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6369 lines (6369 loc) · 504 KB
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HEADER FLUORESCENT PROTEIN 23-MAY-13 4KW4
TITLE CRYSTAL STRUCTURE OF GREEN FLUORESCENT PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GREEN FLUORESCENT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: THE PROTEIN IN THIS STRUCTURE IS A VERSION OF GFP
COMPND 7 CALLED EMERALD GFP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA;
SOURCE 3 ORGANISM_COMMON: JELLYFISH;
SOURCE 4 ORGANISM_TAXID: 6100;
SOURCE 5 GENE: GFP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS BETA BARREL, FLUORESCENT PROTEIN, CHROMOPHORE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.BARNARD,X.YU,N.NOINAJ,J.W.TARASKA
REVDAT 1 09-APR-14 4KW4 0
JRNL AUTH T.J.BARNARD,X.YU,N.NOINAJ,J.W.TARASKA
JRNL TITL CRYSTAL STRUCTURE OF GREEN FLUORESCENT PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.280
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 23.0563 - 4.2001 1.00 2324 156 0.1575 0.1778
REMARK 3 2 4.2001 - 3.3370 1.00 2191 146 0.1431 0.1788
REMARK 3 3 3.3370 - 2.9161 1.00 2155 144 0.1502 0.1811
REMARK 3 4 2.9161 - 2.6499 1.00 2150 144 0.1701 0.1971
REMARK 3 5 2.6499 - 2.4602 1.00 2138 144 0.1570 0.2243
REMARK 3 6 2.4602 - 2.3153 1.00 2134 143 0.1630 0.2033
REMARK 3 7 2.3153 - 2.1995 1.00 2110 141 0.1675 0.2273
REMARK 3 8 2.1995 - 2.1038 1.00 2104 141 0.1639 0.2313
REMARK 3 9 2.1038 - 2.0228 1.00 2100 141 0.1793 0.2297
REMARK 3 10 2.0228 - 1.9531 1.00 2120 141 0.1938 0.2131
REMARK 3 11 1.9531 - 1.8920 1.00 2088 140 0.2226 0.2224
REMARK 3 12 1.8920 - 1.8380 1.00 2097 140 0.2489 0.2530
REMARK 3 13 1.8380 - 1.7896 1.00 2087 141 0.2680 0.3011
REMARK 3 14 1.7896 - 1.7460 1.00 2070 138 0.3050 0.3455
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.00
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 1928
REMARK 3 ANGLE : 1.399 2631
REMARK 3 CHIRALITY : 0.081 284
REMARK 3 PLANARITY : 0.006 348
REMARK 3 DIHEDRAL : 14.575 707
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 2 through 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8131 34.8751 10.6333
REMARK 3 T TENSOR
REMARK 3 T11: 0.1659 T22: 0.2248
REMARK 3 T33: 0.1561 T12: -0.0588
REMARK 3 T13: 0.0471 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 6.9422 L22: 0.9654
REMARK 3 L33: 1.2153 L12: 1.4834
REMARK 3 L13: -0.6529 L23: -0.0309
REMARK 3 S TENSOR
REMARK 3 S11: 0.1399 S12: -0.0676 S13: -0.0329
REMARK 3 S21: 0.0429 S22: 0.0313 S23: -0.0186
REMARK 3 S31: -0.1517 S32: 0.1419 S33: -0.1594
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 25 through 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8511 41.3592 5.1179
REMARK 3 T TENSOR
REMARK 3 T11: 0.2276 T22: 0.1802
REMARK 3 T33: 0.1739 T12: -0.0837
REMARK 3 T13: 0.0497 T23: -0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 2.0235 L22: 2.5201
REMARK 3 L33: 1.5618 L12: 1.3662
REMARK 3 L13: 0.0986 L23: 0.5919
REMARK 3 S TENSOR
REMARK 3 S11: 0.0724 S12: 0.0104 S13: 0.2630
REMARK 3 S21: -0.0952 S22: 0.0666 S23: 0.0649
