HEADER CALCIUM BINDING PROTEIN 22-JUL-15 5CRD
TITLE WILD-TYPE HUMAN SKELETAL CALSEQUESTRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALSEQUESTRIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 35-396;
COMPND 5 SYNONYM: CALMITINE,CALSEQUESTRIN,SKELETAL MUSCLE ISOFORM;
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: CASQ1, CASQ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALCIUM BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.LEWIS,L.A.RONISH,C.KANG
REVDAT 4 27-SEP-23 5CRD 1 JRNL REMARK
REVDAT 3 09-DEC-15 5CRD 1 JRNL
REVDAT 2 28-OCT-15 5CRD 1 JRNL
REVDAT 1 07-OCT-15 5CRD 0
JRNL AUTH K.M.LEWIS,L.A.RONISH,E.RIOS,C.KANG
JRNL TITL CHARACTERIZATION OF TWO HUMAN SKELETAL CALSEQUESTRIN MUTANTS
JRNL TITL 2 IMPLICATED IN MALIGNANT HYPERTHERMIA AND VACUOLAR AGGREGATE
JRNL TITL 3 MYOPATHY.
JRNL REF J.BIOL.CHEM. V. 290 28665 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 26416891
JRNL DOI 10.1074/JBC.M115.686261
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10-2152_1692
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 28775
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.420
REMARK 3 FREE R VALUE TEST SET COUNT : 1560
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 43.9035 - 4.6243 1.00 2622 150 0.1741 0.1806
REMARK 3 2 4.6243 - 3.6710 1.00 2524 145 0.1472 0.1772
REMARK 3 3 3.6710 - 3.2071 1.00 2516 144 0.1753 0.2016
REMARK 3 4 3.2071 - 2.9140 1.00 2470 142 0.1964 0.2117
REMARK 3 5 2.9140 - 2.7051 0.99 2437 139 0.2119 0.2689
REMARK 3 6 2.7051 - 2.5457 0.99 2457 141 0.2096 0.2575
REMARK 3 7 2.5457 - 2.4182 0.99 2455 141 0.2281 0.2818
REMARK 3 8 2.4182 - 2.3129 0.99 2436 139 0.2230 0.2607
REMARK 3 9 2.3129 - 2.2239 0.99 2450 141 0.2452 0.3022
REMARK 3 10 2.2239 - 2.1472 0.99 2427 139 0.2454 0.2654
REMARK 3 11 2.1472 - 2.0800 0.99 2421 139 0.2432 0.2695
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.007 2922
REMARK 3 ANGLE : 0.503 3960
REMARK 3 CHIRALITY : 0.043 429
REMARK 3 PLANARITY : 0.003 528
REMARK 3 DIHEDRAL : 15.081 1748
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 5CRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28782
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 43.894
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX 1.9-1692
REMARK 200 STARTING MODEL: 3TRQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MOPS, 27.5 % (V/V) 2-METHYL-2,4
REMARK 280 -PENTANEDIOL, 0.2 M NACL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.12100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.12100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.58500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.56600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.58500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.56600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.12100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.58500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.56600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.12100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.58500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.56600
REMARK 290 SMTRY3 8 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: 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 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: 6900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -55.12100
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 GLN A 1
REMARK 465 GLU A 350
