HEADER TRANSFERASE 13-JUN-00 1F5A
TITLE CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(A) POLYMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DELETION MUTANT MISSING RESIDUES 514-738;
COMPND 5 EC: 2.7.7.19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MRNA PROCESSING, TRANSFERASE, TRANSCRIPTION, RNA-BINDING,
KEYWDS 2 PHOSPHORYLATION, NUCLEAR PROTEIN, ALTERNATIVE SPLICING HELICAL TURN
KEYWDS 3 MOTIF, NUCLEOTIDYL TRANSFERASE CATALYTIC DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MARTIN,W.KELLER,S.DOUBLIE
REVDAT 3 21-DEC-22 1F5A 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1F5A 1 VERSN
REVDAT 1 13-SEP-00 1F5A 0
JRNL AUTH G.MARTIN,W.KELLER,S.DOUBLIE
JRNL TITL CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE IN COMPLEX
JRNL TITL 2 WITH AN ANALOG OF ATP.
JRNL REF EMBO J. V. 19 4193 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10944102
JRNL DOI 10.1093/EMBOJ/19.16.4193
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.MARTIN,W.KELLER
REMARK 1 TITL MUTATIONAL ANALYSIS OF MAMMALIAN POLY(A) POLYMERASE
REMARK 1 TITL 2 IDENTIFIES A REGION FOR PRIMER BINDING AND CATALYTIC DOMAIN,
REMARK 1 TITL 3 HOMOLOGOUS TO THE FAMILY X POLYMERASES, AND TO OTHER
REMARK 1 TITL 4 NUCLEOTIDYLTRANSFERASES.
REMARK 1 REF EMBO J. V. 15 2593 1996
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.MARTIN,P.JENO,W.KELLER
REMARK 1 TITL MAPPING OF ATP BINDING REGIONS IN POLY(A) POLYMERASES BY
REMARK 1 TITL 2 PHOTOAFFINITY LABELING AND BY MUTATIONAL ANALYSIS IDENTIFIES
REMARK 1 TITL 3 A DOMAIN CONSERVED IN MANY NUCLEOTIDYLTRANSFERASES.
REMARK 1 REF PROTEIN SCI. V. 8 2380 1999
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MHLH
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 19890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1368
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3730
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.29
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.340
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.400 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.050 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.140 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 30.05
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F5A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-99; 20-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0; NULL
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : NSLS; ROTATING ANODE
REMARK 200 BEAMLINE : X12C; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789; 1.5418
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19890
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
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) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, AMMONIUM SULFATE, MES BUFFER,
REMARK 280 CALCIUM CHLORIDE, MANGANESE CHLORIDE, PH 6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 297K
