HEADER CALCIUM-BINDING PROTEIN 27-OCT-11 3UCW
TITLE STRUCTURE OF MG2+ BOUND N-TERMINAL DOMAIN OF CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN RESIDUES 2-80;
COMPND 5 SYNONYM: CAM;
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: CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3,
SOURCE 6 CAMB, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PAED4
KEYWDS EF-HAND, METAL BINDING, CALCIUM REGULATION, CALCIUM-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.T.SENGUEN,Z.GRABAREK
REVDAT 3 28-FEB-24 3UCW 1 REMARK LINK
REVDAT 2 03-OCT-12 3UCW 1 JRNL
REVDAT 1 08-AUG-12 3UCW 0
JRNL AUTH F.T.SENGUEN,Z.GRABAREK
JRNL TITL X-RAY STRUCTURES OF MAGNESIUM AND MANGANESE COMPLEXES WITH
JRNL TITL 2 THE N-TERMINAL DOMAIN OF CALMODULIN: INSIGHTS INTO THE
JRNL TITL 3 MECHANISM AND SPECIFICITY OF METAL ION BINDING TO AN
JRNL TITL 4 EF-HAND.
JRNL REF BIOCHEMISTRY V. 51 6182 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22803592
JRNL DOI 10.1021/BI300698H
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_869
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 26491
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1344
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.3301 - 3.7911 0.98 2599 144 0.1928 0.2366
REMARK 3 2 3.7911 - 3.0094 0.98 2613 130 0.1847 0.1922
REMARK 3 3 3.0094 - 2.6291 0.97 2563 133 0.1906 0.2338
REMARK 3 4 2.6291 - 2.3888 0.97 2527 162 0.1968 0.2357
REMARK 3 5 2.3888 - 2.2176 0.96 2577 140 0.1907 0.2300
REMARK 3 6 2.2176 - 2.0868 0.96 2548 142 0.2018 0.2603
REMARK 3 7 2.0868 - 1.9823 0.95 2520 130 0.2043 0.2557
REMARK 3 8 1.9823 - 1.8960 0.95 2521 119 0.2134 0.2843
REMARK 3 9 1.8960 - 1.8230 0.95 2531 122 0.2400 0.2587
REMARK 3 10 1.8230 - 1.7600 0.81 2148 122 0.2807 0.3549
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 60.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.09030
REMARK 3 B22 (A**2) : -5.49390
REMARK 3 B33 (A**2) : -0.59640
REMARK 3 B12 (A**2) : -0.24830
REMARK 3 B13 (A**2) : 3.24630
REMARK 3 B23 (A**2) : 0.19530
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2506
REMARK 3 ANGLE : 0.877 3441
REMARK 3 CHIRALITY : 0.051 374
REMARK 3 PLANARITY : 0.004 443
REMARK 3 DIHEDRAL : 16.850 953
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NINE QUADRANT
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26501
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM TRIS CACODYLATE, 32% PEG8000,
REMARK 280 25MM MGAC, 1MM EGTA, 50MM KCL, 25% ETHYLENE GLYCOL, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -7.88773
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -42.31105
REMARK 350 BIOMT3 2 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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 ASP A 78
REMARK 465 THR A 79
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 LYS C 77
REMARK 465 ASP C 78
REMARK 465 THR C 79
REMARK 465 ALA D 1
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 ASN C 42 57.82 -159.27
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 MG A 100 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 83.8
