HEADER TRANSFERASE/DNA 06-DEC-10 3PV8
TITLE CRYSTAL STRUCTURE OF BACILLUS DNA POLYMERASE I LARGE FRAGMENT BOUND TO
TITLE 2 DNA AND DDTTP-DA IN CLOSED CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE I;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: BACILLUS FRAGMENT (ANALOGOUS TO E. COLI KLENOW FRAGMENT);
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*CP*CP*TP*GP*AP*CP*TP*CP*(2DT))-3');
COMPND 10 CHAIN: B, E;
COMPND 11 FRAGMENT: DNA PRIMER STRAND;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA (5'-D(*C*AP*TP*AP*AP*GP*AP*GP*TP*CP*AP*GP*G)-3');
COMPND 15 CHAIN: C, F;
COMPND 16 FRAGMENT: DNA TEMPLATE STRAND;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS KAUSTOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1462;
SOURCE 4 GENE: POLA, GK2730;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES
KEYWDS DNA POLYMERASE I, PROTEIN-DNA COMPLEX, THYMINE-ADENINE, CLOSED
KEYWDS 2 CONFORMATION, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.WANG,L.S.BEESE
REVDAT 5 06-SEP-23 3PV8 1 REMARK SEQADV LINK
REVDAT 4 17-JUL-19 3PV8 1 REMARK LINK
REVDAT 3 09-NOV-11 3PV8 1 JRNL
REVDAT 2 02-NOV-11 3PV8 1 JRNL
REVDAT 1 19-OCT-11 3PV8 0
JRNL AUTH W.WANG,H.W.HELLINGA,L.S.BEESE
JRNL TITL STRUCTURAL EVIDENCE FOR THE RARE TAUTOMER HYPOTHESIS OF
JRNL TITL 2 SPONTANEOUS MUTAGENESIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 17644 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 22006298
JRNL DOI 10.1073/PNAS.1114496108
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 88.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 222603
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 10319
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 88.5717 - 4.7228 0.97 7734 404 0.2037 0.2282
REMARK 3 2 4.7228 - 3.7486 0.99 7647 399 0.1617 0.1735
REMARK 3 3 3.7486 - 3.2747 0.99 7537 388 0.1679 0.1822
REMARK 3 4 3.2747 - 2.9753 0.99 7559 384 0.1825 0.2002
REMARK 3 5 2.9753 - 2.7620 0.99 7558 352 0.1846 0.2236
REMARK 3 6 2.7620 - 2.5992 0.99 7556 319 0.1788 0.1922
REMARK 3 7 2.5992 - 2.4690 0.99 7520 314 0.1706 0.1939
REMARK 3 8 2.4690 - 2.3615 0.99 7495 313 0.1710 0.2082
REMARK 3 9 2.3615 - 2.2706 0.96 7319 270 0.1687 0.2047
REMARK 3 10 2.2706 - 2.1922 0.87 6503 313 0.2274 0.2454
REMARK 3 11 2.1922 - 2.1237 0.98 7471 288 0.1711 0.1858
REMARK 3 12 2.1237 - 2.0630 0.98 7423 299 0.1718 0.1893
REMARK 3 13 2.0630 - 2.0086 0.98 7462 262 0.1722 0.2005
REMARK 3 14 2.0086 - 1.9596 0.97 7287 319 0.1789 0.2139
REMARK 3 15 1.9596 - 1.9151 0.86 6402 337 0.2626 0.2825
REMARK 3 16 1.9151 - 1.8743 0.83 6184 325 0.2043 0.2524
REMARK 3 17 1.8743 - 1.8368 0.95 7136 376 0.1815 0.2270
REMARK 3 18 1.8368 - 1.8022 0.96 7131 375 0.1845 0.2371
REMARK 3 19 1.8022 - 1.7700 0.96 7130 375 0.1852 0.2183
REMARK 3 20 1.7700 - 1.7400 0.95 7038 371 0.1899 0.2519
REMARK 3 21 1.7400 - 1.7119 0.94 7010 369 0.1871 0.2263
