HEADER CALCIUM BINDING PROTEIN 01-MAY-18 6DAH
TITLE 2.5 ANGSTROM CRYSTAL STRUCTURE OF THE N97S CAM MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALMODULIN, MUTANT, CALCIUM BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WANG,F.VAN PETEGEM
REVDAT 5 04-OCT-23 6DAH 1 LINK
REVDAT 4 17-APR-19 6DAH 1 REMARK
REVDAT 3 21-NOV-18 6DAH 1 JRNL
REVDAT 2 31-OCT-18 6DAH 1 JRNL
REVDAT 1 17-OCT-18 6DAH 0
JRNL AUTH K.WANG,C.HOLT,J.LU,M.BROHUS,K.T.LARSEN,M.T.OVERGAARD,
JRNL AUTH 2 R.WIMMER,F.VAN PETEGEM
JRNL TITL ARRHYTHMIA MUTATIONS IN CALMODULIN CAUSE CONFORMATIONAL
JRNL TITL 2 CHANGES THAT AFFECT INTERACTIONS WITH THE CARDIAC
JRNL TITL 3 VOLTAGE-GATED CALCIUM CHANNEL.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 10556 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30348784
JRNL DOI 10.1073/PNAS.1808733115
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 43334
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 2159
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 47.2154 - 6.1653 0.95 2734 145 0.1920 0.1930
REMARK 3 2 6.1653 - 4.8952 0.94 2709 138 0.2356 0.2625
REMARK 3 3 4.8952 - 4.2769 0.97 2777 146 0.1753 0.2324
REMARK 3 4 4.2769 - 3.8861 0.95 2749 140 0.1798 0.2918
REMARK 3 5 3.8861 - 3.6076 0.97 2789 150 0.1992 0.2701
REMARK 3 6 3.6076 - 3.3950 0.96 2765 140 0.2243 0.2989
REMARK 3 7 3.3950 - 3.2250 0.97 2801 150 0.2354 0.3636
REMARK 3 8 3.2250 - 3.0847 0.94 2702 139 0.2550 0.3609
REMARK 3 9 3.0847 - 2.9659 0.95 2733 144 0.2622 0.3567
REMARK 3 10 2.9659 - 2.8636 0.96 2778 144 0.2613 0.3409
REMARK 3 11 2.8636 - 2.7741 0.96 2739 149 0.2458 0.3047
REMARK 3 12 2.7741 - 2.6948 0.96 2776 147 0.2539 0.2684
REMARK 3 13 2.6948 - 2.6238 0.96 2761 147 0.2571 0.3406
REMARK 3 14 2.6238 - 2.5598 0.95 2726 139 0.2718 0.3093
REMARK 3 15 2.5598 - 2.5016 0.91 2636 141 0.2839 0.3630
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.800
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.81
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESID -2 THROUGH 78 ) OR (RESID 501
REMARK 3 THROUGH 502))
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5128 -27.4176 3.0680
REMARK 3 T TENSOR
REMARK 3 T11: 0.2112 T22: 0.2941
REMARK 3 T33: 0.3099 T12: 0.0314
REMARK 3 T13: -0.0020 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 2.0178 L22: 6.4495
REMARK 3 L33: 3.3507 L12: 1.9585
REMARK 3 L13: -0.0808 L23: 1.7383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0380 S12: -0.0878 S13: -0.0504
REMARK 3 S21: 0.1184 S22: 0.1989 S23: 0.1730
REMARK 3 S31: -0.0541 S32: 0.2989 S33: -0.2528
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 79 THROUGH 145 ) OR (RESID 503
REMARK 3 THROUGH 504))
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1597 -28.1799 14.9468
REMARK 3 T TENSOR
REMARK 3 T11: 0.3758 T22: 0.3952
REMARK 3 T33: 0.4928 T12: 0.0627
REMARK 3 T13: -0.0665 T23: -0.1241
REMARK 3 L TENSOR
REMARK 3 L11: 5.4652 L22: 3.1540
REMARK 3 L33: 5.7427 L12: -0.4062
REMARK 3 L13: -2.9188 L23: 0.5464
REMARK 3 S TENSOR
REMARK 3 S11: -0.0375 S12: -0.4572 S13: 0.9525
REMARK 3 S21: 0.2242 S22: 0.3865 S23: -0.4634
REMARK 3 S31: -0.1176 S32: 0.2406 S33: -0.3320
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND ((RESID 12 THROUGH 78 ) OR (RESID 501
REMARK 3 THROUGH 502))
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3493 -19.5735 31.6302
REMARK 3 T TENSOR
REMARK 3 T11: 0.2901 T22: 0.4129
REMARK 3 T33: 0.3528 T12: 0.0436
