Header list of 1tlh.pdb file
Complete list - p 17 2 Bytes
HEADER TRANSCRIPTION 09-JUN-04 1TLH TITLE T4 ASIA BOUND TO SIGMA70 REGION 4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 10 KDA ANTI-SIGMA FACTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: AUDREY STEVENS' INHIBITOR, 10 KDA RNA POLYMERASE-ASSOCIATED COMPND 5 PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: RNA POLYMERASE SIGMA FACTOR RPOD; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: SIGMA-70; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_TAXID: 10665; SOURCE 4 GENE: ASIA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-SI; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28B; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 11 ORGANISM_TAXID: 562; SOURCE 12 GENE: RPOD, ALT, B3067; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET-28B KEYWDS ANTI-SIGMA, SIGMA70, RNA POLYMERASE, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.J.LAMBERT,Y.WEI,V.SCHIRF,B.DEMELER,M.H.WERNER REVDAT 3 17-SEP-14 1TLH 1 JRNL VERSN REVDAT 2 24-FEB-09 1TLH 1 VERSN REVDAT 1 23-NOV-04 1TLH 0 JRNL AUTH L.J.LAMBERT,Y.WEI,V.SCHIRF,B.DEMELER,M.H.WERNER JRNL TITL T4 ASIA BLOCKS DNA RECOGNITION BY REMODELING SIGMA(70) JRNL TITL 2 REGION 4 JRNL REF EMBO J. V. 23 2952 2004 JRNL REFN ISSN 0261-4189 JRNL PMID 15257291 JRNL DOI 10.1038/SJ.EMBOJ.7600312 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : CLORE AND SCHWEITERS REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TLH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-04. REMARK 100 THE RCSB ID CODE IS RCSB022747. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 312 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 150 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.7 MM PROTEIN, PHOSPHATE REMARK 210 BUFFERED SALINE, 50 MM SODIUM REMARK 210 AZIDE, 1 MM BENZAMIDINE REMARK 210 HYDROCHLORIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; RESIDUAL DIPOLAR REMARK 210 COUPLINGS IN PF1 PHAGE AT 9 MG/ML REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.2 REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING/ REMARK 210 RESTRAINED ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NULL 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: A, B 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASP B 533 REMARK 465 SER B 534 REMARK 465 ALA B 535 REMARK 465 THR B 536 REMARK 465 THR B 537 REMARK 465 GLU B 538 REMARK 465 SER B 539 REMARK 465 LEU B 540 REMARK 465 ARG B 541 REMARK 465 ALA B 542 REMARK 465 ALA B 543 REMARK 465 THR B 544 REMARK 465 HIS B 545 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-20 REMARK 470 RES CSSEQI ATOMS REMARK 470 LYS A 90 O REMARK 470 ASP B 613 O 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 ARG B 554 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG B 584 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 1 ARG B 596 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 ARG B 599 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 2 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 2 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 2 TYR A 81 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 2 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 2 ARG B 562 