REMARK 3 S31: -0.5582 S32: 0.2005 S33: -0.0565
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 69 through 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3023 21.3211 1.2920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1193 T22: 0.1521
REMARK 3 T33: 0.1664 T12: -0.0459
REMARK 3 T13: -0.0254 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 1.6696 L22: 5.6767
REMARK 3 L33: 2.5332 L12: 1.5808
REMARK 3 L13: 0.5822 L23: 2.1659
REMARK 3 S TENSOR
REMARK 3 S11: 0.0439 S12: -0.1210 S13: -0.1196
REMARK 3 S21: 0.0898 S22: -0.0393 S23: 0.4711
REMARK 3 S31: 0.2803 S32: -0.5372 S33: 0.0129
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 82 through 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5488 30.8642 10.1624
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.2715
REMARK 3 T33: 0.1466 T12: -0.0333
REMARK 3 T13: -0.0008 T23: -0.0825
REMARK 3 L TENSOR
REMARK 3 L11: 1.1908 L22: 1.0013
REMARK 3 L33: 0.6352 L12: 0.6221
REMARK 3 L13: 0.4139 L23: 0.0700
REMARK 3 S TENSOR
REMARK 3 S11: 0.1092 S12: -0.1426 S13: 0.0047
REMARK 3 S21: 0.1590 S22: 0.1229 S23: -0.1214
REMARK 3 S31: 0.1274 S32: 0.4535 S33: -0.1501
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 129 through 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6845 42.0788 -4.9024
REMARK 3 T TENSOR
REMARK 3 T11: 0.3275 T22: 0.5590
REMARK 3 T33: 0.2898 T12: -0.3814
REMARK 3 T13: 0.1150 T23: -0.0850
REMARK 3 L TENSOR
REMARK 3 L11: 0.4808 L22: 0.3889
REMARK 3 L33: 0.3938 L12: 0.0409
REMARK 3 L13: 0.4292 L23: 0.0646
REMARK 3 S TENSOR
REMARK 3 S11: 0.0938 S12: 0.2377 S13: 0.1269
REMARK 3 S21: -0.0993 S22: 0.1807 S23: -0.3286
REMARK 3 S31: -0.5701 S32: 0.7063 S33: 0.3214
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 148 through 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5753 23.0041 0.0983
REMARK 3 T TENSOR
REMARK 3 T11: 0.1403 T22: 0.1898
REMARK 3 T33: 0.1738 T12: 0.0328
REMARK 3 T13: -0.0524 T23: -0.0755
REMARK 3 L TENSOR
REMARK 3 L11: 1.8710 L22: 6.2596
REMARK 3 L33: 3.0751 L12: 2.0227
REMARK 3 L13: -1.3353 L23: -2.7467
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: 0.0609 S13: -0.2071
REMARK 3 S21: 0.1030 S22: 0.0194 S23: -0.4026
REMARK 3 S31: 0.1013 S32: 0.3749 S33: 0.0149
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resid 171 through 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4979 30.8766 -1.8321
REMARK 3 T TENSOR
REMARK 3 T11: 0.1772 T22: 0.3548
REMARK 3 T33: 0.1539 T12: -0.0510
REMARK 3 T13: 0.0049 T23: -0.1128
REMARK 3 L TENSOR
REMARK 3 L11: 1.8902 L22: 0.7366
REMARK 3 L33: 1.0021 L12: -0.2206
REMARK 3 L13: -0.6204 L23: 0.8338
REMARK 3 S TENSOR
REMARK 3 S11: 0.1094 S12: 0.1781 S13: -0.1195
REMARK 3 S21: -0.0944 S22: 0.0897 S23: -0.3348
REMARK 3 S31: -0.1789 S32: 0.7668 S33: -0.0762
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resid 188 through 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1885 32.1855 1.0626
REMARK 3 T TENSOR
REMARK 3 T11: 0.1989 T22: 0.1305
REMARK 3 T33: 0.1266 T12: -0.0554
