HEADER LIGASE/RNA 27-DEC-13 4O8J
TITLE CRYSTAL STRUCTURE OF RTCA, THE RNA 3'-TERMINAL PHOSPHATE CYCLASE FROM
TITLE 2 PYROCOCCUS HORIKOSHII, IN COMPLEX WITH RACAAA3'PHOSPHATE AND ADENINE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA 3'-TERMINAL PHOSPHATE CYCLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNA CYCLASE, RNA-3'-PHOSPHATE CYCLASE;
COMPND 5 EC: 6.5.1.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RNA;
COMPND 9 CHAIN: D, E;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
SOURCE 5 GENE: PH1529, PHCV028, RTCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: SYNTHETIC RNA
KEYWDS 3' RNA CYCLASE, RNA, LIGASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.K.DESAI,C.A.BINGMAN,G.N.PHILLIPS JR.,R.T.RAINES
REVDAT 5 20-SEP-23 4O8J 1 REMARK
REVDAT 4 23-SEP-20 4O8J 1 AUTHOR JRNL REMARK
REVDAT 3 29-NOV-17 4O8J 1 REMARK
REVDAT 2 01-OCT-14 4O8J 1 JRNL
REVDAT 1 10-SEP-14 4O8J 0
JRNL AUTH K.K.DESAI,C.A.BINGMAN,C.L.CHENG,G.N.PHILLIPS JR.,R.T.RAINES
JRNL TITL STRUCTURE OF RNA 3'-PHOSPHATE CYCLASE BOUND TO SUBSTRATE
JRNL TITL 2 RNA.
JRNL REF RNA V. 20 1560 2014
JRNL REFN ISSN 1355-8382
JRNL PMID 25161314
JRNL DOI 10.1261/RNA.045823.114
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 71772
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.740
REMARK 3 FREE R VALUE TEST SET COUNT : 1968
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 46.1514 - 4.9150 1.00 5558 157 0.1825 0.1902
REMARK 3 2 4.9150 - 3.9018 1.00 5394 152 0.1343 0.1653
REMARK 3 3 3.9018 - 3.4088 1.00 5307 149 0.1438 0.1781
REMARK 3 4 3.4088 - 3.0972 1.00 5303 150 0.1488 0.2182
REMARK 3 5 3.0972 - 2.8752 1.00 5275 149 0.1523 0.1767
REMARK 3 6 2.8752 - 2.7057 1.00 5245 148 0.1545 0.1811
REMARK 3 7 2.7057 - 2.5702 1.00 5259 148 0.1515 0.2088
REMARK 3 8 2.5702 - 2.4584 1.00 5233 147 0.1585 0.2206
REMARK 3 9 2.4584 - 2.3637 1.00 5243 149 0.1593 0.2296
REMARK 3 10 2.3637 - 2.2822 1.00 5232 147 0.1700 0.2378
REMARK 3 11 2.2822 - 2.2108 0.99 5168 145 0.1849 0.2530
REMARK 3 12 2.2108 - 2.1476 0.94 4961 141 0.1853 0.2060
REMARK 3 13 2.1476 - 2.0911 0.80 4145 116 0.2072 0.2597
REMARK 3 14 2.0911 - 2.0401 0.47 2481 70 0.2091 0.2846
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.950
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 5674
REMARK 3 ANGLE : 1.363 7735
REMARK 3 CHIRALITY : 0.082 892
REMARK 3 PLANARITY : 0.007 948
REMARK 3 DIHEDRAL : 14.933 2150
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 4O8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DUAL SILICON, K-B MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75619
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4O89
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M PROLINE, 0.1 M HEPES PH 7.5, 10%
REMARK 280 PEG 3350, CRYOPROTECTED BY SUPPLEMENTING WITH 30% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 41.96050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.82400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.13050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.82400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.96050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.13050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 A D 6 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A D 6 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A D 6 N1 C2 N3 C4
