HEADER TRANSFERASE 02-DEC-13 4NTS
TITLE APO STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
TITLE 2 KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 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
KEYWDS PROTEIN KINASE FOLD, PHOSPHORYL TRANSFERASE, KINASE, REGULATORY
KEYWDS 2 SUBUNIT OF PKA, PKI, PHOSPHORYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.BASTIDAS,J.WU,S.S.TAYLOR
REVDAT 2 28-JAN-15 4NTS 1 JRNL
REVDAT 1 15-OCT-14 4NTS 0
JRNL AUTH A.C.BASTIDAS,J.WU,S.S.TAYLOR
JRNL TITL MOLECULAR FEATURES OF PRODUCT RELEASE FOR THE PKA CATALYTIC
JRNL TITL 2 CYCLE.
JRNL REF BIOCHEMISTRY V. 54 2 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 25077557
JRNL DOI 10.1021/BI500684C
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 18013
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 967
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1354
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5223
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.43000
REMARK 3 B22 (A**2) : -5.38000
REMARK 3 B33 (A**2) : -3.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.64000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.088
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.468
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.454
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 54.421
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5361 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7300 ; 1.013 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 684 ; 4.972 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 238 ;39.089 ;23.739
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 771 ;17.373 ;15.039
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;21.362 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 797 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4157 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 126 6
REMARK 3 1 B 10 B 126 6
REMARK 3 2 A 327 A 350 6
REMARK 3 2 B 327 B 350 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 989 ; 0.560 ; 5.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 127 A 326 4
REMARK 3 1 B 127 B 326 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1540 ; 0.450 ; 0.500
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 126
REMARK 3 RESIDUE RANGE : A 327 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7985 56.5646 62.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.4658 T22: 0.3499
REMARK 3 T33: 0.4422 T12: 0.0533
REMARK 3 T13: 0.1346 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 3.3390 L22: 3.6724
REMARK 3 L33: 5.9288 L12: 0.1922
REMARK 3 L13: 1.0381 L23: 0.3431
REMARK 3 S TENSOR
REMARK 3 S11: -0.1503 S12: -0.1029 S13: 0.0819
REMARK 3 S21: 0.6323 S22: 0.1873 S23: 0.3200
REMARK 3 S31: 0.2651 S32: -0.3445 S33: -0.0371
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 126
REMARK 3 RESIDUE RANGE : B 327 B 350
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0126 11.6738 23.5274
REMARK 3 T TENSOR
REMARK 3 T11: 0.6974 T22: 0.3572
REMARK 3 T33: 0.3630 T12: 0.0660
REMARK 3 T13: 0.0904 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 2.0498 L22: 6.4690
REMARK 3 L33: 5.0177 L12: 0.3812
REMARK 3 L13: -0.6180 L23: -1.8665
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: -0.0135 S13: 0.0871
REMARK 3 S21: 1.1849 S22: 0.1880 S23: 0.5525
REMARK 3 S31: -0.7621 S32: -0.3625 S33: -0.2305
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 127 A 300
REMARK 3 RESIDUE RANGE : A 301 A 326
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6262 44.1736 40.9759
REMARK 3 T TENSOR
REMARK 3 T11: 0.2030 T22: 0.4706
REMARK 3 T33: 0.3153 T12: -0.1154
REMARK 3 T13: -0.0826 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 4.0185 L22: 6.6809
REMARK 3 L33: 5.2057 L12: -1.1002
REMARK 3 L13: -0.5023 L23: 1.4189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: 0.3395 S13: -0.2595
REMARK 3 S21: -0.1330 S22: -0.1183 S23: 0.4855
REMARK 3 S31: 0.8882 S32: -0.4588 S33: 0.1661
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 127 B 300
REMARK 3 RESIDUE RANGE : B 301 B 326
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3916 23.9983 1.8924
REMARK 3 T TENSOR
REMARK 3 T11: 0.0600 T22: 0.3045
REMARK 3 T33: 0.2854 T12: -0.0759
