HEADER TRANSFERASE 27-MAR-12 4EDR
TITLE THE STRUCTURE OF THE S. AUREUS DNAG RNA POLYMERASE DOMAIN BOUND TO UTP
TITLE 2 AND MANGANESE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA PRIMASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 111-436;
COMPND 5 EC: 2.7.7.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: DNAG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS CATALYTIC DOMAIN, NUCLEOSIDE TRIPHOSPHATE, NUCLEOSIDE POLYPHOSPHATE,
KEYWDS 2 PROTEIN-LIGAND COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.U.RYMER,F.A.SOLORIO,C.CHU,J.E.CORN,J.D.WANG,J.M.BERGER
REVDAT 5 28-FEB-24 4EDR 1 REMARK SEQADV LINK
REVDAT 4 10-JUL-13 4EDR 1 JRNL
REVDAT 3 22-AUG-12 4EDR 1 REMARK
REVDAT 2 01-AUG-12 4EDR 1 TITLE
REVDAT 1 25-JUL-12 4EDR 0
JRNL AUTH R.U.RYMER,F.A.SOLORIO,A.K.TEHRANCHI,C.CHU,J.E.CORN,J.L.KECK,
JRNL AUTH 2 J.D.WANG,J.M.BERGER
JRNL TITL BINDING MECHANISM OF METAL-NTP SUBSTRATES AND
JRNL TITL 2 STRINGENT-RESPONSE ALARMONES TO BACTERIAL DNAG-TYPE
JRNL TITL 3 PRIMASES.
JRNL REF STRUCTURE V. 20 1478 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22795082
JRNL DOI 10.1016/J.STR.2012.05.017
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 33847
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1713
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 37.0480 - 4.5991 0.99 2790 145 0.1782 0.1883
REMARK 3 2 4.5991 - 3.6515 1.00 2739 130 0.1522 0.1788
REMARK 3 3 3.6515 - 3.1902 1.00 2671 146 0.1693 0.2142
REMARK 3 4 3.1902 - 2.8986 1.00 2704 139 0.1810 0.2366
REMARK 3 5 2.8986 - 2.6909 1.00 2639 163 0.1836 0.2203
REMARK 3 6 2.6909 - 2.5323 1.00 2690 127 0.1741 0.2213
REMARK 3 7 2.5323 - 2.4055 1.00 2657 139 0.1740 0.1975
REMARK 3 8 2.4055 - 2.3008 1.00 2682 144 0.1763 0.1807
REMARK 3 9 2.3008 - 2.2123 1.00 2623 159 0.1644 0.2178
REMARK 3 10 2.2123 - 2.1359 1.00 2640 128 0.1740 0.2375
REMARK 3 11 2.1359 - 2.0692 1.00 2681 150 0.1738 0.2048
REMARK 3 12 2.0692 - 2.0100 1.00 2618 143 0.1796 0.2212
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 : 0.34
REMARK 3 B_SOL : 37.94
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.53160
REMARK 3 B22 (A**2) : 2.53160
REMARK 3 B33 (A**2) : -5.06320
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 : 0.002 2703
REMARK 3 ANGLE : 0.718 3648
REMARK 3 CHIRALITY : 0.047 392
REMARK 3 PLANARITY : 0.003 471
REMARK 3 DIHEDRAL : 12.845 1017
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 108:233)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6995 -62.6804 -3.6664
REMARK 3 T TENSOR
REMARK 3 T11: 0.1933 T22: 0.1210
REMARK 3 T33: 0.0871 T12: 0.0928
REMARK 3 T13: -0.0123 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.7455 L22: 0.7950
REMARK 3 L33: 2.0897 L12: -0.4500
REMARK 3 L13: -0.1414 L23: -0.1893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.0274 S13: -0.0332
REMARK 3 S21: -0.0273 S22: -0.0161 S23: 0.0228
REMARK 3 S31: 0.1832 S32: -0.0468 S33: -0.0039
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 234:343)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4141 -42.6243 6.1443
REMARK 3 T TENSOR
REMARK 3 T11: 0.1539 T22: 0.1068
REMARK 3 T33: 0.1447 T12: 0.1309