REMARK 465 ILE A 351
REMARK 465 ASN A 352
REMARK 465 THR A 353
REMARK 465 GLU A 354
REMARK 465 ASP A 355
REMARK 465 ASP A 356
REMARK 465 ASP A 357
REMARK 465 ASP A 358
REMARK 465 ASP A 359
REMARK 465 ASP A 360
REMARK 465 ASP A 361
REMARK 465 ASP A 362
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 2 CG CD OE1 OE2
REMARK 470 GLU A 31 CG CD OE1 OE2
REMARK 470 LYS A 45 CG CD CE NZ
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 GLU A 330 CG CD OE1 OE2
REMARK 470 GLU A 348 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O HOH A 632 O HOH A 687 2.10
REMARK 500 O HOH A 502 O HOH A 665 2.11
REMARK 500 OE1 GLU A 117 O HOH A 501 2.11
REMARK 500 O LYS A 21 O HOH A 502 2.13
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 GLU A 131 -50.47 -127.32
REMARK 500 SER A 237 25.81 -146.43
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 17 OD1
REMARK 620 2 VAL A 18 O 114.6
REMARK 620 3 LEU A 74 O 121.1 83.0
REMARK 620 4 ASP A 80 OD2 118.2 77.5 120.5
REMARK 620 5 HOH A 555 O 66.5 177.6 94.6 104.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 189 O
REMARK 620 2 THR A 189 OG1 70.8
REMARK 620 3 HOH A 630 O 79.4 129.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 199 OE1
REMARK 620 2 GLU A 199 OE2 53.3
REMARK 620 3 THR A 229 OG1 135.7 82.5
REMARK 620 4 THR A 277 O 130.7 171.4 93.5
REMARK 620 5 THR A 277 OG1 81.9 98.5 110.0 75.8
REMARK 620 6 HOH A 693 O 92.7 93.4 87.3 93.9 160.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 210 O
REMARK 620 2 PRO A 212 O 83.4
REMARK 620 3 GLU A 217 OE1 94.1 102.3
REMARK 620 4 GLU A 217 OE2 139.6 117.8 49.9
REMARK 620 5 HOH A 503 O 164.6 81.5 91.8 52.4
REMARK 620 6 HOH A 678 O 101.1 71.3 162.5 117.8 71.3
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 CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 406
DBREF 5CRD A 1 362 UNP P31415 CASQ1_HUMAN 35 396
SEQRES 1 A 362 GLN GLU GLY LEU ASP PHE PRO GLU TYR ASP GLY VAL ASP
SEQRES 2 A 362 ARG VAL ILE ASN VAL ASN ALA LYS ASN TYR LYS ASN VAL
SEQRES 3 A 362 PHE LYS LYS TYR GLU VAL LEU ALA LEU LEU TYR HIS GLU
SEQRES 4 A 362 PRO PRO GLU ASP ASP LYS ALA SER GLN ARG GLN PHE GLU
SEQRES 5 A 362 MET GLU GLU LEU ILE LEU GLU LEU ALA ALA GLN VAL LEU
SEQRES 6 A 362 GLU ASP LYS GLY VAL GLY PHE GLY LEU VAL ASP SER GLU
SEQRES 7 A 362 LYS ASP ALA ALA VAL ALA LYS LYS LEU GLY LEU THR GLU
SEQRES 8 A 362 VAL ASP SER MET TYR VAL PHE LYS GLY ASP GLU VAL ILE
SEQRES 9 A 362 GLU TYR ASP GLY GLU PHE SER ALA ASP THR ILE VAL GLU
SEQRES 10 A 362 PHE LEU LEU ASP VAL LEU GLU ASP PRO VAL GLU LEU ILE
SEQRES 11 A 362 GLU GLY GLU ARG GLU LEU GLN ALA PHE GLU ASN ILE GLU
SEQRES 12 A 362 ASP GLU ILE LYS LEU ILE GLY TYR PHE LYS SER LYS ASP
SEQRES 13 A 362 SER GLU HIS TYR LYS ALA PHE GLU ASP ALA ALA GLU GLU
SEQRES 14 A 362 PHE HIS PRO TYR ILE PRO PHE PHE ALA THR PHE ASP SER
SEQRES 15 A 362 LYS VAL ALA LYS LYS LEU THR LEU LYS LEU ASN GLU ILE
SEQRES 16 A 362 ASP PHE TYR GLU ALA PHE MET GLU GLU PRO VAL THR ILE
SEQRES 17 A 362 PRO ASP LYS PRO ASN SER GLU GLU GLU ILE VAL ASN PHE
SEQRES 18 A 362 VAL GLU GLU HIS ARG ARG SER THR LEU ARG LYS LEU LYS
SEQRES 19 A 362 PRO GLU SER MET TYR GLU THR TRP GLU ASP ASP MET ASP
SEQRES 20 A 362 GLY ILE HIS ILE VAL ALA PHE ALA GLU GLU ALA ASP PRO
SEQRES 21 A 362 ASP GLY PHE GLU PHE LEU GLU THR LEU LYS ALA VAL ALA
SEQRES 22 A 362 GLN ASP ASN THR GLU ASN PRO ASP LEU SER ILE ILE TRP
SEQRES 23 A 362 ILE ASP PRO ASP ASP PHE PRO LEU LEU VAL PRO TYR TRP
SEQRES 24 A 362 GLU LYS THR PHE ASP ILE ASP LEU SER ALA PRO GLN ILE
