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1g4m.pdb
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HEADER SIGNALING PROTEIN 27-OCT-00 1G4M
TITLE CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-ARRESTIN1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRUNCATION MUTANT: 1-393;
COMPND 5 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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC
KEYWDS SENSORY TRANSDUCTION, ALTERNATIVE SPLICING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SCHUBERT,M.HAN
REVDAT 3 09-AUG-23 1G4M 1 REMARK
REVDAT 2 24-FEB-09 1G4M 1 VERSN
REVDAT 1 03-OCT-01 1G4M 0
JRNL AUTH M.HAN,V.V.GUREVICH,S.A.VISHNIVETSKIY,P.B.SIGLER,C.SCHUBERT
JRNL TITL CRYSTAL STRUCTURE OF BETA-ARRESTIN AT 1.9 A: POSSIBLE
JRNL TITL 2 MECHANISM OF RECEPTOR BINDING AND MEMBRANE TRANSLOCATION.
JRNL REF STRUCTURE V. 9 869 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11566136
JRNL DOI 10.1016/S0969-2126(01)00644-X
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2567021.550
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 70650
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) : 0.235
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 5401
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 36.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2709
REMARK 3 BIN R VALUE (WORKING SET) : 0.3790
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 237
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5657
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 269
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.21000
REMARK 3 B22 (A**2) : 17.93000
REMARK 3 B33 (A**2) : -9.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.42
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) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.110
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.920 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.730 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.380 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 56.45
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.PA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARA
REMARK 3 PARAMETER FILE 3 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G4M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012226.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979, 1.10
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS AND SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS - B4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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 SIRAS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1CF1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 36.85850
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 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 SER A 340
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 MET B 1
REMARK 465 GLY B 2
REMARK 465 ASP B 3
REMARK 465 LYS B 4
REMARK 465 GLY B 332
REMARK 465 GLY B 333
REMARK 465 LEU B 334
REMARK 465 LEU B 335
REMARK 465 GLY B 336
REMARK 465 ASP B 337
REMARK 465 LEU B 338
REMARK 465 GLU B 358
REMARK 465 GLU B 359
REMARK 465 PRO B 360
REMARK 465 PRO B 361
REMARK 465 HIS B 362
REMARK 465 ARG B 363
REMARK 465 GLU B 364
REMARK 465 VAL B 365
REMARK 465 PRO B 366
REMARK 465 GLU B 367
REMARK 465 HIS B 368
REMARK 465 GLU B 369
REMARK 465 THR B 370
REMARK 465 PRO B 371
REMARK 465 VAL B 372
REMARK 465 ASP B 373
REMARK 465 THR B 374
REMARK 465 ASN B 375
REMARK 465 LEU B 376
REMARK 465 ILE B 377
REMARK 465 GLU B 378
REMARK 465 LEU B 379
REMARK 465 ASP B 380
REMARK 465 THR B 381
REMARK 465 ASN B 382
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 ASP A 93 CG OD1 OD2
REMARK 470 SER A 341 OG
REMARK 470 LYS A 357 CG CD CE NZ
REMARK 470 ASP A 383 CG OD1 OD2
REMARK 470 ASP B 383 CG OD1 OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 49 CB CG CD CE NZ
REMARK 480 ARG A 99 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 106 CD CE NZ
REMARK 480 LYS A 107 CG CD CE NZ
REMARK 480 GLU A 134 CG CD OE1 OE2
REMARK 480 GLU A 152 CG CD OE1 OE2
REMARK 480 ASN A 153 CG OD1 ND2
REMARK 480 GLU A 155 CG CD OE1 OE2
REMARK 480 GLU A 156 CD OE1 OE2
REMARK 480 LYS A 157 CG CD CE NZ
REMARK 480 ARG A 177 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 195 CG CD CE NZ
REMARK 480 GLU A 206 CG CD OE1 OE2
REMARK 480 LYS A 229 CG CD CE NZ
REMARK 480 GLU A 283 CB CG CD OE1 OE2
REMARK 480 GLU A 296 CG CD OE1 OE2
REMARK 480 GLU A 308 CG CD OE1 OE2
REMARK 480 GLU B 46 CB CG CD OE1 OE2
REMARK 480 GLU B 92 C O CB CG CD OE1 OE2
REMARK 480 LYS B 95 CB CG CD CE NZ
REMARK 480 ARG B 99 CG CD NE CZ NH1 NH2
REMARK 480 GLU B 102 CG CD OE1 OE2
REMARK 480 GLU B 118 CG CD OE1 OE2
REMARK 480 GLU B 155 CG CD OE1 OE2
REMARK 480 LYS B 157 CD CE NZ
REMARK 480 HIS B 159 CB CG ND1 CD2 CE1 NE2
REMARK 480 LYS B 160 CD CE NZ
REMARK 480 GLN B 181 CB CG CD OE1 NE2
REMARK 480 LYS B 195 CE NZ
REMARK 480 LYS B 284 CG CD CE NZ
REMARK 480 GLU B 296 CG CD OE1 OE2
REMARK 480 GLU B 308 CG CD OE1 OE2
REMARK 480 LYS B 355 CB CG CD CE NZ
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 HOH B 398 O HOH B 471 1.89
REMARK 500 O PHE B 117 O HOH B 492 1.91
REMARK 500 O VAL B 37 O HOH B 458 1.91
REMARK 500 N GLY B 39 O HOH B 459 1.96
REMARK 500 O GLY B 39 O HOH B 460 1.96
REMARK 500 N VAL B 37 O HOH B 492 2.01
REMARK 500 N PHE B 115 O HOH B 460 2.01
REMARK 500 O PHE B 115 O HOH B 459 2.02
REMARK 500 N PHE B 117 O HOH B 458 2.06
REMARK 500 O HOH A 403 O HOH A 461 2.10
REMARK 500 O LYS A 95 N LEU A 97 2.15
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 B 96 C - N - CA ANGL. DEV. = 11.7 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 ILE A 31 -53.75 73.65
REMARK 500 LYS A 49 -106.17 70.81
REMARK 500 ASP A 69 60.32 -161.50
REMARK 500 PRO A 89 -101.08 -38.37
REMARK 500 ALA A 90 151.38 76.58
REMARK 500 PRO A 91 30.09 -56.79
REMARK 500 PRO A 96 87.90 -61.73
REMARK 500 PRO A 178 96.91 -68.78
REMARK 500 LEU A 191 77.09 -115.59
REMARK 500 PHE A 244 -45.50 68.18
REMARK 500 ALA A 279 -34.34 -38.33
REMARK 500 ASN A 281 16.87 -147.56
REMARK 500 ALA A 392 116.76 -28.96
REMARK 500 ILE B 31 -49.65 67.09
REMARK 500 GLU B 50 -34.86 83.18
REMARK 500 GLU B 66 175.27 -41.74
REMARK 500 ASP B 67 -43.87 -15.44
REMARK 500 LEU B 68 48.72 -66.62
REMARK 500 ASP B 69 -15.60 -178.85
REMARK 500 VAL B 70 -68.15 -11.01
REMARK 500 LEU B 73 107.25 -46.26
REMARK 500 THR B 74 -47.30 -22.19
REMARK 500 PRO B 89 -141.31 -43.62
REMARK 500 ALA B 90 -81.87 -86.29
REMARK 500 GLU B 92 -8.09 51.21
REMARK 500 LYS B 95 171.74 -59.39
REMARK 500 PRO B 96 144.10 -38.40
REMARK 500 LYS B 107 -19.35 -143.06
REMARK 500 PRO B 133 62.92 -56.66
REMARK 500 ASP B 135 -72.58 -153.04
REMARK 500 THR B 136 130.35 119.72
REMARK 500 PRO B 178 -93.97 -65.01
REMARK 500 PHE B 244 -46.66 66.73
REMARK 500 ALA B 254 140.05 -177.02
REMARK 500 ASP B 259 47.40 -91.07
REMARK 500 ARG B 282 -177.49 -15.04
REMARK 500 GLU B 308 128.13 -39.71
REMARK 500 PRO B 356 -98.55 -8.42
REMARK 500 ASP B 385 -160.43 176.33
REMARK 500 ALA B 392 110.54 -33.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CF1 RELATED DB: PDB
REMARK 900 1CF1 CONTAINS VISUAL ARRESTIN A DOWNREGULATOR OF THE VISUAL
REMARK 900 TRANSDUCTION CASCADE.
