Header list of 2b1u.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 16-SEP-05 2B1U TITLE SOLUTION STRUCTURE OF CALMODULIN-LIKE SKIN PROTEIN C TERMINAL DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN-LIKE PROTEIN 5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C TERMINAL DOMAIN; COMPND 5 SYNONYM: CALMODULIN-LIKE SKIN PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CALML5; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL1BLUE; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30XA KEYWDS CLSP, CALMODULIN-LIKE SKIN PROTEIN, SOLUTION STRUCTURE, BACKBONE KEYWDS 2 DYNAMIC, STRUCTURAL GENOMICS, STRUCTURAL PROTEOMICS IN EUROPE, KEYWDS 3 SPINE, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR E.BABINI,I.BERTINI,F.CAPOZZI,E.CHIRIVINO,C.LUCHINAT,STRUCTURAL AUTHOR 2 PROTEOMICS IN EUROPE (SPINE) REVDAT 4 09-MAR-22 2B1U 1 REMARK REVDAT 3 24-FEB-09 2B1U 1 VERSN REVDAT 2 27-JUN-06 2B1U 1 JRNL REVDAT 1 30-MAY-06 2B1U 0 JRNL AUTH E.BABINI,I.BERTINI,F.CAPOZZI,E.CHIRIVINO,C.LUCHINAT JRNL TITL A STRUCTURAL AND DYNAMIC CHARACTERIZATION OF THE EF-HAND JRNL TITL 2 PROTEIN CLSP. JRNL REF STRUCTURE V. 14 1029 2006 JRNL REFN ISSN 0969-2126 JRNL PMID 16765896 JRNL DOI 10.1016/J.STR.2006.04.004 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 5.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2B1U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-05. REMARK 100 THE DEPOSITION ID IS D_1000034570. 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 : 100MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2MM 15N PROTEIN SAMPLE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_TOCSY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ; 700 MHZ; 500 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CARA 1.2, CYANA 1.2 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, COUPLED REMARK 210 WITH SIMULATED ANNEALING, REMARK 210 FOLLOWED BY RESTRAINED ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 400 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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: 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: 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 LEU A 83 CB - CG - CD2 ANGL. DEV. = -11.0 DEGREES REMARK 500 4 TYR A 136 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 6 LEU A 83 CB - CG - CD2 ANGL. DEV. = -10.3 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 GLN A 92 -79.51 -79.37 REMARK 500 1 ASP A 93 14.59 -166.49 REMARK 500 1 ALA A 126 46.58 -78.01 REMARK 500 1 ASP A 129 -83.33 -69.77 REMARK 500 1 GLN A 130 38.04 169.21 REMARK 500 1 ASP A 131 -90.43 -167.69 REMARK 500 1 GLN A 145 43.86 -71.61 REMARK 500 2 ALA A 78 -94.71 -79.03 REMARK 500 2 ASP A 91 -159.67 -84.94 REMARK 500 2 GLN