Header list of 1x32.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 28-APR-05 1X32 TITLE THREE DIMENSIONAL SOLUTION STRUCTURE OF THE CHROMO1 DOMAIN OF CPSRP43 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHLOROPLAST SIGNAL RECOGNITION PARTICLE COMPONENT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CHROMO DOMAIN 1; COMPND 5 SYNONYM: CPSRP43, CAO; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SIGNAL RECOGNITION PARTICLE, CPSRP43, CHROMO DOMAIN 1, LHCP, KEYWDS 2 THYLAKOID, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR V.SIVARAJA,T.K.KUMAR,R.HENRY,C.YU REVDAT 4 02-MAR-22 1X32 1 REMARK SEQADV REVDAT 3 24-FEB-09 1X32 1 VERSN REVDAT 2 24-JAN-06 1X32 1 JRNL REVDAT 1 20-SEP-05 1X32 0 JRNL AUTH V.SIVARAJA,T.K.KUMAR,P.S.LEENA,A.N.CHANG,C.VIDYA, JRNL AUTH 2 R.L.GOFORTH,D.RAJALINGAM,K.ARVIND,J.L.YE,J.CHOU,R.HENRY,C.YU JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE CHROMODOMAINS JRNL TITL 2 OF CPSRP43 JRNL REF J.BIOL.CHEM. V. 280 41465 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 16183644 JRNL DOI 10.1074/JBC.M507077200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X32 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024316. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE ,100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : UNLABELED CHROMO 1 DOMAIN, REMARK 210 UNIFORMLY LABELED 15N CHROMO REMARK 210 DOMAIN 1, UNIFORMLY 15N AND 13C REMARK 210 LABELED CHROMO 1 DOMAIN REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D N15 NOESY REMARK 210 -HSQC; 3D 15N-SEPARATED HSQC- REMARK 210 TOCSY; HNHA; 3D_13C-SEPARATED_ REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1 REMARK 210 METHOD USED : TORSIONAL ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR, 3D HETERONUCLEAR NMR EXPERIMENTS 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 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 2 TYR A 38 CE1 TYR A 38 CZ 0.221 REMARK 500 2 TYR A 38 CZ TYR A 38 CE2 -0.204 REMARK 500 3 TYR A 21 CE1 TYR A 21 CZ 0.104 REMARK 500 3 TYR A 38 CZ TYR A 38 CE2 0.092 REMARK 500 5 TYR A 21 CE1 TYR A 21 CZ 0.219 REMARK 500 5 TYR A 21 CZ TYR A 21 CE2 -0.202 REMARK 500 6 TYR A 38 CZ TYR A 38 CE2 0.105 REMARK 500 7 TYR A 21 CE1 TYR A 21 CZ 0.143 REMARK 500 7 TYR A 21 CZ TYR A 21 CE2 -0.145 REMARK 500 7 TYR A 38 CZ TYR A 38 CE2 0.080 REMARK 500 8 TYR A 21 CE1 TYR A 21 CZ 0.189 REMARK 500 8 TYR A 21 CZ TYR A 21 CE2 -0.174 REMARK 500 10 TYR A 21 CE1 TYR A 21 CZ 0.301 REMARK 500 10 TYR A 21 CZ TYR A 21 CE2 -0.296 REMARK 500 12 TYR A 38 CZ TYR A 38 CE2 0.087 REMARK 500 13 TYR A 21 CE1 TYR A 21 CZ 0.271 REMARK 500 13 TYR A 21 CZ TYR A 21 CE2 -0.256 REMARK 500 15 TYR A 38 CE1 TYR A 38 CZ 0.244 REMARK 500 15 TYR A 38 CZ TYR A 38 CE2 -0.235 REMARK 500 16 TYR A 21 CE1 TYR A 21 CZ 0.163 REMARK 500 16 TYR A 21 CZ TYR A 21 CE2 -0.159 REMARK 500 17 TYR A 21 CE1 TYR A 21 CZ 0.123 REMARK 500 17 TYR A 21 CZ TYR A 21 CE2 -0.124 REMARK 500 17 TYR A 38 CZ TYR A 38 CE2 0.099 REMARK 500 19 TYR A 38 CE1 TYR A 38 CZ 0.261 REMARK 500 19 TYR A 38 CZ TYR A 38 CE2 -0.231 REMARK 500 20 TYR A 38 CE1 TYR A 38 CZ 0.108 REMARK 500 20 TYR A 38 CZ TYR A 38 CE2 -0.097 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 2 TYR A 38 CD1 - CE1 - CZ ANGL. DEV. = -5.6 DEGREES REMARK 500 5 TYR A 21 CE1 - CZ - OH ANGL. DEV. = -16.4 DEGREES REMARK 500 10 TYR A 21 CD1 - CE1 - CZ ANGL. DEV. = -6.9 DEGREES REMARK 500 10 TYR A 21 OH - CZ - CE2 ANGL. DEV. = 20.2 DEGREES REMARK 500 10 TYR A 21 CE1 - CZ - OH ANGL. DEV. = -21.2 DEGREES REMARK 500 10 TYR A 21 CZ - CE2 - CD2 ANGL. DEV. = 7.8 DEGREES