DBREF 1G4M A 1 393 UNP P17870 ARRB1_BOVIN 1 393
DBREF 1G4M B 1 393 UNP P17870 ARRB1_BOVIN 1 393
SEQRES 1 A 393 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER
SEQRES 2 A 393 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP
SEQRES 3 A 393 PHE VAL ASP HIS ILE ASP LEU VAL GLU PRO VAL ASP GLY
SEQRES 4 A 393 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG
SEQRES 5 A 393 VAL TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY ARG
SEQRES 6 A 393 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP
SEQRES 7 A 393 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO
SEQRES 8 A 393 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU
SEQRES 9 A 393 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE
SEQRES 10 A 393 GLU ILE PRO PRO ASN LEU PRO CYS SER VAL THR LEU GLN
SEQRES 11 A 393 PRO GLY PRO GLU ASP THR GLY LYS ALA CYS GLY VAL ASP
SEQRES 12 A 393 TYR GLU VAL LYS ALA PHE CYS ALA GLU ASN LEU GLU GLU
SEQRES 13 A 393 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE ARG
SEQRES 14 A 393 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO
SEQRES 15 A 393 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS
SEQRES 16 A 393 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR
SEQRES 17 A 393 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR
SEQRES 18 A 393 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER
SEQRES 19 A 393 VAL ARG GLN TYR ALA ASP ILE CYS LEU PHE ASN THR ALA
SEQRES 20 A 393 GLN TYR LYS CYS PRO VAL ALA MET GLU GLU ALA ASP ASP
SEQRES 21 A 393 THR VAL ALA PRO SER SER THR PHE CYS LYS VAL TYR THR
SEQRES 22 A 393 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY
SEQRES 23 A 393 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN
SEQRES 24 A 393 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG
SEQRES 25 A 393 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL
SEQRES 26 A 393 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU
SEQRES 27 A 393 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU
SEQRES 28 A 393 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU
SEQRES 29 A 393 VAL PRO GLU HIS GLU THR PRO VAL ASP THR ASN LEU ILE
SEQRES 30 A 393 GLU LEU ASP THR ASN ASP ASP ASP ILE VAL PHE GLU ASP
SEQRES 31 A 393 PHE ALA ARG
SEQRES 1 B 393 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER
SEQRES 2 B 393 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP
SEQRES 3 B 393 PHE VAL ASP HIS ILE ASP LEU VAL GLU PRO VAL ASP GLY
SEQRES 4 B 393 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG
SEQRES 5 B 393 VAL TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY ARG
SEQRES 6 B 393 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP
SEQRES 7 B 393 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO
SEQRES 8 B 393 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU
SEQRES 9 B 393 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE
SEQRES 10 B 393 GLU ILE PRO PRO ASN LEU PRO CYS SER VAL THR LEU GLN
SEQRES 11 B 393 PRO GLY PRO GLU ASP THR GLY LYS ALA CYS GLY VAL ASP
SEQRES 12 B 393 TYR GLU VAL LYS ALA PHE CYS ALA GLU ASN LEU GLU GLU
SEQRES 13 B 393 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE ARG
SEQRES 14 B 393 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO
SEQRES 15 B 393 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS
SEQRES 16 B 393 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR
SEQRES 17 B 393 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR
SEQRES 18 B 393 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER
SEQRES 19 B 393 VAL ARG GLN TYR ALA ASP ILE CYS LEU PHE ASN THR ALA
SEQRES 20 B 393 GLN TYR LYS CYS PRO VAL ALA MET GLU GLU ALA ASP ASP
SEQRES 21 B 393 THR VAL ALA PRO SER SER THR PHE CYS LYS VAL TYR THR
SEQRES 22 B 393 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY
SEQRES 23 B 393 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN
SEQRES 24 B 393 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG
SEQRES 25 B 393 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL
SEQRES 26 B 393 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU
SEQRES 27 B 393 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU
