HEADER CONTRACTILE PROTEIN 19-NOV-99 1DFK
TITLE NUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN HEAD;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEAVY CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MYOSIN HEAD;
COMPND 7 CHAIN: Y;
COMPND 8 FRAGMENT: REGULATORY LIGHT CHAIN;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: MYOSIN HEAD;
COMPND 11 CHAIN: Z;
COMPND 12 FRAGMENT: ESSENTIAL LIGHT CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS;
SOURCE 3 ORGANISM_TAXID: 31199;
SOURCE 4 TISSUE: SKELETAL MUSCLE;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS;
SOURCE 7 ORGANISM_TAXID: 31199;
SOURCE 8 TISSUE: SKELETAL MUSCLE;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS;
SOURCE 11 ORGANISM_TAXID: 31199;
SOURCE 12 TISSUE: SKELETAL MUSCLE
KEYWDS MYOSIN MOTOR, CONFORMATIONAL CHANGES, CONTRACTILE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HOUDUSSE,A.G.SZENT-GYORGYI,C.COHEN
REVDAT 5 07-FEB-24 1DFK 1 REMARK LINK
REVDAT 4 31-JAN-18 1DFK 1 REMARK
REVDAT 3 24-FEB-09 1DFK 1 VERSN
REVDAT 2 01-APR-03 1DFK 1 JRNL
REVDAT 1 25-OCT-00 1DFK 0
JRNL AUTH A.HOUDUSSE,A.G.SZENT-GYORGYI,C.COHEN
JRNL TITL THREE CONFORMATIONAL STATES OF SCALLOP MYOSIN S1.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 11238 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 11016966
JRNL DOI 10.1073/PNAS.200376897
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.HOUDUSSE,V.N.KALABOKIS,D.HIMMEL,A.G.SZENT-GYORGYI,C.COHEN
REMARK 1 TITL ATOMIC STRUCTURE OF SCALLOP MYOSIN SUBFRAGMENT S1 COMPLEXED
REMARK 1 TITL 2 WITH MGADP: A NOVEL CONFORMATION OF THE MYOSIN HEAD.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 97 459 1999
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)80756-4
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.HOUDUSSE,C.COHEN
REMARK 1 TITL STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2 A
REMARK 1 TITL 2 RESOLUTION: IMPLICATIONS FOR REGULATION.
REMARK 1 REF STRUCTURE V. 4 21 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(96)00154-2
REMARK 2
REMARK 2 RESOLUTION. 4.20 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 10601
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.415
REMARK 3 FREE R VALUE : 0.410
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 508
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5031
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 2.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 AT THIS RESOLUTION, WE PERFORMED ONLY A RIGID BODY REFINEMENT.
REMARK 3 NO POSITIONAL REFINEMENT WAS DONE.
REMARK 4
REMARK 4 1DFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : CHESS; NULL
REMARK 200 BEAMLINE : A1; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 139608
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.61
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, AMMONIUM SULFATE, CACODYLATE,
REMARK 280 GLYCEROL , PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 4K,
REMARK 280 TEMPERATURE 277.0K
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 26.05000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Y, Z
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 ARG A 17
REMARK 465 LYS A 18
REMARK 465 LYS A 19
REMARK 465 LEU A 20
REMARK 465 MET A 21
REMARK 465 LYS A 22
REMARK 465 GLU A 23
REMARK 465 GLN A 24
REMARK 465 THR A 25
REMARK 465 ALA A 26
REMARK 465 ALA A 27
REMARK 465 ALA A 197
REMARK 465 CYS A 198
REMARK 465 ALA A 199
REMARK 465 VAL A 200
REMARK 465 LYS A 201
REMARK 465 LYS A 202
REMARK 465 LYS A 203
REMARK 465 ASP A 204
REMARK 465 GLU A 205
REMARK 465 GLU A 206
REMARK 465 ALA A 207
REMARK 465 SER A 208
REMARK 465 ASP A 209
REMARK 465 LYS A 210
REMARK 465 LYS A 211
REMARK 465 GLU A 212
REMARK 465 GLY A 213
REMARK 465 SER A 214
REMARK 465 LEU A 215
REMARK 465 ASN A 231
REMARK 465 ALA A 232
REMARK 465 LYS A 233
REMARK 465 THR A 234
REMARK 465 THR A 235
REMARK 465 ARG A 236
REMARK 465 ASN A 237
REMARK 465 ASN A 238
REMARK 465 ASN A 239
REMARK 465 SER A 240
REMARK 465 SER A 241
REMARK 465 GLU A 279
REMARK 465 ARG A 280
REMARK 465 ASN A 281
REMARK 465 TYR A 282
REMARK 465 HIS A 283
REMARK 465 ILE A 284
REMARK 465 PHE A 285
REMARK 465 TYR A 286
REMARK 465 GLN A 287
REMARK 465 ILE A 288
REMARK 465 CYS A 289
REMARK 465 SER A 290
REMARK 465 ASN A 291
REMARK 465 ALA A 292
REMARK 465 GLN A 365
REMARK 465 ARG A 366
REMARK 465 PRO A 367
REMARK 465 ARG A 368
REMARK 465 GLU A 369
REMARK 465 GLU A 370
REMARK 465 GLN A 371
REMARK 465 VAL A 403
REMARK 465 LYS A 404
REMARK 465 VAL A 405
REMARK 465 GLY A 406
REMARK 465 THR A 407
REMARK 465 GLU A 408
REMARK 465 MET A 409
REMARK 465 VAL A 410
REMARK 465 THR A 411
REMARK 465 LYS A 412
REMARK 465 GLY A 413
REMARK 465 GLN A 414
REMARK 465 ASN A 415
REMARK 465 THR A 569
REMARK 465 ARG A 570
REMARK 465 PRO A 571
REMARK 465 PRO A 625
REMARK 465 GLU A 626
REMARK 465 GLU A 627
REMARK 465 PRO A 628
REMARK 465 ALA A 629
REMARK 465 GLY A 630
REMARK 465 GLY A 631
REMARK 465 GLY A 632
REMARK 465 LYS A 633
REMARK 465 LYS A 634
REMARK 465 LYS A 635
REMARK 465 LYS A 636
REMARK 465 GLY A 637
REMARK 465 LYS A 638
REMARK 465 SER A 639
REMARK 465 SER A 640
REMARK 465 ALA A 641
REMARK 465 PHE A 642
REMARK 465 GLN A 643
REMARK 465 GLN A 730
REMARK 465 GLY A 731
REMARK 465 PHE A 732
REMARK 465 VAL A 733
REMARK 465 ASP A 734
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 SER A 6 OG
REMARK 470 ASP A 7 CG OD1 OD2
REMARK 470 PRO A 8 CG CD
REMARK 470 ASP A 9 CG OD1 OD2
REMARK 470 PHE A 10 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 11 CG CD OE1 NE2
REMARK 470 TYR A 12 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 13 CG CD1 CD2
REMARK 470 VAL A 15 CG1 CG2
REMARK 470 ASP A 16 CG OD1 OD2
REMARK 470 PHE A 28 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 29 CG OD1 OD2
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 LYS A 32 CG CD CE NZ
REMARK 470 ASN A 33 CG OD1 ND2
REMARK 470 CYS A 34 SG
REMARK 470 TRP A 35 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 35 CZ3 CH2
REMARK 470 VAL A 36 CG1 CG2
REMARK 470 PRO A 37 CG CD
REMARK 470 ASP A 38 CG OD1 OD2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 GLU A 41 CG CD OE1 OE2
REMARK 470 PHE A 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 45 OG
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 ILE A 48 CG1 CG2 CD1
REMARK 470 GLN A 49 CG CD OE1 NE2
REMARK 470 SER A 50 OG
