARK 3 22 1.9776 - 1.9472 0.97 2622 139 0.2328 0.2628
REMARK 3 23 1.9472 - 1.9186 0.97 2580 134 0.2389 0.3111
REMARK 3 24 1.9186 - 1.8920 0.78 2093 113 0.2813 0.3037
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 42.51
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.67490
REMARK 3 B22 (A**2) : 8.99180
REMARK 3 B33 (A**2) : -5.31690
REMARK 3 B12 (A**2) : 0.04730
REMARK 3 B13 (A**2) : 2.80920
REMARK 3 B23 (A**2) : -1.27740
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 : 0.011 6766
REMARK 3 ANGLE : 1.140 9233
REMARK 3 CHIRALITY : 0.078 1031
REMARK 3 PLANARITY : 0.005 1101
REMARK 3 DIHEDRAL : 16.504 2415
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 4KFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65868
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 48.717
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.940
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.70800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: PDB ENTRY 4KFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 30% PEG8000, 5 MM AMPPCP, PROTEIN IN 50 MM SODIUM
REMARK 280 CITRATE, PH 8.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 350
REMARK 350 BIOMOLECULE: 3
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: C
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 350
REMARK 350 BIOMOLECULE: 4
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: D
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 MET A 1
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 HIS A 212
REMARK 465 MET B 1
REMARK 465 LEU B 43
REMARK 465 LEU B 44
REMARK 465 ARG B 45
REMARK 465 SER B 46
REMARK 465 GLY B 47
REMARK 465 ALA B 75
REMARK 465 LYS B 76
REMARK 465 ASN B 77
REMARK 465 GLU B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
REMARK 465 HIS B 212
REMARK 465 ASN C 42
REMARK 465 LEU C 43
REMARK 465 LEU C 44
REMARK 465 ARG C 45
REMARK 465 SER C 46
REMARK 465 GLY C 47
REMARK 465 ALA C 75
REMARK 465 LYS C 76
REMARK 465 ASN C 77
REMARK 465 ASP C 78
REMARK 465 GLU C 206
REMARK 465 HIS C 207
REMARK 465 HIS C 208
REMARK 465 HIS C 209
REMARK 465 HIS C 210
REMARK 465 HIS C 211
REMARK 465 HIS C 212
REMARK 465 ASN D 42
REMARK 465 LEU D 43
REMARK 465 LEU D 44
REMARK 465 ARG D 45
REMARK 465 SER D 46
REMARK 465 ALA D 75
REMARK 465 LYS D 76
REMARK 465 ASN D 77
REMARK 465 ASP D 78
REMARK 465 LEU D 205
REMARK 465 GLU D 206
REMARK 465 HIS D 207
REMARK 465 HIS D 208
REMARK 465 HIS D 209
REMARK 465 HIS D 210
REMARK 465 HIS D 211
REMARK 465 HIS D 212
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 ASN A 2 CG OD1 ND2
REMARK 470 ARG A 12 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 ARG A 74 CD NE CZ NH1 NH2
REMARK 470 ASP A 79 CG OD1 OD2
REMARK 470 GLN A 113 CD OE1 NE2
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 LEU A 205 CG CD1 CD2
REMARK 470 GLU A 206 CG CD OE1 OE2