REMARK 3 T13: 0.0165 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.2240 L22: 1.2152
REMARK 3 L33: 1.8489 L12: 0.1500
REMARK 3 L13: 0.3857 L23: 0.6047
REMARK 3 S TENSOR
REMARK 3 S11: 0.2021 S12: -0.1131 S13: 0.0922
REMARK 3 S21: 0.2790 S22: -0.2053 S23: 0.1237
REMARK 3 S31: -0.1936 S32: -0.0112 S33: -0.0317
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KW4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB079868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31923
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.746
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.82200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 8.2, 50 MM MGCL2, 22%
REMARK 280 PEG4000, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.98650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.45200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.45200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.49325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.45200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.45200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.47975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.45200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.45200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.49325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.45200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.45200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 85.47975
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.98650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 VAL A 1
REMARK 465 GLY A 232
REMARK 465 MET A 233
REMARK 465 ASP A 234
REMARK 465 GLU A 235
REMARK 465 LEU A 236
REMARK 465 TYR A 237
REMARK 465 LYS A 238
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 3 CD CE NZ
REMARK 470 GLU A 5 CD OE1 OE2
REMARK 470 GLU A 6 CD OE1 OE2
REMARK 470 LYS A 52 CE NZ
REMARK 470 LYS A 107 CE NZ
REMARK 470 LYS A 113 CE NZ
REMARK 470 LYS A 131 NZ
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 158 NZ
REMARK 470 LYS A 162 NZ
REMARK 470 LYS A 166 CD CE NZ
REMARK 470 GLU A 172 CG CD OE1 OE2
REMARK 470 LEU A 178 CG CD1 CD2
REMARK 470 GLN A 184 CD OE1 NE2
REMARK 470 LYS A 206 CE NZ
REMARK 470 LYS A 214 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 HD1 HIS A 204 O HOH A 373 1.46
REMARK 500 O HOH A 459 O HOH A 539 2.19
REMARK 500 O HOH A 386 O HOH A 416 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU A 115 HE2 HIS A 204 3555 1.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KW8 RELATED DB: PDB
REMARK 900 RELATED ID: 4KW9 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 EMERALD GFP HAS LEU AT POSITION 64, THR AT 65, ALA AT 72, LYS AT
REMARK 999 149, THR AT 153, 167, LEU AT 231. RESIDUES THR 65, TYR 66, GLY 67
REMARK 999 FORM A CHROMOPHORE CRO 66
DBREF 4KW4 A 2 238 UNP P42212 GFP_AEQVI 2 238
SEQADV 4KW4 GLY A -2 UNP P42212 EXPRESSION TAG
SEQADV 4KW4 SER A -1 UNP P42212 EXPRESSION TAG
SEQADV 4KW4 MET A 0 UNP P42212 EXPRESSION TAG
SEQADV 4KW4 VAL A 1 UNP P42212 EXPRESSION TAG
