Header list of 1nyb.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION/RNA 12-FEB-03 1NYB
TITLE SOLUTION STRUCTURE OF THE BACTERIOPHAGE PHI21 N PEPTIDE-BOXB RNA
TITLE 2 COMPLEX
CAVEAT 1NYB CHIRALITY ERROR AT THE CB CENTER OF SER A 9. THERE ARE
CAVEAT 2 1NYB SEVERAL CHIRALITY ERRORS IN CHAIN B.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOXB RNA;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PROBABLE REGULATORY PROTEIN N;
COMPND 7 CHAIN: A;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIS OF THE RNA FRAGMENT FROM THE BACTERIOPHAGE
SOURCE 4 PHI21 BOXB;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE PHI21;
SOURCE 7 ORGANISM_TAXID: 10737;
SOURCE 8 GENE: N;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PEPTIDE-RNA COMPLEX, TRANSCRIPTION ANTITERMINATION, TRANSCRIPTION-RNA
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
MDLTYP MINIMIZED AVERAGE
AUTHOR C.D.CILLEY,J.R.WILLIAMSON
REVDAT 4 23-FEB-22 1NYB 1 REMARK ATOM
REVDAT 3 11-AUG-09 1NYB 1 CAVEAT
REVDAT 2 24-FEB-09 1NYB 1 VERSN
REVDAT 1 24-JUN-03 1NYB 0
JRNL AUTH C.D.CILLEY,J.R.WILLIAMSON
JRNL TITL STRUCTURAL MIMICRY IN THE PHAGE PHI21 N PEPTIDE-BOXB RNA
JRNL TITL 2 COMPLEX
JRNL REF RNA V. 9 663 2003
JRNL REFN ISSN 1355-8382
JRNL PMID 12756325
JRNL DOI 10.1261/RNA.2189203
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, CNS 1.0
REMARK 3 AUTHORS : F. DELAGLIO, S. GRZESIEK, G. VUISTER, G. ZHU, J.
REMARK 3 PFEIFER, AND A. BAX (NMRPIPE), A.T. BRUNGER, P.D.
REMARK 3 ADAMS, G.M. CLORE, W.L. DELANO, P. GROS, R.W.
REMARK 3 GROSSE-KUNSTLEVE, J.S. JIANG, J. KUSZEWSKI, M.
REMARK 3 NILGES, N.S. PANNU, R.J. READ, L.M. RICE, T.
REMARK 3 SIMONSON, G.L. WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THERE WERE A TOTAL OF 1016 DISTANCE RESTRAINTS (INCLUDING 48
REMARK 3 HYDROGEN BOND DISTANCE RESTRAINTS) AND 167 TORSION RESTRAINTS USED
REMARK 3 TO DETERMINE THIS STRUCTURE. THE MOLECULAR MODELING OF THE PHI21
REMARK 3 N PEPTIDE-BOXB RNA COMPLEX WAS DONE IN THREE STEPS. FIRST, A
REMARK 3 COMPLETE INTRAMOLECULAR RESTRAINT SET WAS GENERATED FOR EACH
REMARK 3 MOLECULE, AND THEN PEPTIDE AND RNA STRUCTURES WERE GENERATED
REMARK 3 SEPARATELY USING AB INITIO SIMULATED ANNEALING (SA) STARTING FROM
REMARK 3 A RANDOM EXTENDED STRUCTURE IN CNSSOLVE. FOR BOTH THE PEPTIDE AND
REMARK 3 THE RNA, CONSTRAINED (TORSION) DYNAMICS WAS USED AT 50000K. A
REMARK 3 TOTAL OF 100 STRUCTURES EACH OF THE PEPTIDE AND RNA WERE GENERATED.
REMARK 3 IN THE SECOND STEP, EACH OF THE 20 LOWEST ENERGY PEPTIDE AND
REMARK 3 20 LOWEST ENERGY RNA STRUCTURES WERE COMBINED IN SINGLE PDB FILES,
REMARK 3 IN ALL 400 POSSIBLE COMBINATIONS. THE RNA WAS HELD AT THE ORIGIN
REMARK 3 AND THE PEPTIDE WAS RANDOMLY ROTATED AND MOVED 100 ANGSTROMS AWAY
REMARK 3 IN A RANDOM DIRECTION FROM THE ORIGIN. THESE 400 POSSIBLE "
REMARK 3 COMPLEXES" WERE DOCKED USING CNSSOLVE. THE OBJECTIVE OF THE
REMARK 3 DOCKING WAS TO BRING THE PEPTIDE AND RNA TOGETHER WITHOUT
REMARK 3 DRAMATICALLY PERTURBING THEIR FOLDED STRUCTURES FROM THE FIRST
REMARK 3 ROUND OF SA, SO THE TEMPERATURES FOR THE DOCKING WERE SET MUCH
REMARK 3 LOWER THAN IN THE INITIAL CALCULATIONS (1000 VS. 50000K).