REMARK 470 SER A 51 OG
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 ASP A 54 CG OD1 OD2
REMARK 470 GLU A 55 CG CD OE1 OE2
REMARK 470 ILE A 56 CG1 CG2 CD1
REMARK 470 THR A 57 OG1 CG2
REMARK 470 VAL A 58 CG1 CG2
REMARK 470 LYS A 59 CG CD CE NZ
REMARK 470 ILE A 60 CG1 CG2 CD1
REMARK 470 VAL A 61 CG1 CG2
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 SER A 64 OG
REMARK 470 SER A 65 OG
REMARK 470 THR A 66 OG1 CG2
REMARK 470 ARG A 67 CG CD NE CZ NH1 NH2
REMARK 470 THR A 68 OG1 CG2
REMARK 470 VAL A 69 CG1 CG2
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 ASP A 72 CG OD1 OD2
REMARK 470 ASP A 73 CG OD1 OD2
REMARK 470 ILE A 74 CG1 CG2 CD1
REMARK 470 GLN A 75 CG CD OE1 NE2
REMARK 470 SER A 76 OG
REMARK 470 MET A 77 CG SD CE
REMARK 470 ASN A 78 CG OD1 ND2
REMARK 470 PRO A 79 CG CD
REMARK 470 PRO A 80 CG CD
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 PHE A 82 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 LEU A 85 CG CD1 CD2
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 ASP A 87 CG OD1 OD2
REMARK 470 MET A 88 CG SD CE
REMARK 470 ASN A 90 CG OD1 ND2
REMARK 470 MET A 91 CG SD CE
REMARK 470 THR A 92 OG1 CG2
REMARK 470 TYR A 93 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 94 CG CD1 CD2
REMARK 470 ASN A 95 CG OD1 ND2
REMARK 470 GLU A 96 CG CD OE1 OE2
REMARK 470 SER A 98 OG
REMARK 470 VAL A 99 CG1 CG2
REMARK 470 LEU A 100 CG CD1 CD2
REMARK 470 TYR A 101 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 102 CG OD1 ND2
REMARK 470 LEU A 103 CG CD1 CD2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 SER A 105 OG
REMARK 470 ARG A 106 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 107 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 108 OG1 CG2
REMARK 470 SER A 109 OG
REMARK 470 LEU A 111 CG CD1 CD2
REMARK 470 ILE A 112 CG1 CG2 CD1
REMARK 470 TYR A 113 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 114 OG1 CG2
REMARK 470 TYR A 115 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 116 OG
REMARK 470 LEU A 118 CG CD1 CD2
REMARK 470 PHE A 119 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS A 120 SG
REMARK 470 ILE A 121 CG1 CG2 CD1
REMARK 470 VAL A 123 CG1 CG2
REMARK 470 ASN A 124 CG OD1 ND2
REMARK 470 PRO A 125 CG CD
REMARK 470 TYR A 126 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 127 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 129 CG CD1 CD2
REMARK 470 PRO A 130 CG CD
REMARK 470 ILE A 131 CG1 CG2 CD1
REMARK 470 TYR A 132 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 133 OG1 CG2
REMARK 470 ASP A 134 CG OD1 OD2
REMARK 470 SER A 135 OG
REMARK 470 VAL A 136 CG1 CG2
REMARK 470 ILE A 137 CG1 CG2 CD1
REMARK 470 LYS A 139 CG CD CE NZ
REMARK 470 TYR A 140 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 141 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 144 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 THR A 146 OG1 CG2
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 ILE A 148 CG1 CG2 CD1
REMARK 470 PRO A 149 CG CD
REMARK 470 PRO A 150 CG CD
REMARK 470 HIS A 151 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 152 CG CD1 CD2
REMARK 470 PHE A 153 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 154 OG
REMARK 470 VAL A 155 CG1 CG2
REMARK 470 ASP A 157 CG OD1 OD2
REMARK 470 ASN A 158 CG OD1 ND2
REMARK 470 TYR A 160 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 161 CG CD OE1 NE2
REMARK 470 ASN A 162 CG OD1 ND2
REMARK 470 MET A 163 CG SD CE
REMARK 470 VAL A 164 CG1 CG2
REMARK 470 THR A 165 OG1 CG2
REMARK 470 ASP A 166 CG OD1 OD2
REMARK 470 ARG A 167 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 168 CG CD OE1 OE2
REMARK 470 ASN A 169 CG OD1 ND2
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 SER A 171 OG
REMARK 470 CYS A 172 SG
REMARK 470 LEU A 173 CG CD1 CD2
REMARK 470 ILE A 174 CG1 CG2 CD1
REMARK 470 THR A 175 OG1 CG2
REMARK 470 GLU A 177 CG CD OE1 OE2
REMARK 470 SER A 178 OG
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 THR A 183 OG1 CG2
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 ASN A 185 CG OD1 ND2
REMARK 470 THR A 186 OG1 CG2
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 188 CG CD CE NZ
REMARK 470 VAL A 189 CG1 CG2
REMARK 470 ILE A 190 CG1 CG2 CD1
REMARK 470 MET A 191 CG SD CE
REMARK 470 TYR A 192 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 193 CG CD1 CD2
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 VAL A 196 CG1 CG2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 ASP A 217 CG OD1 OD2
REMARK 470 GLN A 218 CG CD OE1 NE2
REMARK 470 ILE A 219 CG1 CG2 CD1
REMARK 470 ILE A 220 CG1 CG2 CD1
REMARK 470 GLN A 221 CG CD OE1 NE2
REMARK 470 ASN A 223 CG OD1 ND2
REMARK 470 PRO A 224 CG CD
REMARK 470 VAL A 225 CG1 CG2
REMARK 470 LEU A 226 CG CD1 CD2
REMARK 470 GLU A 227 CG CD OE1 OE2
REMARK 470 TYR A 229 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 242 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 243 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 245 CG CD CE NZ
REMARK 470 PHE A 246 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 247 CG1 CG2 CD1
REMARK 470 ARG A 248 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 249 CG1 CG2 CD1
REMARK 470 HIS A 250 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 251 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 253 CG CD
REMARK 470 THR A 254 OG1 CG2
REMARK 470 LYS A 256 CG CD CE NZ
REMARK 470 ILE A 257 CG1 CG2 CD1
REMARK 470 ASP A 261 CG OD1 OD2
REMARK 470 ILE A 262 CG1 CG2 CD1
REMARK 470 GLU A 263 CG CD OE1 OE2
REMARK 470 THR A 264 OG1 CG2
REMARK 470 TYR A 265 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 266 CG CD1 CD2
REMARK 470 LEU A 267 CG CD1 CD2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 LYS A 269 CG CD CE NZ
REMARK 470 SER A 270 OG
REMARK 470 ARG A 271 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 272 CG1 CG2
REMARK 470 THR A 273 OG1 CG2
REMARK 470 TYR A 274 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 275 CG CD OE1 NE2
REMARK 470 GLN A 276 CG CD OE1 NE2
REMARK 470 SER A 277 OG
REMARK 470 ILE A 293 CG1 CG2 CD1
REMARK 470 PRO A 294 CG CD
REMARK 470 GLU A 295 CG CD OE1 OE2
REMARK 470 LEU A 296 CG CD1 CD2
REMARK 470 ASN A 297 CG OD1 ND2
REMARK 470 ASP A 298 CG OD1 OD2
REMARK 470 VAL A 299 CG1 CG2
REMARK 470 MET A 300 CG SD CE
REMARK 470 LEU A 301 CG CD1 CD2
REMARK 470 VAL A 302 CG1 CG2
REMARK 470 THR A 303 OG1 CG2