SEQADV 4KW4 LEU A 64 UNP P42212 PHE 64 SEE REMARK 999
SEQADV 4KW4 CRO A 66 UNP P42212 SER 65 CHROMOPHORE, REM 999
SEQADV 4KW4 CRO A 66 UNP P42212 TYR 66 CHROMOPHORE
SEQADV 4KW4 CRO A 66 UNP P42212 GLY 67 CHROMOPHORE
SEQADV 4KW4 ALA A 72 UNP P42212 SER 72 SEE REMARK 999
SEQADV 4KW4 HIS A 147 UNP P42212 SER 147 ENGINEERED MUTATION
SEQADV 4KW4 LYS A 149 UNP P42212 ASN 149 SEE REMARK 999
SEQADV 4KW4 THR A 153 UNP P42212 MET 153 SEE REMARK 999
SEQADV 4KW4 THR A 167 UNP P42212 ILE 167 SEE REMARK 999
SEQADV 4KW4 HIS A 202 UNP P42212 SER 202 ENGINEERED MUTATION
SEQADV 4KW4 HIS A 204 UNP P42212 GLN 204 ENGINEERED MUTATION
SEQADV 4KW4 LYS A 206 UNP P42212 ALA 206 ENGINEERED MUTATION
SEQADV 4KW4 LEU A 231 UNP P42212 HIS 231 SEE REMARK 999
SEQRES 1 A 239 GLY SER MET VAL SER LYS GLY GLU GLU LEU PHE THR GLY
SEQRES 2 A 239 VAL VAL PRO ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN
SEQRES 3 A 239 GLY HIS LYS PHE SER VAL SER GLY GLU GLY GLU GLY ASP
SEQRES 4 A 239 ALA THR TYR GLY LYS LEU THR LEU LYS PHE ILE CYS THR
SEQRES 5 A 239 THR GLY LYS LEU PRO VAL PRO TRP PRO THR LEU VAL THR
SEQRES 6 A 239 THR LEU CRO VAL GLN CYS PHE ALA ARG TYR PRO ASP HIS
SEQRES 7 A 239 MET LYS GLN HIS ASP PHE PHE LYS SER ALA MET PRO GLU
SEQRES 8 A 239 GLY TYR VAL GLN GLU ARG THR ILE PHE PHE LYS ASP ASP
SEQRES 9 A 239 GLY ASN TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY
SEQRES 10 A 239 ASP THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP
SEQRES 11 A 239 PHE LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU
SEQRES 12 A 239 TYR ASN TYR ASN HIS HIS LYS VAL TYR ILE THR ALA ASP
SEQRES 13 A 239 LYS GLN LYS ASN GLY ILE LYS VAL ASN PHE LYS THR ARG
SEQRES 14 A 239 HIS ASN ILE GLU ASP GLY SER VAL GLN LEU ALA ASP HIS
SEQRES 15 A 239 TYR GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU
SEQRES 16 A 239 LEU PRO ASP ASN HIS TYR LEU HIS THR HIS SER LYS LEU
SEQRES 17 A 239 SER LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU
SEQRES 18 A 239 LEU GLU PHE VAL THR ALA ALA GLY ILE THR LEU GLY MET
SEQRES 19 A 239 ASP GLU LEU TYR LYS
MODRES 4KW4 CRO A 66 GLY
MODRES 4KW4 CRO A 66 TYR
MODRES 4KW4 CRO A 66 GLY
HET CRO A 66 22
HETNAM CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-
HETNAM 2 CRO HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-
HETNAM 3 CRO YL}ACETIC ACID
HETSYN CRO PEPTIDE DERIVED CHROMOPHORE
FORMUL 1 CRO C15 H17 N3 O5
FORMUL 2 HOH *303(H2 O)
HELIX 1 1 LYS A 3 THR A 9 5 7
HELIX 2 2 PRO A 56 VAL A 61 5 6
HELIX 3 3 VAL A 68 ALA A 72 5 5
HELIX 4 4 PRO A 75 HIS A 81 5 7
HELIX 5 5 ASP A 82 ALA A 87 1 6
HELIX 6 6 LYS A 156 ASN A 159 5 4
SHEET 1 A12 VAL A 11 VAL A 22 0
SHEET 2 A12 HIS A 25 ASP A 36 -1 O GLY A 31 N VAL A 16
SHEET 3 A12 LYS A 41 CYS A 48 -1 O LYS A 41 N ASP A 36
SHEET 4 A12 HIS A 217 ALA A 227 -1 O LEU A 220 N LEU A 44
SHEET 5 A12 HIS A 199 SER A 208 -1 N HIS A 202 O THR A 225
SHEET 6 A12 HIS A 147 ASP A 155 -1 N ILE A 152 O HIS A 199
SHEET 7 A12 GLY A 160 ASN A 170 -1 O GLY A 160 N ASP A 155
SHEET 8 A12 VAL A 176 PRO A 187 -1 O HIS A 181 N PHE A 165
SHEET 9 A12 TYR A 92 PHE A 100 -1 N GLU A 95 O GLN A 184