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 3 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 3 TYR A 83 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 3 TYR A 87 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 3 ARG B 554 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 3 ARG B 560 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 3 ARG B 562 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 3 ARG B 596 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 4 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 4 ARG B 562 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 4 ARG B 586 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 4 ARG B 588 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 4 ARG B 599 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 4 ARG B 603 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 5 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 5 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 5 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 5 ARG B 560 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 5 ARG B 584 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 5 ARG B 599 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 5 ARG B 599 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 6 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 6 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 6 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 6 ASP A 65 N - CA - CB ANGL. DEV. = -13.0 DEGREES REMARK 500 6 ARG B 603 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 6 ARG B 603 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 6 ARG B 608 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 7 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES REMARK 500 7 ARG A 47 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 7 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 7 ARG B 554 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 7 ARG B 554 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 7 ARG B 560 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 7 ARG B 584 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES REMARK 500 7 ARG B 584 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES REMARK 500 7 ARG B 588 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 7 ARG B 608 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 8 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 8 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 141 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 ARG A 23 -140.05 72.81 REMARK 500 1 GLU A 45 25.37 49.76 REMARK 500 1 MET B 561 -62.04 -94.12 REMARK 500 1 ASN B 568 -34.85 -174.89 REMARK 500 1 LEU B 573 -62.52 -1.71 REMARK 500 1 ASP B 581 -65.39 -24.73 REMARK 500 1 ARG B 608 -125.52 -78.75 REMARK 500 2 ARG A 23 -124.03 67.05 REMARK 500 2 ASP A 25 -75.57 -51.20 REMARK 500 2 PHE A 33 -70.18 -60.90 REMARK 500 2 ILE A 34 -61.84 -22.52 REMARK 500 2 GLU A 45 19.98 56.55 REMARK 500 2 PHE A 73 78.70 -104.70 REMARK 500 2 TYR A 81 -54.72 -28.48 REMARK 500 2 MET B 567 38.20 -153.61 REMARK 500 2 ASN B 568 73.78 -103.18 REMARK 500 2 THR B 569 -155.02 -140.19 REMARK 500 2 LEU B 573 -58.14 -27.40 REMARK 500 2 ARG B 599 -36.15 -131.28 