REMARK 470 PRO A 304 CG CD
REMARK 470 ASP A 305 CG OD1 OD2
REMARK 470 SER A 306 OG
REMARK 470 LEU A 308 CG CD1 CD2
REMARK 470 TYR A 309 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 310 OG
REMARK 470 PHE A 311 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 312 CG1 CG2 CD1
REMARK 470 ASN A 313 CG OD1 ND2
REMARK 470 GLN A 314 CG CD OE1 NE2
REMARK 470 CYS A 316 SG
REMARK 470 LEU A 317 CG CD1 CD2
REMARK 470 THR A 318 OG1 CG2
REMARK 470 VAL A 319 CG1 CG2
REMARK 470 ASP A 320 CG OD1 OD2
REMARK 470 ASN A 321 CG OD1 ND2
REMARK 470 ILE A 322 CG1 CG2 CD1
REMARK 470 ASP A 323 CG OD1 OD2
REMARK 470 ASP A 324 CG OD1 OD2
REMARK 470 VAL A 325 CG1 CG2
REMARK 470 GLU A 326 CG CD OE1 OE2
REMARK 470 GLU A 327 CG CD OE1 OE2
REMARK 470 PHE A 328 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 LEU A 330 CG CD1 CD2
REMARK 470 CYS A 331 SG
REMARK 470 ASP A 332 CG OD1 OD2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 PHE A 335 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 336 CG OD1 OD2
REMARK 470 ILE A 337 CG1 CG2 CD1
REMARK 470 LEU A 338 CG CD1 CD2
REMARK 470 PHE A 340 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 341 OG1 CG2
REMARK 470 LYS A 342 CG CD CE NZ
REMARK 470 GLU A 343 CG CD OE1 OE2
REMARK 470 GLU A 344 CG CD OE1 OE2
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 GLN A 346 CG CD OE1 NE2
REMARK 470 SER A 347 OG
REMARK 470 MET A 348 CG SD CE
REMARK 470 PHE A 349 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 350 CG CD CE NZ
REMARK 470 CYS A 351 SG
REMARK 470 THR A 352 OG1 CG2
REMARK 470 SER A 354 OG
REMARK 470 ILE A 355 CG1 CG2 CD1
REMARK 470 LEU A 356 CG CD1 CD2
REMARK 470 HIS A 357 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 358 CG SD CE
REMARK 470 GLU A 360 CG CD OE1 OE2
REMARK 470 MET A 361 CG SD CE
REMARK 470 LYS A 362 CG CD CE NZ
REMARK 470 PHE A 363 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 364 CG CD CE NZ
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 SER A 374 OG
REMARK 470 ASP A 375 CG OD1 OD2
REMARK 470 THR A 377 OG1 CG2
REMARK 470 GLU A 379 CG CD OE1 OE2
REMARK 470 GLU A 381 CG CD OE1 OE2
REMARK 470 LYS A 382 CG CD CE NZ
REMARK 470 VAL A 383 CG1 CG2
REMARK 470 PHE A 385 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 386 CG CD1 CD2
REMARK 470 CYS A 387 SG
REMARK 470 ILE A 389 CG1 CG2 CD1
REMARK 470 ASN A 390 CG OD1 ND2
REMARK 470 ASP A 393 CG OD1 OD2
REMARK 470 LEU A 394 CG CD1 CD2
REMARK 470 LEU A 395 CG CD1 CD2
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 LEU A 398 CG CD1 CD2
REMARK 470 LEU A 399 CG CD1 CD2
REMARK 470 LYS A 400 CG CD CE NZ
REMARK 470 PRO A 401 CG CD
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 MET A 416 CG SD CE
REMARK 470 ASN A 417 CG OD1 ND2
REMARK 470 GLN A 418 CG CD OE1 NE2
REMARK 470 VAL A 419 CG1 CG2
REMARK 470 VAL A 420 CG1 CG2
REMARK 470 ASN A 421 CG OD1 ND2
REMARK 470 SER A 422 OG
REMARK 470 VAL A 423 CG1 CG2
REMARK 470 LEU A 426 CG CD1 CD2
REMARK 470 LYS A 428 CG CD CE NZ
REMARK 470 SER A 429 OG
REMARK 470 LEU A 430 CG CD1 CD2
REMARK 470 TYR A 431 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 432 CG OD1 OD2
REMARK 470 ARG A 433 CG CD NE CZ NH1 NH2
REMARK 470 MET A 434 CG SD CE
REMARK 470 PHE A 435 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 436 CG OD1 ND2
REMARK 470 TRP A 437 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 437 CZ3 CH2
REMARK 470 LEU A 438 CG CD1 CD2
REMARK 470 VAL A 439 CG1 CG2
REMARK 470 ARG A 440 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 441 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 442 CG1 CG2
REMARK 470 ASN A 443 CG OD1 ND2
REMARK 470 LYS A 444 CG CD CE NZ
REMARK 470 THR A 445 OG1 CG2
REMARK 470 LEU A 446 CG CD1 CD2
REMARK 470 ASP A 447 CG OD1 OD2
REMARK 470 THR A 448 OG1 CG2
REMARK 470 LYS A 449 CG CD CE NZ
REMARK 470 LYS A 451 CG CD CE NZ
REMARK 470 ARG A 452 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 453 CG OD1 ND2
REMARK 470 TYR A 454 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A 455 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 456 CG1 CG2 CD1
REMARK 470 VAL A 458 CG1 CG2
REMARK 470 LEU A 459 CG CD1 CD2
REMARK 470 ASP A 460 CG OD1 OD2
REMARK 470 ILE A 461 CG1 CG2 CD1
REMARK 470 PHE A 464 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 465 CG CD OE1 OE2
REMARK 470 ILE A 466 CG1 CG2 CD1
REMARK 470 PHE A 467 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 468 CG OD1 OD2
REMARK 470 PHE A 469 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 470 CG OD1 ND2
REMARK 470 SER A 471 OG
REMARK 470 PHE A 472 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 473 CG CD OE1 OE2
REMARK 470 GLN A 474 CG CD OE1 NE2
REMARK 470 LEU A 475 CG CD1 CD2
REMARK 470 CYS A 476 SG
REMARK 470 ILE A 477 CG1 CG2 CD1
REMARK 470 ASN A 478 CG OD1 ND2
REMARK 470 TYR A 479 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 480 OG1 CG2
REMARK 470 ASN A 481 CG OD1 ND2
REMARK 470 GLU A 482 CG CD OE1 OE2
REMARK 470 ARG A 483 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 484 CG CD1 CD2
REMARK 470 GLN A 485 CG CD OE1 NE2
REMARK 470 GLN A 486 CG CD OE1 NE2
REMARK 470 PHE A 487 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 488 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 489 CG OD1 ND2
REMARK 470 HIS A 490 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 491 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 492 CG SD CE
REMARK 470 PHE A 493 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 494 CG1 CG2 CD1
REMARK 470 LEU A 495 CG CD1 CD2
REMARK 470 GLU A 496 CG CD OE1 OE2
REMARK 470 GLN A 497 CG CD OE1 NE2
REMARK 470 GLU A 498 CG CD OE1 OE2
REMARK 470 GLU A 499 CG CD OE1 OE2
REMARK 470 TYR A 500 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 501 CG CD CE NZ
REMARK 470 LYS A 502 CG CD CE NZ
REMARK 470 GLU A 503 CG CD OE1 OE2
REMARK 470 ILE A 505 CG1 CG2 CD1
REMARK 470 TRP A 507 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 507 CZ3 CH2
REMARK 470 GLU A 508 CG CD OE1 OE2
REMARK 470 PHE A 509 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 510 CG1 CG2 CD1
REMARK 470 ASP A 511 CG OD1 OD2
REMARK 470 PHE A 512 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 514 CG SD CE
REMARK 470 ASP A 515 CG OD1 OD2
REMARK 470 LEU A 516 CG CD1 CD2
REMARK 470 GLN A 517 CG CD OE1 NE2
REMARK 470 MET A 518 CG SD CE
REMARK 470 CYS A 519 SG
REMARK 470 ILE A 520 CG1 CG2 CD1