REMARK 3 T13: -0.0433 T23: -0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 2.3451 L22: 8.8958
REMARK 3 L33: 3.4095 L12: -1.1263
REMARK 3 L13: 1.1241 L23: -2.8589
REMARK 3 S TENSOR
REMARK 3 S11: 0.1519 S12: -0.0143 S13: 0.0306
REMARK 3 S21: 0.1019 S22: -0.0863 S23: 0.1224
REMARK 3 S31: -0.1332 S32: -0.0598 S33: -0.0656
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 4NTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19014
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 61.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1J3H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% MPD, 0.1 M BICINE, 150 MM AMMONIUM
REMARK 280 ACETATE, 10 MM DTT, 9% METHANOL ADDED TO THE WELL SOLUTION, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 71.30500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 CYS A 7
REMARK 465 GLY B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 CYS B 7
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 LYS A 8 CG CD CE NZ
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 GLN A 12 CG CD OE1 NE2
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 SER A 14 OG
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 ASP A 44 CG OD1 OD2
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 46 CD1
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 THR A 51 OG1 CG2
REMARK 470 VAL A 60 CG1 CG2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 LYS A 63 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 ILE A 73 CD1
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 81 CE NZ
REMARK 470 LEU A 82 CG CD1 CD2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 SER A 114 OG
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 ILE A 135 CD1
REMARK 470 VAL A 191 CG1 CG2
REMARK 470 ILE A 210 CD1
REMARK 470 LYS A 213 CG CD CE NZ
REMARK 470 ILE A 228 CD1
REMARK 470 GLN A 242 CD OE1 NE2
REMARK 470 ILE A 246 CD1
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 SER A 252 OG
REMARK 470 VAL A 255 CG1 CG2
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 SER A 263 OG
REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 275 CG1 CG2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 ILE A 291 CD1
REMARK 470 LYS A 295 CG CD CE NZ
REMARK 470 ILE A 303 CD1
REMARK 470 GLU A 311 CG CD OE1 OE2
REMARK 470 ILE A 315 CD1
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 PRO A 321 CG CD
REMARK 470 ASP A 323 CG OD1 OD2
REMARK 470 THR A 324 OG1 CG2
REMARK 470 SER A 325 OG
REMARK 470 ASN A 326 CG OD1 ND2
REMARK 470 PHE A 327 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 328 CG OD1 OD2
REMARK 470 ASP A 329 CG OD1 OD2
REMARK 470 TYR A 330 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 332 CG CD OE1 OE2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 ILE A 335 CD1
REMARK 470 VAL A 337 CG1 CG2
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 SER B 10 OG
REMARK 470 GLU B 11 CG CD OE1 OE2
REMARK 470 GLN B 12 CG CD OE1 NE2
REMARK 470 SER B 14 OG
REMARK 470 VAL B 15 CG1 CG2
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 GLU B 17 CG CD OE1 OE2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 ASP B 25 CG OD1 OD2
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 46 CD1
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 THR B 51 OG1 CG2
REMARK 470 SER B 53 OG
REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 57 CG1 CG2
REMARK 470 LEU B 59 CG CD1 CD2
REMARK 470 VAL B 60 CG1 CG2
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 GLN B 77 CG CD OE1 NE2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 VAL B 79 CG1 CG2
REMARK 470 LYS B 81 CG CD CE NZ
REMARK 470 LEU B 82 CG CD1 CD2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 GLU B 86 CG CD OE1 OE2
REMARK 470 SER B 109 OG
REMARK 470 SER B 114 OG
REMARK 470 ARG B 133 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 135 CD1
REMARK 470 ILE B 150 CD1
REMARK 470 GLN B 176 CG CD OE1 NE2
REMARK 470 LEU B 198 CG CD1 CD2
REMARK 470 ILE B 210 CD1
REMARK 470 SER B 212 OG
REMARK 470 LYS B 213 CG CD CE NZ
REMARK 470 ILE B 244 CG1 CG2 CD1
REMARK 470 GLN B 245 CG CD OE1 NE2
REMARK 470 ILE B 246 CD1
REMARK 470 LYS B 249 CG CD CE NZ
REMARK 470 ILE B 250 CD1
REMARK 470 SER B 252 OG
REMARK 470 VAL B 255 CG1 CG2
REMARK 470 SER B 263 OG
REMARK 470 LEU B 268 CD1 CD2