REMARK 470 A E 6 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A E 6 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A E 6 N1 C2 N3 C4
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 A 591 O HOH A 751 1.72
REMARK 500 OD1 ASP A 88 O HOH A 663 1.91
REMARK 500 O HOH B 680 O HOH B 749 2.18
REMARK 500 O HOH A 538 O HOH A 662 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 602 O HOH A 799 3655 2.11
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 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 204 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 204 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 CYS A 244 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 204 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 CYS B 244 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 339 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 339 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 A D 1 N1 - C6 - N6 ANGL. DEV. = 4.1 DEGREES
REMARK 500 A E 5 N1 - C6 - N6 ANGL. DEV. = 5.2 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 ASN A 38 40.73 -94.02
REMARK 500 LYS A 78 -134.11 -103.53
REMARK 500 ARG A 110 -27.59 83.80
REMARK 500 LYS A 180 -91.30 -102.65
REMARK 500 SER A 229 -149.71 -156.32
REMARK 500 CYS A 244 -95.37 -112.05
REMARK 500 CYS A 244 -94.76 -112.05
REMARK 500 ILE A 322 -43.33 -134.85
REMARK 500 ASN B 38 35.98 -97.13
REMARK 500 LYS B 78 -140.94 -108.34
REMARK 500 THR B 91 -161.24 -106.49
REMARK 500 ARG B 110 -16.00 85.36
REMARK 500 LYS B 180 -90.36 -97.07
REMARK 500 SER B 229 -154.28 -157.79
REMARK 500 CYS B 244 -87.72 -121.86
REMARK 500 CYS B 244 -87.32 -121.72
REMARK 500 ILE B 322 -36.21 -131.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O89 RELATED DB: PDB
DBREF 4O8J A 1 341 UNP O59198 RTCA_PYRHO 1 341
DBREF 4O8J B 1 341 UNP O59198 RTCA_PYRHO 1 341
DBREF 4O8J D 1 6 PDB 4O8J 4O8J 1 6
DBREF 4O8J E 1 6 PDB 4O8J 4O8J 1 6
SEQRES 1 A 341 MET ILE THR ILE ASP GLY SER TYR GLY GLU GLY GLY GLY
SEQRES 2 A 341 GLN ILE LEU ARG THR SER VAL ALA LEU SER THR ILE THR
SEQRES 3 A 341 GLY GLU PRO VAL ARG ILE VAL ASN ILE ARG ALA ASN ARG
SEQRES 4 A 341 PRO ASN PRO GLY LEU ARG PRO GLN HIS LEU HIS ALA ILE
SEQRES 5 A 341 LEU ALA LEU LYS HIS LEU ALA ASN ALA GLU VAL LYS GLY
SEQRES 6 A 341 ALA HIS VAL GLY SER ARG GLU LEU VAL PHE ILE PRO LYS
SEQRES 7 A 341 LYS LEU GLU ALA LYS GLU ILE SER ILE ASP ILE GLY THR
SEQRES 8 A 341 ALA GLY SER ILE THR LEU VAL LEU GLN ALA LEU LEU PRO
SEQRES 9 A 341 ALA MET VAL PHE ALA ARG GLU LYS VAL LYS PHE ARG ILE
SEQRES 10 A 341 THR GLY GLY THR ASP VAL SER TRP SER PRO PRO VAL ASP
SEQRES 11 A 341 TYR LEU SER ASN VAL THR LEU PHE ALA LEU GLU LYS ILE
SEQRES 12 A 341 GLY ILE HIS GLY GLU ILE ARG VAL ILE ARG ARG GLY HIS
SEQRES 13 A 341 TYR PRO LYS GLY GLY GLY ILE VAL GLU GLY TYR VAL GLU