REMARK 470 ASP A 521 CG OD1 OD2
REMARK 470 LEU A 522 CG CD1 CD2
REMARK 470 ILE A 523 CG1 CG2 CD1
REMARK 470 GLU A 524 CG CD OE1 OE2
REMARK 470 LYS A 525 CG CD CE NZ
REMARK 470 PRO A 526 CG CD
REMARK 470 MET A 527 CG SD CE
REMARK 470 ILE A 529 CG1 CG2 CD1
REMARK 470 LEU A 530 CG CD1 CD2
REMARK 470 SER A 531 OG
REMARK 470 ILE A 532 CG1 CG2 CD1
REMARK 470 LEU A 533 CG CD1 CD2
REMARK 470 GLU A 534 CG CD OE1 OE2
REMARK 470 GLU A 535 CG CD OE1 OE2
REMARK 470 GLU A 536 CG CD OE1 OE2
REMARK 470 CYS A 537 SG
REMARK 470 MET A 538 CG SD CE
REMARK 470 PHE A 539 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 540 CG CD
REMARK 470 LYS A 541 CG CD CE NZ
REMARK 470 ASP A 543 CG OD1 OD2
REMARK 470 ASP A 544 CG OD1 OD2
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 SER A 546 OG
REMARK 470 PHE A 547 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 548 CG CD OE1 NE2
REMARK 470 ASP A 549 CG OD1 OD2
REMARK 470 LYS A 550 CG CD CE NZ
REMARK 470 LEU A 551 CG CD1 CD2
REMARK 470 TYR A 552 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 553 CG CD OE1 NE2
REMARK 470 ASN A 554 CG OD1 ND2
REMARK 470 HIS A 555 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 556 CG SD CE
REMARK 470 LYS A 558 CG CD CE NZ
REMARK 470 ASN A 559 CG OD1 ND2
REMARK 470 ARG A 560 CG CD NE CZ NH1 NH2
REMARK 470 MET A 561 CG SD CE
REMARK 470 PHE A 562 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 563 OG1 CG2
REMARK 470 LYS A 564 CG CD CE NZ
REMARK 470 PRO A 565 CG CD
REMARK 470 LYS A 567 CG CD CE NZ
REMARK 470 PRO A 568 CG CD
REMARK 470 ASN A 572 CG OD1 ND2
REMARK 470 GLN A 573 CG CD OE1 NE2
REMARK 470 PRO A 575 CG CD
REMARK 470 HIS A 577 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 578 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 579 CG CD OE1 OE2
REMARK 470 LEU A 580 CG CD1 CD2
REMARK 470 HIS A 581 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 582 CG ND1 CD2 CE1 NE2
REMARK 470 TYR A 583 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 586 CG OD1 ND2
REMARK 470 VAL A 587 CG1 CG2
REMARK 470 PRO A 588 CG CD
REMARK 470 TYR A 589 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 590 OG
REMARK 470 ILE A 591 CG1 CG2 CD1
REMARK 470 THR A 592 OG1 CG2
REMARK 470 TRP A 594 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 594 CZ3 CH2
REMARK 470 LEU A 595 CG CD1 CD2
REMARK 470 GLU A 596 CG CD OE1 OE2
REMARK 470 LYS A 597 CG CD CE NZ
REMARK 470 ASN A 598 CG OD1 ND2
REMARK 470 LYS A 599 CG CD CE NZ
REMARK 470 ASP A 600 CG OD1 OD2
REMARK 470 PRO A 601 CG CD
REMARK 470 ILE A 602 CG1 CG2 CD1
REMARK 470 ASN A 603 CG OD1 ND2
REMARK 470 GLU A 604 CG CD OE1 OE2
REMARK 470 ASN A 605 CG OD1 ND2
REMARK 470 VAL A 606 CG1 CG2
REMARK 470 VAL A 607 CG1 CG2
REMARK 470 LEU A 609 CG CD1 CD2
REMARK 470 LEU A 610 CG CD1 CD2
REMARK 470 SER A 613 OG
REMARK 470 LYS A 614 CG CD CE NZ
REMARK 470 GLU A 615 CG CD OE1 OE2
REMARK 470 PRO A 616 CG CD
REMARK 470 LEU A 617 CG CD1 CD2
REMARK 470 VAL A 618 CG1 CG2
REMARK 470 GLU A 620 CG CD OE1 OE2
REMARK 470 LEU A 621 CG CD1 CD2
REMARK 470 PHE A 622 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 623 CG CD CE NZ
REMARK 470 THR A 644 OG1 CG2
REMARK 470 ILE A 645 CG1 CG2 CD1
REMARK 470 SER A 646 OG
REMARK 470 VAL A 648 CG1 CG2
REMARK 470 HIS A 649 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 650 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 651 CG CD OE1 OE2
REMARK 470 SER A 652 OG
REMARK 470 LEU A 653 CG CD1 CD2
REMARK 470 ASN A 654 CG OD1 ND2
REMARK 470 LYS A 655 CG CD CE NZ
REMARK 470 LEU A 656 CG CD1 CD2
REMARK 470 MET A 657 CG SD CE
REMARK 470 LYS A 658 CG CD CE NZ
REMARK 470 ASN A 659 CG OD1 ND2
REMARK 470 LEU A 660 CG CD1 CD2
REMARK 470 TYR A 661 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 662 OG
REMARK 470 THR A 663 OG1 CG2
REMARK 470 HIS A 664 CG ND1 CD2 CE1 NE2
REMARK 470 PRO A 665 CG CD
REMARK 470 HIS A 666 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 667 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 668 CG1 CG2
REMARK 470 ARG A 669 CG CD NE CZ NH1 NH2
REMARK 470 CYS A 670 SG
REMARK 470 ILE A 671 CG1 CG2 CD1
REMARK 470 ILE A 672 CG1 CG2 CD1
REMARK 470 PRO A 673 CG CD
REMARK 470 ASN A 674 CG OD1 ND2
REMARK 470 GLU A 675 CG CD OE1 OE2
REMARK 470 LEU A 676 CG CD1 CD2
REMARK 470 LYS A 677 CG CD CE NZ
REMARK 470 GLN A 678 CG CD OE1 NE2
REMARK 470 PRO A 679 CG CD
REMARK 470 LEU A 681 CG CD1 CD2
REMARK 470 VAL A 682 CG1 CG2
REMARK 470 ASP A 683 CG OD1 OD2
REMARK 470 GLU A 685 CG CD OE1 OE2
REMARK 470 LEU A 686 CG CD1 CD2
REMARK 470 VAL A 687 CG1 CG2
REMARK 470 LEU A 688 CG CD1 CD2
REMARK 470 HIS A 689 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 690 CG CD OE1 NE2
REMARK 470 LEU A 691 CG CD1 CD2
REMARK 470 GLN A 692 CG CD OE1 NE2
REMARK 470 CYS A 693 SG
REMARK 470 ASN A 694 CG OD1 ND2
REMARK 470 VAL A 696 CG1 CG2
REMARK 470 LEU A 697 CG CD1 CD2
REMARK 470 GLU A 698 CG CD OE1 OE2
REMARK 470 ILE A 700 CG1 CG2 CD1
REMARK 470 ARG A 701 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 702 CG1 CG2 CD1
REMARK 470 CYS A 703 SG
REMARK 470 ARG A 704 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 705 CG CD CE NZ
REMARK 470 PHE A 707 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 708 CG CD
REMARK 470 SER A 709 OG
REMARK 470 ARG A 710 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 711 CG CD1 CD2
REMARK 470 ILE A 712 CG1 CG2 CD1
REMARK 470 TYR A 713 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 714 OG
REMARK 470 GLU A 715 CG CD OE1 OE2
REMARK 470 PHE A 716 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 717 CG CD CE NZ
REMARK 470 GLN A 718 CG CD OE1 NE2
REMARK 470 ARG A 719 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 720 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 721 OG
REMARK 470 ILE A 722 CG1 CG2 CD1
REMARK 470 LEU A 723 CG CD1 CD2
REMARK 470 PRO A 725 CG CD
REMARK 470 ASN A 726 CG OD1 ND2
REMARK 470 ILE A 728 CG1 CG2 CD1
REMARK 470 PRO A 729 CG CD
REMARK 470 LYS A 736 CG CD CE NZ
REMARK 470 THR A 737 OG1 CG2
REMARK 470 VAL A 738 CG1 CG2
REMARK 470 SER A 739 OG
REMARK 470 GLU A 740 CG CD OE1 OE2
REMARK 470 LYS A 741 CG CD CE NZ
REMARK 470 ILE A 742 CG1 CG2 CD1
REMARK 470 LEU A 743 CG CD1 CD2
REMARK 470 LEU A 746 CG CD1 CD2
REMARK 470 GLN A 747 CG CD OE1 NE2
REMARK 470 MET A 748 CG SD CE
REMARK 470 ASP A 749 CG OD1 OD2
REMARK 470 PRO A 750 CG CD
REMARK 470 GLU A 752 CG CD OE1 OE2