REMARK 500 2 SER B 602 -72.10 -135.00 REMARK 500 2 LEU B 607 49.53 -93.20 REMARK 500 2 SER B 609 -64.30 -100.31 REMARK 500 2 PHE B 610 -72.28 -48.67 REMARK 500 2 LEU B 611 -37.41 -35.84 REMARK 500 3 ARG A 23 -116.89 61.18 REMARK 500 3 ILE A 34 -62.91 -22.61 REMARK 500 3 GLU A 45 17.82 57.77 REMARK 500 3 PHE A 73 68.87 -111.60 REMARK 500 3 MET B 567 53.26 -111.32 REMARK 500 3 ARG B 599 -39.63 -156.52 REMARK 500 3 SER B 609 -70.22 -49.16 REMARK 500 3 LEU B 611 67.21 -115.89 REMARK 500 4 ARG A 23 165.43 82.30 REMARK 500 4 GLU A 24 -23.13 -38.35 REMARK 500 4 GLU A 39 -52.18 -29.24 REMARK 500 4 THR B 569 -121.00 -94.30 REMARK 500 4 ARG B 608 -93.80 -82.17 REMARK 500 4 SER B 609 35.51 -77.44 REMARK 500 5 ILE A 17 -59.09 -28.95 REMARK 500 5 ARG A 23 -119.37 63.62 REMARK 500 5 GLU A 45 27.04 47.17 REMARK 500 5 LEU A 49 82.68 -65.35 REMARK 500 5 GLN A 51 -70.91 -58.56 REMARK 500 5 ASN B 568 46.48 -96.83 REMARK 500 5 SER B 602 -44.85 -160.39 REMARK 500 5 GLU B 605 87.26 -43.77 REMARK 500 5 ARG B 608 -69.60 -151.17 REMARK 500 5 PHE B 610 -83.83 -127.41 REMARK 500 5 LEU B 611 126.13 -12.04 REMARK 500 5 ASP B 612 -94.98 25.63 REMARK 500 REMARK 500 THIS ENTRY HAS 178 RAMACHANDRAN OUTLIERS. 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 PHE A 33 ILE A 34 2 149.12 REMARK 500 PHE A 33 ILE A 34 3 144.68 REMARK 500 PHE B 580 ASP B 581 3 149.97 REMARK 500 PHE B 580 ASP B 581 6 147.01 REMARK 500 PHE A 33 ILE A 34 8 144.72 REMARK 500 PHE B 580 ASP B 581 8 148.50 REMARK 500 LEU B 598 ARG B 599 9 -148.80 REMARK 500 PHE A 33 ILE A 34 10 148.57 REMARK 500 GLU A 28 ASN A 29 11 -145.32 REMARK 500 LEU A 49 ASN A 50 12 147.27 REMARK 500 VAL A 80 TYR A 81 12 148.76 REMARK 500 GLU A 64 ASP A 65 14 147.81 REMARK 500 ILE B 587 ARG B 588 15 147.21 REMARK 500 PHE A 33 ILE A 34 16 145.13 REMARK 500 PHE A 33 ILE A 34 17 149.51 REMARK 500 PHE B 580 ASP B 581 17 139.34 REMARK 500 LEU B 548 ALA B 549 18 149.61 REMARK 500 PHE A 33 ILE A 34 20 148.57 REMARK 500 LEU B 548 ALA B 549 20 144.45 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 ARG A 23 0.09 SIDE CHAIN REMARK 500 1 ARG A 55 0.09 SIDE CHAIN REMARK 500 2 ARG A 30 0.08 SIDE CHAIN REMARK 500 2 ARG B 560 0.07 SIDE CHAIN REMARK 500 2 ARG B 608 0.09 SIDE CHAIN REMARK 500 3 ARG A 23 0.11 SIDE CHAIN REMARK 500 3 ARG A 82 0.08 SIDE CHAIN REMARK 500 3 ARG B 554 0.09 SIDE CHAIN REMARK 500 3 ARG B 562 0.08 SIDE CHAIN REMARK 500 3 ARG B 603 0.09 SIDE CHAIN REMARK 500 4 ARG A 82 0.10 SIDE CHAIN REMARK 500 4 TYR B 571 0.13 SIDE CHAIN REMARK 500 4 ARG B 608 0.09 SIDE CHAIN REMARK 500 5 ARG A 23 0.08 SIDE CHAIN REMARK 500 5 ARG A 47 0.12 SIDE CHAIN REMARK 500 5 ARG B 554 0.08 SIDE CHAIN REMARK 500 5 ARG B 584 0.09 SIDE CHAIN REMARK 500 6 ARG A 47 0.10 SIDE CHAIN REMARK 500 6 TYR A 83 0.07 SIDE CHAIN REMARK 500 6 ARG B 596 0.08 SIDE CHAIN REMARK 500 6 ARG B 603 0.08 SIDE CHAIN REMARK 500 7 ARG A 30 0.11 SIDE CHAIN REMARK 500 7 ARG A 55 0.17 SIDE CHAIN REMARK 500 7 ARG B 562 0.09 SIDE CHAIN REMARK 500 7 ARG B 586 0.11 SIDE CHAIN REMARK 500 8 ARG A 30 0.08 SIDE CHAIN REMARK 500 8 ARG B 588 0.10 SIDE CHAIN REMARK 500 9 ARG A 30 0.10 SIDE CHAIN REMARK 500 9 ARG B 560 0.08 SIDE CHAIN REMARK 500 9 TYR B 571 0.07 SIDE CHAIN REMARK 500 9 ARG B 584 0.12 SIDE CHAIN REMARK 500 10 ARG A 23 0.11 SIDE CHAIN