REMARK 3 22 1.7119 - 1.6856 0.93 6979 367 0.1887 0.2280
REMARK 3 23 1.6856 - 1.6608 0.93 6949 366 0.1934 0.2233
REMARK 3 24 1.6608 - 1.6374 0.93 6948 365 0.1975 0.2279
REMARK 3 25 1.6374 - 1.6152 0.92 6804 358 0.2072 0.2436
REMARK 3 26 1.6152 - 1.5943 0.91 6790 358 0.2088 0.2251
REMARK 3 27 1.5943 - 1.5743 0.90 6729 354 0.2179 0.2467
REMARK 3 28 1.5743 - 1.5554 0.90 6643 350 0.2247 0.2749
REMARK 3 29 1.5554 - 1.5373 0.86 6405 337 0.2301 0.2596
REMARK 3 30 1.5373 - 1.5200 0.80 5935 312 0.2435 0.2591
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.77
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 44.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.450
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) : 1.74890
REMARK 3 B22 (A**2) : -1.29450
REMARK 3 B33 (A**2) : -0.45440
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 : 0.009 10543
REMARK 3 ANGLE : 1.245 14455
REMARK 3 CHIRALITY : 0.067 1615
REMARK 3 PLANARITY : 0.006 1724
REMARK 3 DIHEDRAL : 15.281 4085
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 3PV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97121
REMARK 200 MONOCHROMATOR : NULL
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 231085
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2HVI WITH INSERTION SITE BASE PAIR,
REMARK 200 METAL IONS, AND PROTEIN RESIDUES 681-727 DELETED.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MPD, MGSO4, MES, PH
REMARK 280 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 46.94500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.21000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.21000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.94500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 285
REMARK 465 GLU A 286
REMARK 465 SER A 287
REMARK 465 PRO A 288
REMARK 465 SER A 289
REMARK 465 SER A 290
REMARK 465 GLU A 291
REMARK 465 GLU A 292
REMARK 465 GLU A 293
REMARK 465 LYS A 294
REMARK 465 PRO A 295
REMARK 465 LEU A 296
REMARK 465 ALA A 297
REMARK 465 MET D 285
REMARK 465 GLU D 286
REMARK 465 SER D 287
REMARK 465 PRO D 288
REMARK 465 SER D 289
REMARK 465 SER D 290
REMARK 465 GLU D 291
REMARK 465 GLU D 292
REMARK 465 GLU D 293
REMARK 465 LYS D 294
REMARK 465 PRO D 295
REMARK 465 LEU D 296
REMARK 465 ALA D 297
REMARK 465 DC C 0
REMARK 465 DC F 0
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 LYS D 298 CG CD CE NZ
REMARK 470 DA C 1 P OP1 OP2
REMARK 470 DA F 1 P OP1 OP2
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 HD1 HIS D 664 H ARG D 859 1.27
REMARK 500 HD1 HIS A 328 HE1 TRP A 382 1.34
REMARK 500 OE2 GLU A 325 HH12 ARG A 435 1.43
REMARK 500 HE ARG D 596 O HOH D 1265 1.45
REMARK 500 HE ARG A 596 O HOH A 86 1.50
REMARK 500 HE ARG D 703 O HOH D 1320 1.56
REMARK 500 HH11 ARG A 703 O HOH A 1540 1.58
REMARK 500 O HOH D 1820 O HOH D 1822 2.12