REMARK 470 TYR A 753 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 754 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 755 CG CD1 CD2
REMARK 470 THR A 757 OG1 CG2
REMARK 470 THR A 758 OG1 CG2
REMARK 470 LYS A 759 CG CD CE NZ
REMARK 470 VAL A 760 CG1 CG2
REMARK 470 PHE A 761 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 762 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 763 CG CD CE NZ
REMARK 470 VAL A 766 CG1 CG2
REMARK 470 LEU A 767 CG CD1 CD2
REMARK 470 ASN A 769 CG OD1 ND2
REMARK 470 LEU A 770 CG CD1 CD2
REMARK 470 GLU A 771 CG CD OE1 OE2
REMARK 470 GLU A 772 CG CD OE1 OE2
REMARK 470 MET A 773 CG SD CE
REMARK 470 ARG A 774 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 775 CG OD1 OD2
REMARK 470 GLU A 776 CG CD OE1 OE2
REMARK 470 ARG A 777 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 778 CG CD1 CD2
REMARK 470 SER A 779 OG
REMARK 470 LYS A 780 CG CD CE NZ
REMARK 470 ILE A 781 CG1 CG2 CD1
REMARK 470 ILE A 782 CG1 CG2 CD1
REMARK 470 SER A 783 OG
REMARK 470 MET A 784 CG SD CE
REMARK 470 PHE A 785 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 786 CG CD OE1 NE2
REMARK 470 HIS A 788 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 789 CG1 CG2 CD1
REMARK 470 ARG A 790 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 792 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 793 CG CD1 CD2
REMARK 470 ILE A 794 CG1 CG2 CD1
REMARK 470 ARG A 795 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 796 CG CD CE NZ
REMARK 470 TYR A 798 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 799 CG CD CE NZ
REMARK 470 LYS A 800 CG CD CE NZ
REMARK 470 LEU A 801 CG CD1 CD2
REMARK 470 GLN A 802 CG CD OE1 NE2
REMARK 470 ASP A 803 CG OD1 OD2
REMARK 470 GLN A 804 CG CD OE1 NE2
REMARK 470 ARG A 805 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 806 CG1 CG2 CD1
REMARK 470 LEU A 808 CG CD1 CD2
REMARK 470 SER A 809 OG
REMARK 470 VAL A 810 CG1 CG2
REMARK 470 ILE A 811 CG1 CG2 CD1
REMARK 470 GLN A 812 CG CD OE1 NE2
REMARK 470 ARG A 813 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 814 CG OD1 ND2
REMARK 470 ILE A 815 CG1 CG2 CD1
REMARK 470 ARG A 816 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 817 CG CD CE NZ
REMARK 470 TRP A 818 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 818 CZ3 CH2
REMARK 470 LEU A 819 CG CD1 CD2
REMARK 470 VAL A 820 CG1 CG2
REMARK 470 LEU A 821 CG CD1 CD2
REMARK 470 ARG A 822 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 823 CG OD1 ND2
REMARK 470 TRP A 824 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 824 CZ3 CH2
REMARK 470 GLN A 825 CG CD OE1 NE2
REMARK 470 TRP A 826 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 826 CZ3 CH2
REMARK 470 TRP A 827 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 827 CZ3 CH2
REMARK 470 LYS A 828 CG CD CE NZ
REMARK 470 LEU A 829 CG CD1 CD2
REMARK 470 TYR A 830 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 831 OG
REMARK 470 LYS A 832 CG CD CE NZ
REMARK 470 VAL A 833 CG1 CG2
REMARK 470 LYS A 834 CG CD CE NZ
REMARK 470 PRO A 835 CG CD
REMARK 470 LEU Y 12 CG CD1 CD2
REMARK 470 PRO Y 13 CG CD
REMARK 470 GLN Y 14 CG CD OE1 NE2
REMARK 470 LYS Y 15 CG CD CE NZ
REMARK 470 GLN Y 16 CG CD OE1 NE2
REMARK 470 ILE Y 17 CG1 CG2 CD1
REMARK 470 GLN Y 18 CG CD OE1 NE2
REMARK 470 GLU Y 19 CG CD OE1 OE2
REMARK 470 MET Y 20 CG SD CE
REMARK 470 LYS Y 21 CG CD CE NZ
REMARK 470 GLU Y 22 CG CD OE1 OE2
REMARK 470 PHE Y 24 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER Y 25 OG
REMARK 470 MET Y 26 CG SD CE
REMARK 470 ILE Y 27 CG1 CG2 CD1
REMARK 470 ASP Y 28 CG OD1 OD2
REMARK 470 VAL Y 29 CG1 CG2
REMARK 470 ASP Y 30 CG OD1 OD2
REMARK 470 ARG Y 31 CG CD NE CZ NH1 NH2
REMARK 470 ASP Y 32 CG OD1 OD2
REMARK 470 PHE Y 34 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL Y 35 CG1 CG2
REMARK 470 SER Y 36 OG
REMARK 470 LYS Y 37 CG CD CE NZ
REMARK 470 GLU Y 38 CG CD OE1 OE2
REMARK 470 ASP Y 39 CG OD1 OD2
REMARK 470 ILE Y 40 CG1 CG2 CD1
REMARK 470 LYS Y 41 CG CD CE NZ
REMARK 470 ILE Y 43 CG1 CG2 CD1
REMARK 470 SER Y 44 OG
REMARK 470 GLU Y 45 CG CD OE1 OE2
REMARK 470 GLN Y 46 CG CD OE1 NE2
REMARK 470 LEU Y 47 CG CD1 CD2
REMARK 470 ARG Y 49 CG CD NE CZ NH1 NH2
REMARK 470 PRO Y 51 CG CD
REMARK 470 ASP Y 52 CG OD1 OD2
REMARK 470 ASP Y 53 CG OD1 OD2
REMARK 470 LYS Y 54 CG CD CE NZ
REMARK 470 GLU Y 55 CG CD OE1 OE2
REMARK 470 LEU Y 56 CG CD1 CD2
REMARK 470 THR Y 57 OG1 CG2
REMARK 470 MET Y 59 CG SD CE
REMARK 470 LEU Y 60 CG CD1 CD2
REMARK 470 LYS Y 61 CG CD CE NZ
REMARK 470 GLU Y 62 CG CD OE1 OE2
REMARK 470 PRO Y 64 CG CD
REMARK 470 PRO Y 66 CG CD
REMARK 470 LEU Y 67 CG CD1 CD2
REMARK 470 ASN Y 68 CG OD1 ND2
REMARK 470 PHE Y 69 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR Y 70 OG1 CG2
REMARK 470 MET Y 71 CG SD CE
REMARK 470 PHE Y 72 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU Y 73 CG CD1 CD2
REMARK 470 SER Y 74 OG
REMARK 470 ILE Y 75 CG1 CG2 CD1
REMARK 470 PHE Y 76 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER Y 77 OG
REMARK 470 ASP Y 78 CG OD1 OD2
REMARK 470 LYS Y 79 CG CD CE NZ
REMARK 470 LEU Y 80 CG CD1 CD2
REMARK 470 SER Y 81 OG
REMARK 470 THR Y 83 OG1 CG2
REMARK 470 ASP Y 84 CG OD1 OD2
REMARK 470 SER Y 85 OG
REMARK 470 GLU Y 86 CG CD OE1 OE2
REMARK 470 GLU Y 87 CG CD OE1 OE2
REMARK 470 THR Y 88 OG1 CG2
REMARK 470 ILE Y 89 CG1 CG2 CD1
REMARK 470 ARG Y 90 CG CD NE CZ NH1 NH2
REMARK 470 ASN Y 91 CG OD1 ND2
REMARK 470 PHE Y 93 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET Y 95 CG SD CE
REMARK 470 PHE Y 96 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Y 97 CG OD1 OD2
REMARK 470 GLU Y 98 CG CD OE1 OE2
REMARK 470 GLN Y 99 CG CD OE1 NE2
REMARK 470 GLU Y 100 CG CD OE1 OE2
REMARK 470 THR Y 101 OG1 CG2
REMARK 470 LYS Y 102 CG CD CE NZ
REMARK 470 LYS Y 103 CG CD CE NZ
REMARK 470 LEU Y 104 CG CD1 CD2
REMARK 470 ASN Y 105 CG OD1 ND2
REMARK 470 ILE Y 106 CG1 CG2 CD1
REMARK 470 GLU Y 107 CG CD OE1 OE2
REMARK 470 TYR Y 108 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE Y 109 CG1 CG2 CD1
REMARK 470 LYS Y 110 CG CD CE NZ
REMARK 470 ASP Y 111 CG OD1 OD2
REMARK 470 LEU Y 112 CG CD1 CD2
REMARK 470 LEU Y 113 CG CD1 CD2
REMARK 470 GLU Y 114 CG CD OE1 OE2
REMARK 470 ASN Y 115 CG OD1 ND2
REMARK 470 MET Y 116 CG SD CE
REMARK 470 ASP Y 118 CG OD1 OD2
REMARK 470 ASN Y 119 CG OD1 ND2
REMARK 470 PHE Y 120 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN Y 121 CG OD1 ND2
