Header list of 1krw.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 10-JAN-02 1KRW TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF BERYLLOFLUORIDE-ACTIVATED TITLE 2 NTRC RECEIVER DOMAIN CAVEAT 1KRW CHIRALITY ERROR AT THE CA CENTER OF GLU A 124. COMPND MOL_ID: 1; COMPND 2 MOLECULE: NITROGEN REGULATION PROTEIN NR(I); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN: RECEIVER DOMAIN, RESIDUES 1-124; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM; SOURCE 3 ORGANISM_TAXID: 602; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS TWO COMPONENT SIGNAL TRANSDUCTION, RECEIVER DOMAIN, BEF3, KEYWDS 2 PHOSPHORYLATION, BACTERIAL NITROGEN REGULATORY PROTEIN, SIGNALING KEYWDS 3 PROTEIN EXPDTA SOLUTION NMR NUMMDL 26 AUTHOR C.A.HASTINGS,S.-Y.LEE,H.S.CHO,D.YAN,S.KUSTU,D.E.WEMMER REVDAT 3 23-FEB-22 1KRW 1 REMARK REVDAT 2 24-FEB-09 1KRW 1 VERSN REVDAT 1 19-AUG-03 1KRW 0 JRNL AUTH C.A.HASTINGS,S.-Y.LEE,H.S.CHO,D.YAN,S.KUSTU,D.E.WEMMER JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE JRNL TITL 2 BERYLLOFLUORIDE-ACTIVATED NTRC RECEIVER DOMAIN JRNL REF BIOCHEMISTRY V. 42 9081 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12885241 JRNL DOI 10.1021/BI0273866 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.S.CHO,S.-Y.LEE,D.YAN,X.PAN,J.S.PARKINSON,S.KUSTU, REMARK 1 AUTH 2 D.E.WEMMER,J.G.PELTON REMARK 1 TITL NMR STRUCTURE OF ACTIVATED CHEY REMARK 1 REF J.MOL.BIOL. V. 297 543 2000 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.2000.3595 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.-Y.LEE,H.S.CHO,J.G.PELTON,D.YAN,R.K.HENDERSON,D.S.KING, REMARK 1 AUTH 2 L.HUANG,S.KUSTU,E.A.BERRY,D.E.WEMMER REMARK 1 TITL CRYSTAL STRUCTURE OF AN ACTIVATED RESPONSE REGULATOR BOUND REMARK 1 TITL 2 TO ITS TARGET REMARK 1 REF NAT.STRUCT.BIOL. V. 8 52 2001 REMARK 1 REFN ISSN 1072-8368 REMARK 1 DOI 10.1038/NSB0901-789 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, X-PLOR CNS 1.0 REMARK 3 AUTHORS : GUNTERT (DYANA), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KRW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015276. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303 REMARK 210 PH : 6.75; 6.75; 6.75; 6.75 REMARK 210 IONIC STRENGTH : 50MM NACL, 4.4MM BECL2, 7.2MM REMARK 210 MGCL2, 29MM NAF; 50MM NACL, REMARK 210 4.4MM BECL2, 7.2MM MGCL2, 29MM REMARK 210 NAF; 50MM NACL, 4.4MM BECL2, REMARK 210 7.2MM MGCL2, 29MM NAF; 50MM NACL, REMARK 210 4.4MM BECL2, 7.2MM MGCL2, 29MM REMARK 210 