HEADER METAL BINDING PROTEIN 23-APR-11 2LC5
TITLE CALMODULIN-LIKE PROTEIN FROM ENTAMOEBA HISTOLYTICA: SOLUTION STRUCTURE
TITLE 2 AND CALCIUM-BINDING PROPERTIES OF A PARTIALLY FOLDED PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN, PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-85;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;
SOURCE 3 ORGANISM_TAXID: 294381;
SOURCE 4 STRAIN: HM-1:IMSS;
SOURCE 5 GENE: EHI_100270;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30A
KEYWDS EHCAM, CA-BINDING PROTEIN, ENTAMOEBA HISTOLYTICA, PARTIALLY
KEYWDS 2 STRUCTURED PROTEIN, CAM-LIKE, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.K.ROUT,N.PADHAN,R.P.BARNWAL,A.BHATTACHARYA,K.V.CHARY
REVDAT 2 27-APR-16 2LC5 1 SEQRES VERSN
REVDAT 1 08-JUN-11 2LC5 0
SPRSDE 08-JUN-11 2LC5 2KTG
JRNL AUTH A.K.ROUT,N.PADHAN,R.P.BARNWAL,A.BHATTACHARYA,K.V.CHARY
JRNL TITL CALMODULIN LIKE PROTEIN FROM ENTAMOEBA HISTOLYTICA: SOLUTION
JRNL TITL 2 STRUCTURE AND CALCIUM BINDING PROPERTIES OF A PARTIALLY
JRNL TITL 3 FOLDED PROTEIN.
JRNL REF BIOCHEMISTRY V. 50 181 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 21114322
JRNL DOI 10.1021/BI101411Q
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA_3.0 BETA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB102215.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1 MM [U-100% 15N] PROTEIN-1,
REMARK 210 90% H2O/10% D2O; 1.1 MM [U-100%
REMARK 210 13C] PROTEIN-2, 100% D2O; 1.1 MM
REMARK 210 [U-100% 13C; U-100% 15N] PROTEIN-
REMARK 210 3, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HN(CO)CA; 3D 1H-15N NOESY; 3D 1
REMARK 210 15N TOCSY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TALOS
REMARK 210 METHOD USED : DGSA-DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING, DISTANCE GEOMETRY,
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 ENER
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 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 THR A 86
REMARK 465 GLU A 87
REMARK 465 ASP A 88
REMARK 465 ILE A 89
REMARK 465 LYS A 90
REMARK 465 LYS A 91
REMARK 465 ALA A 92
REMARK 465 PHE A 93
REMARK 465 GLU A 94
REMARK 465 ILE A 95
REMARK 465 PHE A 96
REMARK 465 ASP A 97
REMARK 465 LYS A 98
REMARK 465 GLU A 99
REMARK 465 LYS A 100
REMARK 465 ASN A 101
REMARK 465 GLY A 102
REMARK 465 TYR A 103
REMARK 465 ILE A 104
REMARK 465 SER A 105
REMARK 465 ALA A 106
REMARK 465 SER A 107
REMARK 465 GLU A 108
REMARK 465 LEU A 109
REMARK 465 LYS A 110
REMARK 465 HIS A 111
REMARK 465 VAL A 112
REMARK 465 LEU A 113
REMARK 465 THR A 114
REMARK 465 THR A 115
REMARK 465 LEU A 116
REMARK 465 GLY A 117
REMARK 465 GLU A 118
REMARK 465 LYS A 119
REMARK 465 LEU A 120
REMARK 465 THR A 121
REMARK 465 GLU A 122
REMARK 465 GLN A 123
REMARK 465 GLU A 124
REMARK 465 VAL A 125
REMARK 465 ASP A 126
REMARK 465 ASP A 127
REMARK 465 LEU A 128
REMARK 465 LEU A 129
REMARK 465 LYS A 130
REMARK 465 GLU A 131
REMARK 465 ILE A 132
REMARK 465 GLY A 133
REMARK 465 VAL A 134
REMARK 465 GLU A 135
REMARK 465 GLU A 136
REMARK 465 GLY A 137
REMARK 465 LEU A 138
REMARK 465 ILE A 139
REMARK 465 ASN A 140
REMARK 465 VAL A 141
REMARK 465 ASP A 142
REMARK 465 ASP A 143
REMARK 465 PHE A 144
REMARK 465 VAL A 145
REMARK 465 LYS A 146
REMARK 465 LEU A 147
REMARK 465 ILE A 148
REMARK 465 THR A 149
REMARK 465 SER A 150
REMARK 465 LYS A 151
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 ALA A 45 -75.93 -136.17
REMARK 500 1 ASN A 46 68.36 -175.90