REMARK 470 LYS Y 122 CG CD CE NZ
REMARK 470 ASP Y 123 CG OD1 OD2
REMARK 470 GLU Y 124 CG CD OE1 OE2
REMARK 470 MET Y 125 CG SD CE
REMARK 470 ARG Y 126 CG CD NE CZ NH1 NH2
REMARK 470 MET Y 127 CG SD CE
REMARK 470 THR Y 128 OG1 CG2
REMARK 470 PHE Y 129 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS Y 130 CG CD CE NZ
REMARK 470 GLU Y 131 CG CD OE1 OE2
REMARK 470 PRO Y 133 CG CD
REMARK 470 VAL Y 134 CG1 CG2
REMARK 470 GLU Y 135 CG CD OE1 OE2
REMARK 470 LYS Y 138 CG CD CE NZ
REMARK 470 PHE Y 139 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Y 140 CG OD1 OD2
REMARK 470 TYR Y 141 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL Y 142 CG1 CG2
REMARK 470 LYS Y 143 CG CD CE NZ
REMARK 470 PHE Y 144 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR Y 145 OG1 CG2
REMARK 470 MET Y 147 CG SD CE
REMARK 470 ILE Y 148 CG1 CG2 CD1
REMARK 470 LYS Y 149 CG CD CE NZ
REMARK 470 LEU Z 3 CG CD1 CD2
REMARK 470 SER Z 4 OG
REMARK 470 GLN Z 5 CG CD OE1 NE2
REMARK 470 ASP Z 6 CG OD1 OD2
REMARK 470 GLU Z 7 CG CD OE1 OE2
REMARK 470 ILE Z 8 CG1 CG2 CD1
REMARK 470 ASP Z 9 CG OD1 OD2
REMARK 470 ASP Z 10 CG OD1 OD2
REMARK 470 LEU Z 11 CG CD1 CD2
REMARK 470 LYS Z 12 CG CD CE NZ
REMARK 470 ASP Z 13 CG OD1 OD2
REMARK 470 VAL Z 14 CG1 CG2
REMARK 470 PHE Z 15 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU Z 16 CG CD OE1 OE2
REMARK 470 LEU Z 17 CG CD1 CD2
REMARK 470 PHE Z 18 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Z 19 CG OD1 OD2
REMARK 470 PHE Z 20 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP Z 21 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP Z 21 CZ3 CH2
REMARK 470 ASP Z 22 CG OD1 OD2
REMARK 470 ARG Z 24 CG CD NE CZ NH1 NH2
REMARK 470 ASP Z 25 CG OD1 OD2
REMARK 470 VAL Z 28 CG1 CG2
REMARK 470 ASP Z 29 CG OD1 OD2
REMARK 470 PHE Z 31 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS Z 32 CG CD CE NZ
REMARK 470 LEU Z 33 CG CD1 CD2
REMARK 470 ASP Z 35 CG OD1 OD2
REMARK 470 VAL Z 36 CG1 CG2
REMARK 470 CYS Z 37 SG
REMARK 470 ARG Z 38 CG CD NE CZ NH1 NH2
REMARK 470 CYS Z 39 SG
REMARK 470 LEU Z 40 CG CD1 CD2
REMARK 470 ILE Z 42 CG1 CG2 CD1
REMARK 470 ASN Z 43 CG OD1 ND2
REMARK 470 PRO Z 44 CG CD
REMARK 470 ARG Z 45 CG CD NE CZ NH1 NH2
REMARK 470 ASN Z 46 CG OD1 ND2
REMARK 470 GLU Z 47 CG CD OE1 OE2
REMARK 470 ASP Z 48 CG OD1 OD2
REMARK 470 VAL Z 49 CG1 CG2
REMARK 470 PHE Z 50 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL Z 52 CG1 CG2
REMARK 470 THR Z 55 OG1 CG2
REMARK 470 HIS Z 56 CG ND1 CD2 CE1 NE2
REMARK 470 LYS Z 57 CG CD CE NZ
REMARK 470 MET Z 58 CG SD CE
REMARK 470 GLU Z 60 CG CD OE1 OE2
REMARK 470 LYS Z 61 CG CD CE NZ
REMARK 470 SER Z 62 OG
REMARK 470 LEU Z 63 CG CD1 CD2
REMARK 470 PRO Z 64 CG CD
REMARK 470 PHE Z 65 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU Z 66 CG CD OE1 OE2
REMARK 470 GLU Z 67 CG CD OE1 OE2
REMARK 470 PHE Z 68 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU Z 69 CG CD1 CD2
REMARK 470 PRO Z 70 CG CD
REMARK 470 TYR Z 72 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU Z 73 CG CD OE1 OE2
REMARK 470 LEU Z 75 CG CD1 CD2
REMARK 470 MET Z 76 CG SD CE
REMARK 470 ASP Z 77 CG OD1 OD2
REMARK 470 CYS Z 78 SG
REMARK 470 GLU Z 79 CG CD OE1 OE2
REMARK 470 GLN Z 80 CG CD OE1 NE2
REMARK 470 THR Z 82 OG1 CG2
REMARK 470 PHE Z 83 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Z 85 CG OD1 OD2
REMARK 470 TYR Z 86 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET Z 87 CG SD CE
REMARK 470 GLU Z 88 CG CD OE1 OE2
REMARK 470 PHE Z 90 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS Z 91 CG CD CE NZ
REMARK 470 THR Z 92 OG1 CG2
REMARK 470 PHE Z 93 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Z 94 CG OD1 OD2
REMARK 470 ARG Z 95 CG CD NE CZ NH1 NH2
REMARK 470 GLU Z 96 CG CD OE1 OE2
REMARK 470 GLN Z 98 CG CD OE1 NE2
REMARK 470 PHE Z 100 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE Z 101 CG1 CG2 CD1
REMARK 470 SER Z 102 OG
REMARK 470 GLU Z 105 CG CD OE1 OE2
REMARK 470 LEU Z 106 CG CD1 CD2
REMARK 470 ARG Z 107 CG CD NE CZ NH1 NH2
REMARK 470 HIS Z 108 CG ND1 CD2 CE1 NE2
REMARK 470 VAL Z 109 CG1 CG2
REMARK 470 LEU Z 110 CG CD1 CD2
REMARK 470 THR Z 111 OG1 CG2
REMARK 470 LEU Z 113 CG CD1 CD2
REMARK 470 GLU Z 115 CG CD OE1 OE2
REMARK 470 ARG Z 116 CG CD NE CZ NH1 NH2
REMARK 470 LEU Z 117 CG CD1 CD2
REMARK 470 SER Z 118 OG
REMARK 470 ASP Z 119 CG OD1 OD2
REMARK 470 GLU Z 120 CG CD OE1 OE2
REMARK 470 ASP Z 121 CG OD1 OD2
REMARK 470 VAL Z 122 CG1 CG2
REMARK 470 ASP Z 123 CG OD1 OD2
REMARK 470 GLU Z 124 CG CD OE1 OE2
REMARK 470 ILE Z 125 CG1 CG2 CD1
REMARK 470 ILE Z 126 CG1 CG2 CD1
REMARK 470 LYS Z 127 CG CD CE NZ
REMARK 470 LEU Z 128 CG CD1 CD2
REMARK 470 THR Z 129 OG1 CG2
REMARK 470 ASP Z 130 CG OD1 OD2
REMARK 470 LEU Z 131 CG CD1 CD2
REMARK 470 GLN Z 132 CG CD OE1 NE2
REMARK 470 GLU Z 133 CG CD OE1 OE2
REMARK 470 ASP Z 134 CG OD1 OD2
REMARK 470 LEU Z 135 CG CD1 CD2
REMARK 470 GLU Z 136 CG CD OE1 OE2
REMARK 470 ASN Z 138 CG OD1 ND2
REMARK 470 VAL Z 139 CG1 CG2
REMARK 470 LYS Z 140 CG CD CE NZ
REMARK 470 TYR Z 141 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU Z 142 CG CD OE1 OE2
REMARK 470 ASP Z 143 CG OD1 OD2
REMARK 470 PHE Z 144 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL Z 145 CG1 CG2
REMARK 470 LYS Z 146 CG CD CE NZ
REMARK 470 LYS Z 147 CG CD CE NZ
REMARK 470 VAL Z 148 CG1 CG2
REMARK 470 MET Z 149 CG SD CE
REMARK 470 PRO Z 152 CG CD
REMARK 470 TYR Z 153 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PRO Z 154 CG CD
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 GLU A 268 CA LYS A 269 1.00
REMARK 500 O GLU A 268 N LYS A 269 1.14
REMARK 500 C GLU A 268 CA LYS A 269 1.27
REMARK 500 CA GLU A 268 N LYS A 269 1.37
REMARK 500 O ASP A 515 N LEU A 516 1.38
REMARK 500 O LEU A 770 CB ARG A 774 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 268 C LYS A 269 N -0.719
REMARK 500 THR A 445 C LEU A 446 N -0.241
REMARK 500 ASN A 489 C HIS A 490 N -0.141
REMARK 500 ASP A 515 C LEU A 516 N 0.151
REMARK 500 PRO A 601 C ILE A 602 N 0.231
REMARK 500 ASP A 683 C ALA A 684 N -0.427
REMARK 500 GLU Z 7 C ILE Z 8 N 0.259
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 GLU A 268 CA - C - N ANGL. DEV. = -53.9 DEGREES
REMARK 500 GLU A 268 O - C - N ANGL. DEV. = -56.8 DEGREES
REMARK 500 LYS A 269 C - N - CA ANGL. DEV. = -61.8 DEGREES
REMARK 500 ASP A 515 CA - C - N ANGL. DEV. = 35.3 DEGREES
REMARK 500 ASP A 515 O - C - N ANGL. DEV. = -62.9 DEGREES