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 28.77500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.84500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.84500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.77500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.36000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: THE BIOLOGICAL ASSEMBLY IS A 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 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 MSE A 1
REMARK 465 PRO A 2
REMARK 465 PHE A 3
REMARK 465 PRO A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 GLN A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLN A 11
REMARK 465 GLN A 12
REMARK 465 THR A 13
REMARK 465 GLN A 14
REMARK 465 PRO A 15
REMARK 465 PRO A 16
REMARK 465 GLN A 17
REMARK 465 LYS A 18
REMARK 465 HIS A 19
REMARK 465 PRO A 424
REMARK 465 LYS A 425
REMARK 465 GLU A 426
REMARK 465 ASN A 427
REMARK 465 PRO A 428
REMARK 465 ASP A 429
REMARK 465 LYS A 445
REMARK 465 THR A 446
REMARK 465 GLU A 447
REMARK 465 ASN A 448
REMARK 465 SER A 449
REMARK 465 GLU A 450
REMARK 465 ASN A 451
REMARK 465 LEU A 452
REMARK 465 SER A 453
REMARK 465 VAL A 454
REMARK 465 SER A 499
REMARK 465 HIS A 500
REMARK 465 VAL A 501
REMARK 465 LEU A 502
REMARK 465 GLN A 503
REMARK 465 LYS A 504
REMARK 465 LYS A 505
REMARK 465 LYS A 506
REMARK 465 LYS A 507
REMARK 465 HIS A 508
REMARK 465 SER A 509
REMARK 465 THR A 510
REMARK 465 GLU A 511
REMARK 465 GLY A 512
REMARK 465 VAL A 513
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 292 CG CD OE1 OE2
REMARK 470 ASN A 294 CG OD1 ND2
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 GLU A 409 CG CD OE1 OE2
REMARK 470 GLN A 419 CG CD OE1 NE2
REMARK 470 LYS A 444 CG CD CE NZ
REMARK 470 MSE A 476 CG SE CE
REMARK 470 MSE A 486 CG SE CE
REMARK 470 HIS A 494 CG ND1 CD2 CE1 NE2
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 PRO A 261 C - N - CA ANGL. DEV. = 10.1 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 HIS A 123 9.41 -61.98
REMARK 500 THR A 131 -86.26 -113.91
REMARK 500 LEU A 139 36.77 -96.82
REMARK 500 ASP A 145 38.70 74.93
REMARK 500 ASP A 186 107.69 -53.14
REMARK 500 ASN A 192 -12.81 73.41
REMARK 500 SER A 238 114.92 178.04
REMARK 500 PHE A 243 -148.93 -101.45
REMARK 500 PRO A 282 40.26 -90.04
REMARK 500 ASN A 294 -80.91 -28.72
REMARK 500 LEU A 295 -12.74 30.16
REMARK 500 ASP A 301 91.45 -172.27
REMARK 500 THR A 326 41.25 -140.15
REMARK 500 ASN A 366 99.67 -68.21
REMARK 500 PHE A 368 21.57 -76.10
REMARK 500 GLN A 369 -3.37 -150.04
REMARK 500 LYS A 475 29.59 46.06
REMARK 500 LEU A 497 -85.29 -133.31
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 A1001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 113 OD2
REMARK 620 2 ASP A 115 OD1 94.3
REMARK 620 3 ASP A 167 OD2 93.0 116.4
REMARK 620 4 3AT A1000 N7 166.0 82.9 100.6
