HEADER MOTOR PROTEIN/CALCIUM BINDING PROTEIN 08-DEC-16 5WSV
TITLE CRYSTAL STRUCTURE OF MYOSIN VIIA IQ5 IN COMPLEX WITH CA2+-CAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1-147;
COMPND 5 SYNONYM: CAM;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UNCONVENTIONAL MYOSIN-VIIA;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: UNP RESIDUES 828-870;
COMPND 11 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: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: MYO7A, MYO7;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MOLECULAR MOTOR, CALCIUM SIGNALING, PROTEIN COMPLEX, CALMODULIN,
KEYWDS 2 MOTOR PROTEIN-CALCIUM BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,Y.CHEN,Y.DENG,Q.LU,M.ZHANG
REVDAT 2 08-NOV-23 5WSV 1 LINK
REVDAT 1 07-JUN-17 5WSV 0
JRNL AUTH J.LI,Y.CHEN,Y.DENG,I.C.UNARTA,Q.LU,X.HUANG,M.ZHANG
JRNL TITL CA(2+)-INDUCED RIGIDITY CHANGE OF THE MYOSIN VIIA IQ
JRNL TITL 2 MOTIF-SINGLE ALPHA HELIX LEVER ARM EXTENSION
JRNL REF STRUCTURE V. 25 579 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28262393
JRNL DOI 10.1016/J.STR.2017.02.002
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 11840
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 598
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 769
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE SET COUNT : 29
REMARK 3 BIN FREE R VALUE : 0.4500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2465
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : 1.04000
REMARK 3 B33 (A**2) : -1.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.643
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.289
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.282
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.713
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2517 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2216 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3419 ; 1.246 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5040 ; 0.982 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 339 ; 3.992 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 112 ;34.093 ;25.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 370 ;13.991 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;11.768 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 403 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2965 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 554 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1362 ; 1.515 ; 3.332
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1361 ; 1.515 ; 3.330
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1696 ; 2.506 ; 4.987
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 144
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3881 -75.1683 50.0792
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: 0.0324
REMARK 3 T33: 0.2274 T12: -0.0179
REMARK 3 T13: 0.0092 T23: -0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 0.7383 L22: 0.3693
REMARK 3 L33: 1.2183 L12: 0.1501
REMARK 3 L13: 0.2314 L23: -0.4586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0210 S12: -0.0861 S13: 0.1091
REMARK 3 S21: -0.0804 S22: 0.0691 S23: -0.0956
REMARK 3 S31: 0.1250 S32: -0.1539 S33: -0.0481
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 826 B 854
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1482 -73.0186 52.5876
REMARK 3 T TENSOR
REMARK 3 T11: 0.0695 T22: 0.1471
REMARK 3 T33: 0.1820 T12: -0.0183
REMARK 3 T13: 0.0015 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 1.2311 L22: 0.0907
REMARK 3 L33: 0.8094 L12: 0.0756
REMARK 3 L13: 0.9006 L23: 0.1673
REMARK 3 S TENSOR
REMARK 3 S11: 0.0967 S12: -0.1445 S13: 0.1056
REMARK 3 S21: 0.0271 S22: -0.1227 S23: -0.0069