REMARK 500 O HOH D 1219 O HOH D 1337 2.15
REMARK 500 O HOH F 1594 O HOH F 1597 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 HOH A 1802 O HOH D 1799 2755 2.03
REMARK 500 O HOH D 1388 O HOH D 1419 4545 2.05
REMARK 500 O HOH A 1795 O HOH A 1798 3755 2.11
REMARK 500 O HOH A 1747 O HOH D 1762 2745 2.15
REMARK 500 O HOH D 1120 O HOH D 1183 4445 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DC E 26 O3' DC E 26 C3' -0.045
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DT B 23 O4' - C1' - N1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 DC B 26 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT C 2 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 DT C 8 O4' - C1' - N1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DG C 12 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC E 21 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT E 23 O4' - C1' - N1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC E 26 O4' - C4' - C3' ANGL. DEV. = 3.8 DEGREES
REMARK 500 DC E 26 O4' - C1' - N1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 DT E 27 O5' - P - OP2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DT E 27 C4' - C3' - C2' ANGL. DEV. = -4.7 DEGREES
REMARK 500 DT E 27 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT F 2 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DA F 4 O4' - C1' - C2' ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT F 8 O4' - C1' - N1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 DG F 12 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
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 ASP A 372 69.35 61.45
REMARK 500 ASP A 402 103.12 -163.56
REMARK 500 ASP A 408 11.98 -144.17
REMARK 500 ALA A 421 40.80 -90.17
REMARK 500 ILE A 588 -69.13 -106.99
REMARK 500 LEU A 610 -54.10 -122.61
REMARK 500 ILE A 628 -29.84 -149.34
REMARK 500 GLN A 691 -9.64 91.55
REMARK 500 HIS A 768 20.77 81.70
REMARK 500 ARG A 819 51.86 36.03
REMARK 500 HIS A 829 -53.53 76.93
REMARK 500 ALA A 875 46.74 -73.86
REMARK 500 ASP D 372 61.34 62.80
REMARK 500 ASP D 402 94.79 -167.70
REMARK 500 ALA D 421 45.64 -88.19
REMARK 500 GLU D 540 -60.36 -107.32
REMARK 500 ILE D 588 -72.98 -105.59
REMARK 500 ILE D 588 -70.74 -108.61
REMARK 500 LEU D 610 -52.89 -123.92
REMARK 500 ILE D 628 -29.92 -149.04
REMARK 500 HIS D 768 16.63 84.63
REMARK 500 HIS D 829 -53.99 73.69
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 MG A 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 D3T A 201 O2B
REMARK 620 2 D3T A 201 O2G 86.6
REMARK 620 3 D3T A 201 O2A 84.7 96.0
REMARK 620 4 ASP A 653 OD1 160.3 96.2 114.3
REMARK 620 5 TYR A 654 O 92.8 88.6 174.7 67.9
REMARK 620 6 ASP A 830 OD2 98.2 173.9 88.2 78.0 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 2 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 D3T D 202 O2B