NAF REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT REMARK 210 SAMPLE CONTENTS : U-15N, 1.1-1.5MM NTRC RECEIVER REMARK 210 DOMAIN(1-124), 50MM SODIUM REMARK 210 PHOSPHATE BUFFER(PH6.75), 50MM REMARK 210 NACL, 4.4MM BECL2, 7.2MM MGCL2, REMARK 210 29MM NAF, 95% H2O, 5% D2O; U-15N, REMARK 210 13C, 1.1-1.5MM NTRC RECEIVER REMARK 210 DOMAIN(1-124), 50MM SODIUM REMARK 210 PHOSPHATE BUFFER(PH6.75), 50MM REMARK 210 NACL, 4.4MM BECL2, 7.2MM MGCL2, REMARK 210 29MM NAF, 95% H2O, 5% D2O; 10% REMARK 210 13C, 1.1-1.5MM NTRC RECEIVER REMARK 210 DOMAIN(1-124), 50MM SODIUM REMARK 210 PHOSPHATE BUFFER(PH6.75), 50MM REMARK 210 NACL, 4.4MM BECL2, 7.2MM MGCL2, REMARK 210 29MM NAF, 95% H2O, 5% D2O; U-15N, REMARK 210 1.1-1.5MM NTRC RECEIVER REMARK 210 DOMAIN(1-124), 50MM SODIUM REMARK 210 PHOSPHATE BUFFER(PH6.75), 50MM REMARK 210 NACL, 4.4MM BECL2, 7.2MM MGCL2, REMARK 210 29MM NAF, 95% H2O, 5% D2O, 30MG/ REMARK 210 ML PHAGE PF1 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; REMARK 210 4D_13C/15N-SEPARATED_NOESY; 4D_ REMARK 210 13C-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNCA-J; CBCA(CO) REMARK 210 NH; 13C,1H-HSQC; IPAP-HSQC; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR CNS 1.0, FELIX, NMRVIEW REMARK 210 METHOD USED : DISTANCE GEOMETRY, TORSION ANGLE REMARK 210 DYNAMICS, SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 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: 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 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 O ASP A 54 N ILE A 55 0.42 REMARK 500 O ASP A 54 H ILE A 55 0.43 REMARK 500 C ASP A 54 H ILE A 55 0.43 REMARK 500 O SER A 85 H ASP A 86 0.54 REMARK 500 C MET A 1 H GLN A 2 0.57 REMARK 500 O MET A 1 N GLN A 2 0.62 REMARK 500 C SER A 85 H ASP A 86 0.65 REMARK 500 O SER A 85 N ASP A 86 0.67 REMARK 500 O MET A 1 H GLN A 2 0.78 REMARK 500 C HIS A 84 H SER A 85 1.04 REMARK 500 C GLN A 2 H ARG A 3 1.04 REMARK 500 O HIS A 84 N SER A 85 1.12 REMARK 500 O MET A 1 HA GLN A 2 1.15 REMARK 500 O GLN A 2 N ARG A 3 1.16 REMARK 500 HA MET A 1 H GLN A 2 1.23 REMARK 500 C PRO A 74 H MET A 75 1.23 REMARK 500 CA MET A 1 H GLN A 2 1.30 REMARK 500 O MET A 1 CA GLN A 2 1.31 REMARK 500 C GLY A 97 H ALA A 98 1.34 REMARK 500 O PRO A 74 N MET A 75 1.37 REMARK 500 C ASN A 35 H GLY A 36 1.37 REMARK 500 O HIS A 84 H SER A 85 1.38 REMARK 500 C ASP A 10 H ASP A 11 1.39 REMARK 500 HA MET A 1 N GLN A 2 1.43 REMARK 500 HG2 GLN A 123 N GLU A 124 1.44 