REMARK 3 T13: -0.0037 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 5.0633 L22: 7.8281
REMARK 3 L33: 3.0152 L12: 1.0280
REMARK 3 L13: -0.9194 L23: 0.3480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0526 S12: -0.0850 S13: 0.2303
REMARK 3 S21: -0.0047 S22: -0.0004 S23: -0.6939
REMARK 3 S31: -0.3600 S32: -0.2048 S33: -0.0649
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND ((RESID 79 THROUGH 146 ) OR (RESID 503
REMARK 3 THROUGH 504))
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6542 -22.5511 43.0968
REMARK 3 T TENSOR
REMARK 3 T11: 0.3955 T22: 0.6105
REMARK 3 T33: 0.7296 T12: 0.0692
REMARK 3 T13: 0.0772 T23: 0.0876
REMARK 3 L TENSOR
REMARK 3 L11: 7.1709 L22: 4.8263
REMARK 3 L33: 4.8899 L12: 0.8132
REMARK 3 L13: -3.3860 L23: 0.1817
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: -0.2107 S13: 1.1187
REMARK 3 S21: 0.4592 S22: 0.6037 S23: 1.2041
REMARK 3 S31: -0.0917 S32: -0.0436 S33: -0.5753
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND ((RESID -2 THROUGH 78 ) OR (RESID 501
REMARK 3 THROUGH 502))
REMARK 3 ORIGIN FOR THE GROUP (A): 54.2759 5.8390 4.5662
REMARK 3 T TENSOR
REMARK 3 T11: 0.4439 T22: 0.3746
REMARK 3 T33: 0.6696 T12: 0.0052
REMARK 3 T13: -0.0227 T23: 0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 2.2840 L22: 1.7818
REMARK 3 L33: 1.7484 L12: -0.3129
REMARK 3 L13: 1.0141 L23: -1.4654
REMARK 3 S TENSOR
REMARK 3 S11: 0.1552 S12: -0.1144 S13: -0.4365
REMARK 3 S21: 0.1168 S22: -0.3257 S23: -0.6992
REMARK 3 S31: 0.2854 S32: 0.3255 S33: 0.2087
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND ((RESID 79 THROUGH 146 ) OR (RESID 503
REMARK 3 THROUGH 504))
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9945 0.1313 -6.1178
REMARK 3 T TENSOR
REMARK 3 T11: 0.3498 T22: 0.2707
REMARK 3 T33: 0.3925 T12: -0.0453
REMARK 3 T13: 0.0107 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 2.9827 L22: 5.8991
REMARK 3 L33: 4.9125 L12: 1.7692
REMARK 3 L13: -1.3345 L23: -2.3507
REMARK 3 S TENSOR
REMARK 3 S11: -0.2150 S12: 0.1787 S13: 0.2419
REMARK 3 S21: -0.4233 S22: 0.2258 S23: 0.6041
REMARK 3 S31: 0.4774 S32: -0.3899 S33: -0.0386
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'D' AND ((RESID -2 THROUGH 78 ) OR (RESID 501
REMARK 3 THROUGH 502))
REMARK 3 ORIGIN FOR THE GROUP (A): 53.8185 7.5897 31.1353
REMARK 3 T TENSOR
REMARK 3 T11: 0.3197 T22: 0.4119
REMARK 3 T33: 0.3428 T12: 0.0594
REMARK 3 T13: -0.0098 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 4.0351 L22: 3.8577
REMARK 3 L33: 2.4885 L12: -0.5313
REMARK 3 L13: 1.1683 L23: -0.0973
REMARK 3 S TENSOR
REMARK 3 S11: 0.0990 S12: 0.2611 S13: -0.7459
REMARK 3 S21: 0.0334 S22: -0.0392 S23: 0.1176
REMARK 3 S31: 0.1172 S32: 0.3204 S33: -0.0607
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'D' AND ((RESID 79 THROUGH 144 ) OR (RESID 503
REMARK 3 THROUGH 504))
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2795 3.9329 20.5369
REMARK 3 T TENSOR
REMARK 3 T11: 0.3649 T22: 0.3863
REMARK 3 T33: 0.3821 T12: -0.0867
REMARK 3 T13: 0.1076 T23: -0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 3.5119 L22: 2.5750
REMARK 3 L33: 4.1124 L12: 1.0693
REMARK 3 L13: 2.1077 L23: -1.7569
REMARK 3 S TENSOR
REMARK 3 S11: -0.0687 S12: -0.0632 S13: -0.4886
REMARK 3 S21: -0.1840 S22: 0.2667 S23: -0.2119
REMARK 3 S31: 0.6241 S32: -0.4903 S33: -0.1931
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 6DAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43340
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 47.207