REMARK 620 2 D3T D 202 O2G 79.6
REMARK 620 3 D3T D 202 O2A 83.4 93.9
REMARK 620 4 TYR D 654 O 99.4 91.8 174.0
REMARK 620 5 ASP D 830 OD2 104.2 173.2 81.1 93.1
REMARK 620 6 HOH D1823 O 156.8 82.6 83.0 95.9 92.1
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 MG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3T A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3T D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PX0 RELATED DB: PDB
REMARK 900 RELATED ID: 3PX4 RELATED DB: PDB
REMARK 900 RELATED ID: 3PX6 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE PROTEIN WAS ISOLATED FROM A STRAIN OF
REMARK 999 GEOBACILLUS SPECIES WHOSE SEQUENCE IS NOT AVAILABLE IN THE UNIPROT
REMARK 999 DATABASE. IT DIFFERS FROM UNP Q5KWC1 BY THIS SINGLE RESIDUE.
DBREF 3PV8 A 285 876 UNP Q5KWC1 Q5KWC1_GEOKA 287 878
DBREF 3PV8 D 285 876 UNP Q5KWC1 Q5KWC1_GEOKA 287 878
DBREF 3PV8 B 21 29 PDB 3PV8 3PV8 21 29
DBREF 3PV8 E 21 29 PDB 3PV8 3PV8 21 29
DBREF 3PV8 C 0 12 PDB 3PV8 3PV8 0 12
DBREF 3PV8 F 0 12 PDB 3PV8 3PV8 0 12
SEQADV 3PV8 ALA A 598 UNP Q5KWC1 ASP 600 ENGINEERED MUTATION
SEQADV 3PV8 TYR A 710 UNP Q5KWC1 PHE 712 ENGINEERED MUTATION
SEQADV 3PV8 HIS A 823 UNP Q5KWC1 ARG 825 SEE REMARK 999
SEQADV 3PV8 ALA D 598 UNP Q5KWC1 ASP 600 ENGINEERED MUTATION
SEQADV 3PV8 TYR D 710 UNP Q5KWC1 PHE 712 ENGINEERED MUTATION
SEQADV 3PV8 HIS D 823 UNP Q5KWC1 ARG 825 SEE REMARK 999
SEQRES 1 A 592 MET GLU SER PRO SER SER GLU GLU GLU LYS PRO LEU ALA
SEQRES 2 A 592 LYS MET ALA PHE THR LEU ALA ASP ARG VAL THR GLU GLU
SEQRES 3 A 592 MET LEU ALA ASP LYS ALA ALA LEU VAL VAL GLU VAL VAL
SEQRES 4 A 592 GLU GLU ASN TYR HIS ASP ALA PRO ILE VAL GLY ILE ALA
SEQRES 5 A 592 VAL VAL ASN GLU HIS GLY ARG PHE PHE LEU ARG PRO GLU
SEQRES 6 A 592 THR ALA LEU ALA ASP PRO GLN PHE VAL ALA TRP LEU GLY
SEQRES 7 A 592 ASP GLU THR LYS LYS LYS SER MET PHE ASP SER LYS ARG
SEQRES 8 A 592 ALA ALA VAL ALA LEU LYS TRP LYS GLY ILE GLU LEU CYS
SEQRES 9 A 592 GLY VAL SER PHE ASP LEU LEU LEU ALA ALA TYR LEU LEU
SEQRES 10 A 592 ASP PRO ALA GLN GLY VAL ASP ASP VAL ALA ALA ALA ALA
SEQRES 11 A 592 LYS MET LYS GLN TYR GLU ALA VAL ARG PRO ASP GLU ALA
SEQRES 12 A 592 VAL TYR GLY LYS GLY ALA LYS ARG ALA VAL PRO ASP GLU
SEQRES 13 A 592 PRO VAL LEU ALA GLU HIS LEU VAL ARG LYS ALA ALA ALA
SEQRES 14 A 592 ILE TRP GLU LEU GLU ARG PRO PHE LEU ASP GLU LEU ARG
SEQRES 15 A 592 ARG ASN GLU GLN ASP ARG LEU LEU VAL GLU LEU GLU GLN
SEQRES 16 A 592 PRO LEU SER SER ILE LEU ALA GLU MET GLU PHE ALA GLY
SEQRES 17 A 592 VAL LYS VAL ASP THR LYS ARG LEU GLU GLN MET GLY LYS
SEQRES 18 A 592 GLU LEU ALA GLU GLN LEU GLY THR VAL GLU GLN ARG ILE
SEQRES 19 A 592 TYR GLU LEU ALA GLY GLN GLU PHE ASN ILE ASN SER PRO
SEQRES 20 A 592 LYS GLN LEU GLY VAL ILE LEU PHE GLU LYS LEU GLN LEU
SEQRES 21 A 592 PRO VAL LEU LYS LYS THR LYS THR GLY TYR SER THR SER
SEQRES 22 A 592 ALA ASP VAL LEU GLU LYS LEU ALA PRO TYR HIS GLU ILE