REMARK 620 5 HOH A2155 O 101.5 163.0 57.2 83.2
REMARK 620 6 3PO A4000 O5' 91.5 118.5 124.4 78.0 67.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1002 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 113 OD1
REMARK 620 2 ASP A 115 OD2 104.7
REMARK 620 3 3AT A1000 O2A 166.5 71.8
REMARK 620 4 HOH A2104 O 87.8 84.2 78.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1003 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 3AT A1000 O1G
REMARK 620 2 3AT A1000 O2A 89.2
REMARK 620 3 3AT A1000 O1B 103.7 84.3
REMARK 620 4 3PO A4000 O2A 153.5 67.9 87.6
REMARK 620 5 3PO A4000 O2B 74.9 89.4 173.6 91.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3AT A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PO A 4000
DBREF 1F5A A 1 513 UNP P25500 PAPOA_BOVIN 1 513
SEQADV 1F5A MSE A 1 UNP P25500 MET 0 MODIFIED RESIDUE
SEQADV 1F5A MSE A 251 UNP P25500 MET 251 MODIFIED RESIDUE
SEQADV 1F5A MSE A 313 UNP P25500 MET 313 MODIFIED RESIDUE
SEQADV 1F5A MSE A 335 UNP P25500 MET 335 MODIFIED RESIDUE
SEQADV 1F5A MSE A 337 UNP P25500 MET 337 MODIFIED RESIDUE
SEQADV 1F5A MSE A 436 UNP P25500 MET 436 MODIFIED RESIDUE
SEQADV 1F5A MSE A 476 UNP P25500 MET 476 MODIFIED RESIDUE
SEQADV 1F5A MSE A 481 UNP P25500 MET 476 MODIFIED RESIDUE
SEQADV 1F5A MSE A 486 UNP P25500 MET 486 MODIFIED RESIDUE
SEQRES 1 A 513 MSE PRO PHE PRO VAL THR THR GLN GLY SER GLN GLN THR
SEQRES 2 A 513 GLN PRO PRO GLN LYS HIS TYR GLY ILE THR SER PRO ILE
SEQRES 3 A 513 SER LEU ALA ALA PRO LYS GLU THR ASP CYS LEU LEU THR
SEQRES 4 A 513 GLN LYS LEU VAL GLU THR LEU LYS PRO PHE GLY VAL PHE
SEQRES 5 A 513 GLU GLU GLU GLU GLU LEU GLN ARG ARG ILE LEU ILE LEU
SEQRES 6 A 513 GLY LYS LEU ASN ASN LEU VAL LYS GLU TRP ILE ARG GLU
SEQRES 7 A 513 ILE SER GLU SER LYS ASN LEU PRO GLN SER VAL ILE GLU
SEQRES 8 A 513 ASN VAL GLY GLY LYS ILE PHE THR PHE GLY SER TYR ARG
SEQRES 9 A 513 LEU GLY VAL HIS THR LYS GLY ALA ASP ILE ASP ALA LEU
SEQRES 10 A 513 CYS VAL ALA PRO ARG HIS VAL ASP ARG SER ASP PHE PHE
SEQRES 11 A 513 THR SER PHE TYR ASP LYS LEU LYS LEU GLN GLU GLU VAL
SEQRES 12 A 513 LYS ASP LEU ARG ALA VAL GLU GLU ALA PHE VAL PRO VAL
SEQRES 13 A 513 ILE LYS LEU CYS PHE ASP GLY ILE GLU ILE ASP ILE LEU
SEQRES 14 A 513 PHE ALA ARG LEU ALA LEU GLN THR ILE PRO GLU ASP LEU
SEQRES 15 A 513 ASP LEU ARG ASP ASP SER LEU LEU LYS ASN LEU ASP ILE
SEQRES 16 A 513 ARG CYS ILE ARG SER LEU ASN GLY CYS ARG VAL THR ASP
SEQRES 17 A 513 GLU ILE LEU HIS LEU VAL PRO ASN ILE ASP ASN PHE ARG
SEQRES 18 A 513 LEU THR LEU ARG ALA ILE LYS LEU TRP ALA LYS ARG HIS
SEQRES 19 A 513 ASN ILE TYR SER ASN ILE LEU GLY PHE LEU GLY GLY VAL
SEQRES 20 A 513 SER TRP ALA MSE LEU VAL ALA ARG THR CYS GLN LEU TYR
SEQRES 21 A 513 PRO ASN ALA ILE ALA SER THR LEU VAL HIS LYS PHE PHE
SEQRES 22 A 513 LEU VAL PHE SER LYS TRP GLU TRP PRO ASN PRO VAL LEU
SEQRES 23 A 513 LEU LYS GLN PRO GLU GLU CYS ASN LEU ASN LEU PRO VAL