REMARK 500 ASP A 600 CA - C - N ANGL. DEV. = -18.6 DEGREES
REMARK 500 ASP A 600 O - C - N ANGL. DEV. = -22.9 DEGREES
REMARK 500 PRO A 601 C - N - CA ANGL. DEV. = -14.5 DEGREES
REMARK 500 ILE A 602 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASP A 683 CA - C - N ANGL. DEV. = -25.4 DEGREES
REMARK 500 ASP A 683 O - C - N ANGL. DEV. = 16.9 DEGREES
REMARK 500 ARG A 710 C - N - CA ANGL. DEV. = 18.0 DEGREES
REMARK 500 MET A 773 CA - C - N ANGL. DEV. = -23.4 DEGREES
REMARK 500 MET A 773 O - C - N ANGL. DEV. = 16.0 DEGREES
REMARK 500 LEU Y 12 CB - CA - C ANGL. DEV. = -11.6 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 LYS A 52 65.83 -176.03
REMARK 500 ALA A 62 -84.99 -60.75
REMARK 500 PHE A 82 48.03 -107.52
REMARK 500 LEU A 94 65.08 -112.29
REMARK 500 GLU A 96 -20.49 -38.61
REMARK 500 LEU A 103 -73.65 -54.33
REMARK 500 THR A 108 14.21 -65.97
REMARK 500 SER A 116 81.69 -160.26
REMARK 500 PRO A 130 37.92 -75.99
REMARK 500 THR A 133 170.08 -53.26
REMARK 500 LYS A 145 -38.44 -28.54
REMARK 500 PRO A 149 160.08 -36.88
REMARK 500 VAL A 164 -72.22 -63.95
REMARK 500 ARG A 167 72.35 51.90
REMARK 500 SER A 171 138.03 -176.89
REMARK 500 PRO A 253 -3.80 -58.22
REMARK 500 ALA A 260 145.05 177.71
REMARK 500 LEU A 266 76.76 39.07
REMARK 500 GLU A 268 -135.02 -67.62
REMARK 500 LYS A 269 -36.96 172.81
REMARK 500 GLN A 276 155.56 -48.66
REMARK 500 LEU A 301 37.23 72.16
REMARK 500 PRO A 304 57.41 -58.86
REMARK 500 PHE A 311 -10.28 -48.25
REMARK 500 LEU A 317 -57.31 -120.51
REMARK 500 ASP A 320 114.92 -31.93
REMARK 500 MET A 348 -71.46 -56.36
REMARK 500 THR A 377 -12.24 -164.12
REMARK 500 LEU A 394 -80.84 -73.33
REMARK 500 ALA A 397 6.70 -67.62
REMARK 500 LYS A 400 58.89 -156.53
REMARK 500 LYS A 449 13.84 -67.24
REMARK 500 ALA A 450 178.43 -58.58
REMARK 500 ASN A 453 -81.59 -108.85
REMARK 500 SER A 471 -159.40 -133.12
REMARK 500 TRP A 507 44.28 -171.37
REMARK 500 GLU A 508 -74.22 -20.64
REMARK 500 PHE A 509 177.53 58.95
REMARK 500 MET A 514 -17.53 -42.10
REMARK 500 ASP A 515 -122.23 -79.92
REMARK 500 LEU A 516 -56.50 83.76
REMARK 500 LYS A 525 155.72 -49.53
REMARK 500 PRO A 526 -57.78 -20.30
REMARK 500 MET A 538 -8.06 -56.71
REMARK 500 ALA A 542 161.11 -37.45
REMARK 500 GLN A 573 90.72 -65.80
REMARK 500 ASP A 600 172.69 66.12
REMARK 500 PRO A 601 37.56 -160.86
REMARK 500 LYS A 623 -122.32 -51.10
REMARK 500 TYR A 661 4.32 -69.80
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 515 LEU A 516 111.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU A 268 -84.21
REMARK 500 THR A 445 -10.66
REMARK 500 ASP A 515 70.60
REMARK 500 ASP A 600 -33.29
REMARK 500 PRO A 601 11.66
REMARK 500 ILE A 672 18.89
REMARK 500 MET A 773 11.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA Z 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Z 19 O
REMARK 620 2 GLY Z 23 O 74.2
REMARK 620 3 ALA Z 27 O 116.9 149.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Z 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B7T RELATED DB: PDB
REMARK 900 1B7T CORRESPONDS TO ANOTHER CONFORMATION FOR THE SAME MYOSIN
REMARK 900 FRAGMENT - BUT COMPLEXED WITH MGADP (DETACHED STATE)
REMARK 900 RELATED ID: 1DFL RELATED DB: PDB
REMARK 900 SCALLOP MYOSIN S1 COMPLEXED WITH MGADP VANADATE - TRANSITION STATE
DBREF 1DFK A 6 835 UNP P24733 MYS_AEQIR 6 835
DBREF 1DFK Y 12 150 UNP P13543 MLR_AEQIR 13 151
DBREF 1DFK Z 3 154 UNP P07291 MLE_AEQIR 4 155
SEQRES 1 A 830 SER ASP PRO ASP PHE GLN TYR LEU ALA VAL ASP ARG LYS
SEQRES 2 A 830 LYS LEU MET LYS GLU GLN THR ALA ALA PHE ASP GLY LYS
SEQRES 3 A 830 LYS ASN CYS TRP VAL PRO ASP GLU LYS GLU GLY PHE ALA
SEQRES 4 A 830 SER ALA GLU ILE GLN SER SER LYS GLY ASP GLU ILE THR
SEQRES 5 A 830 VAL LYS ILE VAL ALA ASP SER SER THR ARG THR VAL LYS
SEQRES 6 A 830 LYS ASP ASP ILE GLN SER MET ASN PRO PRO LYS PHE GLU
SEQRES 7 A 830 LYS LEU GLU ASP MET ALA ASN MET THR TYR LEU ASN GLU
SEQRES 8 A 830 ALA SER VAL LEU TYR ASN LEU ARG SER ARG TYR THR SER
SEQRES 9 A 830 GLY LEU ILE TYR THR TYR SER GLY LEU PHE CYS ILE ALA
SEQRES 10 A 830 VAL ASN PRO TYR ARG ARG LEU PRO ILE TYR THR ASP SER
SEQRES 11 A 830 VAL ILE ALA LYS TYR ARG GLY LYS ARG LYS THR GLU ILE
SEQRES 12 A 830 PRO PRO HIS LEU PHE SER VAL ALA ASP ASN ALA TYR GLN
SEQRES 13 A 830 ASN MET VAL THR ASP ARG GLU ASN GLN SER CYS LEU ILE
SEQRES 14 A 830 THR GLY GLU SER GLY ALA GLY LYS THR GLU ASN THR LYS
SEQRES 15 A 830 LYS VAL ILE MET TYR LEU ALA LYS VAL ALA CYS ALA VAL
SEQRES 16 A 830 LYS LYS LYS ASP GLU GLU ALA SER ASP LYS LYS GLU GLY
SEQRES 17 A 830 SER LEU GLU ASP GLN ILE ILE GLN ALA ASN PRO VAL LEU
SEQRES 18 A 830 GLU ALA TYR GLY ASN ALA LYS THR THR ARG ASN ASN ASN
SEQRES 19 A 830 SER SER ARG PHE GLY LYS PHE ILE ARG ILE HIS PHE GLY
SEQRES 20 A 830 PRO THR GLY LYS ILE ALA GLY ALA ASP ILE GLU THR TYR
SEQRES 21 A 830 LEU LEU GLU LYS SER ARG VAL THR TYR GLN GLN SER ALA
SEQRES 22 A 830 GLU ARG ASN TYR HIS ILE PHE TYR GLN ILE CYS SER ASN
SEQRES 23 A 830 ALA ILE PRO GLU LEU ASN ASP VAL MET LEU VAL THR PRO
SEQRES 24 A 830 ASP SER GLY LEU TYR SER PHE ILE ASN GLN GLY CYS LEU
SEQRES 25 A 830 THR VAL ASP ASN ILE ASP ASP VAL GLU GLU PHE LYS LEU
SEQRES 26 A 830 CYS ASP GLU ALA PHE ASP ILE LEU GLY PHE THR LYS GLU
SEQRES 27 A 830 GLU LYS GLN SER MET PHE LYS CYS THR ALA SER ILE LEU
SEQRES 28 A 830 HIS MET GLY GLU MET LYS PHE LYS GLN ARG PRO ARG GLU
SEQRES 29 A 830 GLU GLN ALA GLU SER ASP GLY THR ALA GLU ALA GLU LYS
SEQRES 30 A 830 VAL ALA PHE LEU CYS GLY ILE ASN ALA GLY ASP LEU LEU
SEQRES 31 A 830 LYS ALA LEU LEU LYS PRO LYS VAL LYS VAL GLY THR GLU
SEQRES 32 A 830 MET VAL THR LYS GLY GLN ASN MET ASN GLN VAL VAL ASN
SEQRES 33 A 830 SER VAL GLY ALA LEU ALA LYS SER LEU TYR ASP ARG MET
SEQRES 34 A 830 PHE ASN TRP LEU VAL ARG ARG VAL ASN LYS THR LEU ASP
SEQRES 35 A 830 THR LYS ALA LYS ARG ASN TYR TYR ILE GLY VAL LEU ASP
SEQRES 36 A 830 ILE ALA GLY PHE GLU ILE PHE ASP PHE ASN SER PHE GLU
SEQRES 37 A 830 GLN LEU CYS ILE ASN TYR THR ASN GLU ARG LEU GLN GLN
SEQRES 38 A 830 PHE PHE ASN HIS HIS MET PHE ILE LEU GLU GLN GLU GLU
SEQRES 39 A 830 TYR LYS LYS GLU GLY ILE ALA TRP GLU PHE ILE ASP PHE
SEQRES 40 A 830 GLY MET ASP LEU GLN MET CYS ILE ASP LEU ILE GLU LYS
SEQRES 41 A 830 PRO MET GLY ILE LEU SER ILE LEU GLU GLU GLU CYS MET
SEQRES 42 A 830 PHE PRO LYS ALA ASP ASP LYS SER PHE GLN ASP LYS LEU
SEQRES 43 A 830 TYR GLN ASN HIS MET GLY LYS ASN ARG MET PHE THR LYS
SEQRES 44 A 830 PRO GLY LYS PRO THR ARG PRO ASN GLN GLY PRO ALA HIS