REMARK 470 ASN B 2 CG OD1 ND2
REMARK 470 ARG B 12 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 33 CD CE NZ
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 TYR B 72 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 74 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 78 CG OD1 OD2
REMARK 470 ASP B 79 CG OD1 OD2
REMARK 470 GLU B 82 CD OE1 OE2
REMARK 470 LYS B 83 CE NZ
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 ARG B 127 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 184 CD CE NZ
REMARK 470 LEU B 205 CG CD1 CD2
REMARK 470 ARG C 12 NE CZ NH1 NH2
REMARK 470 LYS C 13 CD CE NZ
REMARK 470 LYS C 14 CG CD CE NZ
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 TYR C 72 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG C 74 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 79 CG OD1 OD2
REMARK 470 LYS C 83 CE NZ
REMARK 470 LYS C 110 NZ
REMARK 470 ARG C 166 CZ NH1 NH2
REMARK 470 GLU C 178 CG CD OE1 OE2
REMARK 470 LYS C 199 CD CE NZ
REMARK 470 LEU C 205 CG CD1 CD2
REMARK 470 MET D 1 CG SD CE
REMARK 470 ARG D 12 NE CZ NH1 NH2
REMARK 470 LYS D 13 CG CD CE NZ
REMARK 470 LYS D 14 CG CD CE NZ
REMARK 470 LYS D 30 NZ
REMARK 470 SER D 48 OG
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 ARG D 74 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 79 CG OD1 OD2
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 LYS D 83 CD CE NZ
REMARK 470 LYS D 184 CD CE NZ
REMARK 470 LYS D 199 CG CD CE NZ
REMARK 470 LYS D 202 CG CD CE NZ
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 O HOH B 422 O HOH B 516 1.99
REMARK 500 O3A ACP C 301 O HOH C 497 2.07
REMARK 500 O SER A 65 OH TYR A 95 2.10
REMARK 500 O HOH C 460 O HOH C 493 2.18
REMARK 500 OG SER A 35 O GLN A 67 2.19
REMARK 500 O HOH D 463 O HOH D 477 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ASP C 4 O HOH A 504 1655 1.98
REMARK 500 O HOH B 516 O HOH D 419 1565 2.18
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 TYR A 24 -64.67 -124.82
REMARK 500 ILE A 172 -77.34 -125.90
REMARK 500 TYR A 186 -2.29 68.71
REMARK 500 LEU A 205 -88.21 -67.95
REMARK 500 GLU B 104 88.56 69.11
REMARK 500 ALA B 105 -116.28 -77.72
REMARK 500 TYR B 106 -25.64 54.92
REMARK 500 ILE B 172 -72.90 -122.82
REMARK 500 TYR B 186 -1.14 68.48
REMARK 500 ALA C 125 32.27 -143.83
REMARK 500 ILE C 172 -69.22 -120.73
REMARK 500 SER C 173 132.52 -174.93
REMARK 500 SER D 48 40.23 -177.63
REMARK 500 ALA D 125 35.10 -143.73
REMARK 500 ARG D 160 12.98 -140.23
REMARK 500 ILE D 172 -78.63 -125.73
REMARK 500 TYR D 186 -4.81 68.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 ACP A 302
REMARK 610 ACP B 302
REMARK 610 ACP C 301
REMARK 610 ACP D 301
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 MG A 307 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 18 OG
REMARK 620 2 ACP A 301 O2G 171.7