REMARK 620 3 ASP A 24 OD1 86.7 91.8
REMARK 620 4 THR A 26 O 91.7 174.6 91.0
REMARK 620 5 HOH A 208 O 171.5 92.0 86.0 92.9
REMARK 620 6 HOH A 224 O 99.7 84.3 172.1 93.5 87.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 62 O
REMARK 620 2 THR A 62 OG1 88.0
REMARK 620 3 HOH A 209 O 170.7 82.6
REMARK 620 4 HOH A 210 O 89.2 87.2 90.5
REMARK 620 5 HOH A 211 O 95.9 175.8 93.4 91.5
REMARK 620 6 HOH A 212 O 91.2 93.8 89.3 178.9 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HOH A 217 O 87.1
REMARK 620 3 ASP B 64 OD2 177.2 91.1
REMARK 620 4 HOH B 201 O 90.9 94.9 87.1
REMARK 620 5 HOH B 202 O 92.0 87.6 90.0 176.2
REMARK 620 6 HOH B 212 O 91.2 174.3 90.8 90.5 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 100 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD1 78.7
REMARK 620 3 ASP B 24 OD1 80.3 82.9
REMARK 620 4 THR B 26 O 78.2 156.8 91.7
REMARK 620 5 HOH B 204 O 101.6 95.2 177.1 90.9
REMARK 620 6 HOH B 205 O 171.5 102.7 91.6 100.0 86.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 62 O
REMARK 620 2 THR B 62 OG1 90.0
REMARK 620 3 HOH B 207 O 91.9 173.9
REMARK 620 4 HOH B 208 O 92.5 93.5 92.2
REMARK 620 5 HOH B 209 O 86.0 85.3 89.0 178.1
REMARK 620 6 HOH B 217 O 170.9 81.0 97.2 86.4 94.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 100 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 20 OD1
REMARK 620 2 ASP C 22 OD1 83.0
REMARK 620 3 ASP C 24 OD1 88.5 93.1
REMARK 620 4 THR C 26 O 89.8 166.7 97.9
REMARK 620 5 HOH C 208 O 172.5 90.7 87.7 97.1
REMARK 620 6 HOH C 209 O 93.5 79.8 172.3 89.6 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 62 O
REMARK 620 2 THR C 62 OG1 84.6
REMARK 620 3 HOH C 204 O 90.9 95.9
REMARK 620 4 HOH C 205 O 96.6 176.3 87.6
REMARK 620 5 HOH C 206 O 168.4 83.8 89.7 95.0
REMARK 620 6 HOH C 216 O 88.5 83.6 179.3 92.9 90.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 64 OD2
REMARK 620 2 HOH C 202 O 97.6
REMARK 620 3 HOH C 203 O 83.8 96.5
REMARK 620 4 HOH C 219 O 90.3 169.5 91.2
REMARK 620 5 HOH C 220 O 92.7 89.6 173.3 83.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 100 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 20 OD1
REMARK 620 2 ASP D 22 OD1 78.8
REMARK 620 3 ASP D 24 OD1 86.8 86.6
REMARK 620 4 THR D 26 O 83.7 162.5 92.8
REMARK 620 5 HOH D 201 O 93.9 87.8 174.1 93.1
REMARK 620 6 HOH D 202 O 175.3 97.9 89.7 99.5 89.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 62 O
REMARK 620 2 THR D 62 OG1 87.9
REMARK 620 3 HOH D 203 O 91.5 93.9
REMARK 620 4 HOH D 204 O 88.4 88.3 177.9
REMARK 620 5 HOH D 212 O 95.5 176.2 87.7 90.2
REMARK 620 6 HOH D 230 O 168.7 81.0 86.9 93.6 95.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UCT RELATED DB: PDB
REMARK 900 RELATED ID: 3UCY RELATED DB: PDB
DBREF 3UCW A 1 79 UNP P62158 CALM_HUMAN 2 80
DBREF 3UCW B 1 79 UNP P62158 CALM_HUMAN 2 80
DBREF 3UCW C 1 79 UNP P62158 CALM_HUMAN 2 80
DBREF 3UCW D 1 79 UNP P62158 CALM_HUMAN 2 80