REMARK 500 C MET A 1 HA GLN A 2 1.45 REMARK 500 C MET A 1 CA GLN A 2 1.46 REMARK 500 CA MET A 1 N GLN A 2 1.48 REMARK 500 O GLY A 97 N ALA A 98 1.50 REMARK 500 O ASN A 35 N GLY A 36 1.54 REMARK 500 O ASP A 10 N ASP A 11 1.56 REMARK 500 C ALA A 83 H HIS A 84 1.56 REMARK 500 O GLN A 2 H ARG A 3 1.58 REMARK 500 C ARG A 56 HB2 MET A 57 1.58 REMARK 500 C GLY A 59 H MET A 60 1.59 REMARK 500 CG GLN A 123 N GLU A 124 1.67 REMARK 500 O ALA A 83 N HIS A 84 1.74 REMARK 500 CB GLN A 123 N GLU A 124 1.76 REMARK 500 O HIS A 73 N PRO A 74 1.77 REMARK 500 O ASP A 54 CA ILE A 55 1.78 REMARK 500 O GLY A 59 N MET A 60 1.78 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 1 MET A 1 N MET A 1 CA -1.114 REMARK 500 1 MET A 1 CA MET A 1 CB -0.807 REMARK 500 1 MET A 1 CB MET A 1 CG -1.196 REMARK 500 1 MET A 1 CG MET A 1 SD -1.128 REMARK 500 1 MET A 1 SD MET A 1 CE -1.545 REMARK 500 1 MET A 1 CA MET A 1 C -0.579 REMARK 500 1 MET A 1 C MET A 1 O -0.850 REMARK 500 1 MET A 1 C GLN A 2 N -0.745 REMARK 500 1 GLN A 2 N GLN A 2 CA -0.541 REMARK 500 1 GLN A 2 CA GLN A 2 CB -0.585 REMARK 500 1 GLN A 2 CB GLN A 2 CG -0.581 REMARK 500 1 GLN A 2 CG GLN A 2 CD -0.673 REMARK 500 1 GLN A 2 CD GLN A 2 OE1 -0.876 REMARK 500 1 GLN A 2 CD GLN A 2 NE2 -0.737 REMARK 500 1 GLN A 2 CA GLN A 2 C -0.204 REMARK 500 1 GLN A 2 C GLN A 2 O -0.529 REMARK 500 1 GLN A 2 C ARG A 3 N -0.466 REMARK 500 1 ARG A 3 N ARG A 3 CA -0.185 REMARK 500 1 ARG A 3 CA ARG A 3 CB -0.207 REMARK 500 1 ARG A 3 CB ARG A 3 CG -0.314 REMARK 500 1 ARG A 3 CG ARG A 3 CD -0.208 REMARK 500 1 ARG A 3 CD ARG A 3 NE -0.638 REMARK 500 1 ARG A 3 NE ARG A 3 CZ -0.567 REMARK 500 1 ARG A 3 CZ ARG A 3 NH1 -0.891 REMARK 500 1 ARG A 3 CZ ARG A 3 NH2 -0.599 REMARK 500 1 ARG A 3 C ARG A 3 O -0.170 REMARK 500 1 ARG A 3 C GLY A 4 N -0.187 REMARK 500 1 ILE A 5 CG1 ILE A 5 CD1 -0.635 REMARK 500 1 VAL A 9 CB VAL A 9 CG1 -0.134 REMARK 500 1 VAL A 9 CB VAL A 9 CG2 -0.134 REMARK 500 1 ASP A 10 CB ASP A 10 CG -0.393 REMARK 500 1 ASP A 10 CG ASP A 10 OD1 -0.782 REMARK 500 1 ASP A 10 CG ASP A 10 OD2 -0.711 REMARK 500 1 ASP A 10 C ASP A 10 O -0.334 REMARK 500 1 ASP A 10 C ASP A 11 N -0.262 REMARK 500 1 ASP A 11 CB ASP A 11 CG -0.314 REMARK 500 1 ASP A 11 CG ASP A 11 OD1 -0.800 REMARK 500 1 ASP A 11 CG ASP A 11 OD2 -0.628 REMARK 500 1 ASP A 11 C ASP A 11 O -0.124 REMARK 500 1 ASP A 12 CB ASP A 12 CG -0.406 REMARK 500 1 ASP A 12 CG ASP A 12 OD1 -0.740 REMARK 500 1 ASP A 12 CG ASP A 12 OD2 -0.733 REMARK 500 1 SER A 13 