SEQRES 28 B 393 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU
SEQRES 29 B 393 VAL PRO GLU HIS GLU THR PRO VAL ASP THR ASN LEU ILE
SEQRES 30 B 393 GLU LEU ASP THR ASN ASP ASP ASP ILE VAL PHE GLU ASP
SEQRES 31 B 393 PHE ALA ARG
FORMUL 3 HOH *269(H2 O)
HELIX 1 1 ASP A 44 LYS A 49 1 6
HELIX 2 2 THR A 98 LEU A 108 1 11
HELIX 3 3 GLY A 132 THR A 136 5 5
HELIX 4 4 ASP A 135 LYS A 138 5 4
HELIX 5 5 HIS A 159 ARG A 161 5 3
HELIX 6 6 PHE A 277 ASN A 281 5 5
HELIX 7 7 ARG A 312 LEU A 315 5 4
HELIX 8 8 ASP B 44 LYS B 49 1 6
HELIX 9 9 THR B 98 LYS B 106 1 9
HELIX 10 10 HIS B 159 ARG B 161 5 3
HELIX 11 11 ARG B 312 LEU B 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 37 O PHE A 117
SHEET 3 A 5 THR A 19 LEU A 22 -1 O THR A 19 N LEU A 42
SHEET 4 A 5 THR A 6 ALA A 12 -1 O PHE A 9 N LEU A 22
SHEET 5 A 5 ILE A 386 ASP A 390 1 O VAL A 387 N VAL A 8
SHEET 1 B 5 PHE A 75 PHE A 87 0
SHEET 2 B 5 ARG A 52 TYR A 63 -1 N VAL A 53 O PHE A 87
SHEET 3 B 5 CYS A 140 ALA A 151 -1 O GLY A 141 N ARG A 62
SHEET 4 B 5 VAL A 127 GLN A 130 -1 O VAL A 127 N VAL A 142
SHEET 5 B 5 LEU A 287 LEU A 289 -1 O LEU A 287 N GLN A 130
SHEET 1 C 5 PHE A 75 PHE A 87 0
SHEET 2 C 5 ARG A 52 TYR A 63 -1 N VAL A 53 O PHE A 87
SHEET 3 C 5 CYS A 140 ALA A 151 -1 O GLY A 141 N ARG A 62
SHEET 4 C 5 SER A 163 GLN A 172 -1 N VAL A 164 O ALA A 148
SHEET 5 C 5 ASP A 26 ASP A 29 1 N PHE A 27 O ARG A 169
SHEET 1 D 4 GLU A 185 GLN A 189 0
SHEET 2 D 4 LEU A 197 LEU A 203 -1 N LEU A 197 O GLN A 189
SHEET 3 D 4 ILE A 214 ASN A 222 -1 N ASN A 217 O SER A 202
SHEET 4 D 4 SER A 266 LEU A 274 -1 O SER A 266 N ASN A 222
SHEET 1 E 5 ILE A 207 TYR A 209 0
SHEET 2 E 5 ASP A 342 MET A 352 1 O THR A 350 N TYR A 208
SHEET 3 E 5 ILE A 317 VAL A 329 -1 O TYR A 321 N PHE A 349
SHEET 4 E 5 VAL A 228 ILE A 241 -1 N LYS A 229 O VAL A 328
SHEET 5 E 5 ALA A 247 ALA A 258 -1 O ALA A 247 N ILE A 241
SHEET 1 F 5 ALA B 112 PHE B 117 0
SHEET 2 F 5 VAL B 37 VAL B 43 -1 N VAL B 37 O PHE B 117
SHEET 3 F 5 LEU B 18 LEU B 22 -1 O THR B 19 N LEU B 42
SHEET 4 F 5 THR B 6 ALA B 12 -1 N PHE B 9 O LEU B 22
SHEET 5 F 5 ILE B 386 ASP B 390 1 O VAL B 387 N VAL B 8
SHEET 1 G 5 PHE B 75 PHE B 87 0
SHEET 2 G 5 ARG B 52 TYR B 63 -1 N VAL B 53 O PHE B 87
SHEET 3 G 5 CYS B 140 ALA B 151 -1 O GLY B 141 N ARG B 62
SHEET 4 G 5 VAL B 127 LEU B 129 -1 O VAL B 127 N VAL B 142
SHEET 5 G 5 ALA B 288 LEU B 289 -1 N LEU B 289 O THR B 128
SHEET 1 H 5 PHE B 75 PHE B 87 0
SHEET 2 H 5 ARG B 52 TYR B 63 -1 N VAL B 53 O PHE B 87
SHEET 3 H 5 CYS B 140 ALA B 151 -1 O GLY B 141 N ARG B 62
SHEET 4 H 5 SER B 163 GLN B 172 -1 N VAL B 164 O ALA B 148
SHEET 5 H 5 ASP B 26 ASP B 29 1 N PHE B 27 O ARG B 169
SHEET 1 I 4 GLU B 185 GLN B 189 0
SHEET 2 I 4 LEU B 197 LEU B 203 -1 N LEU B 197 O GLN B 189
SHEET 3 I 4 ILE B 214 ASN B 222 -1 N ASN B 217 O SER B 202
SHEET 4 I 4 SER B 266 LEU B 274 -1 O SER B 266 N ASN B 222
SHEET 1 J 5 ILE B 207 TYR B 209 0
SHEET 2 J 5 SER B 340 MET B 352 1 O THR B 350 N TYR B 208
SHEET 3 J 5 ILE B 317 SER B 330 -1 O TYR B 321 N PHE B 349
SHEET 4 J 5 VAL B 228 ILE B 241 -1 N LYS B 229 O VAL B 328
SHEET 5 J 5 ALA B 247 ALA B 258 -1 O ALA B 247 N ILE B 241
CISPEP 1 PHE A 87 PRO A 88 0 -2.01
CISPEP 2 PHE B 87 PRO B 88 0 -0.04
CISPEP 3 ALA B 90 PRO B 91 0 -1.09
CRYST1 62.400 73.717 115.760 90.00 98.73 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 0.016026 0.000000 0.002460 0.00000
SCALE2 0.000000 0.013565 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008740 0.00000
ATOM 1 N GLY A 5 56.211 37.123 -6.949 1.00 85.48 N
ATOM 2 CA GLY A 5 54.863 37.350 -7.560 1.00 88.84 C
ATOM 3 C GLY A 5 53.753 37.508 -6.534 1.00 87.89 C
ATOM 4 O GLY A 5 54.019 37.610 -5.334 1.00 91.39 O
ATOM 5 N THR A 6 52.508 37.533 -7.004 1.00 84.79 N
ATOM 6 CA THR A 6 51.354 37.673 -6.115 1.00 81.04 C
ATOM 7 C THR A 6 50.360 36.517 -6.281 1.00 78.27 C
ATOM 8 O THR A 6 49.657 36.421 -7.293 1.00 75.40 O
ATOM 9 CB THR A 6 50.622 39.013 -6.361 1.00 80.47 C
ATOM 10 OG1 THR A 6 51.520 40.099 -6.101 1.00 79.80 O
ATOM 11 CG2 THR A 6 49.416 39.144 -5.438 1.00 79.93 C
ATOM 12 N ARG A 7 50.317 35.640 -5.279 1.00 74.65 N
ATOM 13 CA ARG A 7 49.420 34.487 -5.287 1.00 68.96 C