SEQRES 14 A 341 PRO TRP ASN GLU LYS ARG GLU LEU VAL ALA LYS GLU TYR
SEQRES 15 A 341 SER ARG ILE ILE LYS ILE GLU GLY ILE SER HIS ALA THR
SEQRES 16 A 341 ASN LEU PRO SER HIS VAL ALA GLU ARG GLN ALA ARG ALA
SEQRES 17 A 341 ALA LYS ASP GLU LEU LEU GLN LEU LYS VAL PRO ILE GLU
SEQRES 18 A 341 ILE ARG THR GLU ILE SER ARG SER ILE GLY PRO GLY SER
SEQRES 19 A 341 GLY ILE VAL VAL TRP ALA GLU THR ASP CYS LEU ARG LEU
SEQRES 20 A 341 GLY GLY ASP ALA LEU GLY LYS LYS GLY LYS PRO ALA GLU
SEQRES 21 A 341 ILE VAL GLY LYS GLU ALA ALA GLN GLU LEU LEU ASP GLN
SEQRES 22 A 341 LEU LYS PRO GLY HIS CYS VAL ASP LYS PHE LEU GLY ASP
SEQRES 23 A 341 GLN LEU ILE PRO PHE LEU ALA PHE SER GLY GLY VAL ILE
SEQRES 24 A 341 TRP VAL SER GLU ILE THR ASN HIS LEU LYS THR ASN ILE
SEQRES 25 A 341 TRP VAL VAL GLU SER PHE LEU GLY ARG ILE PHE ASP VAL
SEQRES 26 A 341 ASP GLY ASN VAL GLY GLU PRO GLY LYS ILE ARG VAL ILE
SEQRES 27 A 341 ARG ARG VAL
SEQRES 1 B 341 MET ILE THR ILE ASP GLY SER TYR GLY GLU GLY GLY GLY
SEQRES 2 B 341 GLN ILE LEU ARG THR SER VAL ALA LEU SER THR ILE THR
SEQRES 3 B 341 GLY GLU PRO VAL ARG ILE VAL ASN ILE ARG ALA ASN ARG
SEQRES 4 B 341 PRO ASN PRO GLY LEU ARG PRO GLN HIS LEU HIS ALA ILE
SEQRES 5 B 341 LEU ALA LEU LYS HIS LEU ALA ASN ALA GLU VAL LYS GLY
SEQRES 6 B 341 ALA HIS VAL GLY SER ARG GLU LEU VAL PHE ILE PRO LYS
SEQRES 7 B 341 LYS LEU GLU ALA LYS GLU ILE SER ILE ASP ILE GLY THR
SEQRES 8 B 341 ALA GLY SER ILE THR LEU VAL LEU GLN ALA LEU LEU PRO
SEQRES 9 B 341 ALA MET VAL PHE ALA ARG GLU LYS VAL LYS PHE ARG ILE
SEQRES 10 B 341 THR GLY GLY THR ASP VAL SER TRP SER PRO PRO VAL ASP
SEQRES 11 B 341 TYR LEU SER ASN VAL THR LEU PHE ALA LEU GLU LYS ILE
SEQRES 12 B 341 GLY ILE HIS GLY GLU ILE ARG VAL ILE ARG ARG GLY HIS
SEQRES 13 B 341 TYR PRO LYS GLY GLY GLY ILE VAL GLU GLY TYR VAL GLU
SEQRES 14 B 341 PRO TRP ASN GLU LYS ARG GLU LEU VAL ALA LYS GLU TYR
SEQRES 15 B 341 SER ARG ILE ILE LYS ILE GLU GLY ILE SER HIS ALA THR
SEQRES 16 B 341 ASN LEU PRO SER HIS VAL ALA GLU ARG GLN ALA ARG ALA
SEQRES 17 B 341 ALA LYS ASP GLU LEU LEU GLN LEU LYS VAL PRO ILE GLU
SEQRES 18 B 341 ILE ARG THR GLU ILE SER ARG SER ILE GLY PRO GLY SER
SEQRES 19 B 341 GLY ILE VAL VAL TRP ALA GLU THR ASP CYS LEU ARG LEU
SEQRES 20 B 341 GLY GLY ASP ALA LEU GLY LYS LYS GLY LYS PRO ALA GLU
SEQRES 21 B 341 ILE VAL GLY LYS GLU ALA ALA GLN GLU LEU LEU ASP GLN
SEQRES 22 B 341 LEU LYS PRO GLY HIS CYS VAL ASP LYS PHE LEU GLY ASP
SEQRES 23 B 341 GLN LEU ILE PRO PHE LEU ALA PHE SER GLY GLY VAL ILE
SEQRES 24 B 341 TRP VAL SER GLU ILE THR ASN HIS LEU LYS THR ASN ILE
SEQRES 25 B 341 TRP VAL VAL GLU SER PHE LEU GLY ARG ILE PHE ASP VAL
SEQRES 26 B 341 ASP GLY ASN VAL GLY GLU PRO GLY LYS ILE ARG VAL ILE
SEQRES 27 B 341 ARG ARG VAL
SEQRES 1 D 6 A C A A A A
SEQRES 1 E 6 A C A A A A
HET ADN A 401 32
HET ADN B 401 31
HET EPE B 402 32
HETNAM ADN ADENOSINE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 5 ADN 2(C10 H13 N5 O4)
FORMUL 7 EPE C8 H18 N2 O4 S
FORMUL 8 HOH *610(H2 O)
HELIX 1 1 GLY A 12 GLY A 27 1 16
HELIX 2 2 ARG A 45 ASN A 60 1 16
HELIX 3 3 SER A 94 VAL A 107 1 14
HELIX 4 4 PRO A 128 VAL A 135 1 8