SEQRES 23 A 592 VAL GLU ASN ILE LEU HIS TYR ARG GLN LEU GLY LYS LEU
SEQRES 24 A 592 GLN SER THR TYR ILE GLU GLY LEU LEU LYS VAL VAL ARG
SEQRES 25 A 592 PRO ALA THR LYS LYS VAL HIS THR ILE PHE ASN GLN ALA
SEQRES 26 A 592 LEU THR GLN THR GLY ARG LEU SER SER THR GLU PRO ASN
SEQRES 27 A 592 LEU GLN ASN ILE PRO ILE ARG LEU GLU GLU GLY ARG LYS
SEQRES 28 A 592 ILE ARG GLN ALA PHE VAL PRO SER GLU SER ASP TRP LEU
SEQRES 29 A 592 ILE PHE ALA ALA ASP TYR SER GLN ILE GLU LEU ARG VAL
SEQRES 30 A 592 LEU ALA HIS ILE ALA GLU ASP ASP ASN LEU MET GLU ALA
SEQRES 31 A 592 PHE ARG ARG ASP LEU ASP ILE HIS THR LYS THR ALA MET
SEQRES 32 A 592 ASP ILE PHE GLN VAL SER GLU ASP GLU VAL THR PRO ASN
SEQRES 33 A 592 MET ARG ARG GLN ALA LYS ALA VAL ASN TYR GLY ILE VAL
SEQRES 34 A 592 TYR GLY ILE SER ASP TYR GLY LEU ALA GLN ASN LEU ASN
SEQRES 35 A 592 ILE SER ARG LYS GLU ALA ALA GLU PHE ILE GLU ARG TYR
SEQRES 36 A 592 PHE GLU SER PHE PRO GLY VAL LYS ARG TYR MET GLU ASN
SEQRES 37 A 592 ILE VAL GLN GLU ALA LYS GLN LYS GLY TYR VAL THR THR
SEQRES 38 A 592 LEU LEU HIS ARG ARG ARG TYR LEU PRO ASP ILE THR SER
SEQRES 39 A 592 ARG ASN PHE ASN VAL ARG SER PHE ALA GLU ARG MET ALA
SEQRES 40 A 592 MET ASN THR PRO ILE GLN GLY SER ALA ALA ASP ILE ILE
SEQRES 41 A 592 LYS LYS ALA MET ILE ASP LEU ASN ALA ARG LEU LYS GLU
SEQRES 42 A 592 GLU ARG LEU GLN ALA HIS LEU LEU LEU GLN VAL HIS ASP
SEQRES 43 A 592 GLU LEU ILE LEU GLU ALA PRO LYS GLU GLU MET GLU ARG
SEQRES 44 A 592 LEU CYS ARG LEU VAL PRO GLU VAL MET GLU GLN ALA VAL
SEQRES 45 A 592 THR LEU ARG VAL PRO LEU LYS VAL ASP TYR HIS TYR GLY
SEQRES 46 A 592 SER THR TRP TYR ASP ALA LYS
SEQRES 1 D 592 MET GLU SER PRO SER SER GLU GLU GLU LYS PRO LEU ALA
SEQRES 2 D 592 LYS MET ALA PHE THR LEU ALA ASP ARG VAL THR GLU GLU
SEQRES 3 D 592 MET LEU ALA ASP LYS ALA ALA LEU VAL VAL GLU VAL VAL
SEQRES 4 D 592 GLU GLU ASN TYR HIS ASP ALA PRO ILE VAL GLY ILE ALA
SEQRES 5 D 592 VAL VAL ASN GLU HIS GLY ARG PHE PHE LEU ARG PRO GLU
SEQRES 6 D 592 THR ALA LEU ALA ASP PRO GLN PHE VAL ALA TRP LEU GLY
SEQRES 7 D 592 ASP GLU THR LYS LYS LYS SER MET PHE ASP SER LYS ARG
SEQRES 8 D 592 ALA ALA VAL ALA LEU LYS TRP LYS GLY ILE GLU LEU CYS
SEQRES 9 D 592 GLY VAL SER PHE ASP LEU LEU LEU ALA ALA TYR LEU LEU
SEQRES 10 D 592 ASP PRO ALA GLN GLY VAL ASP ASP VAL ALA ALA ALA ALA
SEQRES 11 D 592 LYS MET LYS GLN TYR GLU ALA VAL ARG PRO ASP GLU ALA
SEQRES 12 D 592 VAL TYR GLY LYS GLY ALA LYS ARG ALA VAL PRO ASP GLU
SEQRES 13 D 592 PRO VAL LEU ALA GLU HIS LEU VAL ARG LYS ALA ALA ALA
SEQRES 14 D 592 ILE TRP GLU LEU GLU ARG PRO PHE LEU ASP GLU LEU ARG
SEQRES 15 D 592 ARG ASN GLU GLN ASP ARG LEU LEU VAL GLU LEU GLU GLN
SEQRES 16 D 592 PRO LEU SER SER ILE LEU ALA GLU MET GLU PHE ALA GLY
SEQRES 17 D 592 VAL LYS VAL ASP THR LYS ARG LEU GLU GLN MET GLY LYS
SEQRES 18 D 592 GLU LEU ALA GLU GLN LEU GLY THR VAL GLU GLN ARG ILE
