HEADER CALCIUM BINDING PROTEIN/PROTEIN BINDING 17-APR-14 4Q5U
TITLE STRUCTURE OF CALMODULIN BOUND TO ITS RECOGNITION SITE FROM CALCINEURIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT
COMPND 8 ALPHA ISOFORM;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: CALMODULIN-BINDING DOMAIN (UNP RESIDUES 391-414);
COMPND 11 SYNONYM: CAM-PRP CATALYTIC SUBUNIT, CALMODULIN-DEPENDENT CALCINEURIN
COMPND 12 A SUBUNIT ALPHA ISOFORM;
COMPND 13 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: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PETCAMI;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606
KEYWDS EF HAND, CALCIUM BINDING PROTEIN-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.GUO,T.B.DUNLAP,T.P.CREAMER,C.W.VANDER KOOI
REVDAT 3 20-SEP-23 4Q5U 1 REMARK LINK
REVDAT 2 01-OCT-14 4Q5U 1 JRNL
REVDAT 1 03-SEP-14 4Q5U 0
JRNL AUTH T.B.DUNLAP,H.F.GUO,E.C.COOK,E.HOLBROOK,J.RUMI-MASANTE,
JRNL AUTH 2 T.E.LESTER,C.L.COLBERT,C.W.VANDER KOOI,T.P.CREAMER
JRNL TITL STOICHIOMETRY OF THE CALCINEURIN REGULATORY
JRNL TITL 2 DOMAIN-CALMODULIN COMPLEX.
JRNL REF BIOCHEMISTRY V. 53 5779 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 25144868
JRNL DOI 10.1021/BI5004734
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 15779
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 801
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 19.1211 - 3.5364 1.00 2871 152 0.1914 0.2354
REMARK 3 2 3.5364 - 2.8098 1.00 2749 151 0.2281 0.2295
REMARK 3 3 2.8098 - 2.4555 1.00 2714 142 0.2314 0.2724
REMARK 3 4 2.4555 - 2.2313 0.93 2531 145 0.2364 0.2608
REMARK 3 5 2.2313 - 2.0716 0.82 2211 111 0.2472 0.2966
REMARK 3 6 2.0716 - 1.9500 0.70 1902 100 0.2711 0.3420
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.040
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 : 0.006 1352
REMARK 3 ANGLE : 0.972 1810
REMARK 3 CHIRALITY : 0.070 200
REMARK 3 PLANARITY : 0.004 244
REMARK 3 DIHEDRAL : 14.430 524
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:73)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7736 10.2143 6.8774
REMARK 3 T TENSOR
REMARK 3 T11: 0.4581 T22: 0.4150
REMARK 3 T33: 0.4407 T12: 0.0503
REMARK 3 T13: -0.0565 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 3.8011 L22: 8.3605
REMARK 3 L33: 4.4845 L12: -0.6887
REMARK 3 L13: -2.5826 L23: 2.7268
REMARK 3 S TENSOR
REMARK 3 S11: -0.1732 S12: -0.0153 S13: -0.2597
REMARK 3 S21: -0.1124 S22: -0.0515 S23: 0.0840
REMARK 3 S31: 0.4012 S32: 0.0583 S33: 0.3139
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 74:97)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2153 22.8885 -4.3999
REMARK 3 T TENSOR
REMARK 3 T11: 0.5042 T22: 0.4474
REMARK 3 T33: 0.5069 T12: 0.0595
REMARK 3 T13: -0.1119 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 5.6530 L22: 2.7600
REMARK 3 L33: 9.3238 L12: 0.0406
REMARK 3 L13: -0.2818 L23: -0.3199
REMARK 3 S TENSOR
REMARK 3 S11: 0.2090 S12: 0.2182 S13: -0.2068
REMARK 3 S21: 0.0644 S22: -0.3618 S23: 0.1089
REMARK 3 S31: 0.9835 S32: -0.3170 S33: 0.1975
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 98:147)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2582 28.1702 -1.9114
REMARK 3 T TENSOR
REMARK 3 T11: 0.3862 T22: 0.7742
REMARK 3 T33: 0.9206 T12: -0.0185
REMARK 3 T13: -0.0914 T23: 0.1001
REMARK 3 L TENSOR
REMARK 3 L11: 4.4794 L22: 4.9089
REMARK 3 L33: 3.3430 L12: 0.1059
REMARK 3 L13: -0.3538 L23: -3.9252
REMARK 3 S TENSOR
REMARK 3 S11: -0.0861 S12: -0.1467 S13: 0.5988
REMARK 3 S21: 0.2157 S22: -0.8049 S23: -1.3760
REMARK 3 S31: -0.4058 S32: 1.7490 S33: 0.7322
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN C AND RESID 391:414)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8319 17.7501 -0.2849
REMARK 3 T TENSOR
REMARK 3 T11: 0.4668 T22: 0.4221
REMARK 3 T33: 0.4269 T12: 0.0160
REMARK 3 T13: -0.1025 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 9.9890 L22: 7.8130
REMARK 3 L33: 7.1995 L12: -2.2740
REMARK 3 L13: -1.8630 L23: 1.0818
REMARK 3 S TENSOR
REMARK 3 S11: 0.0810 S12: 0.4257 S13: -0.0722
REMARK 3 S21: -0.3109 S22: -0.2869 S23: -0.1353
REMARK 3 S31: 0.2894 S32: 0.0088 S33: 0.0776
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 4Q5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15779
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 19.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.37500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2W73
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3:1 10 MG/ML PROTEIN TO MOTHER LIQUOR
REMARK 280 (24% PEG1000, 20% GLYCEROL), FINAL VOLUME 200 NL, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 19.72400
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 19.72400
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 52.74950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.51650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.74950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.51650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.72400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.74950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.51650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 19.72400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.74950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.51650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 340 LIES ON A SPECIAL POSITION.