REMARK 3 FINALLY, THE 100 LOWEST ENERGY DOCKED STRUCTURES WERE
REMARK 3 MINIMIZED BY TWO ROUNDS OF LOW TEMPERATURE ANNEALING USING SANDER,
REMARK 3 A MODULE OF AMBER. AS WITH THE DOCKING, THE TEMPERATURE WAS KEPT
REMARK 3 LOW (1000K). THE 14 LOWEST ENERGY STRUCTURES WERE USED FOR
REMARK 3 GENERATING AN AVERAGE STRUCTURE, WHICH WAS ENERGY MINIMIZED USING
REMARK 3 A CONJUGATE GRADIENT.
REMARK 4
REMARK 4 1NYB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018346.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 2MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM N PEPTIDE-BOXB RNA COMPLEX;
REMARK 210 25MM D6(98%)-SUCCINATE, 2MM NACL,
REMARK 210 0.2MM EDTA, 0.05MM NA-AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.1.3, AMBER 6
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR AND 3D
REMARK 210 HETERONUCLEAR NMR SPECTROSCOPY. THE TWO MOST IMPORTANT SAMPLES
REMARK 210 WERE UNIFORMLY LABELED 15N,13C PEPTIDE OR RNA IN COMPLEX WITH ITS
REMARK 210 UNLABELED COUNTERPART.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 APPLY THE FOLLOWING TO CHAINS: B, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 U B 3 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 C B 5 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 A B 6 C4 - C5 - C6 ANGL. DEV. = -3.2 DEGREES
REMARK 500 1 A B 6 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 A B 6 N1 - C6 - N6 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 C B 7 N3 - C2 - O2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 C B 8 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 C B 10 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 A B 12 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 A B 12 C5 - C6 - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 A B 12 N1 - C6 - N6 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 A B 13 C4 - C5 - C6 ANGL. DEV. = -3.0 DEGREES
REMARK 500 1 A B 13 C5 - C6 - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 A B 13 N1 - C6 - N6 ANGL. DEV. = -5.1 DEGREES
REMARK 500 1 C B 14 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 U B 19 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 A B 21 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 A B 21 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 A B 21 N1 - C6 - N6 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 C B 23 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 C B 24 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 C B 5 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 A B 6 C4 - C5 - C6 ANGL. DEV. = -3.4 DEGREES
REMARK 500 2 A B 6 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 A B 6 N1 - C6 - N6 ANGL. DEV. = -5.1 DEGREES
REMARK 500 2 C B 7 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 2 C B 8 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 2 C B 10 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 A B 12 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 A B 12 C5 - C6 - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A B 12 N1 - C6 - N6 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 A B 13 C4 - C5 - C6 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 A B 13 C5 - C6 - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 A B 13 N1 - C6 - N6 ANGL. DEV. = -5.2 DEGREES
REMARK 500 2 C B 14 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 C B 15 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 A B 21 C4 - C5 - C6 ANGL. DEV. = -3.0 DEGREES
REMARK 500 2 A B 21 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 A B 21 N1 - C6 - N6 ANGL. DEV. = -4.4 DEGREES
REMARK 500 2 C B 23 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 C B 24 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 C B 5 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 3 A B 6 C4 - C5 - C6 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 A B 6 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 A B 6 N1 - C6 - N6 ANGL. DEV. = -4.8 DEGREES
REMARK 500 3 C B 7 N1 - C2 - O2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 C B 7 N3 - C2 - O2 ANGL. DEV. = -5.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 321 ANGLE DEVIATIONS.