A 92 -81.54 -151.01 REMARK 500 2 ASP A 93 48.05 -169.18 REMARK 500 2 ILE A 98 -162.92 -101.83 REMARK 500 2 GLN A 112 72.69 -105.17 REMARK 500 2 ASP A 129 -104.37 -85.27 REMARK 500 2 GLN A 130 67.54 -169.13 REMARK 500 2 ASP A 131 -61.50 -173.27 REMARK 500 3 ALA A 78 68.58 -67.82 REMARK 500 3 ASP A 95 -39.75 -29.56 REMARK 500 3 LEU A 114 61.89 61.31 REMARK 500 3 ASP A 129 -90.07 -81.25 REMARK 500 3 GLN A 130 44.37 -172.41 REMARK 500 3 ASP A 131 -90.13 -168.87 REMARK 500 4 ARG A 77 166.45 81.13 REMARK 500 4 ALA A 78 -89.91 -52.29 REMARK 500 4 ASP A 93 61.73 174.90 REMARK 500 4 ASP A 129 -101.98 -79.88 REMARK 500 4 GLN A 130 50.75 -171.70 REMARK 500 4 ASP A 131 -82.11 -164.06 REMARK 500 4 ARG A 141 -72.10 -62.61 REMARK 500 4 ALA A 144 49.22 -83.17 REMARK 500 4 GLN A 145 44.22 34.75 REMARK 500 5 ALA A 78 -139.60 -77.30 REMARK 500 5 ARG A 88 -34.30 -39.68 REMARK 500 5 GLN A 92 -105.27 -117.66 REMARK 500 5 ASP A 93 46.49 -174.60 REMARK 500 5 GLN A 112 77.76 -107.19 REMARK 500 5 ALA A 126 41.18 -90.43 REMARK 500 5 ASP A 127 55.90 -108.24 REMARK 500 5 ASP A 129 -95.32 -72.61 REMARK 500 5 GLN A 130 34.27 -167.77 REMARK 500 5 ASP A 131 -90.46 -158.50 REMARK 500 5 ASN A 135 108.99 -58.98 REMARK 500 6 ARG A 77 146.73 -178.50 REMARK 500 6 ALA A 78 73.67 -69.05 REMARK 500 6 ARG A 88 5.68 -68.51 REMARK 500 6 PHE A 90 45.00 -103.68 REMARK 500 6 ASP A 93 47.68 175.41 REMARK 500 6 ASP A 95 40.40 38.42 REMARK 500 6 ALA A 126 38.82 -72.39 REMARK 500 6 ASP A 127 70.05 -112.60 REMARK 500 REMARK 500 THIS ENTRY HAS 160 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 ALA A 78 GLY A 79 1 -143.04 REMARK 500 ARG A 77 ALA A 78 3 146.51 REMARK 500 ALA A 78 GLY A 79 3 122.73 REMARK 500 ARG A 77 ALA A 78 6 146.01 REMARK 500 ALA A 78 GLY A 79 6 126.07 REMARK 500 GLY A 94 ASP A 95 6 -143.89 REMARK 500 ARG A 77 ALA A 78 7 139.83 REMARK 500 ALA A 78 GLY A 79 7 -143.04 REMARK 500 ALA A 78 GLY A 79 8 -145.64 REMARK 500 ARG A 77 ALA A 78 9 147.01 REMARK 500 ALA A 78 GLY A 79 12 -136.55 REMARK 500 ARG A 77 ALA A 78 14 143.72 REMARK 500 ASP A 95 GLY A 96 14 144.25 REMARK 500 ARG A 77 ALA A 78 15 135.89 REMARK 500 ASP A 95 GLY A 96 15 144.34 REMARK 500 ARG A 77 ALA A 78 16 135.57 REMARK 500 ILE A 98 THR A 99 16 146.57 REMARK 500 ARG A 77 ALA A 78 17 133.48 REMARK 500 ALA A 78 GLY A 79 17 -126.73 REMARK 500 GLY A 96 HIS A 97 17 -146.16 REMARK 500 ILE A 98 THR A 99 17 145.59 REMARK 500 ARG A 77 ALA A 78 18 145.05 REMARK 500 ALA A 78 GLY A 79 19 -135.66 REMARK 500 HIS A 97 ILE A 98 19 149.96 REMARK 500 ALA A 78 GLY A 79 20 -133.06 REMARK 500 GLY A 79 LEU A 80 20 -149.29 REMARK 500 ASP A 95 GLY A 96 20 149.90 REMARK 500 MET A 142 LEU A 143 20 146.12 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 PHE A 87 0.13 SIDE CHAIN REMARK 