ATOM 14 C ARG A 7 47.998 34.895 -4.927 1.00 62.29 C
ATOM 15 O ARG A 7 47.781 35.753 -4.078 1.00 60.91 O
ATOM 16 CB ARG A 7 49.898 33.433 -4.282 1.00 73.29 C
ATOM 17 CG ARG A 7 51.202 32.746 -4.663 1.00 81.38 C
ATOM 18 CD ARG A 7 52.081 32.516 -3.437 1.00 87.31 C
ATOM 19 NE ARG A 7 51.428 31.687 -2.425 1.00 94.88 N
ATOM 20 CZ ARG A 7 51.227 30.377 -2.542 1.00 96.84 C
ATOM 21 NH1 ARG A 7 51.630 29.735 -3.634 1.00 97.17 N
ATOM 22 NH2 ARG A 7 50.628 29.705 -1.565 1.00 96.39 N
ATOM 23 N VAL A 8 47.034 34.270 -5.586 1.00 54.62 N
ATOM 24 CA VAL A 8 45.642 34.541 -5.328 1.00 54.41 C
ATOM 25 C VAL A 8 44.928 33.197 -5.308 1.00 57.88 C
ATOM 26 O VAL A 8 44.991 32.424 -6.276 1.00 59.25 O
ATOM 27 CB VAL A 8 45.042 35.463 -6.419 1.00 55.07 C
ATOM 28 CG1 VAL A 8 43.538 35.402 -6.389 1.00 51.46 C
ATOM 29 CG2 VAL A 8 45.493 36.900 -6.178 1.00 51.85 C
ATOM 30 N PHE A 9 44.263 32.899 -4.197 1.00 52.82 N
ATOM 31 CA PHE A 9 43.557 31.635 -4.103 1.00 51.05 C
ATOM 32 C PHE A 9 42.181 31.815 -4.689 1.00 49.75 C
ATOM 33 O PHE A 9 41.563 32.868 -4.524 1.00 52.96 O
ATOM 34 CB PHE A 9 43.486 31.179 -2.644 1.00 48.43 C
ATOM 35 CG PHE A 9 44.828 31.110 -1.987 1.00 53.93 C
ATOM 36 CD1 PHE A 9 45.328 32.199 -1.290 1.00 50.13 C
ATOM 37 CD2 PHE A 9 45.630 29.981 -2.131 1.00 53.67 C
ATOM 38 CE1 PHE A 9 46.615 32.167 -0.747 1.00 56.80 C
ATOM 39 CE2 PHE A 9 46.912 29.941 -1.594 1.00 50.94 C
ATOM 40 CZ PHE A 9 47.406 31.036 -0.901 1.00 54.93 C
ATOM 41 N LYS A 10 41.690 30.786 -5.366 1.00 50.10 N
ATOM 42 CA LYS A 10 40.385 30.870 -5.988 1.00 52.04 C
ATOM 43 C LYS A 10 39.647 29.564 -5.921 1.00 47.74 C
ATOM 44 O LYS A 10 40.245 28.500 -5.843 1.00 56.04 O
ATOM 45 CB LYS A 10 40.524 31.272 -7.456 1.00 60.41 C
ATOM 46 CG LYS A 10 41.244 30.241 -8.337 1.00 66.15 C
ATOM 47 CD LYS A 10 41.081 30.601 -9.821 1.00 76.54 C
ATOM 48 CE LYS A 10 41.769 29.602 -10.757 1.00 86.31 C
ATOM 49 NZ LYS A 10 41.115 28.250 -10.794 1.00 89.02 N
ATOM 50 N LYS A 11 38.332 29.651 -5.955 1.00 47.33 N
ATOM 51 CA LYS A 11 37.518 28.467 -5.921 1.00 49.29 C
ATOM 52 C LYS A 11 36.228 28.785 -6.639 1.00 53.87 C
ATOM 53 O LYS A 11 35.574 29.795 -6.356 1.00 52.04 O
ATOM 54 CB LYS A 11 37.233 28.039 -4.484 1.00 53.60 C
ATOM 55 CG LYS A 11 36.391 26.776 -4.396 1.00 55.67 C
ATOM 56 CD LYS A 11 36.279 26.271 -2.972 1.00 58.61 C
ATOM 57 CE LYS A 11 35.510 24.955 -2.926 1.00 56.25 C
ATOM 58 NZ LYS A 11 35.261 24.537 -1.526 1.00 58.65 N
ATOM 59 N ALA A 12 35.873 27.913 -7.577 1.00 52.87 N
ATOM 60 CA ALA A 12 34.667 28.075 -8.361 1.00 52.59 C
ATOM 61 C ALA A 12 33.581 27.194 -7.771 1.00 51.66 C
ATOM 62 O ALA A 12 33.872 26.230 -7.074 1.00 55.63 O
ATOM 63 CB ALA A 12 34.946 27.687 -9.834 1.00 49.43 C
ATOM 64 N SER A 13 32.329 27.545 -8.025 1.00 48.41 N
ATOM 65 CA SER A 13 31.213 26.756 -7.540 1.00 53.32 C
ATOM 66 C SER A 13 31.159 25.452 -8.349 1.00 54.50 C
ATOM 67 O SER A 13 31.961 25.233 -9.265 1.00 54.66 O
ATOM 68 CB SER A 13 29.902 27.524 -7.712 1.00 54.19 C
ATOM 69 OG SER A 13 29.757 27.949 -9.057 1.00 56.99 O
ATOM 70 N PRO A 14 30.224 24.561 -8.005 1.00 52.02 N
ATOM 71 CA PRO A 14 30.145 23.307 -8.760 1.00 57.94 C
ATOM 72 C PRO A 14 29.799 23.594 -10.226 1.00 58.61 C
ATOM 73 O PRO A 14 30.539 23.202 -11.135 1.00 56.94 O
ATOM 74 CB PRO A 14 29.036 22.542 -8.044 1.00 51.53 C
ATOM 75 CG PRO A 14 29.124 23.066 -6.628 1.00 54.57 C
ATOM 76 CD PRO A 14 29.299 24.547 -6.860 1.00 52.62 C
ATOM 77 N ASN A 15 28.690 24.301 -10.445 1.00 61.38 N
ATOM 78 CA ASN A 15 28.252 24.621 -11.803 1.00 63.42 C
ATOM 79 C ASN A 15 29.206 25.559 -12.560 1.00 65.23 C
ATOM 80 O ASN A 15 28.969 25.877 -13.724 1.00 70.01 O
ATOM 81 CB ASN A 15 26.834 25.203 -11.774 1.00 62.70 C
ATOM 82 CG ASN A 15 26.794 26.639 -11.276 1.00 68.59 C
ATOM 83 OD1 ASN A 15 25.731 27.155 -10.905 1.00 66.21 O
ATOM 84 ND2 ASN A 15 27.948 27.296 -11.269 1.00 64.55 N
ATOM 85 N GLY A 16 30.276 25.999 -11.896 1.00 62.74 N
ATOM 86 CA GLY A 16 31.259 26.871 -12.532 1.00 61.36 C
ATOM 87 C GLY A 16 30.847 28.316 -12.778 1.00 58.69 C
ATOM 88 O GLY A 16 31.640 29.123 -13.276 1.00 56.91 O
ATOM 89 N LYS A 17 29.613 28.648 -12.423 1.00 55.10 N
ATOM 90 CA LYS A 17 29.084 29.997 -12.609 1.00 58.91 C
ATOM 91 C LYS A 17 29.644 31.075 -11.660 1.00 59.96 C