REMARK 620 3 ACP A 301 O1B 87.0 99.6
REMARK 620 4 HOH A 403 O 89.0 84.1 174.5
REMARK 620 5 HOH A 429 O 91.0 84.3 88.4 87.8
REMARK 620 6 HOH A 484 O 83.2 99.7 105.8 77.5 164.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 39 OD2
REMARK 620 2 ASP A 39 OD1 56.1
REMARK 620 3 HIS A 41 NE2 97.3 90.9
REMARK 620 4 ASP A 73 OD2 159.2 110.8 99.1
REMARK 620 5 HIS A 108 NE2 89.0 141.5 110.9 97.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 306 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC A 303 OB2
REMARK 620 2 HOH A 503 O 84.8
REMARK 620 3 HOH A 504 O 114.6 156.0
REMARK 620 4 HOH A 505 O 59.0 63.5 137.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 305 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC A 304 OHB
REMARK 620 2 FLC A 304 OB1 52.8
REMARK 620 3 HOH A 506 O 95.7 71.6
REMARK 620 4 HOH A 507 O 76.8 92.5 163.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 307 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 18 OG
REMARK 620 2 ACP B 301 O3G 173.2
REMARK 620 3 ACP B 301 O2B 94.2 88.1
REMARK 620 4 HOH B 409 O 94.6 91.8 88.9
REMARK 620 5 HOH B 412 O 83.6 94.7 174.6 86.4
REMARK 620 6 HOH B 414 O 83.5 89.8 99.0 171.9 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 39 OD2
REMARK 620 2 HIS B 41 NE2 109.1
REMARK 620 3 ASP B 73 OD2 131.9 80.9
REMARK 620 4 HIS B 108 NE2 107.4 116.8 109.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 306 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FLC B 303 OA1
REMARK 620 2 HOH B 515 O 49.9
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 ACP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KFR RELATED DB: PDB
REMARK 900 STRUCTURE OF THE GENOME PACKAGING NTPASE B204 FROM SULFOLOBUS
REMARK 900 TURRETED ICOSAHEDRAL VIRUS 2 IN COMPLEX WITH SULFATE
REMARK 900 RELATED ID: 4KFS RELATED DB: PDB
REMARK 900 STRUCTURE OF THE GENOME PACKAGING NTPASE B204 FROM SULFOLOBUS
REMARK 900 TURRETED ICOSAHEDRAL VIRUS 2 IN COMPLEX WITH AMP
REMARK 900 RELATED ID: 4KFT RELATED DB: PDB
REMARK 900 STRUCTURE OF THE GENOME PACKAGING NTPASE B204 FROM SULFOLOBUS
REMARK 900 TURRETED ICOSAHEDRAL VIRUS 2 IN COMPLEX WITH ATPGAMMAS
DBREF 4KFU A 1 204 UNP D5IEZ9 D5IEZ9_9VIRU 1 204
DBREF 4KFU B 1 204 UNP D5IEZ9 D5IEZ9_9VIRU 1 204
DBREF 4KFU C 1 204 UNP D5IEZ9 D5IEZ9_9VIRU 1 204
DBREF 4KFU D 1 204 UNP D5IEZ9 D5IEZ9_9VIRU 1 204
SEQADV 4KFU LEU A 205 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU GLU A 206 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS A 207 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS A 208 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS A 209 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS A 210 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS A 211 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS A 212 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU LEU