REMARK 500 1 ASN A 63 -74.54 -139.34
REMARK 500 1 SER A 64 -169.17 -176.79
REMARK 500 1 GLN A 81 -35.14 -178.75
REMARK 500 1 GLU A 82 -75.18 69.66
REMARK 500 2 ASP A 24 68.59 -115.84
REMARK 500 2 ALA A 45 -75.80 -138.87
REMARK 500 2 ASN A 46 68.13 -175.71
REMARK 500 2 PRO A 47 -170.92 -69.78
REMARK 500 2 ASN A 63 -74.93 -142.29
REMARK 500 2 SER A 64 -169.14 -179.55
REMARK 500 2 GLN A 81 -74.79 -74.46
REMARK 500 3 ASP A 24 75.89 -117.29
REMARK 500 3 ASP A 26 -169.63 -70.59
REMARK 500 3 ALA A 45 83.27 63.97
REMARK 500 3 ASN A 46 -60.96 179.69
REMARK 500 3 PRO A 47 -170.81 -69.85
REMARK 500 3 ASP A 60 64.46 -104.34
REMARK 500 3 ASN A 63 -74.50 -149.45
REMARK 500 3 SER A 64 -169.32 -178.68
REMARK 500 4 LEU A 8 74.22 -170.76
REMARK 500 4 PRO A 47 -170.85 -69.69
REMARK 500 4 ASP A 60 54.48 -99.39
REMARK 500 4 ASN A 63 -69.41 -152.37
REMARK 500 4 SER A 64 -169.28 -179.33
REMARK 500 4 GLU A 82 -177.26 58.92
REMARK 500 5 SER A 2 -55.37 -167.00
REMARK 500 5 LYS A 6 48.86 -103.44
REMARK 500 5 ASP A 24 68.06 -117.38
REMARK 500 5 ASP A 26 -168.98 -70.38
REMARK 500 5 ALA A 45 32.04 -98.27
REMARK 500 5 PRO A 47 -174.09 -69.72
REMARK 500 5 ASP A 60 69.99 -104.27
REMARK 500 5 ASN A 63 -71.36 -148.79
REMARK 500 5 SER A 64 -169.42 -178.81
REMARK 500 5 GLN A 81 -74.87 -91.65
REMARK 500 5 GLU A 82 -179.89 -176.85
REMARK 500 6 SER A 2 119.25 -166.87
REMARK 500 6 GLU A 3 -63.87 -124.49
REMARK 500 6 ASP A 26 -169.67 -73.82
REMARK 500 6 PRO A 47 -170.76 -69.75
REMARK 500 6 ASN A 63 -74.50 -142.06
REMARK 500 6 SER A 64 -169.19 -178.58
REMARK 500 6 VAL A 83 151.99 65.18
REMARK 500 7 SER A 2 -70.63 -153.11
REMARK 500 7 ASP A 26 -169.62 -75.48
REMARK 500 7 ASN A 46 -61.06 179.78
REMARK 500 7 ASP A 60 50.41 -97.27
REMARK 500 7 ASN A 63 -72.48 -141.03
REMARK 500
REMARK 500 THIS ENTRY HAS 146 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A 250 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 26 OD2
REMARK 620 2 ASP A 24 OD1 103.6
REMARK 620 3 ASP A 26 OD1 47.8 55.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15663 RELATED DB: BMRB
DBREF 2LC5 A 1 151 UNP C4M0U8 C4M0U8_ENTHI 1 151
SEQRES 1 A 151 MET SER GLU GLN LYS LYS VAL LEU THR ALA GLU GLU GLN
SEQRES 2 A 151 GLN GLU TYR LYS GLU ALA PHE GLN LEU PHE ASP LYS ASP
SEQRES 3 A 151 ASN ASP ASN LYS LEU THR ALA GLU GLU LEU GLY THR VAL
SEQRES 4 A 151 MET ARG ALA LEU GLY ALA ASN PRO THR LYS GLN LYS ILE
SEQRES 5 A 151 SER GLU ILE VAL LYS ASP TYR ASP LYS ASP ASN SER GLY
SEQRES 6 A 151 LYS PHE ASP GLN GLU THR PHE LEU THR ILE MET LEU GLU
SEQRES 7 A 151 TYR GLY GLN GLU VAL ASP SER THR GLU ASP ILE LYS LYS
SEQRES 8 A 151 ALA PHE GLU ILE PHE ASP LYS GLU LYS ASN GLY TYR ILE
SEQRES 9 A 151 SER ALA SER GLU LEU LYS HIS VAL LEU THR THR LEU GLY
SEQRES 10 A 151 GLU LYS LEU THR GLU GLN GLU VAL ASP ASP LEU LEU LYS
SEQRES 11 A 151 GLU ILE GLY VAL GLU GLU GLY LEU ILE ASN VAL ASP ASP
SEQRES 12 A 151 PHE VAL LYS LEU ILE THR SER LYS
HET CA A 250 1
HET CA A 300 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 THR A 9 PHE A 23 1 15
HELIX 2 2 ALA A 33 ALA A 42 1 10
HELIX 3 3 THR A 48 ASP A 60 1 13
HELIX 4 4 GLN A 69 GLY A 80 1 12
SHEET 1 A 2 LYS A 30 THR A 32 0
SHEET 2 A 2 LYS A 66 ASP A 68 -1 O PHE A 67 N LEU A 31
LINK OD2 ASP A 26 CA CA A 250 1555 1555 2.12
LINK OD1 ASP A 24 CA CA A 250 1555 1555 2.53
LINK OD1 ASP A 26 CA CA A 250 1555 1555 2.96
SITE 1 AC1 4 ASP A 24 ASP A 26 LYS A 30 GLU A 35
SITE 1 AC2 2 ASP A 60 ASN A 63
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