SEQRES 19 D 592 TYR GLU LEU ALA GLY GLN GLU PHE ASN ILE ASN SER PRO
SEQRES 20 D 592 LYS GLN LEU GLY VAL ILE LEU PHE GLU LYS LEU GLN LEU
SEQRES 21 D 592 PRO VAL LEU LYS LYS THR LYS THR GLY TYR SER THR SER
SEQRES 22 D 592 ALA ASP VAL LEU GLU LYS LEU ALA PRO TYR HIS GLU ILE
SEQRES 23 D 592 VAL GLU ASN ILE LEU HIS TYR ARG GLN LEU GLY LYS LEU
SEQRES 24 D 592 GLN SER THR TYR ILE GLU GLY LEU LEU LYS VAL VAL ARG
SEQRES 25 D 592 PRO ALA THR LYS LYS VAL HIS THR ILE PHE ASN GLN ALA
SEQRES 26 D 592 LEU THR GLN THR GLY ARG LEU SER SER THR GLU PRO ASN
SEQRES 27 D 592 LEU GLN ASN ILE PRO ILE ARG LEU GLU GLU GLY ARG LYS
SEQRES 28 D 592 ILE ARG GLN ALA PHE VAL PRO SER GLU SER ASP TRP LEU
SEQRES 29 D 592 ILE PHE ALA ALA ASP TYR SER GLN ILE GLU LEU ARG VAL
SEQRES 30 D 592 LEU ALA HIS ILE ALA GLU ASP ASP ASN LEU MET GLU ALA
SEQRES 31 D 592 PHE ARG ARG ASP LEU ASP ILE HIS THR LYS THR ALA MET
SEQRES 32 D 592 ASP ILE PHE GLN VAL SER GLU ASP GLU VAL THR PRO ASN
SEQRES 33 D 592 MET ARG ARG GLN ALA LYS ALA VAL ASN TYR GLY ILE VAL
SEQRES 34 D 592 TYR GLY ILE SER ASP TYR GLY LEU ALA GLN ASN LEU ASN
SEQRES 35 D 592 ILE SER ARG LYS GLU ALA ALA GLU PHE ILE GLU ARG TYR
SEQRES 36 D 592 PHE GLU SER PHE PRO GLY VAL LYS ARG TYR MET GLU ASN
SEQRES 37 D 592 ILE VAL GLN GLU ALA LYS GLN LYS GLY TYR VAL THR THR
SEQRES 38 D 592 LEU LEU HIS ARG ARG ARG TYR LEU PRO ASP ILE THR SER
SEQRES 39 D 592 ARG ASN PHE ASN VAL ARG SER PHE ALA GLU ARG MET ALA
SEQRES 40 D 592 MET ASN THR PRO ILE GLN GLY SER ALA ALA ASP ILE ILE
SEQRES 41 D 592 LYS LYS ALA MET ILE ASP LEU ASN ALA ARG LEU LYS GLU
SEQRES 42 D 592 GLU ARG LEU GLN ALA HIS LEU LEU LEU GLN VAL HIS ASP
SEQRES 43 D 592 GLU LEU ILE LEU GLU ALA PRO LYS GLU GLU MET GLU ARG
SEQRES 44 D 592 LEU CYS ARG LEU VAL PRO GLU VAL MET GLU GLN ALA VAL
SEQRES 45 D 592 THR LEU ARG VAL PRO LEU LYS VAL ASP TYR HIS TYR GLY
SEQRES 46 D 592 SER THR TRP TYR ASP ALA LYS
SEQRES 1 B 9 DC DC DT DG DA DC DT DC 2DT
SEQRES 1 C 13 DC DA DT DA DA DG DA DG DT DC DA DG DG
SEQRES 1 E 9 DC DC DT DG DA DC DT DC 2DT
SEQRES 1 F 13 DC DA DT DA DA DG DA DG DT DC DA DG DG
MODRES 3PV8 2DT B 29 DT 3'-DEOXYTHYMIDINE-5'-MONOPHOSPHATE
MODRES 3PV8 2DT E 29 DT 3'-DEOXYTHYMIDINE-5'-MONOPHOSPHATE
HET 2DT B 29 30
HET 2DT E 29 30
HET MG A 1 1
HET D3T A 201 40
HET SO4 A 2 5
HET MG D 2 1
HET D3T D 202 40
HET SO4 D 1 5
HET SO4 D 3 5
HETNAM 2DT 3'-DEOXYTHYMIDINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM D3T 2',3'-DIDEOXY-THYMIDINE-5'-TRIPHOSPHATE
HETNAM SO4 SULFATE ION
HETSYN 2DT 2',3'-DIDEOXYTHYMIDINE-5'-MONOPHOSPHATE
FORMUL 3 2DT 2(C10 H15 N2 O7 P)
FORMUL 7 MG 2(MG 2+)
FORMUL 8 D3T 2(C10 H17 N2 O13 P3)
FORMUL 9 SO4 3(O4 S 2-)
FORMUL 14 HOH *1823(H2 O)
HELIX 1 1 THR A 308 ALA A 313 5 6
HELIX 2 2 ARG A 347 LEU A 352 1 6
HELIX 3 3 ASP A 354 GLY A 362 1 9
HELIX 4 4 ASP A 372 LYS A 383 1 12
HELIX 5 5 LEU A 394 ASP A 402 1 9