REMARK 3 T13: -0.0322 T23: -0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 0.9781 L22: 2.3235
REMARK 3 L33: 0.5755 L12: -0.4567
REMARK 3 L13: -0.2738 L23: 0.2195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0343 S12: -0.1130 S13: 0.1671
REMARK 3 S21: 0.1746 S22: 0.0125 S23: 0.0443
REMARK 3 S31: -0.0086 S32: -0.0084 S33: -0.0265
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 344:362)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3661 -32.3372 -6.8339
REMARK 3 T TENSOR
REMARK 3 T11: 0.3793 T22: 0.2627
REMARK 3 T33: 0.3337 T12: 0.0461
REMARK 3 T13: 0.0413 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.1992 L22: 0.2580
REMARK 3 L33: 0.5951 L12: 0.0414
REMARK 3 L13: 0.0597 L23: 0.1056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: 0.2309 S13: 0.2320
REMARK 3 S21: -0.6264 S22: -0.0836 S23: -0.0703
REMARK 3 S31: -0.7087 S32: 0.2088 S33: -0.0039
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 363:428)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2348 -24.9788 8.2577
REMARK 3 T TENSOR
REMARK 3 T11: 0.1917 T22: 0.1496
REMARK 3 T33: 0.3193 T12: 0.0364
REMARK 3 T13: -0.0024 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 1.4490 L22: 1.2927
REMARK 3 L33: 0.7128 L12: 0.1444
REMARK 3 L13: 0.1117 L23: -0.6230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: -0.2100 S13: 0.2778
REMARK 3 S21: 0.1668 S22: 0.0328 S23: 0.1135
REMARK 3 S31: -0.0012 S32: -0.1047 S33: -0.0018
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 4EDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33865
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 38.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHENIX AUTOMR
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M SODIUM THIOCYANATE, 0.1M BIS
REMARK 280 -TRIS, 13% PEG3350, 2% BENZAMIDINE, 2.5 MM UTP, 5 MM MNCL2, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 12.87767
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 25.75533
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.31650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 32.19417
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 6.43883
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 300 REMARK: MONOMER
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 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 GLN A 429
REMARK 465 PHE A 430
REMARK 465 ASN A 431
REMARK 465 GLN A 432
REMARK 465 ALA A 433
REMARK 465 PRO A 434
REMARK 465 ALA A 435
REMARK 465 ASN A 436
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 GLU A 193 CG CD OE1 OE2
REMARK 470 PHE A 195 CG CD1 CD2 CE1 CE2 CZ
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 270 O HOH A 932 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 ASN A 362 -83.59 -76.37
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 MN A 506 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 310 OD2
REMARK 620 2 ASP A 343 OD2 108.4
REMARK 620 3 UTP A 504 O2A 83.7 164.9
REMARK 620 4 UTP A 504 O2B 152.1 88.0 77.4
REMARK 620 5 HOH A 834 O 86.2 77.7 94.5 75.3
REMARK 620 6 HOH A 932 O 88.4 102.2 86.8 110.6 174.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 507 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 343 OD2