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 1.810
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
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 : 2.430
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 1CLL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1 M BIS-TRIS, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 47.20700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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. (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 THR A 146
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 GLY B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 LEU B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 GLU B 7
REMARK 465 GLN B 8
REMARK 465 ILE B 9
REMARK 465 ALA B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 147
REMARK 465 LYS B 148
REMARK 465 ALA C 147
REMARK 465 LYS C 148
REMARK 465 MET D 145
REMARK 465 THR D 146
REMARK 465 ALA D 147
REMARK 465 LYS D 148
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 7 CG CD OE1 OE2
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 GLU A 14 CG CD OE1 OE2
REMARK 470 SER A 17 OG
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 SER A 38 OG
REMARK 470 GLN A 41 CG CD OE1 NE2
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 LEU A 112 CG CD1 CD2
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 ASP A 122 CG OD1 OD2
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 ARG A 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 MET A 144 CG SD CE
REMARK 470 MET A 145 CG SD CE
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 GLU B 14 CG CD OE1 OE2
REMARK 470 LEU B 18 CG CD1 CD2
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 SER B 38 OG
REMARK 470 LEU B 39 CG CD1 CD2
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 LEU B 112 CG CD1 CD2
REMARK 470 GLU B 114 CG CD OE1 OE2
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 LEU B 116 CG CD1 CD2
REMARK 470 THR B 117 OG1 CG2
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 ARG B 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 ILE B 130 CG1 CG2 CD1
REMARK 470 ASP B 131 CG OD1 OD2
REMARK 470 GLN B 135 CG CD OE1 NE2
REMARK 470 GLU B 139 CG CD OE1 OE2
REMARK 470 GLN B 143 CG CD OE1 NE2
REMARK 470 GLU C 6 CG CD OE1 OE2
REMARK 470 GLU C 7 CG CD OE1 OE2
REMARK 470 LYS C 30 CG CD CE NZ
REMARK 470 ASN C 53 CG OD1 ND2
REMARK 470 ARG C 74 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 90 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 114 CG CD OE1 OE2
REMARK 470 LYS C 115 CG CD CE NZ
REMARK 470 GLU C 120 CG CD OE1 OE2
REMARK 470 GLU C 123 CG CD OE1 OE2
REMARK 470 GLU C 127 CG CD OE1 OE2
REMARK 470 GLN C 143 CG CD OE1 NE2
REMARK 470 GLU D 7 CG CD OE1 OE2
REMARK 470 ILE D 9 CG1 CG2 CD1
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 LYS D 13 CG CD CE NZ
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 GLN D 41 CG CD OE1 NE2
REMARK 470 GLN D 49 CG CD OE1 NE2
REMARK 470 LYS D 77 CG CD CE NZ
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 ARG D 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 GLU D 114 CG CD OE1 OE2
REMARK 470 LYS D 115 CG CD CE NZ
REMARK 470 GLU D 123 CG CD OE1 OE2
REMARK 470 GLU D 127 CG CD OE1 OE2
REMARK 470 GLU D 139 CG CD OE1 OE2
REMARK 470 GLN D 143 CG CD OE1 NE2
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 GLN A 3 38.37 -85.08
REMARK 500 ASN A 42 85.11 -160.70