HELIX 6 6 PRO A 403 GLY A 406 5 4
HELIX 7 7 ASP A 409 LYS A 415 1 7
HELIX 8 8 MET A 416 GLN A 418 5 3
HELIX 9 9 PRO A 424 GLY A 430 1 7
HELIX 10 10 LYS A 431 ARG A 435 5 5
HELIX 11 11 ASP A 439 ASN A 468 1 30
HELIX 12 12 GLN A 470 LEU A 477 1 8
HELIX 13 13 LEU A 477 GLY A 492 1 16
HELIX 14 14 ASP A 496 GLY A 523 1 28
HELIX 15 15 SER A 530 GLU A 540 1 11
HELIX 16 16 SER A 557 LEU A 564 1 8
HELIX 17 17 GLU A 569 ILE A 588 1 20
HELIX 18 18 ILE A 588 VAL A 595 1 8
HELIX 19 19 LEU A 630 LYS A 635 1 6
HELIX 20 20 ILE A 636 GLN A 638 5 3
HELIX 21 21 GLN A 656 GLU A 667 1 12
HELIX 22 22 ASP A 668 ARG A 677 1 10
HELIX 23 23 ASP A 680 GLN A 691 1 12
HELIX 24 24 THR A 698 TYR A 714 1 17
HELIX 25 25 SER A 717 ASN A 726 1 10
HELIX 26 26 SER A 728 PHE A 743 1 16
HELIX 27 27 PHE A 743 GLY A 761 1 19
HELIX 28 28 PRO A 774 SER A 778 5 5
HELIX 29 29 ASN A 780 GLU A 818 1 39
HELIX 30 30 GLU A 840 GLN A 854 1 15
HELIX 31 31 THR D 308 LEU D 312 5 5
HELIX 32 32 ARG D 347 LEU D 352 1 6
HELIX 33 33 ASP D 354 ASP D 363 1 10
HELIX 34 34 ASP D 372 LYS D 383 1 12
HELIX 35 35 LEU D 394 ASP D 402 1 9
HELIX 36 36 PRO D 403 GLY D 406 5 4
HELIX 37 37 ASP D 409 MET D 416 1 8
HELIX 38 38 PRO D 424 GLY D 430 1 7
HELIX 39 39 LYS D 431 ARG D 435 5 5
HELIX 40 40 ASP D 439 ASN D 468 1 30
HELIX 41 41 GLN D 470 LEU D 477 1 8
HELIX 42 42 LEU D 477 GLY D 492 1 16
HELIX 43 43 ASP D 496 GLY D 523 1 28
HELIX 44 44 SER D 530 GLU D 540 1 11
HELIX 45 45 SER D 557 LEU D 564 1 8
HELIX 46 46 GLU D 569 ILE D 588 1 20
HELIX 47 47 ILE D 588 VAL D 595 1 8
HELIX 48 48 LEU D 630 LYS D 635 1 6
HELIX 49 49 ILE D 636 GLN D 638 5 3
HELIX 50 50 GLN D 656 GLU D 667 1 12
HELIX 51 51 ASP D 668 ARG D 677 1 10
HELIX 52 52 ASP D 680 PHE D 690 1 11
HELIX 53 53 SER D 693 VAL D 697 5 5
HELIX 54 54 THR D 698 TYR D 714 1 17
HELIX 55 55 SER D 717 ASN D 726 1 10
HELIX 56 56 SER D 728 PHE D 743 1 16
HELIX 57 57 PHE D 743 GLY D 761 1 19
HELIX 58 58 PRO D 774 SER D 778 5 5
HELIX 59 59 ASN D 780 GLU D 818 1 39
HELIX 60 60 GLU D 840 GLN D 854 1 15
SHEET 1 A 6 THR A 302 LEU A 303 0
SHEET 2 A 6 GLY A 342 LEU A 346 1 O ARG A 343 N THR A 302
SHEET 3 A 6 GLY A 334 ASN A 339 -1 N VAL A 337 O PHE A 344
SHEET 4 A 6 LYS A 315 GLU A 321 -1 N ALA A 317 O VAL A 338
SHEET 5 A 6 LYS A 367 MET A 370 1 O SER A 369 N ALA A 316
SHEET 6 A 6 VAL A 390 ASP A 393 1 O PHE A 392 N MET A 370
SHEET 1 B 3 LYS A 601 VAL A 602 0
SHEET 2 B 3 VAL A 493 VAL A 495 -1 N VAL A 493 O VAL A 602
SHEET 3 B 3 PHE A 640 VAL A 641 -1 O VAL A 641 N LYS A 494
SHEET 1 C 2 LYS A 549 THR A 550 0
SHEET 2 C 2 GLY A 553 TYR A 554 -1 O GLY A 553 N THR A 550
SHEET 1 D 2 ILE A 605 ASN A 607 0
SHEET 2 D 2 SER A 617 THR A 619 -1 O THR A 619 N ILE A 605
SHEET 1 E 4 HIS A 823 GLN A 827 0
SHEET 2 E 4 GLU A 831 PRO A 837 -1 O ILE A 833 N LEU A 825
SHEET 3 E 4 TRP A 647 TYR A 654 -1 N PHE A 650 O LEU A 834