SEQRES 25 A 362 GLY VAL VAL ASN VAL THR ASP ALA ASP SER VAL TRP MET
SEQRES 26 A 362 GLU MET ASP ASP GLU GLU ASP LEU PRO SER ALA GLU GLU
SEQRES 27 A 362 LEU GLU ASP TRP LEU GLU ASP VAL LEU GLU GLY GLU ILE
SEQRES 28 A 362 ASN THR GLU ASP ASP ASP ASP ASP ASP ASP ASP
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET CA A 404 1
HET MPD A 405 8
HET MPD A 406 8
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 CA 4(CA 2+)
FORMUL 6 MPD 2(C6 H14 O2)
FORMUL 8 HOH *233(H2 O)
HELIX 1 AA1 ASN A 22 TYR A 30 1 9
HELIX 2 AA2 ASP A 44 LEU A 65 1 22
HELIX 3 AA3 ASP A 80 GLY A 88 1 9
HELIX 4 AA4 SER A 111 GLU A 124 1 14
HELIX 5 AA5 GLY A 132 ASN A 141 1 10
HELIX 6 AA6 SER A 157 HIS A 171 1 15
HELIX 7 AA7 ASP A 181 LEU A 188 1 8
HELIX 8 AA8 SER A 214 HIS A 225 1 12
HELIX 9 AA9 LYS A 234 GLU A 236 5 3
HELIX 10 AB1 SER A 237 ASP A 244 1 8
HELIX 11 AB2 ASP A 259 ASN A 276 1 18
HELIX 12 AB3 ASP A 288 PHE A 292 5 5
HELIX 13 AB4 LEU A 295 ASP A 304 1 10
HELIX 14 AB5 SER A 335 GLY A 349 1 15
SHEET 1 AA1 5 ILE A 16 ASN A 17 0
SHEET 2 AA1 5 VAL A 70 ASP A 76 1 O PHE A 72 N ILE A 16
SHEET 3 AA1 5 VAL A 32 HIS A 38 1 N ALA A 34 O GLY A 71
SHEET 4 AA1 5 SER A 94 LYS A 99 -1 O TYR A 96 N LEU A 35
SHEET 5 AA1 5 GLU A 102 TYR A 106 -1 O ILE A 104 N VAL A 97
SHEET 1 AA2 5 VAL A 127 LEU A 129 0
SHEET 2 AA2 5 PHE A 176 THR A 179 1 O PHE A 176 N GLU A 128
SHEET 3 AA2 5 LYS A 147 TYR A 151 1 N LEU A 148 O PHE A 177
SHEET 4 AA2 5 ILE A 195 TYR A 198 -1 O TYR A 198 N LYS A 147
SHEET 5 AA2 5 VAL A 206 THR A 207 -1 O VAL A 206 N PHE A 197
SHEET 1 AA3 5 LEU A 230 LYS A 232 0
SHEET 2 AA3 5 ILE A 284 ILE A 287 1 O TRP A 286 N ARG A 231
SHEET 3 AA3 5 ILE A 249 PHE A 254 1 N ALA A 253 O ILE A 287
SHEET 4 AA3 5 GLN A 311 ASN A 316 -1 O VAL A 315 N HIS A 250
SHEET 5 AA3 5 SER A 322 TRP A 324 -1 O VAL A 323 N VAL A 314
LINK OD1 ASN A 17 CA CA A 401 1555 1555 2.42
LINK O VAL A 18 CA CA A 401 1555 1555 2.40
LINK O LEU A 74 CA CA A 401 1555 1555 2.57
LINK OD2 ASP A 80 CA CA A 401 1555 1555 2.38
LINK O THR A 189 CA CA A 404 1555 1555 2.33
LINK OG1 THR A 189 CA CA A 404 1555 1555 2.41
LINK OE1 GLU A 199 CA CA A 402 1555 1555 2.49
LINK OE2 GLU A 199 CA CA A 402 1555 1555 2.40
LINK O ASP A 210 CA CA A 403 1555 1555 2.25
LINK O PRO A 212 CA CA A 403 1555 1555 2.50
LINK OE1 GLU A 217 CA CA A 403 1555 1555 2.42
LINK OE2 GLU A 217 CA CA A 403 1555 1555 2.74
LINK OG1 THR A 229 CA CA A 402 1555 1555 2.46
LINK O THR A 277 CA CA A 402 1555 1555 2.53
LINK OG1 THR A 277 CA CA A 402 1555 1555 2.30
LINK CA CA A 401 O HOH A 555 1555 1555 2.45
LINK CA CA A 402 O HOH A 693 1555 1555 2.26
LINK CA CA A 403 O HOH A 503 1555 1555 2.13
LINK CA CA A 403 O HOH A 678 1555 1555 2.83
LINK CA CA A 404 O HOH A 630 1555 1555 2.48
CISPEP 1 HIS A 171 PRO A 172 0 -2.06
CISPEP 2 LYS A 211 PRO A 212 0 -3.24
SITE 1 AC1 5 ASN A 17 VAL A 18 LEU A 74 ASP A 80
SITE 2 AC1 5 HOH A 555
SITE 1 AC2 4 GLU A 199 THR A 229 THR A 277 HOH A 693
SITE 1 AC3 5 ASP A 210 PRO A 212 GLU A 217 HOH A 503
SITE 2 AC3 5 HOH A 678
SITE 1 AC4 2 THR A 189 HOH A 630
SITE 1 AC5 7 PRO A 7 GLU A 8 GLN A 63 LEU A 294
SITE 2 AC5 7 LEU A 295 HOH A 571 HOH A 668
SITE 1 AC6 4 PHE A 6 TRP A 242 TYR A 298 TRP A 299
CRYST1 59.170 145.132 110.242 90.00 90.00 90.00 C 2 2 21 8
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 0.016900 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006890 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009071 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