SHEET 10 A12 ASN A 105 GLU A 115 -1 O TYR A 106 N ILE A 98
SHEET 11 A12 THR A 118 ILE A 128 -1 O VAL A 120 N LYS A 113
SHEET 12 A12 VAL A 11 VAL A 22 1 N ASP A 21 O GLY A 127
LINK C LEU A 64 N1 CRO A 66 1555 1555 1.33
LINK C3 CRO A 66 N VAL A 68 1555 1555 1.35
CISPEP 1 MET A 88 PRO A 89 0 6.13
CRYST1 72.904 72.904 113.973 90.00 90.00 90.00 P 41 21 2 8
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 0.013717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008774 0.00000
ATOM 1 N SER A 2 -5.112 18.146 9.119 1.00 46.40 N
ANISOU 1 N SER A 2 4363 4730 8536 -491 249 -795 N
ATOM 2 CA SER A 2 -4.513 18.180 10.455 1.00 46.93 C
ANISOU 2 CA SER A 2 4424 4709 8699 -465 183 -414 C
ATOM 3 C SER A 2 -5.223 19.209 11.341 1.00 47.15 C
ANISOU 3 C SER A 2 4560 4948 8406 -524 144 -159 C
ATOM 4 O SER A 2 -5.829 20.157 10.842 1.00 47.19 O
ANISOU 4 O SER A 2 4682 5166 8083 -548 166 -294 O
ATOM 5 CB SER A 2 -3.006 18.498 10.372 1.00 36.38 C
ANISOU 5 CB SER A 2 3082 3364 7376 -425 177 -446 C
ATOM 6 OG SER A 2 -2.785 19.868 10.093 1.00 25.89 O
ANISOU 6 OG SER A 2 1885 2295 5659 -467 181 -526 O
ATOM 7 HA SER A 2 -4.613 17.308 10.868 1.00 56.32 H
ATOM 8 HB2 SER A 2 -2.591 18.279 11.222 1.00 43.65 H
ATOM 9 HB3 SER A 2 -2.610 17.965 9.665 1.00 43.65 H
ATOM 10 HG SER A 2 -1.961 20.024 10.051 1.00 31.07 H
ATOM 11 N LYS A 3 -5.149 19.014 12.655 1.00 44.41 N
ANISOU 11 N LYS A 3 4182 4579 8113 -524 88 221 N
ATOM 12 CA LYS A 3 -5.696 19.981 13.600 1.00 39.63 C
ANISOU 12 CA LYS A 3 3696 4231 7131 -554 65 445 C
ATOM 13 C LYS A 3 -5.092 21.382 13.346 1.00 22.64 C
ANISOU 13 C LYS A 3 1729 2305 4570 -519 81 313 C
ATOM 14 O LYS A 3 -5.801 22.379 13.343 1.00 24.47 O
ANISOU 14 O LYS A 3 2093 2728 4478 -523 107 265 O
ATOM 15 CB LYS A 3 -5.431 19.502 15.036 1.00 42.61 C
ANISOU 15 CB LYS A 3 3967 4613 7609 -581 0 873 C
ATOM 16 CG LYS A 3 -5.221 20.607 16.054 1.00 40.19 C
ANISOU 16 CG LYS A 3 3777 4631 6861 -602 -22 1047 C
ATOM 17 H LYS A 3 -4.785 18.328 13.026 1.00 53.29 H
ATOM 18 HA LYS A 3 -6.656 20.039 13.474 1.00 47.56 H
ATOM 19 HB2 LYS A 3 -6.189 18.974 15.329 1.00 51.13 H
ATOM 20 HB3 LYS A 3 -4.632 18.951 15.034 1.00 51.13 H
ATOM 21 N GLY A 4 -3.784 21.447 13.110 1.00 22.73 N
ANISOU 21 N GLY A 4 1729 2272 4637 -485 72 254 N
ATOM 22 CA GLY A 4 -3.152 22.729 12.830 1.00 21.03 C
ANISOU 22 CA GLY A 4 1668 2241 4079 -462 92 133 C
ATOM 23 C GLY A 4 -3.779 23.455 11.639 1.00 22.73 C
ANISOU 23 C GLY A 4 1985 2552 4100 -457 145 -137 C
ATOM 24 O GLY A 4 -3.896 24.685 11.625 1.00 18.50 O
ANISOU 24 O GLY A 4 1584 2186 3259 -447 167 -155 O
ATOM 25 H GLY A 4 -3.248 20.774 13.106 1.00 27.28 H
ATOM 26 HA2 GLY A 4 -3.227 23.301 13.610 1.00 25.23 H
ATOM 27 HA3 GLY A 4 -2.211 22.590 12.642 1.00 25.23 H
ATOM 28 N GLU A 5 -4.204 22.678 10.648 1.00 26.98 N
ANISOU 28 N GLU A 5 2427 2986 4837 -473 168 -339 N
ATOM 29 CA GLU A 5 -4.779 23.224 9.416 1.00 27.97 C
ANISOU 29 CA GLU A 5 2596 3256 4774 -489 206 -578 C
ATOM 30 C GLU A 5 -6.006 24.083 9.704 1.00 26.00 C
ANISOU 30 C GLU A 5 2450 3161 4270 -488 209 -470 C