REMARK 500 ILE A 130 -20.87 -140.41
REMARK 500 GLN A 143 71.68 -68.92
REMARK 500 ASN B 42 73.87 -151.65
REMARK 500 ASP B 93 73.92 -66.22
REMARK 500 ASP B 95 -72.21 -72.23
REMARK 500 SER B 97 2.82 -63.47
REMARK 500 GLU B 114 10.68 -65.56
REMARK 500 LYS B 115 -79.23 -82.82
REMARK 500 ASP B 118 -159.61 -131.42
REMARK 500 GLU B 120 -2.31 -58.01
REMARK 500 ALA B 128 38.53 -141.50
REMARK 500 ILE B 130 -64.47 -98.80
REMARK 500 MET B 145 6.72 -68.38
REMARK 500 ASP C 93 70.57 -69.84
REMARK 500 ASP D 20 64.86 -69.33
REMARK 500 ASN D 42 75.39 -157.54
REMARK 500 ASP D 93 67.99 -63.35
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 501 CA
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 81.4 87.7
REMARK 620 4 THR A 26 O 82.2 163.6 81.7
REMARK 620 5 GLU A 31 OE1 112.6 119.7 149.5 74.0
REMARK 620 6 GLU A 31 OE2 106.1 68.6 153.7 123.8 51.2
REMARK 620 7 HOH A 604 O 160.2 76.6 94.8 116.7 80.3 69.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 74.6
REMARK 620 3 ASP A 58 OD2 119.5 45.2
REMARK 620 4 ASN A 60 OD1 84.3 71.1 81.4
REMARK 620 5 THR A 62 O 77.4 143.5 155.6 83.3
REMARK 620 6 GLU A 67 OE1 114.2 132.7 105.0 151.7 80.4
REMARK 620 7 GLU A 67 OE2 86.7 85.3 84.0 156.2 116.1 51.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 82.3
REMARK 620 3 SER A 97 OG 92.5 75.6
REMARK 620 4 TYR A 99 O 78.3 149.7 82.2
REMARK 620 5 GLU A 104 OE1 89.9 69.2 144.0 133.2
REMARK 620 6 GLU A 104 OE2 96.8 120.7 162.1 84.8 51.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 80.7
REMARK 620 3 ASP A 133 OD1 76.3 80.5
REMARK 620 4 GLN A 135 O 70.3 141.2 68.2
REMARK 620 5 GLU A 140 OE1 100.7 127.8 151.2 83.7
REMARK 620 6 GLU A 140 OE2 64.1 80.7 138.3 107.6 55.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD1 69.1
REMARK 620 3 ASP B 22 OD2 112.7 43.6
REMARK 620 4 ASP B 24 OD1 75.8 82.5 93.7
REMARK 620 5 THR B 26 O 74.2 141.4 167.1 77.1
REMARK 620 6 GLU B 31 OE1 84.1 77.5 81.3 155.6 110.8
REMARK 620 7 GLU B 31 OE2 100.8 128.1 117.4 146.6 70.2 50.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 56 OD1
REMARK 620 2 ASP B 58 OD1 66.9
REMARK 620 3 ASP B 58 OD2 111.9 47.7
REMARK 620 4 ASN B 60 OD1 89.9 82.1 97.2
REMARK 620 5 THR B 62 O 80.3 139.2 165.3 73.9
REMARK 620 6 GLU B 67 OE1 82.0 74.3 66.0 156.4 125.8
REMARK 620 7 GLU B 67 OE2 101.5 124.3 100.4 153.6 84.5 50.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 93 OD1
REMARK 620 2 ASP B 95 OD1 68.9
REMARK 620 3 SER B 97 OG 96.2 94.4
REMARK 620 4 TYR B 99 O 88.1 153.8 75.1
REMARK 620 5 GLU B 104 OE1 101.8 117.5 147.2 78.3
REMARK 620 6 GLU B 104 OE2 91.7 64.6 153.0 131.0 53.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD1
REMARK 620 2 ASP B 133 OD1 107.8
REMARK 620 3 GLN B 135 O 103.8 79.0
REMARK 620 4 GLU B 140 OE1 93.6 146.8 71.3
REMARK 620 5 GLU B 140 OE2 88.4 153.7 117.9 47.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 20 OD1
REMARK 620 2 ASP C 22 OD1 70.9
REMARK 620 3 ASP C 24 OD1 69.6 71.9
REMARK 620 4 THR C 26 O 83.5 150.0 84.8
REMARK 620 5 GLU C 31 OE1 98.4 72.5 144.5 128.3
REMARK 620 6 GLU C 31 OE2 129.5 124.8 155.9 83.6 55.5
REMARK 620 7 ASP D 118 OD2 66.9 106.7 133.8 75.9 58.5 62.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 56 OD1
REMARK 620 2 ASP C 58 OD1 76.4
REMARK 620 3 ASP C 58 OD2 125.9 54.3
REMARK 620 4 ASN C 60 OD1 82.7 64.3 93.5
REMARK 620 5 THR C 62 O 80.8 135.3 149.9 75.1
REMARK 620 6 GLU C 67 OE1 90.6 87.6 68.6 151.9 130.9
REMARK 620 7 GLU C 67 OE2 111.3 137.3 94.1 155.3 86.8 51.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 93 OD1