REMARK 620 2 UTP A 504 O1G 163.0
REMARK 620 3 UTP A 504 O2B 86.9 76.1
REMARK 620 4 HOH A 634 O 95.1 86.2 98.0
REMARK 620 5 HOH A 930 O 75.6 100.2 73.4 167.4
REMARK 620 6 HOH A 931 O 105.2 91.4 159.4 97.4 93.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 505 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 623 O
REMARK 620 2 HOH A 710 O 175.5
REMARK 620 3 HOH A 738 O 91.0 92.6
REMARK 620 4 HOH A 789 O 91.7 84.8 175.6
REMARK 620 5 HOH A 908 O 97.7 79.4 93.2 89.8
REMARK 620 6 HOH A 923 O 87.8 95.1 87.2 89.6 174.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E2K RELATED DB: PDB
REMARK 900 APO SADNAG RPD
REMARK 900 RELATED ID: 4EDG RELATED DB: PDB
REMARK 900 RELATED ID: 4EDK RELATED DB: PDB
REMARK 900 RELATED ID: 4EDT RELATED DB: PDB
REMARK 900 RELATED ID: 4EDV RELATED DB: PDB
REMARK 900 RELATED ID: 4EE1 RELATED DB: PDB
DBREF 4EDR A 111 436 UNP O05338 PRIM_STAAU 111 436
SEQADV 4EDR SER A 108 UNP O05338 EXPRESSION TAG
SEQADV 4EDR ASN A 109 UNP O05338 EXPRESSION TAG
SEQADV 4EDR ALA A 110 UNP O05338 EXPRESSION TAG
SEQRES 1 A 329 SER ASN ALA ASP ASP LEU GLN MET ILE GLU MET HIS GLU
SEQRES 2 A 329 LEU ILE GLN GLU PHE TYR TYR TYR ALA LEU THR LYS THR
SEQRES 3 A 329 VAL GLU GLY GLU GLN ALA LEU THR TYR LEU GLN GLU ARG
SEQRES 4 A 329 GLY PHE THR ASP ALA LEU ILE LYS GLU ARG GLY ILE GLY
SEQRES 5 A 329 PHE ALA PRO ASP SER SER HIS PHE CYS HIS ASP PHE LEU
SEQRES 6 A 329 GLN LYS LYS GLY TYR ASP ILE GLU LEU ALA TYR GLU ALA
SEQRES 7 A 329 GLY LEU LEU SER ARG ASN GLU GLU ASN PHE SER TYR TYR
SEQRES 8 A 329 ASP ARG PHE ARG ASN ARG ILE MET PHE PRO LEU LYS ASN
SEQRES 9 A 329 ALA GLN GLY ARG ILE VAL GLY TYR SER GLY ARG THR TYR
SEQRES 10 A 329 THR GLY GLN GLU PRO LYS TYR LEU ASN SER PRO GLU THR
SEQRES 11 A 329 PRO ILE PHE GLN LYS ARG LYS LEU LEU TYR ASN LEU ASP
SEQRES 12 A 329 LYS ALA ARG LYS SER ILE ARG LYS LEU ASP GLU ILE VAL
SEQRES 13 A 329 LEU LEU GLU GLY PHE MET ASP VAL ILE LYS SER ASP THR
SEQRES 14 A 329 ALA GLY LEU LYS ASN VAL VAL ALA THR MET GLY THR GLN
SEQRES 15 A 329 LEU SER ASP GLU HIS ILE THR PHE ILE ARG LYS LEU THR
SEQRES 16 A 329 SER ASN ILE THR LEU MET PHE ASP GLY ASP PHE ALA GLY
SEQRES 17 A 329 SER GLU ALA THR LEU LYS THR GLY GLN HIS LEU LEU GLN
SEQRES 18 A 329 GLN GLY LEU ASN VAL PHE VAL ILE GLN LEU PRO SER GLY
SEQRES 19 A 329 MET ASP PRO ASP GLU TYR ILE GLY LYS TYR GLY ASN ASP
SEQRES 20 A 329 ALA PHE THR THR PHE VAL LYS ASN ASP LYS LYS SER PHE
SEQRES 21 A 329 ALA HIS TYR LYS VAL SER ILE LEU LYS ASP GLU ILE ALA
SEQRES 22 A 329 HIS ASN ASP LEU SER TYR GLU ARG TYR LEU LYS GLU LEU
SEQRES 23 A 329 SER HIS ASP ILE SER LEU MET LYS SER SER ILE LEU GLN
SEQRES 24 A 329 GLN LYS ALA ILE ASN ASP VAL ALA PRO PHE PHE ASN VAL
SEQRES 25 A 329 SER PRO GLU GLN LEU ALA ASN GLU ILE GLN PHE ASN GLN
SEQRES 26 A 329 ALA PRO ALA ASN
HET BEN A 501 9
HET BEN A 502 9
HET BEN A 503 9
HET UTP A 504 29
HET MN A 505 1
HET MN A 506 1
HET MN A 507 1
HETNAM BEN BENZAMIDINE
HETNAM UTP URIDINE 5'-TRIPHOSPHATE
HETNAM MN MANGANESE (II) ION
FORMUL 2 BEN 3(C7 H8 N2)
FORMUL 5 UTP C9 H15 N2 O15 P3
FORMUL 6 MN 3(MN 2+)
FORMUL 9 HOH *377(H2 O)