REMARK 470 THR B 278 OG1 CG2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 LYS B 295 CD CE NZ
REMARK 470 ILE B 303 CD1
REMARK 470 LYS B 309 CG CD CE NZ
REMARK 470 GLU B 311 CG CD OE1 OE2
REMARK 470 ILE B 315 CD1
REMARK 470 LYS B 317 CG CD CE NZ
REMARK 470 LYS B 319 CG CD CE NZ
REMARK 470 PRO B 321 CG CD
REMARK 470 ASP B 323 CG OD1 OD2
REMARK 470 THR B 324 OG1 CG2
REMARK 470 SER B 325 OG
REMARK 470 ASN B 326 CG OD1 ND2
REMARK 470 PHE B 327 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 328 CG OD1 OD2
REMARK 470 ASP B 329 CG OD1 OD2
REMARK 470 TYR B 330 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 331 CG CD OE1 OE2
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 GLU B 334 CG CD OE1 OE2
REMARK 470 ILE B 335 CG1 CG2 CD1
REMARK 470 ILE B 339 CG1 CG2 CD1
REMARK 470 GLU B 341 CG CD OE1 OE2
REMARK 470 LYS B 342 CG CD CE NZ
REMARK 470 LYS B 345 CG CD CE NZ
REMARK 470 GLU B 349 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU B 132 O ILE B 135 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 10 -30.18 84.32
REMARK 500 ASP A 166 38.99 -151.53
REMARK 500 ASN A 216 -157.37 -153.59
REMARK 500 ASN A 283 52.03 -114.28
REMARK 500 LEU A 284 -160.72 -125.51
REMARK 500 LYS A 317 52.24 -98.87
REMARK 500 THR A 324 -132.79 45.45
REMARK 500 ASP A 328 -112.44 44.50
REMARK 500 ASP A 329 -93.46 -126.99
REMARK 500 GLU A 331 -160.85 -125.41
REMARK 500 GLU A 333 125.58 -174.87
REMARK 500 ILE B 46 75.01 -116.50
REMARK 500 LYS B 47 157.30 80.74
REMARK 500 ASP B 112 -164.97 -123.31
REMARK 500 ARG B 165 4.32 58.73
REMARK 500 ASP B 166 54.85 -149.40
REMARK 500 ASN B 216 -159.04 -145.91
REMARK 500 LEU B 273 35.06 -76.93
REMARK 500 PHE B 318 -171.88 73.44
REMARK 500 LYS B 319 -6.54 91.65
REMARK 500 ASP B 328 -169.56 -69.38
REMARK 500 GLU B 331 43.54 -69.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MYR A 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J3H RELATED DB: PDB
REMARK 900 PREVIOUS APO STRUCTURE OF THE C-SUBUNIT
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C-SUBUNIT WITH ATP AND IP20
REMARK 900 RELATED ID: 1CMK RELATED DB: PDB
REMARK 900 OPEN STRUCTURE OF THE C-SUBUNIT BOUND TO IP20
REMARK 900 RELATED ID: 1SYK RELATED DB: PDB
REMARK 900 APO STRUCTURE OF THE C-SUBUNIT WITH E230Q MUTATION
REMARK 900 RELATED ID: 4DFY RELATED DB: PDB
REMARK 900 APO STRUCTURE OF THE C-SUBUNIT LACKING PHOSPHORYLATION ON
REMARK 900 THE ACTIVATION LOOP
DBREF 4NTS A 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4NTS B 1 350 UNP P05132 KAPCA_MOUSE 2 351
SEQADV 4NTS CYS A 7 UNP P05132 LYS 8 ENGINEERED MUTATION
SEQADV 4NTS CYS B 7 UNP P05132 LYS 8 ENGINEERED MUTATION
SEQRES 1 A 350 GLY ASN ALA ALA ALA ALA CYS LYS GLY SER GLU GLN GLU
SEQRES 2 A 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 A 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 A 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 A 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 A 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 A 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 A 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 A 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 A 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 A 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 A 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 A 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 A 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 A 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 A 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 A 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 A 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 A 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 A 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 A 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 A 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 A 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 A 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 A 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 A 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 A 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 B 350 GLY ASN ALA ALA ALA ALA CYS LYS GLY SER GLU GLN GLU