REMARK 620 2 ASP C 95 OD1 87.2
REMARK 620 3 SER C 97 OG 83.5 76.1
REMARK 620 4 TYR C 99 O 86.4 152.7 76.8
REMARK 620 5 GLU C 104 OE1 111.3 71.4 143.1 135.4
REMARK 620 6 GLU C 104 OE2 104.6 127.4 154.8 79.9 56.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 129 OD1
REMARK 620 2 ASP C 131 OD1 72.1
REMARK 620 3 ASP C 133 OD1 84.9 84.1
REMARK 620 4 GLN C 135 O 74.9 142.7 75.9
REMARK 620 5 GLU C 140 OE1 105.9 130.6 145.2 75.3
REMARK 620 6 GLU C 140 OE2 94.6 80.3 163.7 119.7 50.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 20 OD1
REMARK 620 2 ASP D 22 OD1 73.8
REMARK 620 3 ASP D 24 OD1 70.9 82.7
REMARK 620 4 THR D 26 O 71.7 144.1 77.2
REMARK 620 5 GLU D 31 OE1 126.0 129.9 144.5 79.9
REMARK 620 6 GLU D 31 OE2 106.6 78.4 160.8 120.8 52.7
REMARK 620 7 HOH D 601 O 154.5 85.0 93.0 125.2 78.6 82.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 56 OD1
REMARK 620 2 ASP D 58 OD1 75.1
REMARK 620 3 ASN D 60 OD1 90.2 85.6
REMARK 620 4 THR D 62 O 85.9 155.8 79.6
REMARK 620 5 GLU D 67 OE1 105.1 125.9 147.3 73.1
REMARK 620 6 GLU D 67 OE2 85.2 76.1 161.7 117.7 50.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 93 OD1
REMARK 620 2 ASP D 95 OD1 85.4
REMARK 620 3 SER D 97 OG 87.2 75.4
REMARK 620 4 TYR D 99 O 82.4 158.3 86.1
REMARK 620 5 GLU D 104 OE1 101.2 72.1 145.5 127.9
REMARK 620 6 GLU D 104 OE2 110.7 127.5 150.5 73.8 56.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 129 OD1
REMARK 620 2 ASP D 131 OD2 102.8
REMARK 620 3 ASP D 133 OD1 70.1 113.1
REMARK 620 4 GLN D 135 O 77.5 179.6 66.7
REMARK 620 5 GLU D 140 OE1 81.0 65.0 150.1 115.4
REMARK 620 6 GLU D 140 OE2 101.4 101.9 145.0 78.3 47.8
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 504
DBREF 6DAH A 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6DAH B 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6DAH C 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6DAH D 0 148 UNP P0DP23 CALM1_HUMAN 1 149
SEQADV 6DAH GLY A -2 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH HIS A -1 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH SER A 97 UNP P0DP23 ASN 98 ENGINEERED MUTATION
SEQADV 6DAH GLY B -2 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH HIS B -1 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH SER B 97 UNP P0DP23 ASN 98 ENGINEERED MUTATION
SEQADV 6DAH GLY C -2 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH HIS C -1 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH SER C 97 UNP P0DP23 ASN 98 ENGINEERED MUTATION
SEQADV 6DAH GLY D -2 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH HIS D -1 UNP P0DP23 EXPRESSION TAG
SEQADV 6DAH SER D 97 UNP P0DP23 ASN 98 ENGINEERED MUTATION
SEQRES 1 A 151 GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA
SEQRES 2 A 151 GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY
SEQRES 3 A 151 ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET
SEQRES 4 A 151 ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN
SEQRES 5 A 151 ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR
SEQRES 6 A 151 ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS
SEQRES 7 A 151 MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA
SEQRES 8 A 151 PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER
SEQRES 9 A 151 ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU
SEQRES 10 A 151 LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU
SEQRES 11 A 151 ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU
SEQRES 12 A 151 PHE VAL GLN MET MET THR ALA LYS
SEQRES 1 B 151 GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA
SEQRES 2 B 151 GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY
SEQRES 3 B 151 ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET
SEQRES 4 B 151 ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN
SEQRES 5 B 151 ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR
SEQRES 6 B 151 ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS
SEQRES 7 B 151 MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA
SEQRES 8 B 151 PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER
SEQRES 9 B 151 ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU
SEQRES 10 B 151 LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU
SEQRES 11 B 151 ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU
SEQRES 12 B 151 PHE VAL GLN MET MET THR ALA LYS
SEQRES 1 C 151 GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA
SEQRES 2 C 151 GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY
SEQRES 3 C 151 ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET
SEQRES 4 C 151 ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN
SEQRES 5 C 151 ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR
SEQRES 6 C 151 ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS
SEQRES 7 C 151 MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA
SEQRES 8 C 151 PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER
SEQRES 9 C 151 ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU
SEQRES 10 C 151 LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU
SEQRES 11 C 151 ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU
SEQRES 12 C 151 PHE VAL GLN MET MET THR ALA LYS
SEQRES 1 D 151 GLY HIS MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA
SEQRES 2 D 151 GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY
SEQRES 3 D 151 ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET
SEQRES 4 D 151 ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN
SEQRES 5 D 151 ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR
SEQRES 6 D 151 ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS
SEQRES 7 D 151 MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA
SEQRES 8 D 151 PHE ARG VAL PHE ASP LYS ASP GLY SER GLY TYR ILE SER
SEQRES 9 D 151 ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU
SEQRES 10 D 151 LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU
SEQRES 11 D 151 ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU
SEQRES 12 D 151 PHE VAL GLN MET MET THR ALA LYS
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HET CA B 501 1
HET CA B 502 1
HET CA B 503 1
HET CA B 504 1
HET CA C 501 1
HET CA C 502 1
HET CA C 503 1
HET CA C 504 1
HET CA D 501 1
HET CA D 502 1
HET CA D 503 1
HET CA D 504 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 16(CA 2+)
FORMUL 21 HOH *34(H2 O)
HELIX 1 AA1 HIS A -1 GLN A 3 5 5
HELIX 2 AA2 THR A 5 SER A 17 1 13
HELIX 3 AA3 THR A 28 LEU A 39 1 12
HELIX 4 AA4 THR A 44 GLU A 54 1 11
HELIX 5 AA5 PHE A 65 ASP A 93 1 29
HELIX 6 AA6 SER A 101 LEU A 112 1 12
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 TYR A 138 GLN A 143 1 6
HELIX 9 AA9 LYS B 13 ASP B 20 1 8
HELIX 10 AB1 THR B 28 LEU B 39 1 12
HELIX 11 AB2 THR B 44 ASP B 56 1 13
HELIX 12 AB3 PHE B 65 ASP B 93 1 29
HELIX 13 AB4 SER B 101 LEU B 112 1 12
HELIX 14 AB5 GLU B 120 ALA B 128 1 9
HELIX 15 AB6 ASN B 137 MET B 145 1 9