REMARK 3 S31: 0.1167 S32: -0.2333 S33: 0.0260
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 146
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8390 -76.7024 28.0984
REMARK 3 T TENSOR
REMARK 3 T11: 0.0582 T22: 0.0524
REMARK 3 T33: 0.1421 T12: -0.0205
REMARK 3 T13: 0.0243 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.6681 L22: 0.7751
REMARK 3 L33: 2.5131 L12: -0.5214
REMARK 3 L13: 0.5828 L23: 0.4005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: 0.1271 S13: 0.0970
REMARK 3 S21: -0.0212 S22: -0.1598 S23: -0.0527
REMARK 3 S31: 0.1059 S32: -0.0222 S33: 0.0967
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 828 D 856
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5869 -79.1803 28.7990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1404 T22: 0.1132
REMARK 3 T33: 0.1036 T12: 0.0055
REMARK 3 T13: -0.0161 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.2804 L22: 2.9689
REMARK 3 L33: 0.9590 L12: -1.2767
REMARK 3 L13: 0.9990 L23: -1.1730
REMARK 3 S TENSOR
REMARK 3 S11: 0.2314 S12: -0.1676 S13: -0.0527
REMARK 3 S21: -0.2284 S22: -0.1909 S23: -0.0270
REMARK 3 S31: 0.0548 S32: -0.1365 S33: -0.0404
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 5WSV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1300001627.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-14
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
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 : 12459
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : 0.36000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
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: 3G43
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 27.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS
REMARK 280 (PH 6.5), 25%(W/V) PEG 3,500, VAPOR DIFFUSION, TEMPERATURE 289K
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 44.87750
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
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: 3060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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: 3900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 GLY A -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 MET A 145
REMARK 465 THR A 146
REMARK 465 GLY B 824
REMARK 465 PRO B 825
REMARK 465 LEU B 855
REMARK 465 HIS B 856
REMARK 465 ARG B 857
REMARK 465 ARG B 858
REMARK 465 LEU B 859
REMARK 465 ARG B 860
REMARK 465 VAL B 861
REMARK 465 GLU B 862
REMARK 465 TYR B 863
REMARK 465 GLN B 864
REMARK 465 ARG B 865
REMARK 465 ARG B 866
REMARK 465 LEU B 867
REMARK 465 GLU B 868
REMARK 465 ALA B 869
REMARK 465 GLU B 870
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 GLN C 3
REMARK 465 LEU C 4
REMARK 465 GLY D 824
REMARK 465 PRO D 825
REMARK 465 GLY D 826
REMARK 465 SER D 827
REMARK 465 ARG D 857
REMARK 465 ARG D 858
REMARK 465 LEU D 859
REMARK 465 ARG D 860
REMARK 465 VAL D 861
REMARK 465 GLU D 862
REMARK 465 TYR D 863
REMARK 465 GLN D 864
REMARK 465 ARG D 865
REMARK 465 ARG D 866
REMARK 465 LEU D 867
REMARK 465 GLU D 868
REMARK 465 ALA D 869
REMARK 465 GLU D 870
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 LEU A 4 CG CD1 CD2
REMARK 470 GLU A 6 CG CD OE1 OE2
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 45 CG CD OE1 OE2
REMARK 470 GLU A 54 CG CD OE1 OE2
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 75 CG CD CE NZ
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 GLU A 119 CG CD OE1 OE2
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 LYS B 831 CE NZ
REMARK 470 ARG B 834 NE CZ NH1 NH2
REMARK 470 ARG B 853 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 854 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 6 CG CD OE1 OE2
REMARK 470 GLU C 7 CG CD OE1 OE2
REMARK 470 GLN C 8 CG CD OE1 NE2
