HEADER TRANSFERASE/PROTEIN BINDING 29-SEP-18 6MM6
TITLE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE A IN COMPLEX WITH
TITLE 2 RYR2 PHOSPHORYLATION DOMAIN (2699-2904)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: C, E;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RYANODINE RECEPTOR 2;
COMPND 9 CHAIN: F, D;
COMPND 10 FRAGMENT: RESIDUES 2699-2904;
COMPND 11 SYNONYM: RYR2,CARDIAC MUSCLE RYANODINE RECEPTOR,CARDIAC MUSCLE
COMPND 12 RYANODINE RECEPTOR-CALCIUM RELEASE CHANNEL,TYPE 2 RYANODINE RECEPTOR;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: RYR2;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, COMPLEX, ION CHANNEL, ENZYME, PROTEIN BINDING, TRANSFERASE-
KEYWDS 2 PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VAN PETEGEM,O.HAJI-GHASSEMI
REVDAT 2 08-JAN-20 6MM6 1 REMARK
REVDAT 1 08-MAY-19 6MM6 0
JRNL AUTH O.HAJI-GHASSEMI,Z.YUCHI,F.VAN PETEGEM
JRNL TITL CAMP-DEPENDENT PROTEIN KINASE A IN COMPLEX WITH RYR2 PEPTIDE
JRNL TITL 2 (2799-2810)
JRNL REF MOL.CELL 2019
JRNL REFN ISSN 1097-2765
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0232
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 53257
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2830
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) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3850
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8512
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 83
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : -0.59000
REMARK 3 B13 (A**2) : -0.85000
REMARK 3 B23 (A**2) : 0.23000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.397
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.264
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.253
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.792
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8876 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 8174 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12014 ; 1.416 ; 1.653
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18962 ; 1.209 ; 1.581
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1035 ; 6.430 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 464 ;34.978 ;22.263
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1570 ;17.515 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;22.316 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1134 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9680 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1910 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : C 18 C 401
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3893 -33.2000-196.6503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0409 T22: 0.2695
REMARK 3 T33: 0.1993 T12: -0.0069
REMARK 3 T13: 0.0820 T23: -0.0682
REMARK 3 L TENSOR
REMARK 3 L11: 3.0444 L22: 0.3192
REMARK 3 L33: 1.2074 L12: -0.2014
REMARK 3 L13: -0.5306 L23: 0.0162
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: 0.0523 S13: -0.0149
REMARK 3 S21: -0.0076 S22: 0.0239 S23: 0.0596
REMARK 3 S31: -0.0296 S32: -0.0807 S33: -0.0082
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 : E 18 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2226 -25.7699-155.6884
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: 0.3407
REMARK 3 T33: 0.1953 T12: 0.0191
REMARK 3 T13: 0.0733 T23: -0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 2.9576 L22: 0.6591