SEQRES 45 A 830 PHE GLU LEU HIS HIS TYR ALA GLY ASN VAL PRO TYR SER
SEQRES 46 A 830 ILE THR GLY TRP LEU GLU LYS ASN LYS ASP PRO ILE ASN
SEQRES 47 A 830 GLU ASN VAL VAL ALA LEU LEU GLY ALA SER LYS GLU PRO
SEQRES 48 A 830 LEU VAL ALA GLU LEU PHE LYS ALA PRO GLU GLU PRO ALA
SEQRES 49 A 830 GLY GLY GLY LYS LYS LYS LYS GLY LYS SER SER ALA PHE
SEQRES 50 A 830 GLN THR ILE SER ALA VAL HIS ARG GLU SER LEU ASN LYS
SEQRES 51 A 830 LEU MET LYS ASN LEU TYR SER THR HIS PRO HIS PHE VAL
SEQRES 52 A 830 ARG CYS ILE ILE PRO ASN GLU LEU LYS GLN PRO GLY LEU
SEQRES 53 A 830 VAL ASP ALA GLU LEU VAL LEU HIS GLN LEU GLN CYS ASN
SEQRES 54 A 830 GLY VAL LEU GLU GLY ILE ARG ILE CYS ARG LYS GLY PHE
SEQRES 55 A 830 PRO SER ARG LEU ILE TYR SER GLU PHE LYS GLN ARG TYR
SEQRES 56 A 830 SER ILE LEU ALA PRO ASN ALA ILE PRO GLN GLY PHE VAL
SEQRES 57 A 830 ASP GLY LYS THR VAL SER GLU LYS ILE LEU ALA GLY LEU
SEQRES 58 A 830 GLN MET ASP PRO ALA GLU TYR ARG LEU GLY THR THR LYS
SEQRES 59 A 830 VAL PHE PHE LYS ALA GLY VAL LEU GLY ASN LEU GLU GLU
SEQRES 60 A 830 MET ARG ASP GLU ARG LEU SER LYS ILE ILE SER MET PHE
SEQRES 61 A 830 GLN ALA HIS ILE ARG GLY TYR LEU ILE ARG LYS ALA TYR
SEQRES 62 A 830 LYS LYS LEU GLN ASP GLN ARG ILE GLY LEU SER VAL ILE
SEQRES 63 A 830 GLN ARG ASN ILE ARG LYS TRP LEU VAL LEU ARG ASN TRP
SEQRES 64 A 830 GLN TRP TRP LYS LEU TYR SER LYS VAL LYS PRO
SEQRES 1 Y 139 LEU PRO GLN LYS GLN ILE GLN GLU MET LYS GLU ALA PHE
SEQRES 2 Y 139 SER MET ILE ASP VAL ASP ARG ASP GLY PHE VAL SER LYS
SEQRES 3 Y 139 GLU ASP ILE LYS ALA ILE SER GLU GLN LEU GLY ARG ALA
SEQRES 4 Y 139 PRO ASP ASP LYS GLU LEU THR ALA MET LEU LYS GLU ALA
SEQRES 5 Y 139 PRO GLY PRO LEU ASN PHE THR MET PHE LEU SER ILE PHE
SEQRES 6 Y 139 SER ASP LYS LEU SER GLY THR ASP SER GLU GLU THR ILE
SEQRES 7 Y 139 ARG ASN ALA PHE ALA MET PHE ASP GLU GLN GLU THR LYS
SEQRES 8 Y 139 LYS LEU ASN ILE GLU TYR ILE LYS ASP LEU LEU GLU ASN
SEQRES 9 Y 139 MET GLY ASP ASN PHE ASN LYS ASP GLU MET ARG MET THR
SEQRES 10 Y 139 PHE LYS GLU ALA PRO VAL GLU GLY GLY LYS PHE ASP TYR
SEQRES 11 Y 139 VAL LYS PHE THR ALA MET ILE LYS GLY
SEQRES 1 Z 152 LEU SER GLN ASP GLU ILE ASP ASP LEU LYS ASP VAL PHE
SEQRES 2 Z 152 GLU LEU PHE ASP PHE TRP ASP GLY ARG ASP GLY ALA VAL
SEQRES 3 Z 152 ASP ALA PHE LYS LEU GLY ASP VAL CYS ARG CYS LEU GLY
SEQRES 4 Z 152 ILE ASN PRO ARG ASN GLU ASP VAL PHE ALA VAL GLY GLY
SEQRES 5 Z 152 THR HIS LYS MET GLY GLU LYS SER LEU PRO PHE GLU GLU
SEQRES 6 Z 152 PHE LEU PRO ALA TYR GLU GLY LEU MET ASP CYS GLU GLN
SEQRES 7 Z 152 GLY THR PHE ALA ASP TYR MET GLU ALA PHE LYS THR PHE
SEQRES 8 Z 152 ASP ARG GLU GLY GLN GLY PHE ILE SER GLY ALA GLU LEU
SEQRES 9 Z 152 ARG HIS VAL LEU THR ALA LEU GLY GLU ARG LEU SER ASP
SEQRES 10 Z 152 GLU ASP VAL ASP GLU ILE ILE LYS LEU THR ASP LEU GLN
SEQRES 11 Z 152 GLU ASP LEU GLU GLY ASN VAL LYS TYR GLU ASP PHE VAL
SEQRES 12 Z 152 LYS LYS VAL MET ALA GLY PRO TYR PRO
HET CA Z 501 1
HETNAM CA CALCIUM ION
FORMUL 4 CA CA 2+
HELIX 1 1 ASP A 7 GLN A 11 5 5
HELIX 2 2 ASP A 72 ILE A 74 5 3
HELIX 3 3 PRO A 79 GLU A 83 5 5
HELIX 4 4 MET A 88 MET A 91 5 4
HELIX 5 5 ASN A 95 THR A 108 1 14
HELIX 6 6 THR A 133 ARG A 141 1 9
HELIX 7 7 HIS A 151 ARG A 167 1 17
HELIX 8 8 GLY A 181 VAL A 196 1 16
HELIX 9 9 GLU A 216 GLN A 221 1 6
HELIX 10 10 GLN A 221 GLY A 230 1 10
HELIX 11 11 LYS A 269 THR A 273 5 5
HELIX 12 12 ILE A 293 GLU A 295 5 3
HELIX 13 13 LEU A 296 LEU A 301 1 6
HELIX 14 14 ASP A 305 TYR A 309 5 5
HELIX 15 15 TYR A 309 ASN A 313 5 5
HELIX 16 16 ASP A 323 LEU A 338 1 16
HELIX 17 17 GLU A 343 GLY A 359 1 17
HELIX 18 18 THR A 377 CYS A 387 1 11
HELIX 19 19 ASN A 390 LYS A 400 1 11
HELIX 20 20 MET A 416 THR A 445 1 30
HELIX 21 21 SER A 471 GLY A 504 1 34
HELIX 22 22 PHE A 512 ASP A 515 5 4
HELIX 23 23 LEU A 516 LYS A 525 1 10
HELIX 24 24 GLY A 528 MET A 538 1 11
HELIX 25 25 ASP A 543 MET A 556 1 14
HELIX 26 26 GLY A 593 ASP A 600 1 8
HELIX 27 27 ASN A 605 LEU A 610 1 6
HELIX 28 28 GLY A 611 SER A 613 5 3
HELIX 29 29 GLU A 615 PHE A 622 1 8
HELIX 30 30 THR A 644 TYR A 661 1 18
HELIX 31 31 ASP A 683 ASN A 694 1 12
HELIX 32 32 GLY A 695 GLY A 706 1 12
HELIX 33 33 TYR A 713 SER A 721 1 9
HELIX 34 34 THR A 737 LEU A 746 1 10
HELIX 35 35 GLY A 765 ALA A 797 1 33
HELIX 36 36 LYS A 799 LEU A 821 1 23
HELIX 37 37 TRP A 824 LYS A 834 1 11
HELIX 38 38 GLN Y 14 ASP Y 28 1 15
HELIX 39 39 SER Y 36 GLN Y 46 1 11
HELIX 40 40 ASP Y 52 LYS Y 61 1 10
HELIX 41 41 ASN Y 68 ASP Y 78 1 11
HELIX 42 42 SER Y 85 MET Y 95 1 11
HELIX 43 43 ILE Y 106 MET Y 116 1 11
HELIX 44 44 ASN Y 121 LYS Y 130 1 10
HELIX 45 45 ASP Y 140 LYS Y 149 1 10
HELIX 46 46 SER Z 4 ASP Z 22 1 19
HELIX 47 47 LYS Z 32 LEU Z 40 1 9
HELIX 48 48 ARG Z 45 GLY Z 53 1 9
HELIX 49 49 PRO Z 64 LEU Z 75 1 12
HELIX 50 50 THR Z 82 THR Z 92 1 11
HELIX 51 51 SER Z 102 LEU Z 113 1 12
HELIX 52 52 SER Z 118 ASP Z 130 1 13
HELIX 53 53 LYS Z 140 GLY Z 151 1 12
SHEET 1 A 4 ASN A 33 PRO A 37 0
SHEET 2 A 4 PHE A 43 SER A 50 -1 N ALA A 44 O VAL A 36
SHEET 3 A 4 GLU A 55 ILE A 60 -1 O THR A 57 N GLN A 49
SHEET 4 A 4 THR A 66 LYS A 70 -1 O ARG A 67 N VAL A 58
SHEET 1 B 7 TYR A 113 SER A 116 0
SHEET 2 B 7 PHE A 119 VAL A 123 -1 O PHE A 119 N SER A 116
SHEET 3 B 7 THR A 663 ILE A 671 1 O PHE A 667 N CYS A 120
SHEET 4 B 7 ASN A 169 GLY A 176 1 O ASN A 169 N HIS A 664
SHEET 5 B 7 TYR A 454 ASP A 460 1 O TYR A 455 N GLN A 170
SHEET 6 B 7 GLY A 244 PHE A 251 -1 O LYS A 245 N ASP A 460
SHEET 7 B 7 ILE A 257 TYR A 265 -1 N ALA A 258 O HIS A 250
SHEET 1 C 3 PHE A 562 THR A 563 0
SHEET 2 C 3 PHE A 578 HIS A 582 -1 O GLU A 579 N THR A 563
SHEET 3 C 3 GLY A 585 TYR A 589 -1 N GLY A 585 O HIS A 582
SHEET 1 D 3 ARG A 710 ILE A 712 0
SHEET 2 D 3 LYS A 759 PHE A 762 -1 N VAL A 760 O LEU A 711
SHEET 3 D 3 TYR A 753 ARG A 754 -1 O ARG A 754 N PHE A 761
SHEET 1 E 2 LEU Y 104 ASN Y 105 0
SHEET 2 E 2 LYS Y 138 PHE Y 139 -1 N PHE Y 139 O LEU Y 104
SHEET 1 F 2 VAL Z 28 ASP Z 29 0
SHEET 2 F 2 SER Z 62 LEU Z 63 -1 N LEU Z 63 O VAL Z 28
LINK O ASP Z 19 CA CA Z 501 1555 1555 2.34
LINK O GLY Z 23 CA CA Z 501 1555 1555 2.58
LINK O ALA Z 27 CA CA Z 501 1555 1555 2.27
SITE 1 AC1 4 ASP Z 19 ASP Z 22 GLY Z 23 ALA Z 27
CRYST1 86.500 52.100 164.600 90.00 100.30 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011554 0.000000 0.002095 0.00000
SCALE2 0.000000 0.019200 -0.000001 0.00000
SCALE3 0.000000 0.000000 0.006176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