REMARK 470 LYS C 21 CG CD CE NZ
REMARK 470 LYS C 30 CG CD CE NZ
REMARK 470 GLU C 45 CG CD OE1 OE2
REMARK 470 GLU C 47 CG CD OE1 OE2
REMARK 470 ARG C 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 75 CE NZ
REMARK 470 GLU C 82 CG CD OE1 OE2
REMARK 470 GLU C 83 CG CD OE1 OE2
REMARK 470 ARG C 86 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 94 CE NZ
REMARK 470 ARG C 106 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 115 CG CD CE NZ
REMARK 470 LEU C 116 CG CD1 CD2
REMARK 470 ASP C 118 CG OD1 OD2
REMARK 470 GLU C 119 CG CD OE1 OE2
REMARK 470 GLU C 120 CG CD OE1 OE2
REMARK 470 ASP C 122 CG OD1 OD2
REMARK 470 GLU C 123 CG CD OE1 OE2
REMARK 470 ARG C 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 127 CG CD OE1 OE2
REMARK 470 GLU C 139 CG CD OE1 OE2
REMARK 470 GLN C 143 CG CD OE1 NE2
REMARK 470 LEU D 828 CG CD1 CD2
REMARK 470 ARG D 830 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 831 CG CD CE NZ
REMARK 470 TYR D 846 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 853 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 854 NE CZ NH1 NH2
REMARK 470 LEU D 855 CG CD1 CD2
REMARK 470 HIS D 856 CG ND1 CD2 CE1 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 LYS C 115 77.31 -109.68
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 83.7
REMARK 620 3 ASP A 24 OD1 74.4 89.8
REMARK 620 4 ASP A 24 OD2 116.7 75.6 46.9
REMARK 620 5 THR A 26 O 70.4 148.3 66.2 99.4
REMARK 620 6 GLU A 31 OE1 94.9 79.3 165.6 136.5 119.9
REMARK 620 7 GLU A 31 OE2 117.5 126.6 141.2 122.9 82.7 52.3
REMARK 620 N 1 2 3 4 5 6
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 56 OD1
REMARK 620 2 ASP A 58 OD1 66.4
REMARK 620 3 ASN A 60 OD1 71.6 83.3
REMARK 620 4 THR A 62 O 74.8 138.8 71.4
REMARK 620 5 GLU A 67 OE1 73.8 71.3 143.1 111.3
REMARK 620 6 GLU A 67 OE2 104.1 123.6 149.6 78.4 53.4
REMARK 620 N 1 2 3 4 5
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 93 OD1
REMARK 620 2 ASP A 95 OD2 89.5
REMARK 620 3 ASN A 97 OD1 72.9 76.2
REMARK 620 4 TYR A 99 O 81.5 155.2 79.1
REMARK 620 5 GLU A 104 OE1 109.5 127.8 155.2 77.0
REMARK 620 6 GLU A 104 OE2 100.8 78.8 154.2 125.5 50.6
REMARK 620 7 HOH A 301 O 168.6 87.4 95.7 96.9 80.9 89.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 74.8
REMARK 620 3 ASP A 133 OD1 79.9 74.6
REMARK 620 4 ASP A 133 OD2 123.4 77.7 45.2
REMARK 620 5 GLN A 135 O 73.1 140.8 78.2 102.2
REMARK 620 6 GLU A 140 OE1 103.1 126.2 159.1 132.9 82.9
REMARK 620 7 GLU A 140 OE2 79.9 76.2 147.9 138.1 118.7 51.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 20 OD1
REMARK 620 2 ASP C 22 OD1 86.8
REMARK 620 3 ASP C 24 OD1 78.6 91.1
REMARK 620 4 THR C 26 O 71.9 158.5 87.2
REMARK 620 5 GLU C 31 OE1 107.7 61.8 151.1 121.7
REMARK 620 6 GLU C 31 OE2 117.4 106.2 156.5 82.3 44.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 56 OD1
REMARK 620 2 ASP C 58 OD1 64.8
REMARK 620 3 ASN C 60 OD1 77.0 72.7
REMARK 620 4 THR C 62 O 81.6 139.3 78.2
REMARK 620 5 GLU C 67 OE1 90.8 119.4 157.4 81.3
REMARK 620 6 GLU C 67 OE2 69.8 66.1 134.9 124.1 53.3
REMARK 620 7 HOH C 304 O 153.6 128.9 85.9 75.3 98.0 134.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 93 OD1
REMARK 620 2 ASP C 95 OD1 92.3
REMARK 620 3 ASN C 97 OD1 86.5 76.1
REMARK 620 4 TYR C 99 O 76.4 161.0 87.8
REMARK 620 5 GLU C 104 OE1 101.2 125.6 156.0 72.3
REMARK 620 6 GLU C 104 OE2 89.1 76.2 151.7 118.2 52.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 131 OD1
REMARK 620 2 ASP C 133 OD1 78.2
REMARK 620 3 GLN C 135 O 151.1 78.0
REMARK 620 4 GLU C 140 OE1 76.5 153.8 123.6
REMARK 620 5 GLU C 140 OE2 124.3 156.3 82.1 49.8
REMARK 620 6 HOH C 306 O 92.3 86.2 102.1 101.6 85.7
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 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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5WST RELATED DB: PDB