REMARK 3 L33: 1.2815 L12: 0.1895
REMARK 3 L13: -0.6837 L23: 0.2782
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: -0.0867 S13: 0.0162
REMARK 3 S21: 0.0039 S22: 0.0244 S23: -0.1132
REMARK 3 S31: 0.0034 S32: 0.0841 S33: -0.0293
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 : F 2701 F 2904
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1012 -57.2789-149.1702
REMARK 3 T TENSOR
REMARK 3 T11: 0.3198 T22: 0.5810
REMARK 3 T33: 0.2768 T12: -0.0022
REMARK 3 T13: 0.1161 T23: -0.1192
REMARK 3 L TENSOR
REMARK 3 L11: 2.4025 L22: 1.8191
REMARK 3 L33: 1.6937 L12: 0.5920
REMARK 3 L13: -0.4703 L23: -0.9915
REMARK 3 S TENSOR
REMARK 3 S11: -0.1181 S12: 0.3990 S13: -0.1159
REMARK 3 S21: -0.6269 S22: 0.0513 S23: 0.0566
REMARK 3 S31: 0.2289 S32: -0.1073 S33: 0.0668
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 2700 D 2904
REMARK 3 ORIGIN FOR THE GROUP (A): 80.7731 -65.2663-203.4741
REMARK 3 T TENSOR
REMARK 3 T11: 0.3275 T22: 0.4465
REMARK 3 T33: 0.3138 T12: 0.0218
REMARK 3 T13: 0.1197 T23: -0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 3.0244 L22: 1.3056
REMARK 3 L33: 2.1066 L12: -0.9403
REMARK 3 L13: -1.0100 L23: 1.1926
REMARK 3 S TENSOR
REMARK 3 S11: -0.1027 S12: -0.2519 S13: -0.1338
REMARK 3 S21: 0.4958 S22: 0.0965 S23: -0.0702
REMARK 3 S31: 0.3727 S32: 0.1803 S33: 0.0062
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6MM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237189.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-18
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 : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
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 : 56090
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.73500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6MM5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M HEPES, 0.05 M KCL, 0.01M MGCL2,
REMARK 280 15% (W/V) PEG 6K, AND 25% (V/V) ETHYLENE GLYCOL, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SER C 12
REMARK 465 ASN C 13
REMARK 465 ALA C 14
REMARK 465 VAL C 15
REMARK 465 LYS C 16
REMARK 465 GLU C 17
REMARK 465 LYS C 319
REMARK 465 GLY C 320
REMARK 465 PRO C 321
REMARK 465 GLY C 322
REMARK 465 ASP C 323
REMARK 465 THR C 324
REMARK 465 SER C 325
REMARK 465 ASN C 326
REMARK 465 PHE C 327
REMARK 465 ASP C 328
REMARK 465 ASP C 329
REMARK 465 SER E 12
REMARK 465 ASN E 13
REMARK 465 ALA E 14
REMARK 465 VAL E 15
REMARK 465 LYS E 16
REMARK 465 GLU E 17
REMARK 465 LYS E 319
REMARK 465 GLY E 320
REMARK 465 PRO E 321
REMARK 465 GLY E 322
REMARK 465 ASP E 323
REMARK 465 THR E 324
REMARK 465 SER E 325
REMARK 465 ASN E 326
REMARK 465 PHE E 327
REMARK 465 ASP E 328
REMARK 465 ASP E 329
REMARK 465 TYR E 330
REMARK 465 GLU E 331
REMARK 465 SER F 2696
REMARK 465 ASN F 2697
REMARK 465 ALA F 2698
REMARK 465 ASN F 2699
REMARK 465 PHE F 2700
REMARK 465 GLU F 2860
REMARK 465 SER F 2861
REMARK 465 LYS F 2862
REMARK 465 GLY F 2863
REMARK 465 GLY F 2864
REMARK 465 GLY F 2865
REMARK 465 SER D 2696
REMARK 465 ASN D 2697
REMARK 465 ALA D 2698
REMARK 465 ASN D 2699
REMARK 465 GLY D 2864
REMARK 465 GLY D 2865
REMARK 465 ASN D 2866
REMARK 465 HIS D 2867
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 PHE C 18 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE C 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR C 330 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE E 18 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU E 19 CG CD1 CD2