REMARK 500 10 TYR A 83 0.07 SIDE CHAIN REMARK 500 10 TYR A 87 0.08 SIDE CHAIN REMARK 500 10 ARG B 599 0.12 SIDE CHAIN REMARK 500 11 ARG A 82 0.09 SIDE CHAIN REMARK 500 11 ARG B 560 0.09 SIDE CHAIN REMARK 500 11 ARG B 562 0.08 SIDE CHAIN REMARK 500 11 TYR B 571 0.07 SIDE CHAIN REMARK 500 12 ARG A 82 0.12 SIDE CHAIN REMARK 500 12 ARG B 554 0.12 SIDE CHAIN REMARK 500 12 ARG B 562 0.09 SIDE CHAIN REMARK 500 12 TYR B 571 0.08 SIDE CHAIN REMARK 500 13 ARG A 23 0.10 SIDE CHAIN REMARK 500 13 ARG A 47 0.13 SIDE CHAIN REMARK 500 13 ARG A 55 0.15 SIDE CHAIN REMARK 500 13 ARG B 562 0.08 SIDE CHAIN REMARK 500 13 ARG B 588 0.09 SIDE CHAIN REMARK 500 13 ARG B 608 0.09 SIDE CHAIN REMARK 500 14 ARG A 47 0.11 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 83 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 1 ARG A 23 23.3 L L OUTSIDE RANGE REMARK 500 2 VAL A 8 23.4 L L OUTSIDE RANGE REMARK 500 2 ARG A 23 24.2 L L OUTSIDE RANGE REMARK 500 2 LEU A 49 23.5 L L OUTSIDE RANGE REMARK 500 2 LEU B 611 23.6 L L OUTSIDE RANGE REMARK 500 3 ARG A 23 24.5 L L OUTSIDE RANGE REMARK 500 3 TYR A 83 23.2 L L OUTSIDE RANGE REMARK 500 7 LEU A 49 21.0 L L OUTSIDE RANGE REMARK 500 7 LEU B 607 23.7 L L OUTSIDE RANGE REMARK 500 9 ARG A 23 24.8 L L OUTSIDE RANGE REMARK 500 9 GLU A 45 23.2 L L OUTSIDE RANGE REMARK 500 11 ARG A 23 25.0 L L OUTSIDE RANGE REMARK 500 13 ARG A 23 23.6 L L OUTSIDE RANGE REMARK 500 16 LEU A 49 23.9 L L OUTSIDE RANGE REMARK 500 18 GLU A 45 22.1 L L OUTSIDE RANGE REMARK 500 18 PHE A 73 24.5 L L OUTSIDE RANGE REMARK 500 18 GLU B 575 24.6 L L OUTSIDE RANGE REMARK 500 19 GLU A 45 23.5 L L OUTSIDE RANGE REMARK 500 20 ARG A 23 22.4 L L OUTSIDE RANGE REMARK 500 20 LEU A 49 24.6 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1TKV RELATED DB: PDB REMARK 900 T4 ASIA DIMER REMARK 900 RELATED ID: 1TL6 RELATED DB: PDB REMARK 900 T4 ASIA MONOMER DBREF 1TLH A 1 90 UNP P32267 ASIA_BPT4 1 90 DBREF 1TLH B 533 613 UNP P00579 RPOD_ECOLI 533 613 SEQRES 1 A 90 MET ASN LYS ASN ILE ASP THR VAL ARG GLU ILE ILE THR SEQRES 2 A 90 VAL ALA SER ILE LEU ILE LYS PHE SER ARG GLU ASP ILE SEQRES 3 A 90 VAL GLU ASN ARG ALA ASN PHE ILE ALA PHE LEU ASN GLU SEQRES 4 A 90 ILE GLY VAL THR HIS GLU GLY ARG LYS LEU ASN GLN ASN SEQRES 5 A 90 SER PHE ARG LYS ILE VAL SER GLU LEU THR GLN GLU ASP SEQRES 6 A 90 LYS LYS THR LEU ILE ASP GLU PHE ASN GLU GLY PHE GLU SEQRES 7 A 90 GLY VAL TYR ARG TYR LEU GLU MET TYR THR ASN LYS SEQRES 1 B 81 ASP SER ALA THR THR GLU SER LEU ARG ALA ALA THR HIS SEQRES 2 B 81 ASP VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS VAL SEQRES 3 B 81 LEU ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP TYR SEQRES 4 B 81 THR LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR ARG SEQRES 5 B 81 GLU ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG LYS SEQRES 6 B 81 LEU ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER PHE SEQRES 7 B 81 LEU ASP ASP HELIX 1 1 ASN A 4 LYS A 20 1 17 HELIX 2 2 GLU A 24 GLU A 28 1 5 HELIX 3 3 ARG A 30 GLU A 39 1 10 HELIX 4 4 GLN A 51 SER A 59 1 9 HELIX 5 5 GLN A 63 ASP A 71 1 9 HELIX 6 6 GLU A 75 TYR A 87 1 13 HELIX 7 7 ASP B 546 GLY B 550 1 5 HELIX 8 8 ALA B 553 MET B 561 1 9 HELIX 9 9 LEU B 573 ARG B 596 1 24 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 - p 17 2 Bytes