REMARK 900 RELATED ID: 5WSU RELATED DB: PDB
DBREF 5WSV A 0 146 UNP P62158 CALM_HUMAN 1 147
DBREF 5WSV B 828 870 UNP P97479 MYO7A_MOUSE 828 870
DBREF 5WSV C 0 146 UNP P62158 CALM_HUMAN 1 147
DBREF 5WSV D 828 870 UNP P97479 MYO7A_MOUSE 828 870
SEQADV 5WSV GLY A -4 UNP P62158 EXPRESSION TAG
SEQADV 5WSV PRO A -3 UNP P62158 EXPRESSION TAG
SEQADV 5WSV GLY A -2 UNP P62158 EXPRESSION TAG
SEQADV 5WSV SER A -1 UNP P62158 EXPRESSION TAG
SEQADV 5WSV GLY B 824 UNP P97479 EXPRESSION TAG
SEQADV 5WSV PRO B 825 UNP P97479 EXPRESSION TAG
SEQADV 5WSV GLY B 826 UNP P97479 EXPRESSION TAG
SEQADV 5WSV SER B 827 UNP P97479 EXPRESSION TAG
SEQADV 5WSV GLY C -4 UNP P62158 EXPRESSION TAG
SEQADV 5WSV PRO C -3 UNP P62158 EXPRESSION TAG
SEQADV 5WSV GLY C -2 UNP P62158 EXPRESSION TAG
SEQADV 5WSV SER C -1 UNP P62158 EXPRESSION TAG
SEQADV 5WSV GLY D 824 UNP P97479 EXPRESSION TAG
SEQADV 5WSV PRO D 825 UNP P97479 EXPRESSION TAG
SEQADV 5WSV GLY D 826 UNP P97479 EXPRESSION TAG
SEQADV 5WSV SER D 827 UNP P97479 EXPRESSION TAG
SEQRES 1 A 151 GLY PRO GLY SER MET ALA ASP GLN LEU THR GLU GLU GLN
SEQRES 2 A 151 ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS
SEQRES 3 A 151 ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU GLY THR
SEQRES 4 A 151 VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU
SEQRES 5 A 151 LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN
SEQRES 6 A 151 GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA
SEQRES 7 A 151 ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG
SEQRES 8 A 151 GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR
SEQRES 9 A 151 ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU
SEQRES 10 A 151 GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE
SEQRES 11 A 151 ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR
SEQRES 12 A 151 GLU GLU PHE VAL GLN MET MET THR
SEQRES 1 B 47 GLY PRO GLY SER LEU VAL ARG LYS ALA PHE ARG HIS ARG
SEQRES 2 B 47 LEU TRP ALA VAL ILE THR VAL GLN ALA TYR ALA ARG GLY
SEQRES 3 B 47 MET ILE ALA ARG ARG LEU HIS ARG ARG LEU ARG VAL GLU
SEQRES 4 B 47 TYR GLN ARG ARG LEU GLU ALA GLU
SEQRES 1 C 151 GLY PRO GLY SER MET ALA ASP GLN LEU THR GLU GLU GLN
SEQRES 2 C 151 ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS
SEQRES 3 C 151 ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU GLY THR
SEQRES 4 C 151 VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU
SEQRES 5 C 151 LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN
SEQRES 6 C 151 GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA
SEQRES 7 C 151 ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG
SEQRES 8 C 151 GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR
SEQRES 9 C 151 ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU
SEQRES 10 C 151 GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE
SEQRES 11 C 151 ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR
SEQRES 12 C 151 GLU GLU PHE VAL GLN MET MET THR
SEQRES 1 D 47 GLY PRO GLY SER LEU VAL ARG LYS ALA PHE ARG HIS ARG
SEQRES 2 D 47 LEU TRP ALA VAL ILE THR VAL GLN ALA TYR ALA ARG GLY
SEQRES 3 D 47 MET ILE ALA ARG ARG LEU HIS ARG ARG LEU ARG VAL GLU
SEQRES 4 D 47 TYR GLN ARG ARG LEU GLU ALA GLU
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA A 204 1
HET CA C 201 1
HET CA C 202 1
HET CA C 203 1
HET CA C 204 1
HET SO4 C 205 5
HET SO4 D 901 5
HET SO4 D 902 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 5 CA 8(CA 2+)
FORMUL 13 SO4 3(O4 S 2-)
FORMUL 16 HOH *12(H2 O)
HELIX 1 AA1 THR A 5 ASP A 20 1 16
HELIX 2 AA2 THR A 28 LEU A 39 1 12
HELIX 3 AA3 THR A 44 ASP A 56 1 13
HELIX 4 AA4 PHE A 65 ALA A 73 1 9
HELIX 5 AA5 SER A 81 ASP A 93 1 13
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 ASN A 137 MET A 144 1 8