HELIX 5 5 VAL A 135 ILE A 143 1 9
HELIX 6 6 PRO A 198 LEU A 214 1 17
HELIX 7 7 GLN A 215 LYS A 217 5 3
HELIX 8 8 PRO A 258 LYS A 275 1 18
HELIX 9 9 ASP A 281 GLY A 296 1 16
HELIX 10 10 THR A 305 GLY A 320 1 16
HELIX 11 11 GLY B 12 GLY B 27 1 16
HELIX 12 12 ARG B 45 ASN B 60 1 16
HELIX 13 13 SER B 94 VAL B 107 1 14
HELIX 14 14 PRO B 128 VAL B 135 1 8
HELIX 15 15 VAL B 135 ILE B 143 1 9
HELIX 16 16 PRO B 198 LEU B 214 1 17
HELIX 17 17 GLN B 215 LYS B 217 5 3
HELIX 18 18 PRO B 258 LYS B 275 1 18
HELIX 19 19 ASP B 281 GLY B 296 1 16
HELIX 20 20 THR B 305 GLY B 320 1 16
SHEET 1 A 4 ILE A 2 ASP A 5 0
SHEET 2 A 4 VAL A 30 VAL A 33 1 O ARG A 31 N ILE A 4
SHEET 3 A 4 LEU A 73 ILE A 76 -1 O PHE A 75 N VAL A 30
SHEET 4 A 4 GLU A 62 LYS A 64 -1 N LYS A 64 O VAL A 74
SHEET 1 B 4 ILE A 85 ASP A 88 0
SHEET 2 B 4 VAL A 113 GLY A 119 1 O LYS A 114 N ILE A 85
SHEET 3 B 4 GLY A 162 VAL A 168 -1 O VAL A 164 N ILE A 117
SHEET 4 B 4 GLY A 147 ARG A 153 -1 N ARG A 150 O GLU A 165
SHEET 1 C 4 LEU A 177 ALA A 179 0
SHEET 2 C 4 GLY A 297 VAL A 301 1 O VAL A 298 N ALA A 179
SHEET 3 C 4 GLY A 333 VAL A 337 -1 O ILE A 335 N ILE A 299
SHEET 4 C 4 PHE A 323 ASP A 326 -1 N ASP A 326 O LYS A 334
SHEET 1 D 4 ILE A 220 SER A 227 0
SHEET 2 D 4 ILE A 185 THR A 195 1 N SER A 192 O ARG A 223
SHEET 3 D 4 GLY A 233 THR A 242 -1 O GLY A 233 N THR A 195
SHEET 4 D 4 ARG A 246 LEU A 252 -1 O GLY A 249 N VAL A 238
SHEET 1 E 4 ILE B 2 ASP B 5 0
SHEET 2 E 4 VAL B 30 VAL B 33 1 O ARG B 31 N ILE B 4
SHEET 3 E 4 LEU B 73 ILE B 76 -1 O PHE B 75 N VAL B 30
SHEET 4 E 4 GLU B 62 LYS B 64 -1 N GLU B 62 O ILE B 76
SHEET 1 F 4 ILE B 85 ASP B 88 0
SHEET 2 F 4 VAL B 113 GLY B 119 1 O LYS B 114 N ILE B 85
SHEET 3 F 4 GLY B 162 VAL B 168 -1 O VAL B 164 N ILE B 117
SHEET 4 F 4 GLY B 147 ARG B 153 -1 N ARG B 150 O GLU B 165
SHEET 1 G 4 LEU B 177 ALA B 179 0
SHEET 2 G 4 GLY B 297 VAL B 301 1 O VAL B 298 N ALA B 179
SHEET 3 G 4 GLY B 333 VAL B 337 -1 O ILE B 335 N ILE B 299
SHEET 4 G 4 PHE B 323 ASP B 326 -1 N ASP B 326 O LYS B 334
SHEET 1 H 4 ILE B 220 SER B 227 0
SHEET 2 H 4 ILE B 185 THR B 195 1 N SER B 192 O ARG B 223
SHEET 3 H 4 GLY B 233 THR B 242 -1 O GLY B 233 N THR B 195
SHEET 4 H 4 ARG B 246 LEU B 252 -1 O GLY B 249 N VAL B 238
SSBOND 1 CYS A 244 CYS A 279 1555 1555 2.06
SSBOND 2 CYS B 244 CYS B 279 1555 1555 2.06
CISPEP 1 TYR A 157 PRO A 158 0 7.56
CISPEP 2 TYR B 157 PRO B 158 0 7.70
SITE 1 AC1 11 GLN A 14 ARG A 17 LEU A 97 GLN A 100
SITE 2 AC1 11 PRO A 127 ASP A 250 PHE A 283 ASP A 286
SITE 3 AC1 11 GLN A 287 HIS A 307 A E 6
SITE 1 AC2 11 GLN B 14 LEU B 97 GLN B 100 SER B 126
SITE 2 AC2 11 PRO B 127 ASP B 250 PHE B 283 ASP B 286
SITE 3 AC2 11 GLN B 287 HIS B 307 HOH B 740
SITE 1 AC3 9 VAL B 63 LYS B 64 GLY B 65 ALA B 66
SITE 2 AC3 9 LYS B 180 GLU B 181 TRP B 300 HOH B 707
SITE 3 AC3 9 HOH B 711
CRYST1 83.921 110.261 127.648 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 0.011916 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009069 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007834 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