ATOM 92 O LYS A 17 29.838 32.225 -12.061 1.00 57.41 O
ATOM 93 CB LYS A 17 27.558 29.938 -12.498 1.00 59.18 C
ATOM 94 CG LYS A 17 26.851 29.856 -13.845 1.00 69.52 C
ATOM 95 CD LYS A 17 27.681 29.112 -14.887 1.00 75.61 C
ATOM 96 CE LYS A 17 27.287 29.532 -16.295 1.00 77.89 C
ATOM 97 NZ LYS A 17 28.224 28.978 -17.318 1.00 77.16 N
ATOM 98 N LEU A 18 29.904 30.687 -10.412 1.00 60.28 N
ATOM 99 CA LEU A 18 30.417 31.583 -9.365 1.00 58.27 C
ATOM 100 C LEU A 18 31.868 31.261 -9.008 1.00 59.45 C
ATOM 101 O LEU A 18 32.231 30.094 -8.873 1.00 61.46 O
ATOM 102 CB LEU A 18 29.557 31.422 -8.113 1.00 56.83 C
ATOM 103 CG LEU A 18 29.088 32.630 -7.305 1.00 60.97 C
ATOM 104 CD1 LEU A 18 28.196 33.504 -8.174 1.00 60.47 C
ATOM 105 CD2 LEU A 18 28.302 32.159 -6.083 1.00 55.01 C
ATOM 106 N THR A 19 32.696 32.288 -8.851 1.00 54.99 N
ATOM 107 CA THR A 19 34.085 32.079 -8.484 1.00 53.00 C
ATOM 108 C THR A 19 34.520 33.106 -7.444 1.00 53.70 C
ATOM 109 O THR A 19 34.220 34.285 -7.580 1.00 50.91 O
ATOM 110 CB THR A 19 35.001 32.181 -9.708 1.00 56.47 C
ATOM 111 OG1 THR A 19 34.525 31.290 -10.719 1.00 64.76 O
ATOM 112 CG2 THR A 19 36.438 31.789 -9.345 1.00 52.15 C
ATOM 113 N VAL A 20 35.211 32.650 -6.401 1.00 51.16 N
ATOM 114 CA VAL A 20 35.687 33.530 -5.336 1.00 45.99 C
ATOM 115 C VAL A 20 37.207 33.564 -5.343 1.00 46.39 C
ATOM 116 O VAL A 20 37.870 32.547 -5.596 1.00 43.38 O
ATOM 117 CB VAL A 20 35.185 33.056 -3.943 1.00 48.57 C
ATOM 118 CG1 VAL A 20 35.928 33.796 -2.837 1.00 56.64 C
ATOM 119 CG2 VAL A 20 33.706 33.310 -3.815 1.00 51.35 C
ATOM 120 N TYR A 21 37.762 34.746 -5.093 1.00 40.72 N
ATOM 121 CA TYR A 21 39.208 34.929 -5.064 1.00 41.97 C
ATOM 122 C TYR A 21 39.548 35.576 -3.718 1.00 42.13 C
ATOM 123 O TYR A 21 38.796 36.420 -3.243 1.00 42.70 O
ATOM 124 CB TYR A 21 39.676 35.844 -6.212 1.00 44.15 C
ATOM 125 CG TYR A 21 39.284 35.382 -7.597 1.00 47.11 C
ATOM 126 CD1 TYR A 21 37.949 35.431 -8.023 1.00 42.43 C
ATOM 127 CD2 TYR A 21 40.242 34.867 -8.478 1.00 44.15 C
ATOM 128 CE1 TYR A 21 37.580 34.973 -9.286 1.00 48.39 C
ATOM 129 CE2 TYR A 21 39.883 34.406 -9.746 1.00 49.52 C
ATOM 130 CZ TYR A 21 38.552 34.458 -10.143 1.00 53.22 C
ATOM 131 OH TYR A 21 38.188 33.967 -11.379 1.00 53.93 O
ATOM 132 N LEU A 22 40.647 35.150 -3.097 1.00 43.83 N
ATOM 133 CA LEU A 22 41.093 35.710 -1.814 1.00 42.64 C
ATOM 134 C LEU A 22 42.595 35.810 -1.874 1.00 41.67 C
ATOM 135 O LEU A 22 43.237 35.031 -2.555 1.00 44.58 O
ATOM 136 CB LEU A 22 40.694 34.822 -0.618 1.00 39.64 C
ATOM 137 CG LEU A 22 39.222 34.760 -0.188 1.00 42.82 C
ATOM 138 CD1 LEU A 22 39.031 33.643 0.857 1.00 36.58 C
ATOM 139 CD2 LEU A 22 38.802 36.112 0.403 1.00 37.10 C
ATOM 140 N GLY A 23 43.157 36.786 -1.178 1.00 38.71 N
ATOM 141 CA GLY A 23 44.603 36.946 -1.187 1.00 42.75 C
ATOM 142 C GLY A 23 45.333 36.012 -0.240 1.00 46.40 C
ATOM 143 O GLY A 23 46.560 35.904 -0.276 1.00 46.19 O
ATOM 144 N LYS A 24 44.582 35.352 0.632 1.00 48.97 N
ATOM 145 CA LYS A 24 45.175 34.395 1.554 1.00 49.30 C
ATOM 146 C LYS A 24 44.168 33.456 2.192 1.00 43.78 C
ATOM 147 O LYS A 24 42.945 33.607 2.037 1.00 42.14 O
ATOM 148 CB LYS A 24 46.006 35.098 2.633 1.00 52.88 C
ATOM 149 CG LYS A 24 45.468 36.404 3.169 1.00 43.42 C
ATOM 150 CD LYS A 24 46.557 37.056 4.012 1.00 52.15 C
ATOM 151 CE LYS A 24 46.160 38.419 4.526 1.00 57.32 C
ATOM 152 NZ LYS A 24 47.357 39.126 5.077 1.00 63.59 N
ATOM 153 N ARG A 25 44.699 32.476 2.912 1.00 44.97 N
ATOM 154 CA ARG A 25 43.874 31.473 3.567 1.00 42.78 C
ATOM 155 C ARG A 25 43.768 31.726 5.055 1.00 37.58 C
ATOM 156 O ARG A 25 42.750 31.386 5.663 1.00 35.83 O
ATOM 157 CB ARG A 25 44.486 30.088 3.366 1.00 42.70 C
ATOM 158 CG ARG A 25 44.701 29.642 1.919 1.00 49.92 C
ATOM 159 CD ARG A 25 45.021 28.144 1.960 1.00 51.10 C
ATOM 160 NE ARG A 25 45.140 27.519 0.653 1.00 52.08 N
ATOM 161 CZ ARG A 25 46.290 27.139 0.115 1.00 56.23 C
ATOM 162 NH1 ARG A 25 47.429 27.320 0.776 1.00 55.72 N
ATOM 163 NH2 ARG A 25 46.297 26.578 -1.087 1.00 59.86 N
ATOM 164 N ASP A 26 44.823 32.301 5.635 1.00 40.69 N
ATOM 165 CA ASP A 26 44.854 32.579 7.074 1.00 39.30 C
ATOM 166 C ASP A 26 44.902 34.090 7.357 1.00 36.28 C