B 205 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU GLU B 206 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS B 207 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS B 208 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS B 209 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS B 210 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS B 211 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS B 212 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU LEU C 205 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU GLU C 206 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS C 207 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS C 208 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS C 209 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS C 210 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS C 211 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS C 212 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU LEU D 205 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU GLU D 206 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS D 207 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS D 208 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS D 209 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS D 210 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS D 211 UNP D5IEZ9 EXPRESSION TAG
SEQADV 4KFU HIS D 212 UNP D5IEZ9 EXPRESSION TAG
SEQRES 1 A 212 MET ASN PRO ASP ASP ILE VAL VAL LEU VAL GLY ARG LYS
SEQRES 2 A 212 LYS SER GLY LYS SER TYR LEU ILE LYS HIS TYR PHE ILE
SEQRES 3 A 212 PRO VAL LEU LYS ALA HIS LYS ILE SER TYR ILE ILE ASP
SEQRES 4 A 212 ASP HIS ASN LEU LEU ARG SER GLY SER GLU TYR SER LYS
SEQRES 5 A 212 PHE GLY TYR ASN ALA THR SER LEU SER ASP ILE VAL SER
SEQRES 6 A 212 LYS GLN TYR VAL VAL VAL TYR ASP ARG ALA LYS ASN ASP
SEQRES 7 A 212 ASP PHE PHE GLU LYS LEU TRP GLN ALA SER LYS LEU HIS
SEQRES 8 A 212 SER LYS LYS TYR GLY THR THR VAL LEU ILE ILE ASP GLU
SEQRES 9 A 212 ALA TYR TYR HIS PHE LYS TYR LYS GLN LYS VAL THR PRO
SEQRES 10 A 212 ALA ILE ASP GLU ALA LEU HIS ALA ASN ARG HIS ALA GLY
SEQRES 11 A 212 LEU GLY LEU ILE LEU SER THR GLN ARG VAL TYR ASP LEU
SEQRES 12 A 212 MET PRO ILE VAL TYR LYS GLN ALA ASP LEU ILE ILE MET
SEQRES 13 A 212 PHE TYR THR ARG GLU PRO ASN GLU LEU ARG TRP ILE SER
SEQRES 14 A 212 LYS TYR ILE SER ALA GLU ALA ALA GLU LYS VAL LYS THR
SEQRES 15 A 212 LEU LYS GLN TYR HIS PHE LEU ILE TYR ASP VAL ASN SER
SEQRES 16 A 212 GLN THR ILE LYS ILE HIS LYS PRO ILE LEU GLU HIS HIS
SEQRES 17 A 212 HIS HIS HIS HIS
SEQRES 1 B 212 MET ASN PRO ASP ASP ILE VAL VAL LEU VAL GLY ARG LYS
SEQRES 2 B 212 LYS SER GLY LYS SER TYR LEU ILE LYS HIS TYR PHE ILE
SEQRES 3 B 212 PRO VAL LEU LYS ALA HIS LYS ILE SER TYR ILE ILE ASP
SEQRES 4 B 212 ASP HIS ASN LEU LEU ARG SER GLY SER GLU TYR SER LYS