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 1 SER A 9 15.30 -68.58
REMARK 500 1 ARG A 28 -83.49 -32.94
REMARK 500 2 LYS A 10 27.09 -67.42
REMARK 500 3 SER A 9 46.28 -79.46
REMARK 500 4 LYS A 10 -77.87 -92.40
REMARK 500 6 ARG A 28 15.56 59.99
REMARK 500 7 ARG A 28 52.42 37.63
REMARK 500 13 SER A 9 -51.42 65.00
REMARK 500 13 ARG A 28 19.06 54.25
REMARK 500 15 SER A 9 -8.72 64.62
REMARK 500 15 LYS A 10 -107.28 43.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 8 SER A 9 1 -136.83
REMARK 500 ARG A 28 ARG A 29 1 146.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 U B 4 0.08 SIDE CHAIN
REMARK 500 1 A B 6 0.07 SIDE CHAIN
REMARK 500 1 C B 8 0.09 SIDE CHAIN
REMARK 500 1 C B 10 0.06 SIDE CHAIN
REMARK 500 1 U B 11 0.07 SIDE CHAIN
REMARK 500 1 A B 12 0.05 SIDE CHAIN
REMARK 500 1 G B 22 0.09 SIDE CHAIN
REMARK 500 1 C B 23 0.06 SIDE CHAIN
REMARK 500 1 ARG A 28 0.08 SIDE CHAIN
REMARK 500 2 G B 1 0.08 SIDE CHAIN
REMARK 500 2 C B 8 0.10 SIDE CHAIN
REMARK 500 2 U B 9 0.08 SIDE CHAIN
REMARK 500 2 C B 10 0.06 SIDE CHAIN
REMARK 500 2 G B 22 0.07 SIDE CHAIN
REMARK 500 3 C B 8 0.07 SIDE CHAIN
REMARK 500 3 U B 11 0.09 SIDE CHAIN
REMARK 500 4 G B 2 0.11 SIDE CHAIN
REMARK 500 4 U B 3 0.08 SIDE CHAIN
REMARK 500 4 C B 8 0.10 SIDE CHAIN
REMARK 500 4 U B 11 0.12 SIDE CHAIN
REMARK 500 4 G B 18 0.05 SIDE CHAIN
REMARK 500 5 C B 5 0.06 SIDE CHAIN
REMARK 500 5 U B 11 0.08 SIDE CHAIN
REMARK 500 5 A B 12 0.06 SIDE CHAIN
REMARK 500 5 G B 18 0.06 SIDE CHAIN
REMARK 500 5 U B 19 0.07 SIDE CHAIN
REMARK 500 5 G B 20 0.07 SIDE CHAIN
REMARK 500 5 G B 22 0.07 SIDE CHAIN
REMARK 500 6 G B 1 0.11 SIDE CHAIN
REMARK 500 6 G B 2 0.07 SIDE CHAIN
REMARK 500 6 C B 8 0.12 SIDE CHAIN
REMARK 500 6 C B 10 0.09 SIDE CHAIN
REMARK 500 6 U B 11 0.09 SIDE CHAIN
REMARK 500 6 G B 17 0.07 SIDE CHAIN
REMARK 500 6 TYR A 17 0.07 SIDE CHAIN
REMARK 500 7 C B 8 0.13 SIDE CHAIN
REMARK 500 7 C B 10 0.07 SIDE CHAIN
REMARK 500 7 U B 11 0.12 SIDE CHAIN
REMARK 500 7 A B 21 0.07 SIDE CHAIN
REMARK 500 8 C B 5 0.07 SIDE CHAIN
REMARK 500 8 U B 19 0.12 SIDE CHAIN
REMARK 500 8 G B 20 0.09 SIDE CHAIN
REMARK 500 8 G B 22 0.06 SIDE CHAIN
REMARK 500 9 G B 1 0.07 SIDE CHAIN
REMARK 500 9 G B 2 0.05 SIDE CHAIN
REMARK 500 9 C B 8 0.08 SIDE CHAIN
REMARK 500 9 U B 11 0.09 SIDE CHAIN
REMARK 500 9 C B 15 0.09 SIDE CHAIN
REMARK 500 9 U B 19 0.09 SIDE CHAIN
REMARK 500 9 G B 22 0.07 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A4T RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR,
REMARK 900 20 STRUCTURES
DBREF 1NYB A 8 29 UNP P07243 REGN_BPPH3 8 29
DBREF 1NYB B 1 24 PDB 1NYB 1NYB 1 24
SEQRES 1 B 24 G G U U C A C C U C U A A
SEQRES 2 B 24 C C G G G U G A G C C
SEQRES 1 A 22 GLU SER LYS GLY THR ALA LYS SER ARG TYR LYS ALA ARG
SEQRES 2 A 22 ARG ALA GLU LEU ILE ALA GLU ARG ARG
HELIX 1 1 THR A 12 ALA A 26 1 15
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes