HEADER SIGNALING PROTEIN 19-AUG-01 1JSY
TITLE CRYSTAL STRUCTURE OF BOVINE ARRESTIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOVINE ARRESTIN-2 (FULL LENGTH);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-LYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRCHISB (WITHOUT THE HIS TAG)
KEYWDS NONVISUAL ARRESTINS, BETA-ARRESTINS, DESENSITIZATION, ENDOCYTOSIS,
KEYWDS 2 DOWN-REGULATION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.MILANO,H.C.PACE,Y.M.KIM,C.BRENNER,J.L.BENOVIC
REVDAT 3 16-AUG-23 1JSY 1 REMARK
REVDAT 2 24-FEB-09 1JSY 1 VERSN
REVDAT 1 27-MAR-02 1JSY 0
JRNL AUTH S.K.MILANO,H.C.PACE,Y.M.KIM,C.BRENNER,J.L.BENOVIC
JRNL TITL SCAFFOLDING FUNCTIONS OF ARRESTIN-2 REVEALED BY CRYSTAL
JRNL TITL 2 STRUCTURE AND MUTAGENESIS.
JRNL REF BIOCHEMISTRY V. 41 3321 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11876640
JRNL DOI 10.1021/BI015905J
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 13136
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 SET) : 0.230
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1320
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1821
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 193
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2829
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 76
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 70.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.09000
REMARK 3 B22 (A**2) : -4.09000
REMARK 3 B33 (A**2) : 8.17000
REMARK 3 B12 (A**2) : 8.12000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.47
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.140
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 27.74
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JSY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.948
REMARK 200 MONOCHROMATOR : BENT, TRIANGULAR SI(111)
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 19.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 19.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 7.40000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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: AMORE
REMARK 200 STARTING MODEL: 1CF1; CHAIN B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM FORMATE, POLYPROPYLENE
REMARK 280 GLYCOL 400, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.94933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.97467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.97467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.94933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ASP A 3
REMARK 465 LYS A 4
REMARK 465 GLY A 5
REMARK 465 ARG A 331
REMARK 465 GLY A 332
REMARK 465 GLY A 333
REMARK 465 LEU A 334
REMARK 465 LEU A 335
REMARK 465 GLY A 336
REMARK 465 ASP A 337
REMARK 465 LEU A 338
REMARK 465 ALA A 339
REMARK 465 PRO A 356
REMARK 465 LYS A 357
REMARK 465 GLU A 358
REMARK 465 GLU A 359
REMARK 465 PRO A 360
REMARK 465 PRO A 361
REMARK 465 HIS A 362
REMARK 465 ARG A 363
REMARK 465 GLU A 364
REMARK 465 VAL A 365
REMARK 465 PRO A 366
REMARK 465 GLU A 367
REMARK 465 HIS A 368
REMARK 465 GLU A 369
REMARK 465 THR A 370
REMARK 465 PRO A 371
REMARK 465 VAL A 372
REMARK 465 ASP A 373
REMARK 465 THR A 374
REMARK 465 ASN A 375