SEQRES 24 A 513 TRP ASP PRO ARG VAL ASN PRO SER ASP ARG TYR HIS LEU
SEQRES 25 A 513 MSE PRO ILE ILE THR PRO ALA TYR PRO GLN GLN ASN SER
SEQRES 26 A 513 THR TYR ASN VAL SER VAL SER THR ARG MSE VAL MSE VAL
SEQRES 27 A 513 GLU GLU PHE LYS GLN GLY LEU ALA ILE THR ASP GLU ILE
SEQRES 28 A 513 LEU LEU SER LYS ALA GLU TRP SER LYS LEU PHE GLU ALA
SEQRES 29 A 513 PRO ASN PHE PHE GLN LYS TYR LYS HIS TYR ILE VAL LEU
SEQRES 30 A 513 LEU ALA SER ALA PRO THR GLU LYS GLN ARG LEU GLU TRP
SEQRES 31 A 513 VAL GLY LEU VAL GLU SER LYS ILE ARG ILE LEU VAL GLY
SEQRES 32 A 513 SER LEU GLU LYS ASN GLU PHE ILE THR LEU ALA HIS VAL
SEQRES 33 A 513 ASN PRO GLN SER PHE PRO ALA PRO LYS GLU ASN PRO ASP
SEQRES 34 A 513 LYS GLU GLU PHE ARG THR MSE TRP VAL ILE GLY LEU VAL
SEQRES 35 A 513 PHE LYS LYS THR GLU ASN SER GLU ASN LEU SER VAL ASP
SEQRES 36 A 513 LEU THR TYR ASP ILE GLN SER PHE THR ASP THR VAL TYR
SEQRES 37 A 513 ARG GLN ALA ILE ASN SER LYS MSE PHE GLU VAL ASP MSE
SEQRES 38 A 513 LYS ILE ALA ALA MSE HIS VAL LYS ARG LYS GLN LEU HIS
SEQRES 39 A 513 GLN LEU LEU PRO SER HIS VAL LEU GLN LYS LYS LYS LYS
SEQRES 40 A 513 HIS SER THR GLU GLY VAL
MODRES 1F5A MSE A 251 MET SELENOMETHIONINE
MODRES 1F5A MSE A 313 MET SELENOMETHIONINE
MODRES 1F5A MSE A 335 MET SELENOMETHIONINE
MODRES 1F5A MSE A 337 MET SELENOMETHIONINE
MODRES 1F5A MSE A 436 MET SELENOMETHIONINE
MODRES 1F5A MSE A 476 MET SELENOMETHIONINE
MODRES 1F5A MSE A 481 MET SELENOMETHIONINE
MODRES 1F5A MSE A 486 MET SELENOMETHIONINE
HET MSE A 251 8
HET MSE A 313 8
HET MSE A 335 8
HET MSE A 337 8
HET MSE A 436 8
HET MSE A 476 5
HET MSE A 481 8
HET MSE A 486 5
HET MN A1001 1
HET MN A1002 1
HET MN A1003 1
HET 3AT A1000 30
HET 3PO A4000 13
HETNAM MSE SELENOMETHIONINE
HETNAM MN MANGANESE (II) ION
HETNAM 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE
HETNAM 3PO TRIPHOSPHATE
HETSYN 3AT CORDYCEPIN TRIPHOSPHATE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 MN 3(MN 2+)
FORMUL 5 3AT C10 H16 N5 O12 P3
FORMUL 6 3PO H5 O10 P3
FORMUL 7 HOH *170(H2 O)
HELIX 1 1 LYS A 32 LYS A 47 1 16
HELIX 2 2 PRO A 48 GLY A 50 5 3
HELIX 3 3 GLU A 54 LYS A 83 1 30
HELIX 4 4 PRO A 86 GLU A 91 1 6
HELIX 5 5 PHE A 100 GLY A 106 1 7
HELIX 6 6 ASP A 125 PHE A 130 1 6
HELIX 7 7 THR A 131 LEU A 139 1 9
HELIX 8 8 ASP A 186 LEU A 190 5 5
HELIX 9 9 ASP A 194 LEU A 213 1 20
HELIX 10 10 ASN A 216 HIS A 234 1 19
HELIX 11 11 GLY A 245 TYR A 260 1 16
HELIX 12 12 ILE A 264 LYS A 278 1 15
HELIX 13 13 ASN A 305 HIS A 311 5 7
HELIX 14 14 SER A 330 LEU A 353 1 24
HELIX 15 15 GLU A 357 LEU A 361 5 5
HELIX 16 16 ASN A 366 TYR A 371 1 6
HELIX 17 17 THR A 383 SER A 396 1 14
HELIX 18 18 LYS A 397 LYS A 407 1 11
HELIX 19 19 LEU A 456 SER A 474 1 19
HELIX 20 20 LYS A 491 LEU A 497 5 7
SHEET 1 A 5 LYS A 96 THR A 99 0
SHEET 2 A 5 ILE A 114 ALA A 120 -1 N LEU A 117 O PHE A 98
SHEET 3 A 5 ILE A 164 ARG A 172 1 O GLU A 165 N ILE A 114
SHEET 4 A 5 VAL A 156 PHE A 161 -1 O ILE A 157 N ILE A 168