REMARK 500 13 TYR A 21 CD1 - CE1 - CZ ANGL. DEV. = -6.2 DEGREES REMARK 500 13 TYR A 21 CE1 - CZ - OH ANGL. DEV. = -19.7 DEGREES REMARK 500 13 TYR A 21 CZ - CE2 - CD2 ANGL. DEV. = 6.2 DEGREES REMARK 500 15 TYR A 38 CD1 - CE1 - CZ ANGL. DEV. = -6.2 DEGREES REMARK 500 15 TYR A 38 OH - CZ - CE2 ANGL. DEV. = 16.9 DEGREES REMARK 500 15 TYR A 38 CE1 - CZ - OH ANGL. DEV. = -17.1 DEGREES REMARK 500 15 TYR A 38 CZ - CE2 - CD2 ANGL. DEV. = 5.9 DEGREES REMARK 500 19 TYR A 38 CD1 - CE1 - CZ ANGL. DEV. = -6.7 DEGREES REMARK 500 19 TYR A 38 CE1 - CZ - OH ANGL. DEV. = -19.3 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 1 ASN A 6 44.51 82.06 REMARK 500 1 LYS A 7 -143.20 -119.76 REMARK 500 1 THR A 13 -80.82 -116.67 REMARK 500 1 ALA A 14 -58.79 -150.30 REMARK 500 1 MET A 19 26.01 -165.47 REMARK 500 1 TYR A 21 -53.96 -155.17 REMARK 500 1 ILE A 23 -117.61 -7.54 REMARK 500 1 GLU A 24 24.00 48.88 REMARK 500 1 TRP A 25 31.13 -145.81 REMARK 500 1 LYS A 26 33.98 33.54 REMARK 500 1 SER A 30 106.68 40.43 REMARK 500 1 PRO A 31 130.63 -33.53 REMARK 500 1 SER A 36 28.08 41.20 REMARK 500 1 SER A 37 -131.85 -166.23 REMARK 500 1 TYR A 38 98.92 -170.45 REMARK 500 1 ALA A 40 89.98 -69.82 REMARK 500 1 ALA A 41 42.25 152.96 REMARK 500 1 ASP A 42 88.67 54.76 REMARK 500 1 GLU A 46 -173.04 177.80 REMARK 500 2 GLU A 4 12.98 58.29 REMARK 500 2 ASN A 6 71.66 39.09 REMARK 500 2 LYS A 7 -141.98 -150.77 REMARK 500 2 ILE A 8 106.44 -56.49 REMARK 500 2 THR A 13 -85.42 -115.69 REMARK 500 2 ALA A 14 -51.57 -146.03 REMARK 500 2 MET A 19 24.58 -162.74 REMARK 500 2 TYR A 21 9.66 -157.61 REMARK 500 2 TRP A 25 32.57 -86.98 REMARK 500 2 SER A 30 117.23 32.43 REMARK 500 2 PRO A 31 118.93 -31.50 REMARK 500 2 SER A 36 -51.72 79.90 REMARK 500 2 SER A 37 -65.49 -144.16 REMARK 500 2 TYR A 38 140.88 178.70 REMARK 500 2 ILE A 39 30.79 -161.10 REMARK 500 2 ALA A 40 89.85 -66.23 REMARK 500 2 ALA A 41 41.10 156.62 REMARK 500 2 ASP A 42 84.09 58.18 REMARK 500 2 VAL A 43 -151.51 -157.21 REMARK 500 2 GLU A 46 147.01 179.05 REMARK 500 3 ASN A 6 79.10 47.50 REMARK 500 3 LYS A 7 -98.61 -135.68 REMARK 500 3 THR A 13 -78.21 -116.36 REMARK 500 3 ALA A 14 -54.94 -149.96 REMARK 500 3 MET A 19 51.88 -164.23 REMARK 500 3 GLU A 20 -124.39 -151.01 REMARK 500 3 TYR A 21 -126.78 -155.72 REMARK 500 3 GLU A 24 38.67 178.88 REMARK 500 3 TRP A 25 32.92 -153.15 REMARK 500 3 SER A 30 107.48 37.63 REMARK 500 3 PRO A 31 125.67 -33.85 REMARK 500 REMARK 500 THIS ENTRY HAS 405 RAMACHANDRAN OUTLIERS. 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 3 TYR A 21 0.10 SIDE CHAIN REMARK 500 3 TYR A 38 0.10 SIDE CHAIN REMARK 500 5 TYR A 21 0.06 SIDE CHAIN REMARK 500 6 TYR A 38 0.08 SIDE CHAIN REMARK 500 7 TYR A 38 0.09 SIDE CHAIN REMARK 500 8 TYR A 21 0.06 SIDE CHAIN REMARK 500 9 TYR A 38 0.08 SIDE CHAIN REMARK 500 12 TYR A 38 0.06 SIDE CHAIN REMARK 500 13 TYR A 21 0.06 SIDE CHAIN REMARK 500 14 TYR A 21 0.07 SIDE CHAIN REMARK 500 14 TYR A 38 0.06 SIDE CHAIN REMARK 500 16 TYR A 38 0.07 SIDE CHAIN REMARK 500 17 TYR A 38 0.09 SIDE CHAIN REMARK 500 18 TYR A 38 0.08 SIDE CHAIN REMARK 500 19 TYR A 38 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1X32 A 3 47 UNP O22265 O22265_ARATH 84 128 SEQADV 1X32 GLY A 1 UNP O22265 CLONING ARTIFACT SEQADV 1X32 SER A 2 UNP O22265 CLONING ARTIFACT SEQRES 1 A 47 GLY SER GLY GLU VAL ASN LYS ILE ILE GLY SER ARG THR SEQRES 2 A 47 ALA GLY GLU GLY ALA MET GLU TYR LEU ILE GLU TRP LYS SEQRES 3 A 47 ASP GLY HIS SER PRO SER TRP VAL PRO SER SER TYR ILE SEQRES 4 A 47 ALA ALA ASP VAL VAL SER GLU TYR 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 - r 2 2 Bytes