SEQRES 5 B 212 PHE GLY TYR ASN ALA THR SER LEU SER ASP ILE VAL SER
SEQRES 6 B 212 LYS GLN TYR VAL VAL VAL TYR ASP ARG ALA LYS ASN ASP
SEQRES 7 B 212 ASP PHE PHE GLU LYS LEU TRP GLN ALA SER LYS LEU HIS
SEQRES 8 B 212 SER LYS LYS TYR GLY THR THR VAL LEU ILE ILE ASP GLU
SEQRES 9 B 212 ALA TYR TYR HIS PHE LYS TYR LYS GLN LYS VAL THR PRO
SEQRES 10 B 212 ALA ILE ASP GLU ALA LEU HIS ALA ASN ARG HIS ALA GLY
SEQRES 11 B 212 LEU GLY LEU ILE LEU SER THR GLN ARG VAL TYR ASP LEU
SEQRES 12 B 212 MET PRO ILE VAL TYR LYS GLN ALA ASP LEU ILE ILE MET
SEQRES 13 B 212 PHE TYR THR ARG GLU PRO ASN GLU LEU ARG TRP ILE SER
SEQRES 14 B 212 LYS TYR ILE SER ALA GLU ALA ALA GLU LYS VAL LYS THR
SEQRES 15 B 212 LEU LYS GLN TYR HIS PHE LEU ILE TYR ASP VAL ASN SER
SEQRES 16 B 212 GLN THR ILE LYS ILE HIS LYS PRO ILE LEU GLU HIS HIS
SEQRES 17 B 212 HIS HIS HIS HIS
SEQRES 1 C 212 MET ASN PRO ASP ASP ILE VAL VAL LEU VAL GLY ARG LYS
SEQRES 2 C 212 LYS SER GLY LYS SER TYR LEU ILE LYS HIS TYR PHE ILE
SEQRES 3 C 212 PRO VAL LEU LYS ALA HIS LYS ILE SER TYR ILE ILE ASP
SEQRES 4 C 212 ASP HIS ASN LEU LEU ARG SER GLY SER GLU TYR SER LYS
SEQRES 5 C 212 PHE GLY TYR ASN ALA THR SER LEU SER ASP ILE VAL SER
SEQRES 6 C 212 LYS GLN TYR VAL VAL VAL TYR ASP ARG ALA LYS ASN ASP
SEQRES 7 C 212 ASP PHE PHE GLU LYS LEU TRP GLN ALA SER LYS LEU HIS
SEQRES 8 C 212 SER LYS LYS TYR GLY THR THR VAL LEU ILE ILE ASP GLU
SEQRES 9 C 212 ALA TYR TYR HIS PHE LYS TYR LYS GLN LYS VAL THR PRO
SEQRES 10 C 212 ALA ILE ASP GLU ALA LEU HIS ALA ASN ARG HIS ALA GLY
SEQRES 11 C 212 LEU GLY LEU ILE LEU SER THR GLN ARG VAL TYR ASP LEU
SEQRES 12 C 212 MET PRO ILE VAL TYR LYS GLN ALA ASP LEU ILE ILE MET
SEQRES 13 C 212 PHE TYR THR ARG GLU PRO ASN GLU LEU ARG TRP ILE SER
SEQRES 14 C 212 LYS TYR ILE SER ALA GLU ALA ALA GLU LYS VAL LYS THR
SEQRES 15 C 212 LEU LYS GLN TYR HIS PHE LEU ILE TYR ASP VAL ASN SER
SEQRES 16 C 212 GLN THR ILE LYS ILE HIS LYS PRO ILE LEU GLU HIS HIS
SEQRES 17 C 212 HIS HIS HIS HIS
SEQRES 1 D 212 MET ASN PRO ASP ASP ILE VAL VAL LEU VAL GLY ARG LYS
SEQRES 2 D 212 LYS SER GLY LYS SER TYR LEU ILE LYS HIS TYR PHE ILE
SEQRES 3 D 212 PRO VAL LEU LYS ALA HIS LYS ILE SER TYR ILE ILE ASP
SEQRES 4 D 212 ASP HIS ASN LEU LEU ARG SER GLY SER GLU TYR SER LYS
SEQRES 5 D 212 PHE GLY TYR ASN ALA THR SER LEU SER ASP ILE VAL SER
SEQRES 6 D 212 LYS GLN TYR VAL VAL VAL TYR ASP ARG ALA LYS ASN ASP
SEQRES 7 D 212 ASP PHE PHE GLU LYS LEU TRP GLN ALA SER LYS LEU HIS
SEQRES 8 D 212 SER LYS LYS TYR GLY THR THR VAL LEU ILE ILE ASP GLU
SEQRES 9 D 212 ALA TYR TYR HIS PHE LYS TYR LYS GLN LYS VAL THR PRO
SEQRES 10 D 212 ALA ILE ASP GLU ALA LEU HIS ALA ASN ARG HIS ALA GLY
SEQRES 11 D 212 LEU GLY LEU ILE LEU SER THR GLN ARG VAL TYR ASP LEU
SEQRES 12 D 212 MET PRO ILE VAL TYR LYS GLN ALA ASP LEU ILE ILE MET
SEQRES 13 D 212 PHE TYR THR ARG GLU PRO ASN GLU LEU ARG TRP ILE SER