HELIX 16 AB7 HIS C -1 LEU C 4 5 6
HELIX 17 AB8 THR C 5 ASP C 20 1 16
HELIX 18 AB9 THR C 28 LEU C 39 1 12
HELIX 19 AC1 THR C 44 GLU C 54 1 11
HELIX 20 AC2 ASP C 64 ASP C 93 1 30
HELIX 21 AC3 SER C 101 ASN C 111 1 11
HELIX 22 AC4 THR C 117 ASP C 129 1 13
HELIX 23 AC5 ASN C 137 MET C 145 1 9
HELIX 24 AC6 MET D 0 LEU D 4 5 5
HELIX 25 AC7 THR D 5 ASP D 20 1 16
HELIX 26 AC8 THR D 28 LEU D 39 1 12
HELIX 27 AC9 THR D 44 ASP D 56 1 13
HELIX 28 AD1 PHE D 65 ASP D 93 1 29
HELIX 29 AD2 SER D 101 LEU D 112 1 12
HELIX 30 AD3 THR D 117 ASP D 129 1 13
HELIX 31 AD4 ASN D 137 GLN D 143 1 7
SHEET 1 AA1 2 THR A 26 ILE A 27 0
SHEET 2 AA1 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 AA2 2 TYR A 99 ILE A 100 0
SHEET 2 AA2 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
SHEET 1 AA3 2 THR B 26 ILE B 27 0
SHEET 2 AA3 2 ILE B 63 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 AA4 2 THR D 26 ILE D 27 0
SHEET 2 AA4 2 ILE D 63 ASP D 64 -1 O ILE D 63 N ILE D 27
LINK OD1 ASP A 20 CA CA A 501 1555 1555 2.27
LINK OD1 ASP A 22 CA CA A 501 1555 1555 2.41
LINK OD1 ASP A 24 CA CA A 501 1555 1555 2.31
LINK O THR A 26 CA CA A 501 1555 1555 2.24
LINK OE1 GLU A 31 CA CA A 501 1555 1555 2.69
LINK OE2 GLU A 31 CA CA A 501 1555 1555 2.33
LINK OD1 ASP A 56 CA CA A 502 1555 1555 2.29
LINK OD1 ASP A 58 CA CA A 502 1555 1555 2.37
LINK OD2 ASP A 58 CA CA A 502 1555 1555 3.10
LINK OD1 ASN A 60 CA CA A 502 1555 1555 2.42
LINK O THR A 62 CA CA A 502 1555 1555 2.41
LINK OE1 GLU A 67 CA CA A 502 1555 1555 2.52
LINK OE2 GLU A 67 CA CA A 502 1555 1555 2.57
LINK OD1 ASP A 93 CA CA A 503 1555 1555 2.19
LINK OD1 ASP A 95 CA CA A 503 1555 1555 2.18
LINK OG SER A 97 CA CA A 503 1555 1555 2.60
LINK O TYR A 99 CA CA A 503 1555 1555 2.20
LINK OE1 GLU A 104 CA CA A 503 1555 1555 2.61
LINK OE2 GLU A 104 CA CA A 503 1555 1555 2.43
LINK OD1 ASP A 129 CA CA A 504 1555 1555 2.51
LINK OD1 ASP A 131 CA CA A 504 1555 1555 2.20
LINK OD1 ASP A 133 CA CA A 504 1555 1555 2.32
LINK O GLN A 135 CA CA A 504 1555 1555 2.52
LINK OE1 GLU A 140 CA CA A 504 1555 1555 2.23
LINK OE2 GLU A 140 CA CA A 504 1555 1555 2.46
LINK CA CA A 501 O HOH A 604 1555 1555 2.82
LINK OD1 ASP B 20 CA CA B 501 1555 1555 2.38
LINK OD1 ASP B 22 CA CA B 501 1555 1555 2.45
LINK OD2 ASP B 22 CA CA B 501 1555 1555 3.17
LINK OD1 ASP B 24 CA CA B 501 1555 1555 2.42
LINK O THR B 26 CA CA B 501 1555 1555 2.47
LINK OE1 GLU B 31 CA CA B 501 1555 1555 2.72
LINK OE2 GLU B 31 CA CA B 501 1555 1555 2.41
LINK OD1 ASP B 56 CA CA B 502 1555 1555 2.46
LINK OD1 ASP B 58 CA CA B 502 1555 1555 2.45
LINK OD2 ASP B 58 CA CA B 502 1555 1555 2.89
LINK OD1 ASN B 60 CA CA B 502 1555 1555 2.40
LINK O THR B 62 CA CA B 502 1555 1555 2.42
LINK OE1 GLU B 67 CA CA B 502 1555 1555 2.60
LINK OE2 GLU B 67 CA CA B 502 1555 1555 2.60
LINK OD1 ASP B 93 CA CA B 503 1555 1555 2.24
LINK OD1 ASP B 95 CA CA B 503 1555 1555 2.48
LINK OG SER B 97 CA CA B 503 1555 1555 2.30
LINK O TYR B 99 CA CA B 503 1555 1555 2.32
LINK OE1 GLU B 104 CA CA B 503 1555 1555 2.37
LINK OE2 GLU B 104 CA CA B 503 1555 1555 2.48
LINK OD1 ASP B 129 CA CA B 504 1555 1555 2.75
LINK OD1 ASP B 133 CA CA B 504 1555 1555 2.61
LINK O GLN B 135 CA CA B 504 1555 1555 2.48
LINK OE1 GLU B 140 CA CA B 504 1555 1555 2.94
LINK OE2 GLU B 140 CA CA B 504 1555 1555 2.41
LINK OD1 ASP C 20 CA CA C 501 1555 1555 2.29
LINK OD1 ASP C 22 CA CA C 501 1555 1555 2.71
LINK OD1 ASP C 24 CA CA C 501 1555 1555 2.49
LINK O THR C 26 CA CA C 501 1555 1555 2.39