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 MET A 0
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 LYS A 148
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 LYS A 115 69.26 -116.33
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 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 72.7
REMARK 620 3 ASP A 24 OD1 83.8 79.0
REMARK 620 4 THR A 26 O 83.7 153.6 87.0
REMARK 620 5 GLU A 31 OE2 92.1 69.2 147.6 124.6
REMARK 620 6 GLU A 31 OE1 107.9 122.9 157.1 75.2 53.7
REMARK 620 7 HOH A 370 O 162.1 90.8 86.3 110.6 88.3 86.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 69.5
REMARK 620 3 ASN A 60 OD1 86.8 80.1
REMARK 620 4 THR A 62 O 83.0 147.7 81.9
REMARK 620 5 GLU A 67 OE2 96.9 115.0 164.9 84.1
REMARK 620 6 GLU A 67 OE1 76.5 64.8 144.5 125.7 50.3
REMARK 620 7 HOH A 339 O 141.5 72.8 93.9 135.2 92.2 81.2
REMARK 620 8 HOH A 369 O 148.4 125.1 70.6 72.3 99.8 134.2 64.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 74.7
REMARK 620 3 ASN A 97 OD1 87.3 75.0
REMARK 620 4 TYR A 99 O 94.9 157.6 84.8
REMARK 620 5 GLU A 104 OE1 93.9 74.8 148.3 126.4
REMARK 620 6 GLU A 104 OE2 101.2 126.9 157.8 74.1 52.3
REMARK 620 7 HOH A 341 O 161.7 87.2 85.4 101.1 83.8 91.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 81.3
REMARK 620 3 ASP A 133 OD1 85.0 80.5
REMARK 620 4 GLN A 135 O 85.4 155.0 77.3
REMARK 620 5 GLU A 140 OE2 94.2 74.8 155.1 127.5
REMARK 620 6 GLU A 140 OE1 115.9 126.7 146.2 78.2 55.0
REMARK 620 7 HOH A 327 O 158.4 83.2 77.7 103.0 96.2 85.4
REMARK 620 N 1 2 3 4 5 6
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204
DBREF 4Q5U A 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 4Q5U C 391 414 UNP Q08209 PP2BA_HUMAN 391 414
SEQRES 1 A 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 149 GLN MET MET THR ALA LYS
SEQRES 1 C 24 ALA ARG LYS GLU VAL ILE ARG ASN LYS ILE ARG ALA ILE
SEQRES 2 C 24 GLY LYS MET ALA ARG VAL PHE SER VAL LEU ARG
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA A 204 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *100(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 ALA A 73 1 9
HELIX 5 5 LYS A 77 ASP A 93 1 17
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 THR A 146 1 9
HELIX 9 9 ARG C 392 ARG C 414 1 23
SHEET 1 A 2 THR A 26 ILE A 27 0
SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 TYR A 99 ILE A 100 0
SHEET 2 B 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 201 1555 1555 2.29
LINK OD1 ASP A 22 CA CA A 201 1555 1555 2.35
LINK OD1 ASP A 24 CA CA A 201 1555 1555 2.27
LINK O THR A 26 CA CA A 201 1555 1555 2.30
LINK OE2 GLU A 31 CA CA A 201 1555 1555 2.44
LINK OE1 GLU A 31 CA CA A 201 1555 1555 2.45
LINK OD1 ASP A 56 CA CA A 204 1555 1555 2.35
LINK OD1 ASP A 58 CA CA A 204 1555 1555 2.55
LINK OD1 ASN A 60 CA CA A 204 1555 1555 2.35
LINK O THR A 62 CA CA A 204 1555 1555 2.35
LINK OE2 GLU A 67 CA CA A 204 1555 1555 2.49
LINK OE1 GLU A 67 CA CA A 204 1555 1555 2.66
LINK OD1 ASP A 93 CA CA A 202 1555 1555 2.37
LINK OD1 ASP A 95 CA CA A 202 1555 1555 2.36
LINK OD1 ASN A 97 CA CA A 202 1555 1555 2.37
LINK O TYR A 99 CA CA A 202 1555 1555 2.21
LINK OE1 GLU A 104 CA CA A 202 1555 1555 2.45
LINK OE2 GLU A 104 CA CA A 202 1555 1555 2.53
LINK OD1 ASP A 129 CA CA A 203 1555 1555 2.39
LINK OD1 ASP A 131 CA CA A 203 1555 1555 2.30
LINK OD1 ASP A 133 CA CA A 203 1555 1555 2.37
LINK O GLN A 135 CA CA A 203 1555 1555 2.27
LINK OE2 GLU A 140 CA CA A 203 1555 1555 2.33
LINK OE1 GLU A 140 CA CA A 203 1555 1555 2.43
LINK CA CA A 201 O HOH A 370 1555 1555 2.19
LINK CA CA A 202 O HOH A 341 1555 1555 2.46
LINK CA CA A 203 O HOH A 327 1555 1555 2.35
LINK CA CA A 204 O HOH A 339 1555 1555 2.40
LINK CA CA A 204 O HOH A 369 1555 1555 2.52
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A 370
SITE 1 AC2 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC2 6 GLU A 104 HOH A 341
SITE 1 AC3 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC3 6 GLU A 140 HOH A 327
SITE 1 AC4 7 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC4 7 GLU A 67 HOH A 339 HOH A 369
CRYST1 105.499 111.033 39.448 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 0.009479 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025350 0.00000
(ATOM LINES ARE NOT SHOWN.)
END