SEQRES 14 D 212 LYS TYR ILE SER ALA GLU ALA ALA GLU LYS VAL LYS THR
SEQRES 15 D 212 LEU LYS GLN TYR HIS PHE LEU ILE TYR ASP VAL ASN SER
SEQRES 16 D 212 GLN THR ILE LYS ILE HIS LYS PRO ILE LEU GLU HIS HIS
SEQRES 17 D 212 HIS HIS HIS HIS
HET ACP A 301 31
HET ACP A 302 23
HET FLC A 303 13
HET FLC A 304 13
HET MG A 305 1
HET MG A 306 1
HET MG A 307 1
HET ZN A 308 1
HET ACP B 301 31
HET ACP B 302 23
HET FLC B 303 13
HET FLC B 304 13
HET MG B 305 1
HET MG B 306 1
HET MG B 307 1
HET ZN B 308 1
HET ACP C 301 23
HET ACP D 301 23
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM FLC CITRATE ANION
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 5 ACP 6(C11 H18 N5 O12 P3)
FORMUL 7 FLC 4(C6 H5 O7 3-)
FORMUL 9 MG 6(MG 2+)
FORMUL 12 ZN 2(ZN 2+)
FORMUL 23 HOH *428(H2 O)
HELIX 1 1 GLY A 16 TYR A 24 1 9
HELIX 2 2 TYR A 24 HIS A 32 1 9
HELIX 3 3 TYR A 50 GLY A 54 5 5
HELIX 4 4 SER A 59 LYS A 66 1 8
HELIX 5 5 ASN A 77 GLY A 96 1 20
HELIX 6 6 GLU A 104 HIS A 108 5 5
HELIX 7 7 THR A 116 ALA A 125 1 10
HELIX 8 8 ARG A 139 LEU A 143 5 5
HELIX 9 9 MET A 144 ALA A 151 1 8
HELIX 10 10 GLU A 161 ILE A 172 1 12
HELIX 11 11 SER A 173 VAL A 180 1 8
HELIX 12 12 LYS A 181 LEU A 183 5 3
HELIX 13 13 GLY B 16 TYR B 24 1 9
HELIX 14 14 TYR B 24 HIS B 32 1 9
HELIX 15 15 TYR B 50 GLY B 54 5 5
HELIX 16 16 SER B 59 LYS B 66 1 8
HELIX 17 17 ASP B 79 GLY B 96 1 18
HELIX 18 18 THR B 116 ALA B 125 1 10
HELIX 19 19 ALA B 125 GLY B 130 1 6
HELIX 20 20 ARG B 139 LEU B 143 5 5
HELIX 21 21 MET B 144 ALA B 151 1 8
HELIX 22 22 GLU B 161 ILE B 172 1 12
HELIX 23 23 SER B 173 VAL B 180 1 8
HELIX 24 24 LYS B 181 LEU B 183 5 3
HELIX 25 25 GLY C 16 TYR C 24 1 9
HELIX 26 26 TYR C 24 HIS C 32 1 9
HELIX 27 27 TYR C 50 GLY C 54 5 5
HELIX 28 28 LEU C 60 LYS C 66 1 7
HELIX 29 29 PHE C 80 GLY C 96 1 17
HELIX 30 30 GLU C 104 HIS C 108 5 5
HELIX 31 31 THR C 116 ALA C 125 1 10
HELIX 32 32 ALA C 125 GLY C 130 1 6
HELIX 33 33 ARG C 139 LEU C 143 5 5
HELIX 34 34 MET C 144 ALA C 151 1 8
HELIX 35 35 GLU C 161 ILE C 172 1 12
HELIX 36 36 SER C 173 VAL C 180 1 8
HELIX 37 37 LYS C 181 LEU C 183 5 3
HELIX 38 38 GLY D 16 TYR D 24 1 9
HELIX 39 39 TYR D 24 HIS D 32 1 9
HELIX 40 40 TYR D 50 GLY D 54 5 5
HELIX 41 41 SER D 59 LYS D 66 1 8
HELIX 42 42 PHE D 80 GLY D 96 1 17
HELIX 43 43 ALA D 105 LYS D 110 1 6
HELIX 44 44 THR D 116 ALA D 125 1 10
HELIX 45 45 ALA D 125 GLY D 130 1 6
HELIX 46 46 ARG D 139 LEU D 143 5 5
HELIX 47 47 MET D 144 ALA D 151 1 8
HELIX 48 48 GLU D 161 ILE D 172 1 12
HELIX 49 49 SER D 173 VAL D 180 1 8
HELIX 50 50 LYS D 181 LEU D 183 5 3
SHEET 1 A 9 TYR A 55 ASN A 56 0
SHEET 2 A 9 TYR A 68 TYR A 72 1 O TYR A 68 N TYR A 55
SHEET 3 A 9 SER A 35 ASP A 40 1 N ILE A 38 O VAL A 71
SHEET 4 A 9 THR A 98 ILE A 102 1 O ILE A 101 N ASP A 39
SHEET 5 A 9 LEU A 131 THR A 137 1 O ILE A 134 N ILE A 102
SHEET 6 A 9 ILE A 6 VAL A 10 1 N LEU A 9 O LEU A 135