SHEET 4 E 4 VAL A 864 GLY A 869 -1 O HIS A 867 N ALA A 651
SHEET 1 F 2 TYR A 762 THR A 764 0
SHEET 2 F 2 ARG A 770 TYR A 772 -1 O ARG A 771 N VAL A 763
SHEET 1 G 6 THR D 302 LEU D 303 0
SHEET 2 G 6 GLY D 342 LEU D 346 1 O PHE D 345 N THR D 302
SHEET 3 G 6 GLY D 334 ASN D 339 -1 N ILE D 335 O LEU D 346
SHEET 4 G 6 LYS D 315 GLU D 321 -1 N ALA D 317 O VAL D 338
SHEET 5 G 6 LYS D 367 MET D 370 1 O SER D 369 N ALA D 316
SHEET 6 G 6 VAL D 390 ASP D 393 1 O PHE D 392 N MET D 370
SHEET 1 H 3 LYS D 601 VAL D 602 0
SHEET 2 H 3 VAL D 493 VAL D 495 -1 N VAL D 493 O VAL D 602
SHEET 3 H 3 PHE D 640 VAL D 641 -1 O VAL D 641 N LYS D 494
SHEET 1 I 2 LYS D 549 THR D 550 0
SHEET 2 I 2 GLY D 553 TYR D 554 -1 O GLY D 553 N THR D 550
SHEET 1 J 2 ILE D 605 ASN D 607 0
SHEET 2 J 2 SER D 617 THR D 619 -1 O THR D 619 N ILE D 605
SHEET 1 K 4 HIS D 823 GLN D 827 0
SHEET 2 K 4 GLU D 831 PRO D 837 -1 O ILE D 833 N LEU D 825
SHEET 3 K 4 TRP D 647 TYR D 654 -1 N PHE D 650 O LEU D 834
SHEET 4 K 4 VAL D 864 GLY D 869 -1 O HIS D 867 N ALA D 651
SHEET 1 L 2 TYR D 762 THR D 764 0
SHEET 2 L 2 ARG D 770 TYR D 772 -1 O ARG D 771 N VAL D 763
LINK O3' DC B 28 P 2DT B 29 1555 1555 1.62
LINK O3' DC E 28 P 2DT E 29 1555 1555 1.62
LINK MG MG A 1 O2B D3T A 201 1555 1555 2.18
LINK MG MG A 1 O2G D3T A 201 1555 1555 2.21
LINK MG MG A 1 O2A D3T A 201 1555 1555 2.25
LINK MG MG A 1 OD1AASP A 653 1555 1555 2.44
LINK MG MG A 1 O TYR A 654 1555 1555 2.31
LINK MG MG A 1 OD2 ASP A 830 1555 1555 2.08
LINK MG MG D 2 O2B D3T D 202 1555 1555 2.18
LINK MG MG D 2 O2G D3T D 202 1555 1555 2.23
LINK MG MG D 2 O2A D3T D 202 1555 1555 2.33
LINK MG MG D 2 O TYR D 654 1555 1555 2.24
LINK MG MG D 2 OD2 ASP D 830 1555 1555 1.98
LINK MG MG D 2 O HOH D1823 1555 1555 2.02
CISPEP 1 GLU A 620 PRO A 621 0 0.91
CISPEP 2 GLU D 620 PRO D 621 0 -1.15
SITE 1 AC1 4 D3T A 201 ASP A 653 TYR A 654 ASP A 830
SITE 1 AC2 19 MG A 1 HOH A 120 HOH A 141 ARG A 615
SITE 2 AC2 19 ASP A 653 TYR A 654 GLN A 656 ILE A 657
SITE 3 AC2 19 GLU A 658 HIS A 682 ARG A 702 LYS A 706
SITE 4 AC2 19 TYR A 710 ASP A 830 HOH A1311 2DT B 29
SITE 5 AC2 19 HOH B 192 DA C 3 DA C 4
SITE 1 AC3 3 ARG A 517 ASN A 573 LYS D 730
SITE 1 AC4 4 D3T D 202 TYR D 654 ASP D 830 HOH D1823
SITE 1 AC5 22 MG D 2 HOH D 26 HOH D 40 ARG D 615
SITE 2 AC5 22 TYR D 654 SER D 655 GLN D 656 ILE D 657
SITE 3 AC5 22 GLU D 658 HIS D 682 ARG D 702 LYS D 706
SITE 4 AC5 22 TYR D 710 ASP D 830 HOH D1107 HOH D1690
SITE 5 AC5 22 HOH D1820 HOH D1823 2DT E 29 HOH E 136
SITE 6 AC5 22 DA F 3 DA F 4
SITE 1 AC6 5 MET D 299 ALA D 300 ARG D 343 ARG D 677
SITE 2 AC6 5 HOH D1451
SITE 1 AC7 3 ARG D 629 ARG D 703 HOH D 956
CRYST1 93.890 109.300 150.420 90.00 90.00 90.00 P 21 21 21 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 0.010651 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006648 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