CB SER A 13 OG -0.746 REMARK 500 1 SER A 14 CB SER A 14 OG -0.292 REMARK 500 1 ARG A 16 CD ARG A 16 NE -0.545 REMARK 500 1 ARG A 16 NE ARG A 16 CZ -0.273 REMARK 500 1 ARG A 16 CZ ARG A 16 NH1 -0.940 REMARK 500 1 ARG A 16 CZ ARG A 16 NH2 -0.546 REMARK 500 1 LEU A 19 CG LEU A 19 CD1 -0.876 REMARK 500 1 LEU A 19 CG LEU A 19 CD2 -0.681 REMARK 500 REMARK 500 THIS ENTRY HAS 257 BOND DEVIATIONS. 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 MET A 1 CB - CA - C ANGL. DEV. = 47.5 DEGREES REMARK 500 1 MET A 1 N - CA - CB ANGL. DEV. = -89.4 DEGREES REMARK 500 1 MET A 1 CA - CB - CG ANGL. DEV. = 19.9 DEGREES REMARK 500 1 MET A 1 CB - CG - SD ANGL. DEV. = 22.7 DEGREES REMARK 500 1 MET A 1 CG - SD - CE ANGL. DEV. = 20.4 DEGREES REMARK 500 1 MET A 1 N - CA - C ANGL. DEV. = 51.7 DEGREES REMARK 500 1 MET A 1 CA - C - O ANGL. DEV. = 14.6 DEGREES REMARK 500 1 MET A 1 CA - C - N ANGL. DEV. = 31.4 DEGREES REMARK 500 1 MET A 1 O - C - N ANGL. DEV. = -46.1 DEGREES REMARK 500 1 GLN A 2 C - N - CA ANGL. DEV. = 29.2 DEGREES REMARK 500 1 GLN A 2 CB - CG - CD ANGL. DEV. = 16.0 DEGREES REMARK 500 1 GLN A 2 OE1 - CD - NE2 ANGL. DEV. = -32.3 DEGREES REMARK 500 1 GLN A 2 CG - CD - NE2 ANGL. DEV. = 28.8 DEGREES REMARK 500 1 GLN A 2 CA - C - N ANGL. DEV. = 18.3 DEGREES REMARK 500 1 GLN A 2 O - C - N ANGL. DEV. = -27.8 DEGREES REMARK 500 1 ARG A 3 C - N - CA ANGL. DEV. = 16.9 DEGREES REMARK 500 1 ARG A 3 CA - CB - CG ANGL. DEV. = 33.3 DEGREES REMARK 500 1 ARG A 3 CG - CD - NE ANGL. DEV. = 19.0 DEGREES REMARK 500 1 ARG A 3 CD - NE - CZ ANGL. DEV. = 25.1 DEGREES REMARK 500 1 ARG A 3 NH1 - CZ - NH2 ANGL. DEV. = -16.7 DEGREES REMARK 500 1 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -8.8 DEGREES REMARK 500 1 ARG A 3 NE - CZ - NH2 ANGL. DEV. = 25.6 DEGREES REMARK 500 1 ILE A 5 CB - CG1 - CD1 ANGL. DEV. = 23.4 DEGREES REMARK 500 1 ASP A 10 OD1 - CG - OD2 ANGL. DEV. = -64.0 DEGREES REMARK 500 1 ASP A 10 CB - CG - OD1 ANGL. DEV. = 29.7 DEGREES REMARK 500 1 ASP A 10 CB - CG - OD2 ANGL. DEV. = 34.5 DEGREES REMARK 500 1 ASP A 10 O - C - N ANGL. DEV. = -18.6 DEGREES REMARK 500 1 ASP A 11 OD1 - CG - OD2 ANGL. DEV. = -65.5 DEGREES REMARK 500 1 ASP A 11 CB - CG - OD1 ANGL. DEV. = 27.8 DEGREES REMARK 500 1 ASP A 11 CB - CG - OD2 ANGL. DEV. = 37.9 DEGREES REMARK 500 1 ASP A 12 CA - CB - CG ANGL. DEV. = 14.9 DEGREES REMARK 500 1 ASP A 12 OD1 - CG - OD2 ANGL. DEV. = -58.2 DEGREES REMARK 500 1 ASP A 12 CB - CG - OD1 ANGL. DEV. = 28.9 DEGREES REMARK 