LINK OE1 GLU C 31 CA CA C 501 1555 1555 2.36
LINK OE2 GLU C 31 CA CA C 501 1555 1555 2.40
LINK OD1 ASP C 56 CA CA C 502 1555 1555 2.28
LINK OD1 ASP C 58 CA CA C 502 1555 1555 2.39
LINK OD2 ASP C 58 CA CA C 502 1555 1555 2.44
LINK OD1 ASN C 60 CA CA C 502 1555 1555 2.54
LINK O THR C 62 CA CA C 502 1555 1555 2.46
LINK OE1 GLU C 67 CA CA C 502 1555 1555 2.54
LINK OE2 GLU C 67 CA CA C 502 1555 1555 2.54
LINK OD1 ASP C 93 CA CA C 503 1555 1555 2.43
LINK OD1 ASP C 95 CA CA C 503 1555 1555 2.36
LINK OG SER C 97 CA CA C 503 1555 1555 2.52
LINK O TYR C 99 CA CA C 503 1555 1555 2.34
LINK OE1 GLU C 104 CA CA C 503 1555 1555 2.34
LINK OE2 GLU C 104 CA CA C 503 1555 1555 2.36
LINK OD1 ASP C 129 CA CA C 504 1555 1555 2.50
LINK OD1 ASP C 131 CA CA C 504 1555 1555 2.34
LINK OD1 ASP C 133 CA CA C 504 1555 1555 2.44
LINK O GLN C 135 CA CA C 504 1555 1555 2.44
LINK OE1 GLU C 140 CA CA C 504 1555 1555 2.61
LINK OE2 GLU C 140 CA CA C 504 1555 1555 2.57
LINK CA CA C 501 OD2 ASP D 118 1455 1555 2.79
LINK OD1 ASP D 20 CA CA D 501 1555 1555 2.33
LINK OD1 ASP D 22 CA CA D 501 1555 1555 2.38
LINK OD1 ASP D 24 CA CA D 501 1555 1555 2.47
LINK O THR D 26 CA CA D 501 1555 1555 2.48
LINK OE1 GLU D 31 CA CA D 501 1555 1555 2.63
LINK OE2 GLU D 31 CA CA D 501 1555 1555 2.28
LINK OD1 ASP D 56 CA CA D 502 1555 1555 2.29
LINK OD1 ASP D 58 CA CA D 502 1555 1555 2.40
LINK OD1 ASN D 60 CA CA D 502 1555 1555 2.35
LINK O THR D 62 CA CA D 502 1555 1555 2.34
LINK OE1 GLU D 67 CA CA D 502 1555 1555 2.66
LINK OE2 GLU D 67 CA CA D 502 1555 1555 2.46
LINK OD1 ASP D 93 CA CA D 503 1555 1555 2.25
LINK OD1 ASP D 95 CA CA D 503 1555 1555 2.31
LINK OG SER D 97 CA CA D 503 1555 1555 2.77
LINK O TYR D 99 CA CA D 503 1555 1555 2.28
LINK OE1 GLU D 104 CA CA D 503 1555 1555 2.35
LINK OE2 GLU D 104 CA CA D 503 1555 1555 2.30
LINK OD1 ASP D 129 CA CA D 504 1555 1555 2.52
LINK OD2 ASP D 131 CA CA D 504 1555 1555 2.48
LINK OD1 ASP D 133 CA CA D 504 1555 1555 2.28
LINK O GLN D 135 CA CA D 504 1555 1555 2.79
LINK OE1 GLU D 140 CA CA D 504 1555 1555 2.84
LINK OE2 GLU D 140 CA CA D 504 1555 1555 2.52
LINK CA CA D 501 O HOH D 601 1555 1555 2.44
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 604
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 SER A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 5 GLU A 140
SITE 1 AC5 5 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 2 AC5 5 GLU B 31
SITE 1 AC6 5 ASP B 56 ASP B 58 ASN B 60 THR B 62
SITE 2 AC6 5 GLU B 67
SITE 1 AC7 5 ASP B 93 ASP B 95 SER B 97 TYR B 99
SITE 2 AC7 5 GLU B 104
SITE 1 AC8 6 ASP B 129 ASP B 131 GLY B 132 ASP B 133
SITE 2 AC8 6 GLN B 135 GLU B 140
SITE 1 AC9 6 ASP C 20 ASP C 22 ASP C 24 THR C 26
SITE 2 AC9 6 GLU C 31 ASP D 118
SITE 1 AD1 5 ASP C 56 ASP C 58 ASN C 60 THR C 62
SITE 2 AD1 5 GLU C 67
SITE 1 AD2 5 ASP C 93 ASP C 95 SER C 97 TYR C 99
SITE 2 AD2 5 GLU C 104
SITE 1 AD3 5 ASP C 129 ASP C 131 ASP C 133 GLN C 135
SITE 2 AD3 5 GLU C 140
SITE 1 AD4 6 ASP D 20 ASP D 22 ASP D 24 THR D 26
SITE 2 AD4 6 GLU D 31 HOH D 601
SITE 1 AD5 5 ASP D 56 ASP D 58 ASN D 60 THR D 62
SITE 2 AD5 5 GLU D 67
SITE 1 AD6 5 ASP D 93 ASP D 95 SER D 97 TYR D 99
SITE 2 AD6 5 GLU D 104
SITE 1 AD7 5 ASP D 129 ASP D 131 ASP D 133 GLN D 135
SITE 2 AD7 5 GLU D 140
CRYST1 59.117 94.414 60.977 90.00 94.42 90.00 P 1 21 1 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 0.016916 0.000000 0.001308 0.00000
SCALE2 0.000000 0.010592 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END