SEQRES 2 B 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 B 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 B 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 B 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 B 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 B 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 B 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 B 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 B 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 B 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 B 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 B 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 B 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 B 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 B 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 B 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 B 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 B 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 B 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 B 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 B 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 B 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 B 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 B 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 B 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 B 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
MODRES 4NTS TPO A 197 THR PHOSPHOTHREONINE
MODRES 4NTS SEP A 338 SER PHOSPHOSERINE
MODRES 4NTS TPO B 197 THR PHOSPHOTHREONINE
MODRES 4NTS SEP B 338 SER PHOSPHOSERINE
HET TPO A 197 11
HET SEP A 338 10
HET TPO B 197 11
HET SEP B 338 10
HET MYR A 401 4
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM MYR MYRISTIC ACID
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 MYR C14 H28 O2
HELIX 1 1 GLU A 13 THR A 32 1 20
HELIX 2 2 GLN A 39 ASP A 41 5 3
HELIX 3 3 LYS A 76 LYS A 83 1 8
HELIX 4 4 GLN A 84 VAL A 98 1 15
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SER A 139 LEU A 160 1 22
HELIX 7 7 LYS A 168 GLU A 170 5 3
HELIX 8 8 THR A 201 LEU A 205 5 5
HELIX 9 9 ALA A 206 SER A 212 1 7
HELIX 10 10 LYS A 217 GLY A 234 1 18
HELIX 11 11 GLN A 242 SER A 252 1 11
HELIX 12 12 SER A 262 LEU A 273 1 12
HELIX 13 13 VAL A 288 ASN A 293 1 6
HELIX 14 14 HIS A 294 ALA A 298 5 5
HELIX 15 15 ASP A 301 ARG A 308 1 8
HELIX 16 16 GLU B 13 THR B 32 1 20
HELIX 17 17 GLN B 39 ASP B 41 5 3
HELIX 18 18 LYS B 76 LEU B 82 1 7
HELIX 19 19 GLN B 84 VAL B 98 1 15
HELIX 20 20 GLU B 127 ILE B 135 1 9
HELIX 21 21 SER B 139 LEU B 160 1 22
HELIX 22 22 LYS B 168 GLU B 170 5 3
HELIX 23 23 THR B 201 LEU B 205 5 5
HELIX 24 24 ALA B 206 LEU B 211 1 6
HELIX 25 25 ALA B 218 GLY B 234 1 17
HELIX 26 26 GLN B 242 GLY B 253 1 12
HELIX 27 27 SER B 262 LEU B 273 1 12
HELIX 28 28 VAL B 288 ASN B 293 1 6
HELIX 29 29 HIS B 294 ALA B 298 5 5
HELIX 30 30 ASP B 301 GLN B 307 1 7
SHEET 1 A 5 PHE A 43 THR A 51 0
SHEET 2 A 5 GLY A 55 HIS A 62 -1 O VAL A 57 N GLY A 50
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O ILE A 73 N ARG A 56
SHEET 4 A 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 A 5 LEU A 106 LYS A 111 -1 N PHE A 110 O TYR A 117
SHEET 1 B 2 LEU A 162 ILE A 163 0
SHEET 2 B 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 C 2 LEU A 172 ILE A 174 0
SHEET 2 C 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
SHEET 1 D 5 PHE B 43 THR B 51 0
SHEET 2 D 5 GLY B 55 HIS B 62 -1 O LYS B 61 N ASP B 44
SHEET 3 D 5 HIS B 68 ASP B 75 -1 O ILE B 73 N ARG B 56
SHEET 4 D 5 ASN B 115 GLU B 121 -1 O LEU B 116 N LEU B 74
SHEET 5 D 5 LEU B 106 LYS B 111 -1 N PHE B 110 O TYR B 117
SHEET 1 E 2 LEU B 162 ILE B 163 0
SHEET 2 E 2 LYS B 189 ARG B 190 -1 O LYS B 189 N ILE B 163
SHEET 1 F 2 LEU B 172 ILE B 174 0
SHEET 2 F 2 ILE B 180 VAL B 182 -1 O GLN B 181 N LEU B 173
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
LINK C TRP B 196 N TPO B 197 1555 1555 1.34
LINK C TPO B 197 N LEU B 198 1555 1555 1.33
LINK C VAL B 337 N SEP B 338 1555 1555 1.33
LINK C SEP B 338 N ILE B 339 1555 1555 1.33
SITE 1 AC1 2 PHE A 18 GLU A 155
CRYST1 50.960 142.610 63.160 90.00 103.65 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 0.019623 0.000000 0.004765 0.00000
SCALE2 0.000000 0.007012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016293 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