ATOM 167 O ASP A 26 45.690 34.829 6.759 1.00 40.02 O
ATOM 168 CB ASP A 26 46.079 31.926 7.749 1.00 33.43 C
ATOM 169 CG ASP A 26 46.205 30.424 7.472 1.00 43.37 C
ATOM 170 OD1 ASP A 26 45.172 29.722 7.313 1.00 41.47 O
ATOM 171 OD2 ASP A 26 47.366 29.947 7.439 1.00 39.07 O
ATOM 172 N PHE A 27 44.041 34.550 8.252 1.00 36.53 N
ATOM 173 CA PHE A 27 44.024 35.970 8.590 1.00 36.63 C
ATOM 174 C PHE A 27 44.463 36.119 10.033 1.00 36.76 C
ATOM 175 O PHE A 27 43.900 35.521 10.957 1.00 34.83 O
ATOM 176 CB PHE A 27 42.632 36.562 8.339 1.00 34.25 C
ATOM 177 CG PHE A 27 42.183 36.402 6.918 1.00 42.57 C
ATOM 178 CD1 PHE A 27 41.774 35.158 6.447 1.00 43.22 C
ATOM 179 CD2 PHE A 27 42.263 37.472 6.019 1.00 42.30 C
ATOM 180 CE1 PHE A 27 41.449 34.964 5.089 1.00 41.09 C
ATOM 181 CE2 PHE A 27 41.943 37.298 4.656 1.00 32.77 C
ATOM 182 CZ PHE A 27 41.535 36.044 4.192 1.00 47.47 C
ATOM 183 N VAL A 28 45.489 36.933 10.212 1.00 39.10 N
ATOM 184 CA VAL A 28 46.065 37.160 11.522 1.00 36.42 C
ATOM 185 C VAL A 28 45.315 38.116 12.430 1.00 41.87 C
ATOM 186 O VAL A 28 45.001 39.251 12.044 1.00 35.12 O
ATOM 187 CB VAL A 28 47.504 37.655 11.376 1.00 38.20 C
ATOM 188 CG1 VAL A 28 48.117 37.944 12.768 1.00 38.85 C
ATOM 189 CG2 VAL A 28 48.300 36.633 10.642 1.00 37.68 C
ATOM 190 N ASP A 29 45.022 37.636 13.633 1.00 39.24 N
ATOM 191 CA ASP A 29 44.371 38.423 14.678 1.00 37.04 C
ATOM 192 C ASP A 29 45.557 39.051 15.449 1.00 44.43 C
ATOM 193 O ASP A 29 46.419 38.332 15.973 1.00 39.87 O
ATOM 194 CB ASP A 29 43.576 37.500 15.596 1.00 38.34 C
ATOM 195 CG ASP A 29 42.922 38.216 16.748 1.00 37.09 C
ATOM 196 OD1 ASP A 29 43.593 39.027 17.445 1.00 38.10 O
ATOM 197 OD2 ASP A 29 41.727 37.932 16.995 1.00 37.19 O
ATOM 198 N HIS A 30 45.607 40.380 15.480 1.00 43.72 N
ATOM 199 CA HIS A 30 46.689 41.111 16.161 1.00 44.90 C
ATOM 200 C HIS A 30 46.231 41.660 17.507 1.00 43.92 C
ATOM 201 O HIS A 30 46.762 42.674 17.983 1.00 48.10 O
ATOM 202 CB HIS A 30 47.158 42.273 15.280 1.00 48.16 C
ATOM 203 CG HIS A 30 47.920 41.840 14.072 1.00 43.72 C
ATOM 204 ND1 HIS A 30 49.270 41.574 14.106 1.00 49.66 N
ATOM 205 CD2 HIS A 30 47.522 41.620 12.796 1.00 44.82 C
ATOM 206 CE1 HIS A 30 49.677 41.215 12.900 1.00 49.49 C
ATOM 207 NE2 HIS A 30 48.637 41.234 12.085 1.00 50.90 N
ATOM 208 N ILE A 31 45.238 40.990 18.095 1.00 37.87 N
ATOM 209 CA ILE A 31 44.635 41.331 19.377 1.00 42.15 C
ATOM 210 C ILE A 31 43.752 42.546 19.271 1.00 42.61 C
ATOM 211 O ILE A 31 42.582 42.517 19.666 1.00 40.81 O
ATOM 212 CB ILE A 31 45.690 41.617 20.466 1.00 43.08 C
ATOM 213 CG1 ILE A 31 46.638 40.411 20.591 1.00 45.62 C
ATOM 214 CG2 ILE A 31 44.989 41.935 21.773 1.00 41.44 C
ATOM 215 CD1 ILE A 31 47.586 40.457 21.785 1.00 41.07 C
ATOM 216 N ASP A 32 44.308 43.630 18.747 1.00 45.33 N
ATOM 217 CA ASP A 32 43.523 44.847 18.629 1.00 47.10 C
ATOM 218 C ASP A 32 42.644 44.788 17.384 1.00 48.52 C
ATOM 219 O ASP A 32 41.524 45.290 17.391 1.00 48.66 O
ATOM 220 CB ASP A 32 44.470 46.045 18.593 1.00 46.90 C
ATOM 221 CG ASP A 32 45.418 46.041 19.777 1.00 48.41 C
ATOM 222 OD1 ASP A 32 46.654 45.863 19.584 1.00 47.63 O
ATOM 223 OD2 ASP A 32 44.900 46.190 20.910 1.00 48.16 O
ATOM 224 N LEU A 33 43.153 44.171 16.321 1.00 45.87 N
ATOM 225 CA LEU A 33 42.378 44.051 15.103 1.00 49.59 C
ATOM 226 C LEU A 33 42.779 42.801 14.337 1.00 43.81 C
ATOM 227 O LEU A 33 43.811 42.198 14.621 1.00 46.31 O
ATOM 228 CB LEU A 33 42.555 45.287 14.209 1.00 51.06 C
ATOM 229 CG LEU A 33 43.810 45.449 13.353 1.00 59.73 C
ATOM 230 CD1 LEU A 33 43.390 45.917 11.965 1.00 66.34 C
ATOM 231 CD2 LEU A 33 44.766 46.452 13.977 1.00 66.74 C
ATOM 232 N VAL A 34 41.949 42.416 13.373 1.00 41.31 N
ATOM 233 CA VAL A 34 42.213 41.246 12.554 1.00 39.18 C
ATOM 234 C VAL A 34 42.393 41.695 11.119 1.00 40.51 C
ATOM 235 O VAL A 34 41.707 42.615 10.678 1.00 43.03 O
ATOM 236 CB VAL A 34 41.010 40.219 12.620 1.00 36.85 C
ATOM 237 CG1 VAL A 34 41.350 38.937 11.815 1.00 42.50 C
ATOM 238 CG2 VAL A 34 40.666 39.912 14.070 1.00 41.50 C
ATOM 239 N GLU A 35 43.315 41.073 10.391 1.00 39.93 N
ATOM 240 CA GLU A 35 43.498 41.412 8.984 1.00 43.08 C
ATOM 241 C GLU A 35 42.138 41.282 8.297 1.00 44.13 C
ATOM 242 O GLU A 35 41.400 40.321 8.524 1.00 44.01 O
ATOM 243 CB GLU A 35 44.519 40.484 8.318 1.00 46.36 C
ATOM 244 CG GLU A 35 45.869 40.504 9.009 1.00 46.24 C
ATOM 245 CD GLU A 35 46.889 39.590 8.369 1.00 54.74 C
ATOM 246 OE1 GLU A 35 46.553 38.420 8.083 1.00 47.55 O
ATOM 247 OE2 GLU A 35 48.043 40.031 8.167 1.00 61.12 O
ATOM 248 N PRO A 36 41.781 42.271 7.462 1.00 45.27 N
ATOM 249 CA PRO A 36 40.507 42.288 6.740 1.00 42.70 C
ATOM 250 C PRO A 36 40.350 41.099 5.801 1.00 35.47 C
ATOM 251 O PRO A 36 41.325 40.647 5.211 1.00 33.36 O
ATOM 252 CB PRO A 36 40.573 43.596 5.932 1.00 43.65 C
ATOM 253 CG PRO A 36 41.488 44.477 6.765 1.00 51.26 C
ATOM 254 CD PRO A 36 42.558 43.504 7.210 1.00 48.43 C
ATOM 255 N VAL A 37 39.127 40.607 5.644 1.00 36.86 N
ATOM 256 CA VAL A 37 38.948 39.520 4.675 1.00 38.65 C
ATOM 257 C VAL A 37 38.476 40.237 3.401 1.00 33.63 C
ATOM 258 O VAL A 37 37.306 40.593 3.264 1.00 39.93 O
ATOM 259 CB VAL A 37 37.918 38.459 5.136 1.00 40.77 C
ATOM 260 CG1 VAL A 37 37.899 37.300 4.135 1.00 40.93 C
ATOM 261 CG2 VAL A 37 38.317 37.913 6.497 1.00 42.60 C
ATOM 262 N ASP A 38 39.417 40.499 2.509 1.00 37.98 N
ATOM 263 CA ASP A 38 39.114 41.221 1.267 1.00 46.48 C
ATOM 264 C ASP A 38 39.187 40.317 0.045 1.00 39.54 C
ATOM 265 O ASP A 38 40.270 39.846 -0.340 1.00 43.72 O
ATOM 266 CB ASP A 38 40.084 42.403 1.096 1.00 50.87 C
ATOM 267 CG ASP A 38 41.526 41.951 0.944 1.00 59.41 C
ATOM 268 OD1 ASP A 38 42.013 41.225 1.838 1.00 54.40 O
ATOM 269 OD2 ASP A 38 42.171 42.317 -0.068 1.00 60.73 O
ATOM 270 N GLY A 39 38.030 40.086 -0.562 1.00 40.56 N
ATOM 271 CA GLY A 39 37.987 39.225 -1.729 1.00 43.62 C
ATOM 272 C GLY A 39 37.216 39.811 -2.906 1.00 48.13 C
ATOM 273 O GLY A 39 36.776 40.979 -2.897 1.00 41.87 O
ATOM 274 N VAL A 40 37.071 38.974 -3.928 1.00 49.89 N
ATOM 275 CA VAL A 40 36.351 39.301 -5.137 1.00 50.55 C
ATOM 276 C VAL A 40 35.579 38.072 -5.590 1.00 52.43 C
ATOM 277 O VAL A 40 36.044 36.938 -5.435 1.00 47.58 O
ATOM 278 CB VAL A 40 37.313 39.711 -6.263 1.00 54.42 C
ATOM 279 CG1 VAL A 40 36.566 39.753 -7.580 1.00 56.68 C
ATOM 280 CG2 VAL A 40 37.915 41.079 -5.967 1.00 54.35 C
ATOM 281 N VAL A 41 34.378 38.293 -6.108 1.00 51.28 N
ATOM 282 CA VAL A 41 33.581 37.206 -6.631 1.00 52.29 C
ATOM 283 C VAL A 41 33.291 37.494 -8.113 1.00 58.76 C
ATOM 284 O VAL A 41 32.730 38.542 -8.455 1.00 57.19 O
ATOM 285 CB VAL A 41 32.255 37.033 -5.851 1.00 55.45 C
ATOM 286 CG1 VAL A 41 31.469 38.323 -5.823 1.00 50.85 C
ATOM 287 CG2 VAL A 41 31.419 35.934 -6.497 1.00 58.61 C
ATOM 288 N LEU A 42 33.722 36.587 -8.989 1.00 59.83 N
ATOM 289 CA LEU A 42 33.477 36.724 -10.430 1.00 61.22 C
ATOM 290 C LEU A 42 32.065 36.213 -10.700 1.00 60.63 C
ATOM 291 O LEU A 42 31.743 35.057 -10.400 1.00 59.14 O
ATOM 292 CB LEU A 42 34.490 35.907 -11.229 1.00 62.23 C
ATOM 293 CG LEU A 42 34.442 36.038 -12.759 1.00 60.96 C
ATOM 294 CD1 LEU A 42 34.353 37.513 -13.179 1.00 58.77 C
ATOM 295 CD2 LEU A 42 35.697 35.408 -13.339 1.00 54.14 C
ATOM 296 N VAL A 43 31.226 37.077 -11.264 1.00 59.76 N
ATOM 297 CA VAL A 43 29.828 36.739 -11.529 1.00 62.02 C
ATOM 298 C VAL A 43 29.458 36.505 -13.012 1.00 63.17 C
ATOM 299 O VAL A 43 30.270 36.737 -13.913 1.00 62.63 O
ATOM 300 CB VAL A 43 28.928 37.845 -10.915 1.00 63.04 C
ATOM 301 CG1 VAL A 43 27.485 37.601 -11.248 1.00 68.46 C
ATOM 302 CG2 VAL A 43 29.117 37.879 -9.391 1.00 59.05 C
ATOM 303 N ASP A 44 28.233 36.028 -13.242 1.00 62.77 N
ATOM 304 CA ASP A 44 27.700 35.740 -14.587 1.00 70.51 C
ATOM 305 C ASP A 44 26.246 36.235 -14.691 1.00 68.55 C
ATOM 306 O ASP A 44 25.303 35.485 -14.423 1.00 65.14 O
ATOM 307 CB ASP A 44 27.745 34.231 -14.848 1.00 72.03 C
ATOM 308 CG ASP A 44 27.540 33.881 -16.312 1.00 75.02 C
ATOM 309 OD1 ASP A 44 26.442 34.144 -16.852 1.00 73.94 O
ATOM 310 OD2 ASP A 44 28.491 33.342 -16.917 1.00 70.79 O
ATOM 311 N PRO A 45 26.052 37.506 -15.088 1.00 70.64 N
ATOM 312 CA PRO A 45 24.724 38.124 -15.224 1.00 74.28 C
ATOM 313 C PRO A 45 23.706 37.347 -16.052 1.00 77.08 C
ATOM 314 O PRO A 45 22.565 37.144 -15.624 1.00 74.53 O
ATOM 315 CB PRO A 45 25.041 39.484 -15.833 1.00 72.25 C
ATOM 316 CG PRO A 45 26.389 39.790 -15.260 1.00 70.90 C
ATOM 317 CD PRO A 45 27.107 38.472 -15.437 1.00 70.52 C