REMARK 470 LYS E 21 CG CD CE NZ
REMARK 470 GLU E 86 CG CD OE1 OE2
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU E 332 CG CD OE1 OE2
REMARK 470 ASN F2701 CG OD1 ND2
REMARK 470 LYS F2715 CG CD CE NZ
REMARK 470 SER F2749 OG
REMARK 470 SER F2750 OG
REMARK 470 LYS F2765 CG CD CE NZ
REMARK 470 GLN F2811 CG CD OE1 NE2
REMARK 470 LYS F2854 CG CD CE NZ
REMARK 470 LYS F2855 CG CD CE NZ
REMARK 470 ASN F2866 CG OD1 ND2
REMARK 470 ILE D2752 CG1 CG2 CD1
REMARK 470 LYS D2760 CG CD CE NZ
REMARK 470 ASP D2815 CG OD1 OD2
REMARK 470 LYS D2862 CG CD CE NZ
REMARK 470 LYS D2883 CG CD CE NZ
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 ARG C 165 28.18 44.91
REMARK 500 ASP C 166 24.46 -142.81
REMARK 500 LYS C 168 156.66 173.27
REMARK 500 ASP C 175 -168.41 -75.42
REMARK 500 LEU C 273 41.50 -82.87
REMARK 500 ARG E 165 27.02 44.41
REMARK 500 ASP E 166 24.12 -141.85
REMARK 500 LYS E 168 157.55 173.51
REMARK 500 ASP E 175 -166.80 -76.38
REMARK 500 LEU E 273 40.44 -82.62
REMARK 500 THR F2791 155.82 -48.04
REMARK 500 ILE F2814 12.19 -143.46
REMARK 500 LYS F2856 25.01 -72.87
REMARK 500 SER D2833 159.81 -43.39
REMARK 500 LYS D2862 64.95 -64.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 3001
DBREF 6MM6 C 15 350 UNP P05132 KAPCA_MOUSE 16 351
DBREF 6MM6 E 15 350 UNP P05132 KAPCA_MOUSE 16 351
DBREF 6MM6 F 2699 2904 UNP E9Q401 RYR2_MOUSE 2699 2904
DBREF 6MM6 D 2699 2904 UNP E9Q401 RYR2_MOUSE 2699 2904
SEQADV 6MM6 SER C 12 UNP P05132 EXPRESSION TAG
SEQADV 6MM6 ASN C 13 UNP P05132 EXPRESSION TAG
SEQADV 6MM6 ALA C 14 UNP P05132 EXPRESSION TAG
SEQADV 6MM6 SER E 12 UNP P05132 EXPRESSION TAG
SEQADV 6MM6 ASN E 13 UNP P05132 EXPRESSION TAG
SEQADV 6MM6 ALA E 14 UNP P05132 EXPRESSION TAG
SEQADV 6MM6 SER F 2696 UNP E9Q401 EXPRESSION TAG
SEQADV 6MM6 ASN F 2697 UNP E9Q401 EXPRESSION TAG
SEQADV 6MM6 ALA F 2698 UNP E9Q401 EXPRESSION TAG
SEQADV 6MM6 ALA F 2879 UNP E9Q401 LYS 2879 ENGINEERED MUTATION
SEQADV 6MM6 SER D 2696 UNP E9Q401 EXPRESSION TAG
SEQADV 6MM6 ASN D 2697 UNP E9Q401 EXPRESSION TAG
SEQADV 6MM6 ALA D 2698 UNP E9Q401 EXPRESSION TAG
SEQADV 6MM6 ALA D 2879 UNP E9Q401 LYS 2879 ENGINEERED MUTATION
SEQRES 1 C 339 SER ASN ALA VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU
SEQRES 2 C 339 ASP PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR
SEQRES 3 C 339 ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY
SEQRES 4 C 339 THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS
SEQRES 5 C 339 GLU SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS
SEQRES 6 C 339 GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU
SEQRES 7 C 339 ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE
SEQRES 8 C 339 LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN
SEQRES 9 C 339 LEU TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET
SEQRES 10 C 339 PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO
SEQRES 11 C 339 HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE
SEQRES 12 C 339 GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU
SEQRES 13 C 339 LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE
SEQRES 14 C 339 GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY
SEQRES 15 C 339 ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA
SEQRES 16 C 339 PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL
SEQRES 17 C 339 ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA
SEQRES 18 C 339 ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN
SEQRES 19 C 339 ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO
SEQRES 20 C 339 SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN
SEQRES 21 C 339 LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU
SEQRES 22 C 339 LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE
SEQRES 23 C 339 ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL
SEQRES 24 C 339 GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP
SEQRES 25 C 339 THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG
SEQRES 26 C 339 VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU
SEQRES 27 C 339 PHE
SEQRES 1 E 339 SER ASN ALA VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU
SEQRES 2 E 339 ASP PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR
SEQRES 3 E 339 ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY
SEQRES 4 E 339 THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS
SEQRES 5 E 339 GLU SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS
SEQRES 6 E 339 GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU
SEQRES 7 E 339 ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE
SEQRES 8 E 339 LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN
SEQRES 9 E 339 LEU TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET
SEQRES 10 E 339 PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO
SEQRES 11 E 339 HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE
SEQRES 12 E 339 GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU
SEQRES 13 E 339 LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE
SEQRES 14 E 339 GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY
SEQRES 15 E 339 ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA
SEQRES 16 E 339 PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL
SEQRES 17 E 339 ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA
SEQRES 18 E 339 ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN
SEQRES 19 E 339 ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO
SEQRES 20 E 339 SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN
SEQRES 21 E 339 LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU
SEQRES 22 E 339 LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE
SEQRES 23 E 339 ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL
SEQRES 24 E 339 GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP
SEQRES 25 E 339 THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG
SEQRES 26 E 339 VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU
SEQRES 27 E 339 PHE
SEQRES 1 F 209 SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER
SEQRES 2 F 209 ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN
SEQRES 3 F 209 LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MET ASP
SEQRES 4 F 209 LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER
SEQRES 5 F 209 ASP SER SER LYS ILE GLN PRO LEU MET LYS PRO TYR LYS
SEQRES 6 F 209 LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO
SEQRES 7 F 209 ILE LYS GLU SER LEU LYS THR MET LEU ALA TRP GLY TRP
SEQRES 8 F 209 ARG ILE GLU ARG THR ARG GLU GLY ASP SER MET ALA LEU
SEQRES 9 F 209 TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL
SEQRES 10 F 209 SER ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE
SEQRES 11 F 209 ASP MET SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA
SEQRES 12 F 209 MET ALA GLU MET MET ALA GLU ASN TYR HIS ASN ILE TRP
SEQRES 13 F 209 ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY
SEQRES 14 F 209 GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR
SEQRES 15 F 209 ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP
SEQRES 16 F 209 ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER
SEQRES 17 F 209 ARG
SEQRES 1 D 209 SER ASN ALA ASN PHE ASN PRO GLN PRO VAL ASP THR SER
SEQRES 2 D 209 ASN ILE THR ILE PRO GLU LYS LEU GLU TYR PHE ILE ASN
SEQRES 3 D 209 LYS TYR ALA GLU HIS SER HIS ASP LYS TRP SER MET ASP
SEQRES 4 D 209 LYS LEU ALA ASN GLY TRP ILE TYR GLY GLU ILE TYR SER
SEQRES 5 D 209 ASP SER SER LYS ILE GLN PRO LEU MET LYS PRO TYR LYS
SEQRES 6 D 209 LEU LEU SER GLU LYS GLU LYS GLU ILE TYR ARG TRP PRO
SEQRES 7 D 209 ILE LYS GLU SER LEU LYS THR MET LEU ALA TRP GLY TRP
SEQRES 8 D 209 ARG ILE GLU ARG THR ARG GLU GLY ASP SER MET ALA LEU
SEQRES 9 D 209 TYR ASN ARG THR ARG ARG ILE SER GLN THR SER GLN VAL
SEQRES 10 D 209 SER ILE ASP ALA ALA HIS GLY TYR SER PRO ARG ALA ILE
SEQRES 11 D 209 ASP MET SER ASN VAL THR LEU SER ARG ASP LEU HIS ALA
SEQRES 12 D 209 MET ALA GLU MET MET ALA GLU ASN TYR HIS ASN ILE TRP
SEQRES 13 D 209 ALA LYS LYS LYS LYS LEU GLU LEU GLU SER LYS GLY GLY
SEQRES 14 D 209 GLY ASN HIS PRO LEU LEU VAL PRO TYR ASP THR LEU THR
SEQRES 15 D 209 ALA ALA GLU LYS ALA LYS ASP ARG GLU LYS ALA GLN ASP
SEQRES 16 D 209 ILE PHE LYS PHE LEU GLN ILE SER GLY TYR VAL VAL SER
SEQRES 17 D 209 ARG
MODRES 6MM6 TPO C 197 THR MODIFIED RESIDUE
MODRES 6MM6 SEP C 338 SER MODIFIED RESIDUE
MODRES 6MM6 TPO E 197 THR MODIFIED RESIDUE
MODRES 6MM6 SEP E 338 SER MODIFIED RESIDUE
HET TPO C 197 11
HET SEP C 338 10
HET TPO E 197 11
HET SEP E 338 10
HET ACT C 401 4
HET ANP C 402 62
HET PGE C 403 10
HET CL C 404 1
HET ANP E 401 62
HET EDO E 402 4
HET CL E 403 1
HET CL F3001 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM ACT ACETATE ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 5 ACT C2 H3 O2 1-
FORMUL 6 ANP 2(C10 H17 N6 O12 P3)
FORMUL 7 PGE C6 H14 O4
FORMUL 8 CL 3(CL 1-)
FORMUL 10 EDO C2 H6 O2
FORMUL 13 HOH *365(H2 O)
HELIX 1 AA1 LEU C 19 THR C 32 1 14
HELIX 2 AA2 GLN C 39 ASP C 41 5 3
HELIX 3 AA3 LYS C 76 LEU C 82 1 7
HELIX 4 AA4 GLN C 84 VAL C 98 1 15
HELIX 5 AA5 MET C 128 GLY C 136 1 9
HELIX 6 AA6 SER C 139 LEU C 160 1 22
HELIX 7 AA7 LYS C 168 GLU C 170 5 3
HELIX 8 AA8 THR C 201 LEU C 205 5 5
HELIX 9 AA9 ALA C 206 LEU C 211 1 6
HELIX 10 AB1 LYS C 217 GLY C 234 1 18
HELIX 11 AB2 GLN C 242 GLY C 253 1 12
HELIX 12 AB3 SER C 262 LEU C 273 1 12
HELIX 13 AB4 ASP C 276 ARG C 280 5 5
HELIX 14 AB5 VAL C 288 ASN C 293 1 6
HELIX 15 AB6 HIS C 294 ALA C 298 5 5
HELIX 16 AB7 ASP C 301 GLN C 307 1 7
HELIX 17 AB8 LEU E 19 THR E 32 1 14
HELIX 18 AB9 GLN E 39 ASP E 41 5 3
HELIX 19 AC1 LYS E 76 LEU E 82 1 7
HELIX 20 AC2 GLN E 84 GLN E 96 1 13
HELIX 21 AC3 MET E 128 GLY E 136 1 9
HELIX 22 AC4 SER E 139 LEU E 160 1 22
HELIX 23 AC5 LYS E 168 GLU E 170 5 3
HELIX 24 AC6 THR E 201 LEU E 205 5 5
HELIX 25 AC7 ALA E 206 LEU E 211 1 6
HELIX 26 AC8 LYS E 217 GLY E 234 1 18
HELIX 27 AC9 GLN E 242 GLY E 253 1 12
HELIX 28 AD1 SER E 262 LEU E 273 1 12
HELIX 29 AD2 ASP E 276 ARG E 280 5 5
HELIX 30 AD3 VAL E 288 ASN E 293 1 6
HELIX 31 AD4 HIS E 294 ALA E 298 5 5
HELIX 32 AD5 ASP E 301 GLN E 307 1 7
HELIX 33 AD6 PRO F 2713 LYS F 2715 5 3