HELIX 9 AA9 SER B 827 ARG B 854 1 28
HELIX 10 AB1 GLU C 6 ASP C 20 1 15
HELIX 11 AB2 THR C 28 LEU C 39 1 12
HELIX 12 AB3 THR C 44 ASP C 56 1 13
HELIX 13 AB4 PHE C 65 ALA C 73 1 9
HELIX 14 AB5 SER C 81 ASP C 93 1 13
HELIX 15 AB6 SER C 101 LEU C 112 1 12
HELIX 16 AB7 THR C 117 ASP C 129 1 13
HELIX 17 AB8 ASN C 137 THR C 146 1 10
HELIX 18 AB9 VAL D 829 HIS D 856 1 28
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 THR C 26 ILE C 27 0
SHEET 2 AA2 2 ILE C 63 ASP C 64 -1 O ILE C 63 N ILE C 27
LINK OD1 ASP A 20 CA CA A 201 1555 1555 2.06
LINK OD1 ASP A 22 CA CA A 201 1555 1555 2.34
LINK OD1 ASP A 24 CA CA A 201 1555 1555 2.57
LINK OD2 ASP A 24 CA CA A 201 1555 1555 2.94
LINK O THR A 26 CA CA A 201 1555 1555 2.51
LINK OE1 GLU A 31 CA CA A 201 1555 1555 2.34
LINK OE2 GLU A 31 CA CA A 201 1555 1555 2.67
LINK OD1 ASP A 56 CA CA A 202 1555 1555 2.42
LINK OD1 ASP A 58 CA CA A 202 1555 1555 2.72
LINK OD1 ASN A 60 CA CA A 202 1555 1555 2.33
LINK O THR A 62 CA CA A 202 1555 1555 2.59
LINK OE1 GLU A 67 CA CA A 202 1555 1555 2.46
LINK OE2 GLU A 67 CA CA A 202 1555 1555 2.34
LINK OD1 ASP A 93 CA CA A 203 1555 1555 2.34
LINK OD2 ASP A 95 CA CA A 203 1555 1555 2.44
LINK OD1 ASN A 97 CA CA A 203 1555 1555 2.40
LINK O TYR A 99 CA CA A 203 1555 1555 2.26
LINK OE1 GLU A 104 CA CA A 203 1555 1555 2.69
LINK OE2 GLU A 104 CA CA A 203 1555 1555 2.38
LINK OD1 ASP A 129 CA CA A 204 1555 1555 2.21
LINK OD1 ASP A 131 CA CA A 204 1555 1555 2.45
LINK OD1 ASP A 133 CA CA A 204 1555 1555 2.16
LINK OD2 ASP A 133 CA CA A 204 1555 1555 3.08
LINK O GLN A 135 CA CA A 204 1555 1555 2.39
LINK OE1 GLU A 140 CA CA A 204 1555 1555 2.57
LINK OE2 GLU A 140 CA CA A 204 1555 1555 2.52
LINK CA CA A 203 O HOH A 301 1555 1555 2.37
LINK OD1 ASP C 20 CA CA C 201 1555 1555 2.56
LINK OD1 ASP C 22 CA CA C 201 1555 1555 2.18
LINK OD1 ASP C 24 CA CA C 201 1555 1555 2.35
LINK O THR C 26 CA CA C 201 1555 1555 2.36
LINK OE1 GLU C 31 CA CA C 201 1555 1555 3.09
LINK OE2 GLU C 31 CA CA C 201 1555 1555 2.43
LINK OD1 ASP C 56 CA CA C 202 1555 1555 2.85
LINK OD1 ASP C 58 CA CA C 202 1555 1555 2.86
LINK OD1 ASN C 60 CA CA C 202 1555 1555 2.07
LINK O THR C 62 CA CA C 202 1555 1555 2.45
LINK OE1 GLU C 67 CA CA C 202 1555 1555 2.53
LINK OE2 GLU C 67 CA CA C 202 1555 1555 2.36
LINK OD1 ASP C 93 CA CA C 203 1555 1555 2.23
LINK OD1 ASP C 95 CA CA C 203 1555 1555 2.43
LINK OD1 ASN C 97 CA CA C 203 1555 1555 2.33
LINK O TYR C 99 CA CA C 203 1555 1555 2.21
LINK OE1 GLU C 104 CA CA C 203 1555 1555 2.53
LINK OE2 GLU C 104 CA CA C 203 1555 1555 2.47
LINK OD1 ASP C 131 CA CA C 204 1555 1555 2.26
LINK OD1 ASP C 133 CA CA C 204 1555 1555 2.23
LINK O GLN C 135 CA CA C 204 1555 1555 2.38
LINK OE1 GLU C 140 CA CA C 204 1555 1555 2.38
LINK OE2 GLU C 140 CA CA C 204 1555 1555 2.71
LINK CA CA C 202 O HOH C 304 1555 1555 2.35
LINK CA CA C 204 O HOH C 306 1555 1555 2.40
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 ASP A 64 GLU A 67
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 301
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 C 20 ASP C 22 ASP C 24 THR C 26
SITE 2 AC5 5 GLU C 31
SITE 1 AC6 6 ASP C 56 ASP C 58 ASN C 60 THR C 62
SITE 2 AC6 6 GLU C 67 HOH C 304
SITE 1 AC7 5 ASP C 93 ASP C 95 ASN C 97 TYR C 99
SITE 2 AC7 5 GLU C 104
SITE 1 AC8 6 ASP C 129 ASP C 131 ASP C 133 GLN C 135
SITE 2 AC8 6 GLU C 140 HOH C 306
SITE 1 AC9 2 TYR C 99 ASN C 137
SITE 1 AD1 6 ASN A 97 GLU C 47 MET C 51 ALA D 832
SITE 2 AD1 6 ARG D 836 HOH D1001
SITE 1 AD2 3 LYS C 75 ARG D 830 ARG D 834
CRYST1 38.683 89.755 45.724 90.00 106.03 90.00 P 1 21 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 0.025851 0.000000 0.007428 0.00000
SCALE2 0.000000 0.011141 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022755 0.00000
(ATOM LINES ARE NOT SHOWN.)
END