ATOM 318 N GLU A 46 24.117 36.923 -17.242 1.00 82.68 N
ATOM 319 CA GLU A 46 23.222 36.181 -18.116 1.00 87.69 C
ATOM 320 C GLU A 46 22.682 34.977 -17.359 1.00 88.23 C
ATOM 321 O GLU A 46 21.532 34.576 -17.545 1.00 88.99 O
ATOM 322 CB GLU A 46 23.961 35.733 -19.383 1.00 90.58 C
ATOM 323 CG GLU A 46 23.099 34.927 -20.354 1.00 97.01 C
ATOM 324 CD GLU A 46 23.808 34.634 -21.667 1.00101.73 C
ATOM 325 OE1 GLU A 46 24.958 34.142 -21.627 1.00103.23 O
ATOM 326 OE2 GLU A 46 23.211 34.891 -22.741 1.00103.85 O
ATOM 327 N TYR A 47 23.519 34.423 -16.485 1.00 87.41 N
ATOM 328 CA TYR A 47 23.140 33.267 -15.693 1.00 86.89 C
ATOM 329 C TYR A 47 22.205 33.595 -14.535 1.00 85.64 C
ATOM 330 O TYR A 47 21.315 32.810 -14.214 1.00 85.09 O
ATOM 331 CB TYR A 47 24.386 32.571 -15.138 1.00 89.10 C
ATOM 332 CG TYR A 47 24.051 31.475 -14.153 1.00 92.23 C
ATOM 333 CD1 TYR A 47 23.406 30.311 -14.573 1.00 93.23 C
ATOM 334 CD2 TYR A 47 24.315 31.629 -12.786 1.00 92.26 C
ATOM 335 CE1 TYR A 47 23.022 29.327 -13.659 1.00 93.63 C
ATOM 336 CE2 TYR A 47 23.936 30.653 -11.863 1.00 93.05 C
ATOM 337 CZ TYR A 47 23.286 29.507 -12.309 1.00 94.81 C
ATOM 338 OH TYR A 47 22.869 28.558 -11.408 1.00 96.46 O
ATOM 339 N LEU A 48 22.393 34.751 -13.906 1.00 86.52 N
ATOM 340 CA LEU A 48 21.559 35.106 -12.762 1.00 87.80 C
ATOM 341 C LEU A 48 20.360 36.005 -13.011 1.00 87.13 C
ATOM 342 O LEU A 48 19.231 35.610 -12.736 1.00 89.57 O
ATOM 343 CB LEU A 48 22.428 35.718 -11.661 1.00 91.00 C
ATOM 344 CG LEU A 48 23.314 36.920 -11.992 1.00 92.05 C
ATOM 345 CD1 LEU A 48 22.539 38.228 -11.855 1.00 94.44 C
ATOM 346 CD2 LEU A 48 24.479 36.921 -11.028 1.00 89.99 C
ATOM 347 N LYS A 49 20.606 37.210 -13.518 1.00 85.59 N
ATOM 348 CA LYS A 49 19.544 38.175 -13.775 1.00 81.44 C
ATOM 349 C LYS A 49 18.967 38.732 -12.475 1.00 82.59 C
ATOM 350 O LYS A 49 19.611 39.546 -11.801 1.00 82.21 O
ATOM 351 CB LYS A 49 18.438 37.537 -14.614 0.00 79.44 C
ATOM 352 CG LYS A 49 18.934 37.031 -15.950 0.00 74.84 C
ATOM 353 CD LYS A 49 17.815 36.407 -16.754 0.00 71.51 C
ATOM 354 CE LYS A 49 18.335 35.894 -18.082 0.00 69.61 C
ATOM 355 NZ LYS A 49 17.241 35.330 -18.912 0.00 67.68 N
ATOM 356 N GLU A 50 17.760 38.298 -12.116 1.00 83.92 N
ATOM 357 CA GLU A 50 17.118 38.786 -10.894 1.00 86.02 C
ATOM 358 C GLU A 50 17.855 38.356 -9.624 1.00 85.23 C
ATOM 359 O GLU A 50 17.784 39.036 -8.596 1.00 84.16 O
ATOM 360 CB GLU A 50 15.656 38.319 -10.818 1.00 87.22 C
ATOM 361 CG GLU A 50 15.460 36.810 -10.689 1.00 91.07 C
ATOM 362 CD GLU A 50 15.713 36.067 -11.989 1.00 94.01 C
ATOM 363 OE1 GLU A 50 16.875 36.020 -12.444 1.00 93.86 O
ATOM 364 OE2 GLU A 50 14.739 35.529 -12.559 1.00 97.75 O
ATOM 365 N ARG A 51 18.559 37.228 -9.696 1.00 82.56 N
ATOM 366 CA ARG A 51 19.299 36.732 -8.541 1.00 81.51 C
ATOM 367 C ARG A 51 20.515 37.594 -8.220 1.00 81.30 C
ATOM 368 O ARG A 51 21.337 37.886 -9.092 1.00 80.25 O
ATOM 369 CB ARG A 51 19.749 35.286 -8.769 1.00 79.90 C
ATOM 370 CG ARG A 51 18.635 34.260 -8.658 1.00 76.50 C
ATOM 371 CD ARG A 51 19.172 32.852 -8.885 1.00 77.01 C
ATOM 372 NE ARG A 51 19.830 32.719 -10.183 1.00 74.40 N
ATOM 373 CZ ARG A 51 20.235 31.563 -10.701 1.00 75.76 C
ATOM 374 NH1 ARG A 51 20.049 30.435 -10.027 1.00 76.84 N
ATOM 375 NH2 ARG A 51 20.820 31.532 -11.894 1.00 73.84 N
ATOM 376 N ARG A 52 20.614 38.003 -6.958 1.00 80.05 N
ATOM 377 CA ARG A 52 21.731 38.817 -6.492 1.00 75.39 C
ATOM 378 C ARG A 52 22.795 37.856 -5.997 1.00 72.36 C
ATOM 379 O ARG A 52 22.504 36.691 -5.722 1.00 71.70 O
ATOM 380 CB ARG A 52 21.291 39.713 -5.331 1.00 76.84 C
ATOM 381 CG ARG A 52 20.040 40.533 -5.608 1.00 81.17 C
ATOM 382 CD ARG A 52 19.518 41.181 -4.335 1.00 84.40 C
ATOM 383 NE ARG A 52 18.102 41.519 -4.445 1.00 87.21 N
ATOM 384 CZ ARG A 52 17.327 41.852 -3.415 1.00 91.98 C
ATOM 385 NH1 ARG A 52 17.825 41.898 -2.183 1.00 91.16 N
ATOM 386 NH2 ARG A 52 16.043 42.128 -3.614 1.00 93.76 N
ATOM 387 N VAL A 53 24.031 38.330 -5.906 1.00 67.89 N
ATOM 388 CA VAL A 53 25.101 37.487 -5.389 1.00 63.97 C
ATOM 389 C VAL A 53 25.481 37.993 -4.005 1.00 60.66 C
ATOM 390 O VAL A 53 25.894 39.143 -3.842 1.00 58.92 O
ATOM 391 CB VAL A 53 26.353 37.502 -6.280 1.00 58.82 C
ATOM 392 CG1 VAL A 53 27.430 36.589 -5.673 1.00 53.46 C