HELIX 34 AD7 LEU F 2716 ASN F 2738 1 23
HELIX 35 AD8 GLN F 2753 LYS F 2757 5 5
HELIX 36 AD9 PRO F 2758 LEU F 2762 5 5
HELIX 37 AE1 SER F 2763 TRP F 2784 1 22
HELIX 38 AE2 ASP F 2795 TYR F 2800 1 6
HELIX 39 AE3 SER F 2833 LYS F 2856 1 24
HELIX 40 AE4 PRO F 2872 LEU F 2876 5 5
HELIX 41 AE5 THR F 2877 SER F 2898 1 22
HELIX 42 AE6 PRO D 2713 LYS D 2715 5 3
HELIX 43 AE7 LEU D 2716 ASN D 2738 1 23
HELIX 44 AE8 PRO D 2758 LEU D 2762 5 5
HELIX 45 AE9 SER D 2763 TRP D 2784 1 22
HELIX 46 AF1 SER D 2833 GLU D 2860 1 28
HELIX 47 AF2 PRO D 2872 LEU D 2876 5 5
HELIX 48 AF3 THR D 2877 SER D 2898 1 22
SHEET 1 AA1 5 PHE C 43 THR C 51 0
SHEET 2 AA1 5 ARG C 56 HIS C 62 -1 O LEU C 59 N LYS C 47
SHEET 3 AA1 5 HIS C 68 ASP C 75 -1 O ILE C 73 N ARG C 56
SHEET 4 AA1 5 ASN C 115 GLU C 121 -1 O MET C 120 N ALA C 70
SHEET 5 AA1 5 LEU C 106 LYS C 111 -1 N PHE C 108 O VAL C 119
SHEET 1 AA2 3 GLY C 126 GLU C 127 0
SHEET 2 AA2 3 LEU C 172 ILE C 174 -1 O ILE C 174 N GLY C 126
SHEET 3 AA2 3 ILE C 180 VAL C 182 -1 O GLN C 181 N LEU C 173
SHEET 1 AA3 2 LEU C 162 ILE C 163 0
SHEET 2 AA3 2 LYS C 189 ARG C 190 -1 O LYS C 189 N ILE C 163
SHEET 1 AA4 2 LEU C 198 GLY C 200 0
SHEET 2 AA4 2 GLN D2808 SER D2810 -1 O GLN D2808 N GLY C 200
SHEET 1 AA5 5 PHE E 43 THR E 51 0
SHEET 2 AA5 5 ARG E 56 HIS E 62 -1 O LEU E 59 N LYS E 47
SHEET 3 AA5 5 HIS E 68 ASP E 75 -1 O ILE E 73 N ARG E 56
SHEET 4 AA5 5 ASN E 115 GLU E 121 -1 O MET E 120 N ALA E 70
SHEET 5 AA5 5 LEU E 106 LYS E 111 -1 N PHE E 108 O VAL E 119
SHEET 1 AA6 3 GLY E 126 GLU E 127 0
SHEET 2 AA6 3 LEU E 172 ILE E 174 -1 O ILE E 174 N GLY E 126
SHEET 3 AA6 3 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
SHEET 1 AA7 2 LEU E 162 ILE E 163 0
SHEET 2 AA7 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
SHEET 1 AA8 2 CYS E 199 GLY E 200 0
SHEET 2 AA8 2 GLN F2808 THR F2809 -1 O GLN F2808 N GLY E 200
SHEET 1 AA9 2 ARG F2787 ARG F2790 0
SHEET 2 AA9 2 TYR F2900 SER F2903 -1 O VAL F2901 N GLU F2789
SHEET 1 AB1 2 ARG D2787 ARG D2790 0
SHEET 2 AB1 2 TYR D2900 SER D2903 -1 O VAL D2901 N GLU D2789
LINK C TRP C 196 N TPO C 197 1555 1555 1.34
LINK C TPO C 197 N LEU C 198 1555 1555 1.34
LINK C VAL C 337 N SEP C 338 1555 1555 1.33
LINK C SEP C 338 N ILE C 339 1555 1555 1.34
LINK C TRP E 196 N TPO E 197 1555 1555 1.33
LINK C TPO E 197 N LEU E 198 1555 1555 1.34
LINK C VAL E 337 N SEP E 338 1555 1555 1.34
LINK C SEP E 338 N ILE E 339 1555 1555 1.34
SITE 1 AC1 4 TYR C 235 PHE C 239 ALA D2798 TYR D2800
SITE 1 AC2 13 THR C 51 GLY C 52 SER C 53 VAL C 57
SITE 2 AC2 13 ALA C 70 LYS C 72 GLU C 121 TYR C 122
SITE 3 AC2 13 VAL C 123 GLU C 127 HOH C 534 HOH C 588
SITE 4 AC2 13 ARG D2804
SITE 1 AC3 7 GLU C 155 HIS C 158 SER C 159 LYS C 217
SITE 2 AC3 7 TRP C 221 GLY C 282 HOH C 538
SITE 1 AC4 2 GLY C 200 GLN D2808
SITE 1 AC5 14 LEU E 49 THR E 51 GLY E 52 SER E 53
SITE 2 AC5 14 VAL E 57 ALA E 70 LYS E 72 GLU E 121
SITE 3 AC5 14 TYR E 122 VAL E 123 ASP E 184 HOH E 514
SITE 4 AC5 14 HOH E 516 HOH E 574
SITE 1 AC6 6 LYS E 72 GLU E 91 LEU E 95 MET E 118
SITE 2 AC6 6 MET E 120 THR E 183
SITE 1 AC7 3 TRP D2786 ARG D2904 GLU E 140
SITE 1 AC8 4 GLU C 140 TRP F2786 MET F2842 ARG F2904
CRYST1 58.451 74.944 88.690 105.51 90.14 94.39 P 1 2
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 0.017108 0.001314 0.000410 0.00000
SCALE2 0.000000 0.013383 0.003728 0.00000
SCALE3 0.000000 0.000000 0.011705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