SHEET 5 A 5 VAL A 143 VAL A 149 -1 O LYS A 144 N CYS A 160
SHEET 1 B 4 LYS A 482 LYS A 489 0
SHEET 2 B 4 HIS A 373 SER A 380 -1 O TYR A 374 N VAL A 488
SHEET 3 B 4 ARG A 434 PHE A 443 -1 N THR A 435 O ALA A 379
SHEET 4 B 4 ILE A 411 VAL A 416 -1 N THR A 412 O VAL A 442
SHEET 1 C 4 LYS A 482 LYS A 489 0
SHEET 2 C 4 HIS A 373 SER A 380 -1 O TYR A 374 N VAL A 488
SHEET 3 C 4 ARG A 434 PHE A 443 -1 N THR A 435 O ALA A 379
SHEET 4 C 4 PHE A 421 PRO A 422 -1 N PHE A 421 O MSE A 436
LINK C ALA A 250 N MSE A 251 1555 1555 1.33
LINK C MSE A 251 N LEU A 252 1555 1555 1.33
LINK C LEU A 312 N MSE A 313 1555 1555 1.32
LINK C MSE A 313 N PRO A 314 1555 1555 1.33
LINK C ARG A 334 N MSE A 335 1555 1555 1.33
LINK C MSE A 335 N VAL A 336 1555 1555 1.33
LINK C VAL A 336 N MSE A 337 1555 1555 1.33
LINK C MSE A 337 N VAL A 338 1555 1555 1.33
LINK C THR A 435 N MSE A 436 1555 1555 1.33
LINK C MSE A 436 N TRP A 437 1555 1555 1.33
LINK C LYS A 475 N MSE A 476 1555 1555 1.33
LINK C MSE A 476 N PHE A 477 1555 1555 1.33
LINK C ASP A 480 N MSE A 481 1555 1555 1.33
LINK C MSE A 481 N LYS A 482 1555 1555 1.32
LINK C ALA A 485 N MSE A 486 1555 1555 1.33
LINK C MSE A 486 N HIS A 487 1555 1555 1.33
LINK OD2 ASP A 113 MN MN A1001 1555 1555 2.66
LINK OD1 ASP A 113 MN MN A1002 1555 1555 2.19
LINK OD1 ASP A 115 MN MN A1001 1555 1555 2.27
LINK OD2 ASP A 115 MN MN A1002 1555 1555 2.48
LINK OD2 ASP A 167 MN MN A1001 1555 1555 2.42
LINK N7 3AT A1000 MN MN A1001 1555 1555 2.37
LINK O2A 3AT A1000 MN MN A1002 1555 1555 2.28
LINK O1G 3AT A1000 MN MN A1003 1555 1555 2.50
LINK O2A 3AT A1000 MN MN A1003 1555 1555 2.59
LINK O1B 3AT A1000 MN MN A1003 1555 1555 2.58
LINK MN MN A1001 O HOH A2155 1555 1555 2.70
LINK MN MN A1001 O5' 3PO A4000 1555 1555 2.07
LINK MN MN A1002 O HOH A2104 1555 1555 2.46
LINK MN MN A1003 O2A 3PO A4000 1555 1555 2.48
LINK MN MN A1003 O2B 3PO A4000 1555 1555 2.66
CISPEP 1 TRP A 281 PRO A 282 0 0.13
CISPEP 2 TYR A 320 PRO A 321 0 -0.02
SITE 1 AC1 7 ASP A 113 ASP A 115 ASP A 167 3AT A1000
SITE 2 AC1 7 MN A1002 HOH A2155 3PO A4000
SITE 1 AC2 7 ASP A 113 ASP A 115 3AT A1000 MN A1001
SITE 2 AC2 7 MN A1003 HOH A2104 3PO A4000
SITE 1 AC3 3 3AT A1000 MN A1002 3PO A4000
SITE 1 AC4 23 PHE A 100 GLY A 101 SER A 102 THR A 109
SITE 2 AC4 23 ASP A 115 VAL A 154 LYS A 158 ASP A 167
SITE 3 AC4 23 LYS A 228 TYR A 237 GLY A 246 VAL A 247
SITE 4 AC4 23 MN A1001 MN A1002 MN A1003 HOH A2010
SITE 5 AC4 23 HOH A2045 HOH A2104 HOH A2127 HOH A2129
SITE 6 AC4 23 HOH A2155 HOH A2167 3PO A4000
SITE 1 AC5 7 ALA A 112 ASP A 113 3AT A1000 MN A1001
SITE 2 AC5 7 MN A1002 MN A1003 HOH A2155
CRYST1 57.550 62.720 179.690 90.00 90.00 90.00 P 21 21 21 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 0.017376 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015944 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005565 0.00000
(ATOM LINES ARE NOT SHOWN.)
END