500 1 ARG A 104 0.13 SIDE CHAIN REMARK 500 1 TYR A 136 0.07 SIDE CHAIN REMARK 500 2 ARG A 104 0.19 SIDE CHAIN REMARK 500 2 PHE A 139 0.14 SIDE CHAIN REMARK 500 3 PHE A 87 0.20 SIDE CHAIN REMARK 500 3 ARG A 104 0.09 SIDE CHAIN REMARK 500 4 PHE A 87 0.16 SIDE CHAIN REMARK 500 5 PHE A 87 0.14 SIDE CHAIN REMARK 500 5 TYR A 136 0.10 SIDE CHAIN REMARK 500 6 ARG A 77 0.08 SIDE CHAIN REMARK 500 6 PHE A 90 0.10 SIDE CHAIN REMARK 500 6 ARG A 104 0.14 SIDE CHAIN REMARK 500 6 ARG A 105 0.10 SIDE CHAIN REMARK 500 6 TYR A 136 0.13 SIDE CHAIN REMARK 500 7 PHE A 87 0.11 SIDE CHAIN REMARK 500 7 ARG A 104 0.14 SIDE CHAIN REMARK 500 7 TYR A 136 0.15 SIDE CHAIN REMARK 500 8 PHE A 87 0.08 SIDE CHAIN REMARK 500 8 ARG A 104 0.09 SIDE CHAIN REMARK 500 8 ARG A 133 0.08 SIDE CHAIN REMARK 500 9 PHE A 87 0.23 SIDE CHAIN REMARK 500 9 ARG A 104 0.11 SIDE CHAIN REMARK 500 9 ARG A 124 0.08 SIDE CHAIN REMARK 500 9 TYR A 136 0.10 SIDE CHAIN REMARK 500 10 PHE A 87 0.16 SIDE CHAIN REMARK 500 10 ARG A 104 0.13 SIDE CHAIN REMARK 500 10 TYR A 136 0.13 SIDE CHAIN REMARK 500 11 PHE A 87 0.10 SIDE CHAIN REMARK 500 11 TYR A 136 0.08 SIDE CHAIN REMARK 500 12 PHE A 87 0.23 SIDE CHAIN REMARK 500 12 ARG A 104 0.11 SIDE CHAIN REMARK 500 12 TYR A 136 0.10 SIDE CHAIN REMARK 500 12 PHE A 139 0.09 SIDE CHAIN REMARK 500 13 ARG A 77 0.08 SIDE CHAIN REMARK 500 13 PHE A 87 0.14 SIDE CHAIN REMARK 500 13 ARG A 88 0.09 SIDE CHAIN REMARK 500 14 PHE A 90 0.09 SIDE CHAIN REMARK 500 14 ARG A 104 0.11 SIDE CHAIN REMARK 500 14 ARG A 105 0.10 SIDE CHAIN REMARK 500 15 PHE A 87 0.11 SIDE CHAIN REMARK 500 15 PHE A 90 0.08 SIDE CHAIN REMARK 500 15 ARG A 104 0.10 SIDE CHAIN REMARK 500 15 TYR A 136 0.08 SIDE CHAIN REMARK 500 16 ARG A 77 0.11 SIDE CHAIN REMARK 500 16 PHE A 87 0.14 SIDE CHAIN REMARK 500 16 PHE A 90 0.08 SIDE CHAIN REMARK 500 16 ARG A 104 0.11 SIDE CHAIN REMARK 500 16 TYR A 136 0.10 SIDE CHAIN REMARK 500 17 PHE A 87 0.13 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 64 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2B1U A 76 146 UNP Q9NZT1 CALL5_HUMAN 76 146 SEQRES 1 A 71 ALA ARG ALA GLY LEU GLU ASP LEU GLN VAL ALA PHE ARG SEQRES 2 A 71 ALA PHE ASP GLN ASP GLY ASP GLY HIS ILE THR VAL ASP SEQRES 3 A 71 GLU LEU ARG ARG ALA MET ALA GLY LEU GLY GLN PRO LEU SEQRES 4 A 71 PRO GLN GLU GLU LEU ASP ALA MET ILE ARG GLU ALA ASP SEQRES 5 A 71 VAL ASP GLN ASP GLY ARG VAL ASN TYR GLU GLU PHE ALA SEQRES 6 A 71 ARG MET LEU ALA GLN GLU HELIX 1 1 GLY A 79 ARG A 88 1 10 HELIX 2 2 VAL A 100 MET A 107 1 8 HELIX 3 3 ALA A 108 LEU A 110 5 3 HELIX 4 4 PRO A 115 ALA A 126 1 12 HELIX 5 5 GLU A 137 ALA A 144 1 8 SHEET 1 A 2 HIS A 97 THR A 99 0 SHEET 2 A 2 ARG A 133 ASN A 135 -1 O VAL A 134 N ILE A 98 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 9 2 Bytes