HELIX 1 1 SER A 108 THR A 133 1 26
HELIX 2 2 GLY A 136 ARG A 146 1 11
HELIX 3 3 THR A 149 GLY A 157 1 9
HELIX 4 4 HIS A 166 LYS A 175 1 10
HELIX 5 5 ASP A 178 ALA A 185 1 8
HELIX 6 6 ASN A 248 ASP A 260 1 13
HELIX 7 7 GLY A 267 GLY A 278 1 12
HELIX 8 8 SER A 291 THR A 302 1 12
HELIX 9 9 ASP A 312 GLN A 329 1 18
HELIX 10 10 ASP A 343 GLY A 352 1 10
HELIX 11 11 GLY A 352 ASP A 363 1 12
HELIX 12 12 PHE A 367 LEU A 375 1 9
HELIX 13 13 LEU A 375 ASN A 382 1 8
HELIX 14 14 ASN A 382 MET A 400 1 19
HELIX 15 15 SER A 402 ALA A 414 1 13
HELIX 16 16 PRO A 415 ASN A 418 5 4
HELIX 17 17 SER A 420 ILE A 428 1 9
SHEET 1 A 4 GLY A 159 ALA A 161 0
SHEET 2 A 4 ARG A 204 LYS A 210 -1 O ARG A 204 N ALA A 161
SHEET 3 A 4 ILE A 216 ARG A 222 -1 O ARG A 222 N ILE A 205
SHEET 4 A 4 TYR A 231 ASN A 233 -1 O LEU A 232 N GLY A 221
SHEET 1 B 2 LEU A 188 ASN A 191 0
SHEET 2 B 2 SER A 196 ASP A 199 -1 O TYR A 198 N SER A 189
SHEET 1 C 5 VAL A 282 ALA A 284 0
SHEET 2 C 5 ILE A 262 LEU A 265 1 N LEU A 265 O VAL A 283
SHEET 3 C 5 ASN A 304 LEU A 307 1 O THR A 306 N ILE A 262
SHEET 4 C 5 ASN A 332 VAL A 335 1 O PHE A 334 N LEU A 307
SHEET 5 C 5 LYS A 365 SER A 366 -1 O LYS A 365 N VAL A 335
LINK OD2 ASP A 310 MN MN A 506 1555 1555 2.46
LINK OD2 ASP A 343 MN MN A 506 1555 1555 2.45
LINK OD2 ASP A 343 MN MN A 507 1555 1555 2.42
LINK O2A UTP A 504 MN MN A 506 1555 1555 2.44
LINK O2B UTP A 504 MN MN A 506 1555 1555 2.49
LINK O1G UTP A 504 MN MN A 507 1555 1555 2.41
LINK O2B UTP A 504 MN MN A 507 1555 1555 2.57
LINK MN MN A 505 O HOH A 623 1555 1555 2.53
LINK MN MN A 505 O HOH A 710 1555 1555 2.66
LINK MN MN A 505 O HOH A 738 1555 1555 2.63
LINK MN MN A 505 O HOH A 789 1555 1555 2.64
LINK MN MN A 505 O HOH A 908 1555 1555 2.65
LINK MN MN A 505 O HOH A 923 1555 1555 2.59
LINK MN MN A 506 O HOH A 834 1555 1555 2.57
LINK MN MN A 506 O HOH A 932 1555 1555 2.45
LINK MN MN A 507 O HOH A 634 1555 1555 2.51
LINK MN MN A 507 O HOH A 930 1555 1555 2.56
LINK MN MN A 507 O HOH A 931 1555 1555 2.51
CISPEP 1 GLU A 228 PRO A 229 0 -1.82
SITE 1 AC1 6 GLU A 117 PHE A 125 TYR A 128 VAL A 134
SITE 2 AC1 6 HOH A 702 HOH A 734
SITE 1 AC2 6 GLN A 289 LEU A 290 SER A 291 ASP A 292
SITE 2 AC2 6 LYS A 321 HIS A 325
SITE 1 AC3 4 GLY A 287 UTP A 504 HOH A 796 HOH A 855
SITE 1 AC4 25 ARG A 146 ARG A 222 PRO A 229 LYS A 230
SITE 2 AC4 25 TYR A 231 ASN A 233 GLU A 266 GLY A 267
SITE 3 AC4 25 PHE A 268 ASP A 270 MET A 286 GLY A 287
SITE 4 AC4 25 ASP A 310 ASP A 343 BEN A 503 MN A 506
SITE 5 AC4 25 MN A 507 HOH A 618 HOH A 634 HOH A 652
SITE 6 AC4 25 HOH A 738 HOH A 796 HOH A 834 HOH A 930
SITE 7 AC4 25 HOH A 965
SITE 1 AC5 6 HOH A 623 HOH A 710 HOH A 738 HOH A 789
SITE 2 AC5 6 HOH A 908 HOH A 923
SITE 1 AC6 6 ASP A 310 ASP A 343 UTP A 504 MN A 507
SITE 2 AC6 6 HOH A 834 HOH A 932
SITE 1 AC7 6 ASP A 343 UTP A 504 MN A 506 HOH A 634
SITE 2 AC7 6 HOH A 930 HOH A 931
CRYST1 150.582 150.582 38.633 90.00 90.00 120.00 P 61 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 0.006641 0.003834 0.000000 0.00000
SCALE2 0.000000 0.007668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025885 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