SEQRES 1 A 79 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 79 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 79 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 79 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 79 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 79 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 79 THR
SEQRES 1 B 79 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 B 79 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 B 79 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 B 79 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 B 79 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 B 79 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 B 79 THR
SEQRES 1 C 79 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 C 79 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 C 79 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 C 79 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 C 79 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 C 79 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 C 79 THR
SEQRES 1 D 79 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 D 79 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 D 79 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 D 79 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 D 79 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 D 79 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 D 79 THR
HET MG A 100 1
HET MG A 101 1
HET MG A 102 1
HET MG B 100 1
HET MG B 101 1
HET MG C 100 1
HET MG C 101 1
HET MG C 102 1
HET MG D 100 1
HET MG D 101 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG 10(MG 2+)
FORMUL 15 HOH *147(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 GLU A 31 SER A 38 1 8
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 MET A 76 1 12
HELIX 5 5 THR B 5 ASP B 20 1 16
HELIX 6 6 GLU B 31 LEU B 39 1 9
HELIX 7 7 THR B 44 ASP B 56 1 13
HELIX 8 8 PHE B 65 LYS B 77 1 13
HELIX 9 9 THR C 5 ASP C 20 1 16
HELIX 10 10 GLU C 31 LEU C 39 1 9
HELIX 11 11 THR C 44 ASP C 56 1 13
HELIX 12 12 PHE C 65 MET C 76 1 12
HELIX 13 13 THR D 5 ASP D 20 1 16
HELIX 14 14 GLU D 31 LEU D 39 1 9
HELIX 15 15 THR D 44 ASP D 56 1 13
HELIX 16 16 PHE D 65 LYS D 77 1 13
SHEET 1 A 2 THR A 26 THR A 28 0
SHEET 2 A 2 THR A 62 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 THR B 26 THR B 28 0
SHEET 2 B 2 THR B 62 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 C 2 THR C 26 THR C 28 0
SHEET 2 C 2 THR C 62 ASP C 64 -1 O ILE C 63 N ILE C 27
SHEET 1 D 2 THR D 26 THR D 28 0
SHEET 2 D 2 THR D 62 ASP D 64 -1 O ILE D 63 N ILE D 27
LINK OD1 ASP A 20 MG MG A 100 1555 1555 1.98
LINK OD1 ASP A 22 MG MG A 100 1555 1555 2.14
LINK OD1 ASP A 24 MG MG A 100 1555 1555 2.15
LINK O THR A 26 MG MG A 100 1555 1555 2.17
LINK O THR A 62 MG MG A 101 1555 1555 2.04
LINK OG1 THR A 62 MG MG A 101 1555 1555 2.14
LINK OD2 ASP A 64 MG MG A 102 1555 1555 2.09
LINK MG MG A 100 O HOH A 208 1555 1555 2.09
LINK MG MG A 100 O HOH A 224 1555 1555 2.06
LINK MG MG A 101 O HOH A 209 1555 1555 2.08
LINK MG MG A 101 O HOH A 210 1555 1555 2.05
LINK MG MG A 101 O HOH A 211 1555 1555 2.10
LINK MG MG A 101 O HOH A 212 1555 1555 2.06
LINK MG MG A 102 O HOH A 217 1555 1555 2.06