SHEET 7 A 9 LEU A 153 MET A 156 1 O ILE A 155 N VAL A 8
SHEET 8 A 9 PHE A 188 ASP A 192 -1 O TYR A 191 N ILE A 154
SHEET 9 A 9 THR A 197 HIS A 201 -1 O HIS A 201 N PHE A 188
SHEET 1 B 9 TYR B 55 ALA B 57 0
SHEET 2 B 9 TYR B 68 TYR B 72 1 O TYR B 68 N TYR B 55
SHEET 3 B 9 SER B 35 ASP B 40 1 N ILE B 38 O VAL B 71
SHEET 4 B 9 THR B 98 ASP B 103 1 O ILE B 101 N ASP B 39
SHEET 5 B 9 LEU B 131 THR B 137 1 O ILE B 134 N ILE B 102
SHEET 6 B 9 ILE B 6 VAL B 10 1 N LEU B 9 O LEU B 135
SHEET 7 B 9 LEU B 153 MET B 156 1 O ILE B 155 N VAL B 8
SHEET 8 B 9 PHE B 188 ASP B 192 -1 O TYR B 191 N ILE B 154
SHEET 9 B 9 THR B 197 HIS B 201 -1 O HIS B 201 N PHE B 188
SHEET 1 C 9 TYR C 55 ASN C 56 0
SHEET 2 C 9 TYR C 68 TYR C 72 1 O VAL C 70 N TYR C 55
SHEET 3 C 9 SER C 35 ASP C 40 1 N ILE C 38 O VAL C 71
SHEET 4 C 9 THR C 98 ILE C 102 1 O ILE C 101 N ASP C 39
SHEET 5 C 9 LEU C 131 THR C 137 1 O ILE C 134 N ILE C 102
SHEET 6 C 9 ILE C 6 VAL C 10 1 N VAL C 7 O LEU C 133
SHEET 7 C 9 LEU C 153 MET C 156 1 O ILE C 155 N VAL C 8
SHEET 8 C 9 PHE C 188 ASP C 192 -1 O TYR C 191 N ILE C 154
SHEET 9 C 9 THR C 197 HIS C 201 -1 O HIS C 201 N PHE C 188
SHEET 1 D 9 TYR D 55 ALA D 57 0
SHEET 2 D 9 TYR D 68 TYR D 72 1 O TYR D 68 N TYR D 55
SHEET 3 D 9 SER D 35 ASP D 40 1 N ILE D 38 O VAL D 71
SHEET 4 D 9 THR D 98 ILE D 102 1 O ILE D 101 N ILE D 37
SHEET 5 D 9 LEU D 131 THR D 137 1 O ILE D 134 N ILE D 102
SHEET 6 D 9 ILE D 6 VAL D 10 1 N VAL D 7 O LEU D 133
SHEET 7 D 9 LEU D 153 MET D 156 1 O ILE D 155 N VAL D 8
SHEET 8 D 9 PHE D 188 ASP D 192 -1 O TYR D 191 N ILE D 154
SHEET 9 D 9 THR D 197 HIS D 201 -1 O HIS D 201 N PHE D 188
LINK OG SER A 18 MG MG A 307 1555 1555 2.16
LINK OD2 ASP A 39 ZN ZN A 308 1555 1555 2.26
LINK OD1 ASP A 39 ZN ZN A 308 1555 1555 2.37
LINK NE2 HIS A 41 ZN ZN A 308 1555 1555 2.07
LINK OD2 ASP A 73 ZN ZN A 308 1555 1555 2.04
LINK NE2 HIS A 108 ZN ZN A 308 1555 1555 2.02
LINK O2G ACP A 301 MG MG A 307 1555 1555 1.73
LINK O1B ACP A 301 MG MG A 307 1555 1555 1.90
LINK OB2 FLC A 303 MG MG A 306 1555 1555 2.87
LINK OHB FLC A 304 MG MG A 305 1555 1555 2.97
LINK OB1 FLC A 304 MG MG A 305 1555 1555 2.98
LINK MG MG A 305 O HOH A 506 1555 1555 3.00
LINK MG MG A 305 O HOH A 507 1555 1555 2.85
LINK MG MG A 306 O HOH A 503 1555 1555 2.86
LINK MG MG A 306 O HOH A 504 1555 1555 2.71
LINK MG MG A 306 O HOH A 505 1555 1555 2.99
LINK MG MG A 307 O HOH A 403 1555 1555 2.10
LINK MG MG A 307 O HOH A 429 1555 1555 2.08
LINK MG MG A 307 O HOH A 484 1555 1555 2.09
LINK OG SER B 18 MG MG B 307 1555 1555 2.02
LINK OD2 ASP B 39 ZN ZN B 308 1555 1555 2.19
LINK NE2 HIS B 41 ZN ZN B 308 1555 1555 1.97
LINK OD2 ASP B 73 ZN ZN B 308 1555 1555 2.10
LINK NE2 HIS B 108 ZN ZN B 308 1555 1555 2.32
LINK O3G ACP B 301 MG MG B 307 1555 1555 1.99
LINK O2B ACP B 301 MG MG B 307 1555 1555 2.03
LINK OA1 FLC B 303 MG MG B 306 1555 1555 2.93