500 1 ASP A 12 CB - CG - OD2 ANGL. DEV. = 29.4 DEGREES REMARK 500 1 SER A 13 CA - CB - OG ANGL. DEV. = 27.5 DEGREES REMARK 500 1 ARG A 16 CG - CD - NE ANGL. DEV. = 37.6 DEGREES REMARK 500 1 ARG A 16 CD - NE - CZ ANGL. DEV. = 41.1 DEGREES REMARK 500 1 ARG A 16 NH1 - CZ - NH2 ANGL. DEV. = -66.7 DEGREES REMARK 500 1 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 24.0 DEGREES REMARK 500 1 ARG A 16 NE - CZ - NH2 ANGL. DEV. = 42.8 DEGREES REMARK 500 1 LEU A 19 CD1 - CG - CD2 ANGL. DEV. = -50.7 DEGREES REMARK 500 1 LEU A 19 CB - CG - CD1 ANGL. DEV. = 30.8 DEGREES REMARK 500 1 LEU A 19 CB - CG - CD2 ANGL. DEV. = 39.0 DEGREES REMARK 500 1 GLU A 20 OE1 - CD - OE2 ANGL. DEV. = -24.4 DEGREES REMARK 500 1 GLU A 20 CG - CD - OE2 ANGL. DEV. = 15.4 DEGREES REMARK 500 1 ARG A 21 CG - CD - NE ANGL. DEV. = 16.5 DEGREES REMARK 500 1 ARG A 21 NH1 - CZ - NH2 ANGL. DEV. = -11.1 DEGREES REMARK 500 1 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES REMARK 500 1 ARG A 21 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 LEU A 23 CD1 - CG - CD2 ANGL. DEV. = -73.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 232 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 ASP A 11 -10.47 -44.89 REMARK 500 1 ASP A 12 -147.53 76.01 REMARK 500 1 SER A 13 -85.74 22.05 REMARK 500 1 ASN A 35 -61.73 -161.25 REMARK 500 1 ILE A 55 97.83 32.72 REMARK 500 1 ARG A 56 47.77 -158.85 REMARK 500 1 MET A 57 28.48 88.93 REMARK 500 1 PRO A 58 -101.48 -65.36 REMARK 500 1 MET A 60 63.28 -118.10 REMARK 500 1 ASP A 61 -42.67 62.99 REMARK 500 1 MET A 75 31.21 -159.83 REMARK 500 1 HIS A 84 -163.74 -25.71 REMARK 500 1 SER A 85 6.71 -32.87 REMARK 500 1 ASP A 86 44.23 -148.27 REMARK 500 1 ASP A 100 -167.30 173.07 REMARK 500 1 PRO A 103 -84.64 -68.19 REMARK 500 1 PHE A 106 -105.57 -166.73 REMARK 500 1 ASP A 107 -179.44 42.49 REMARK 500 1 GLN A 123 -178.20 -34.99 REMARK 500 2 ARG A 3 -20.05 76.19 REMARK 500 2 ASP A 10 -155.14 -161.33 REMARK 500 2 ASP A 11 12.15 -69.58 REMARK 500 2 ASP A 12 -152.40 46.94 REMARK 500 2 SER A 13 -91.51 38.02 REMARK 500 2 ASN A 35 -62.99 -166.07 REMARK 500 2 ILE A 55 65.27 -158.15 REMARK 500 2 ARG A 56 65.07 -177.18 REMARK 500 2 MET A 57 -64.44 -161.97 REMARK 500 2 PRO A 58 -173.15 -65.99 REMARK 500 2 ASP A 61 -77.80 42.41 REMARK 500 2 PRO A 74 -70.77 -56.76 REMARK 500 2 HIS A 84 -159.34 -66.87 REMARK 500 2 ASP A 86 26.60 175.74 REMARK 500 2 ALA A 98 152.70 -41.95 REMARK 500 2 ASP A 100 -176.19 170.79 REMARK 500 2 PRO