REMARK 465 LEU A 376
REMARK 465 ILE A 377
REMARK 465 GLU A 378
REMARK 465 LEU A 379
REMARK 465 ASP A 380
REMARK 465 THR A 381
REMARK 465 ASN A 382
REMARK 465 LYS A 400
REMARK 465 ASP A 401
REMARK 465 ASP A 402
REMARK 465 LYS A 403
REMARK 465 GLU A 404
REMARK 465 GLU A 405
REMARK 465 GLU A 406
REMARK 465 GLU A 407
REMARK 465 ASP A 408
REMARK 465 GLY A 409
REMARK 465 THR A 410
REMARK 465 GLY A 411
REMARK 465 SER A 412
REMARK 465 PRO A 413
REMARK 465 ARG A 414
REMARK 465 LEU A 415
REMARK 465 ASN A 416
REMARK 465 ASP A 417
REMARK 465 ARG A 418
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 ARG A 7 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 65 CG CD NE CZ NH1 NH2
REMARK 470 SER A 86 OG
REMARK 470 ASP A 383 CG OD1 OD2
REMARK 470 ASP A 384 CG OD1 OD2
REMARK 470 ASP A 385 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 269 CB CYS A 269 SG -0.110
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 121 C - N - CA ANGL. DEV. = 9.4 DEGREES
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 PRO A 14 -36.41 -39.97
REMARK 500 HIS A 30 -125.79 -97.33
REMARK 500 GLU A 35 134.07 -38.35
REMARK 500 ASP A 44 76.23 -116.58
REMARK 500 PRO A 45 -38.88 -38.35
REMARK 500 LYS A 49 -96.26 -58.81
REMARK 500 ARG A 51 155.98 -47.39
REMARK 500 ARG A 65 -149.18 -84.59
REMARK 500 LEU A 71 55.01 -104.39
REMARK 500 PHE A 80 149.37 -170.86
REMARK 500 GLN A 85 99.65 -68.66
REMARK 500 PHE A 87 -75.47 -61.14
REMARK 500 PRO A 88 99.63 -60.91
REMARK 500 ASP A 93 45.21 -77.41
REMARK 500 LEU A 97 123.17 89.84
REMARK 500 SER A 126 102.60 -47.59
REMARK 500 ASP A 135 128.01 -34.13
REMARK 500 ALA A 151 149.09 -177.83
REMARK 500 GLU A 156 171.27 -30.98
REMARK 500 GLU A 176 106.12 62.87
REMARK 500 ARG A 177 -157.26 -91.68
REMARK 500 MET A 192 31.98 70.45
REMARK 500 SER A 193 147.20 -175.93
REMARK 500 LEU A 243 -87.54 -140.40
REMARK 500 PHE A 244 -71.18 -65.94
REMARK 500 ALA A 254 129.09 -178.10
REMARK 500 GLU A 256 75.79 -158.82
REMARK 500 ASP A 259 33.25 -76.31
REMARK 500 ASN A 281 -9.15 -141.65
REMARK 500 GLU A 283 10.81 -67.61
REMARK 500 ASP A 297 21.70 -78.53
REMARK 500 LEU A 306 127.96 -178.28
REMARK 500 GLU A 308 128.66 60.29
REMARK 500 SER A 341 106.04 37.86
REMARK 500 PRO A 354 -132.17 -62.87
REMARK 500 ASP A 385 13.94 -144.59
REMARK 500 ILE A 386 -102.78 54.85
REMARK 500 VAL A 387 87.62 72.83
REMARK 500 ASP A 390 171.73 -51.27
REMARK 500 ALA A 392 134.32 -39.64
REMARK 500 LEU A 396 -112.50 -83.10
REMARK 500 LYS A 397 -33.60 -150.39
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JSY A 1 418 UNP P17870 ARRB1_BOVIN 1 418
SEQRES 1 A 418 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER
SEQRES 2 A 418 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP
SEQRES 3 A 418 PHE VAL ASP HIS ILE ASP LEU VAL GLU PRO VAL ASP GLY
SEQRES 4 A 418 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG
SEQRES 5 A 418 VAL TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY ARG
SEQRES 6 A 418 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP
SEQRES 7 A 418 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO
SEQRES 8 A 418 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU
SEQRES 9 A 418 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE
SEQRES 10 A 418 GLU ILE PRO PRO ASN LEU PRO CYS SER VAL THR LEU GLN
SEQRES 11 A 418 PRO GLY PRO GLU ASP THR GLY LYS ALA CYS GLY VAL ASP
SEQRES 12 A 418 TYR GLU VAL LYS ALA PHE CYS ALA GLU ASN LEU GLU GLU
SEQRES 13 A 418 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE ARG
SEQRES 14 A 418 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO
SEQRES 15 A 418 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS
SEQRES 16 A 418 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR
SEQRES 17 A 418 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR
SEQRES 18 A 418 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER
SEQRES 19 A 418 VAL ARG GLN TYR ALA ASP ILE CYS LEU PHE ASN THR ALA
SEQRES 20 A 418 GLN TYR LYS CYS PRO VAL ALA MET GLU GLU ALA ASP ASP
SEQRES 21 A 418 THR VAL ALA PRO SER SER THR PHE CYS LYS VAL TYR THR
SEQRES 22 A 418 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY
SEQRES 23 A 418 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN
SEQRES 24 A 418 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG
SEQRES 25 A 418 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL
SEQRES 26 A 418 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU
SEQRES 27 A 418 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU
SEQRES 28 A 418 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU
SEQRES 29 A 418 VAL PRO GLU HIS GLU THR PRO VAL ASP THR ASN LEU ILE
SEQRES 30 A 418 GLU LEU ASP THR ASN ASP ASP ASP ILE VAL PHE GLU ASP
SEQRES 31 A 418 PHE ALA ARG GLN ARG LEU LYS GLY MET LYS ASP ASP LYS
SEQRES 32 A 418 GLU GLU GLU GLU ASP GLY THR GLY SER PRO ARG LEU ASN
SEQRES 33 A 418 ASP ARG
FORMUL 2 HOH *76(H2 O)
HELIX 1 1 THR A 98 GLY A 109 1 12
HELIX 2 2 PHE A 277 ASN A 281 5 5
HELIX 3 3 ARG A 312 LEU A 315 5 4
SHEET 1 A 5 ALA A 112 PHE A 117 0
SHEET 2 A 5 VAL A 37 LEU A 42 -1 N VAL A 41 O TYR A 113
SHEET 3 A 5 THR A 19 LEU A 22 -1 N TYR A 21 O VAL A 40
SHEET 4 A 5 VAL A 8 ALA A 12 -1 N PHE A 9 O LEU A 22
SHEET 5 A 5 PHE A 388 GLU A 389 1 O GLU A 389 N VAL A 8
SHEET 1 B 5 PHE A 75 GLN A 85 0
SHEET 2 B 5 ARG A 52 GLY A 64 -1 N CYS A 59 O LEU A 79
SHEET 3 B 5 ALA A 139 ALA A 151 -1 O LYS A 147 N THR A 56
SHEET 4 B 5 VAL A 127 LEU A 129 0
SHEET 5 B 5 ALA A 288 LEU A 289 -1 O LEU A 289 N THR A 128
SHEET 1 C 5 PHE A 75 GLN A 85 0
SHEET 2 C 5 ARG A 52 GLY A 64 -1 N CYS A 59 O LEU A 79
SHEET 3 C 5 ALA A 139 ALA A 151 -1 O LYS A 147 N THR A 56
SHEET 4 C 5 VAL A 164 GLN A 172 0
SHEET 5 C 5 ASP A 26 ASP A 29 1 N PHE A 27 O ARG A 169
SHEET 1 D 4 THR A 183 GLN A 189 0
SHEET 2 D 4 PRO A 196 LEU A 203 -1 O ALA A 201 N ALA A 184
SHEET 3 D 4 ILE A 214 ASN A 222 -1 O THR A 221 N HIS A 198
SHEET 4 D 4 THR A 267 LEU A 274 -1 O PHE A 268 N VAL A 220
SHEET 1 E 5 ILE A 207 TYR A 209 0
SHEET 2 E 5 VAL A 343 MET A 352 1 O MET A 352 N TYR A 208
SHEET 3 E 5 ILE A 317 VAL A 329 -1 N VAL A 323 O LEU A 347
SHEET 4 E 5 VAL A 228 ILE A 241 -1 N SER A 234 O LYS A 324
SHEET 5 E 5 ALA A 247 ALA A 258 -1 O TYR A 249 N ALA A 239
CRYST1 78.952 78.952 158.924 90.00 90.00 120.00 P 32 2 1 6
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 0.012666 0.007313 0.000000 0.00000
SCALE2 0.000000 0.014625 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006292 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