LINK OG1 FLC B 304 MG MG B 305 1555 1555 2.88
LINK MG MG B 306 O HOH B 515 1555 1555 2.64
LINK MG MG B 307 O HOH B 409 1555 1555 2.09
LINK MG MG B 307 O HOH B 412 1555 1555 2.10
LINK MG MG B 307 O HOH B 414 1555 1555 2.10
SITE 1 AC1 20 ARG A 12 LYS A 13 LYS A 14 SER A 15
SITE 2 AC1 20 GLY A 16 LYS A 17 SER A 18 TYR A 19
SITE 3 AC1 20 GLN A 138 TYR A 186 ILE A 204 MG A 307
SITE 4 AC1 20 HOH A 401 HOH A 403 HOH A 412 HOH A 416
SITE 5 AC1 20 HOH A 417 HOH A 429 HOH A 466 HOH A 484
SITE 1 AC2 10 TYR A 158 LEU A 183 LYS A 184 GLN A 185
SITE 2 AC2 10 MET C 1 ASN C 2 PRO C 3 VAL C 28
SITE 3 AC2 10 HIS C 32 ILE C 34
SITE 1 AC3 13 PRO A 162 MG A 306 HOH A 453 HOH A 493
SITE 2 AC3 13 HOH A 503 HOH A 505 HIS C 124 ALA C 125
SITE 3 AC3 13 ASN C 126 ARG C 127 HIS C 128 GLN C 150
SITE 4 AC3 13 HOH C 404
SITE 1 AC4 8 ARG A 160 MG A 305 HOH A 506 HOH A 507
SITE 2 AC4 8 HOH A 508 ASN C 2 ASP C 192 ASN C 194
SITE 1 AC5 5 FLC A 304 HOH A 506 HOH A 507 HOH A 508
SITE 2 AC5 5 ASP C 5
SITE 1 AC6 7 FLC A 303 HOH A 503 HOH A 504 HOH A 505
SITE 2 AC6 7 ASN C 126 ARG C 127 ASP C 152
SITE 1 AC7 5 SER A 18 ACP A 301 HOH A 403 HOH A 429
SITE 2 AC7 5 HOH A 484
SITE 1 AC8 4 ASP A 39 HIS A 41 ASP A 73 HIS A 108
SITE 1 AC9 20 ARG B 12 LYS B 13 LYS B 14 SER B 15
SITE 2 AC9 20 GLY B 16 LYS B 17 SER B 18 TYR B 19
SITE 3 AC9 20 TYR B 186 ILE B 204 MG B 307 HOH B 403
SITE 4 AC9 20 HOH B 404 HOH B 408 HOH B 409 HOH B 412
SITE 5 AC9 20 HOH B 414 HOH B 419 HOH B 449 HOH B 500
SITE 1 BC1 11 TYR B 158 LEU B 183 LYS B 184 GLN B 185
SITE 2 BC1 11 MET D 1 ASN D 2 PRO D 3 VAL D 28
SITE 3 BC1 11 LEU D 29 HIS D 32 ILE D 34
SITE 1 BC2 14 PRO B 162 MG B 306 HOH B 491 HOH B 492
SITE 2 BC2 14 HOH B 514 HOH B 515 HIS D 124 ALA D 125
SITE 3 BC2 14 ASN D 126 ARG D 127 HIS D 128 GLN D 150
SITE 4 BC2 14 HOH D 419 HOH D 480
SITE 1 BC3 10 ARG B 160 MG B 305 HOH B 517 HOH B 518
SITE 2 BC3 10 HOH B 519 MET D 1 ASP D 192 ASN D 194
SITE 3 BC3 10 HOH D 410 HOH D 420
SITE 1 BC4 10 ARG B 160 FLC B 304 HOH B 422 HOH B 516
SITE 2 BC4 10 HOH B 517 HOH B 518 ASN D 2 ASP D 5
SITE 3 BC4 10 ASP D 152 ASN D 194
SITE 1 BC5 5 FLC B 303 HOH B 515 GLN D 150 ASP D 152
SITE 2 BC5 5 HOH D 414
SITE 1 BC6 5 SER B 18 ACP B 301 HOH B 409 HOH B 412
SITE 2 BC6 5 HOH B 414
SITE 1 BC7 4 ASP B 39 HIS B 41 ASP B 73 HIS B 108
SITE 1 BC8 10 LYS C 14 GLY C 16 LYS C 17 SER C 18
SITE 2 BC8 10 TYR C 19 TYR C 186 PRO C 203 ILE C 204
SITE 3 BC8 10 HOH C 497 HOH C 504
SITE 1 BC9 10 LYS D 14 GLY D 16 LYS D 17 SER D 18
SITE 2 BC9 10 TYR D 19 TYR D 186 ILE D 204 HOH D 458
SITE 3 BC9 10 HOH D 467 HOH D 468
CRYST1 46.558 65.227 72.118 90.85 93.77 91.56 P 1 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 0.021479 0.000585 0.001425 0.00000
SCALE2 0.000000 0.015337 0.000255 0.00000
SCALE3 0.000000 0.000000 0.013898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