A 103 -164.29 -66.51 REMARK 500 2 PHE A 106 -99.93 -162.16 REMARK 500 2 ASP A 107 -177.20 40.06 REMARK 500 2 GLN A 123 177.45 57.69 REMARK 500 3 ASP A 10 -158.21 -161.65 REMARK 500 3 ASP A 12 -156.20 46.25 REMARK 500 3 SER A 13 -95.09 35.83 REMARK 500 3 ILE A 55 93.57 33.51 REMARK 500 3 PRO A 58 -74.05 -61.26 REMARK 500 3 ASP A 61 -62.88 55.92 REMARK 500 3 HIS A 84 -158.87 46.77 REMARK 500 3 ASP A 100 -164.55 167.77 REMARK 500 3 PHE A 106 -102.05 -170.80 REMARK 500 3 ASP A 107 178.46 43.26 REMARK 500 3 GLN A 123 -169.14 42.44 REMARK 500 REMARK 500 THIS ENTRY HAS 432 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DC7 RELATED DB: PDB REMARK 900 INACTIVE CONFORMATION OF NTRC RECEIVER DOMAIN REMARK 900 RELATED ID: 1DC8 RELATED DB: PDB REMARK 900 TRANSIENTLY PHOSPHORYLATED FORM OF NTRC RECEIVER DOMAIN REMARK 900 RELATED ID: 1DJM RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF ACTIVE CHEY, THE HOMOLOG OF NTRC RECEIVER REMARK 900 DOMAIN REMARK 900 RELATED ID: 1F4V RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ACTIVE CHEY BOUND TO ITS DOWNSTREAM TARGET REMARK 900 DOMAIN REMARK 900 RELATED ID: 1KRX RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF BERYLLOFLUORIDE-ACTIVATED NTRC RECEIVER REMARK 900 DOMAIN: MODEL STRUCTURES INCORPORATING ACTIVE SITE CONTACTS DBREF 1KRW A 1 124 UNP P41789 NTRC_SALTY 1 124 SEQRES 1 A 124 MET GLN ARG GLY ILE VAL TRP VAL VAL ASP ASP ASP SER SEQRES 2 A 124 SER ILE ARG TRP VAL LEU GLU ARG ALA LEU ALA GLY ALA SEQRES 3 A 124 GLY LEU THR CYS THR THR PHE GLU ASN GLY ASN GLU VAL SEQRES 4 A 124 LEU ALA ALA LEU ALA SER LYS THR PRO ASP VAL LEU LEU SEQRES 5 A 124 SER ASP ILE ARG MET PRO GLY MET ASP GLY LEU ALA LEU SEQRES 6 A 124 LEU LYS GLN ILE LYS GLN ARG HIS PRO MET LEU PRO VAL SEQRES 7 A 124 ILE ILE MET THR ALA HIS SER ASP LEU ASP ALA ALA VAL SEQRES 8 A 124 SER ALA TYR GLN GLN GLY ALA PHE ASP TYR LEU PRO LYS SEQRES 9 A 124 PRO PHE ASP ILE ASP GLU ALA VAL ALA LEU VAL GLU ARG SEQRES 10 A 124 ALA ILE SER HIS TYR GLN GLU HELIX 1 1 ASP A 12 ALA A 26 1 15 HELIX 2 2 GLY A 36 ALA A 44 1 9 HELIX 3 3 GLY A 62 HIS A 73 1 12 HELIX 4 4 ASP A 86 GLY A 97 1 12 HELIX 5 5 PHE A 106 GLN A 123 1 18 SHEET 1 A 5 THR A 29 PHE A 33 0 SHEET 2 A 5 ILE A 5 VAL A 9 1 N VAL A 8 O THR A 31 SHEET 3 A 5 VAL A 50 SER A 53 1 O LEU A 52 N VAL A 9 SHEET 4 A 5 VAL A 78 ILE A 80 1 O ILE A 79 N SER A 53 SHEET 5 A 5 ALA A 98 TYR A 101 1 O PHE A 99 N VAL A 78 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