LINK MG MG A 102 OD2 ASP B 64 1555 1555 2.07
LINK MG MG A 102 O HOH B 201 1555 1555 2.03
LINK MG MG A 102 O HOH B 202 1555 1555 2.05
LINK MG MG A 102 O HOH B 212 1555 1555 2.07
LINK OD1 ASP B 20 MG MG B 100 1555 1555 2.09
LINK OD1 ASP B 22 MG MG B 100 1555 1555 2.10
LINK OD1 ASP B 24 MG MG B 100 1555 1555 2.10
LINK O THR B 26 MG MG B 100 1555 1555 2.22
LINK O THR B 62 MG MG B 101 1555 1555 2.15
LINK OG1 THR B 62 MG MG B 101 1555 1555 2.17
LINK MG MG B 100 O HOH B 204 1555 1555 2.07
LINK MG MG B 100 O HOH B 205 1555 1555 2.07
LINK MG MG B 101 O HOH B 207 1555 1555 2.10
LINK MG MG B 101 O HOH B 208 1555 1555 2.08
LINK MG MG B 101 O HOH B 209 1555 1555 2.06
LINK MG MG B 101 O HOH B 217 1555 1555 2.07
LINK OD1 ASP C 20 MG MG C 100 1555 1555 2.02
LINK OD1 ASP C 22 MG MG C 100 1555 1555 2.11
LINK OD1 ASP C 24 MG MG C 100 1555 1555 2.04
LINK O THR C 26 MG MG C 100 1555 1555 2.08
LINK O THR C 62 MG MG C 101 1555 1555 2.09
LINK OG1 THR C 62 MG MG C 101 1555 1555 2.23
LINK OD2 ASP C 64 MG MG C 102 1555 1555 2.02
LINK MG MG C 100 O HOH C 208 1555 1555 2.05
LINK MG MG C 100 O HOH C 209 1555 1555 2.03
LINK MG MG C 101 O HOH C 204 1555 1555 2.10
LINK MG MG C 101 O HOH C 205 1555 1555 2.09
LINK MG MG C 101 O HOH C 206 1555 1555 2.12
LINK MG MG C 101 O HOH C 216 1555 1555 2.09
LINK MG MG C 102 O HOH C 202 1555 1555 2.07
LINK MG MG C 102 O HOH C 203 1555 1555 2.08
LINK MG MG C 102 O HOH C 219 1555 1555 2.08
LINK MG MG C 102 O HOH C 220 1555 1555 2.08
LINK OD1 ASP D 20 MG MG D 100 1555 1555 2.03
LINK OD1 ASP D 22 MG MG D 100 1555 1555 2.08
LINK OD1 ASP D 24 MG MG D 100 1555 1555 2.07
LINK O THR D 26 MG MG D 100 1555 1555 2.13
LINK O THR D 62 MG MG D 101 1555 1555 2.10
LINK OG1 THR D 62 MG MG D 101 1555 1555 2.20
LINK MG MG D 100 O HOH D 201 1555 1555 2.07
LINK MG MG D 100 O HOH D 202 1555 1555 2.09
LINK MG MG D 101 O HOH D 203 1555 1555 2.04
LINK MG MG D 101 O HOH D 204 1555 1555 2.06
LINK MG MG D 101 O HOH D 212 1555 1555 2.08
LINK MG MG D 101 O HOH D 230 1555 1555 2.13
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 HOH A 208 HOH A 224
SITE 1 AC2 5 THR A 62 HOH A 209 HOH A 210 HOH A 211
SITE 2 AC2 5 HOH A 212
SITE 1 AC3 6 ASP A 64 HOH A 217 ASP B 64 HOH B 201
SITE 2 AC3 6 HOH B 202 HOH B 212
SITE 1 AC4 6 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 2 AC4 6 HOH B 204 HOH B 205
SITE 1 AC5 5 THR B 62 HOH B 207 HOH B 208 HOH B 209
SITE 2 AC5 5 HOH B 217
SITE 1 AC6 6 ASP C 20 ASP C 22 ASP C 24 THR C 26
SITE 2 AC6 6 HOH C 208 HOH C 209
SITE 1 AC7 5 THR C 62 HOH C 204 HOH C 205 HOH C 206
SITE 2 AC7 5 HOH C 216
SITE 1 AC8 6 ASP C 64 HOH C 202 HOH C 203 HOH C 219
SITE 2 AC8 6 HOH C 220 ASP D 64
SITE 1 AC9 6 ASP D 20 ASP D 22 ASP D 24 THR D 26
SITE 2 AC9 6 HOH D 201 HOH D 202
SITE 1 BC1 5 THR D 62 HOH D 203 HOH D 204 HOH D 212
SITE 2 BC1 5 HOH D 230
CRYST1 34.435 43.040 53.689 68.44 88.62 79.44 P 1 4
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 0.029040 -0.005414 0.001399 0.00000
SCALE2 0.000000 0.023634 -0.009396 0.00000
SCALE3 0.000000 0.000000 0.020049 0.00000
(ATOM LINES ARE NOT SHOWN.)
END