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
(ATOM LINES ARE NOT SHOWN.)
END