ATOM 31 O GLU A 5 -6.292 25.051 8.993 1.00 22.42 O
ANISOU 31 O GLU A 5 2067 2873 3577 -480 229 -546 O
ATOM 32 CB GLU A 5 -5.157 22.070 8.479 1.00 39.76 C
ANISOU 32 CB GLU A 5 3925 4642 6539 -538 233 -825 C
ATOM 33 CG GLU A 5 -5.678 22.501 7.133 1.00 44.07 C
ANISOU 33 CG GLU A 5 4465 5407 6873 -583 265 -1079 C
ATOM 34 H GLU A 5 -4.172 21.818 10.663 1.00 32.37 H
ATOM 35 HA GLU A 5 -4.118 23.776 8.970 1.00 33.56 H
ATOM 36 HB2 GLU A 5 -4.370 21.524 8.328 1.00 47.71 H
ATOM 37 HB3 GLU A 5 -5.847 21.538 8.905 1.00 47.71 H
ATOM 38 HG2 GLU A 5 -6.074 21.735 6.688 1.00 52.88 H
ATOM 39 HG3 GLU A 5 -6.346 23.192 7.260 1.00 52.88 H
ATOM 40 N GLU A 6 -6.744 23.732 10.751 1.00 19.28 N
ANISOU 40 N GLU A 6 1582 2259 3484 -497 192 -273 N
ATOM 41 CA GLU A 6 -7.976 24.448 11.066 1.00 18.23 C
ANISOU 41 CA GLU A 6 1515 2259 3150 -497 207 -193 C
ATOM 42 C GLU A 6 -7.686 25.906 11.418 1.00 20.81 C
ANISOU 42 C GLU A 6 1977 2727 3202 -460 231 -142 C
ATOM 43 O GLU A 6 -8.556 26.781 11.285 1.00 24.77 O
ANISOU 43 O GLU A 6 2529 3334 3549 -441 260 -142 O
ATOM 44 CB GLU A 6 -8.708 23.737 12.221 1.00 19.06 C
ANISOU 44 CB GLU A 6 1556 2308 3377 -531 189 15 C
ATOM 45 CG GLU A 6 -8.909 22.242 11.972 1.00 27.45 C
ANISOU 45 CG GLU A 6 2461 3170 4800 -572 172 -10 C
ATOM 46 H GLU A 6 -6.557 23.089 11.290 1.00 23.13 H
ATOM 47 HA GLU A 6 -8.557 24.437 10.289 1.00 21.87 H
ATOM 48 HB2 GLU A 6 -8.188 23.837 13.034 1.00 22.87 H
ATOM 49 HB3 GLU A 6 -9.583 24.140 12.336 1.00 22.87 H
ATOM 50 N LEU A 7 -6.459 26.181 11.851 1.00 18.92 N
ANISOU 50 N LEU A 7 1776 2476 2936 -450 223 -105 N
ATOM 51 CA LEU A 7 -6.078 27.546 12.215 1.00 15.87 C
ANISOU 51 CA LEU A 7 1498 2198 2332 -431 259 -90 C
ATOM 52 C LEU A 7 -5.914 28.481 10.998 1.00 15.26 C
ANISOU 52 C LEU A 7 1477 2171 2150 -399 287 -221 C
ATOM 53 O LEU A 7 -5.780 29.692 11.166 1.00 18.66 O
ANISOU 53 O LEU A 7 1981 2654 2455 -381 328 -209 O
ATOM 54 CB LEU A 7 -4.777 27.547 13.019 1.00 15.99 C
ANISOU 54 CB LEU A 7 1519 2215 2340 -447 240 -20 C
ATOM 55 CG LEU A 7 -4.761 26.694 14.297 1.00 19.60 C
ANISOU 55 CG LEU A 7 1890 2682 2876 -493 198 182 C
ATOM 56 CD1 LEU A 7 -3.339 26.613 14.843 1.00 20.58 C
ANISOU 56 CD1 LEU A 7 1986 2829 3006 -508 162 258 C
ATOM 57 CD2 LEU A 7 -5.704 27.238 15.360 1.00 25.52 C
ANISOU 57 CD2 LEU A 7 2653 3589 3455 -533 232 273 C
ATOM 58 H LEU A 7 -5.831 25.600 11.943 1.00 22.70 H
ATOM 59 HA LEU A 7 -6.773 27.919 12.780 1.00 19.04 H
ATOM 60 HB2 LEU A 7 -4.066 27.219 12.446 1.00 19.18 H
ATOM 61 HB3 LEU A 7 -4.582 28.460 13.280 1.00 19.18 H
ATOM 62 HG LEU A 7 -5.047 25.794 14.077 1.00 23.52 H
ATOM 63 HD11 LEU A 7 -3.341 26.073 15.648 1.00 24.70 H
ATOM 64 HD12 LEU A 7 -2.767 26.207 14.173 1.00 24.70 H
ATOM 65 HD13 LEU A 7 -3.028 27.509 15.045 1.00 24.70 H
ATOM 66 HD21 LEU A 7 -5.658 26.668 16.143 1.00 30.63 H
ATOM 67 HD22 LEU A 7 -5.433 28.140 15.590 1.00 30.63 H
ATOM 68 HD23 LEU A 7 -6.607 27.244 15.007 1.00 30.63 H
ATOM 69 N PHE A 8 -5.933 27.930 9.787 1.00 15.59 N
ANISOU 69 N PHE A 8 1460 2212 2253 -407 270 -343 N
ATOM 70 CA PHE A 8 -5.649 28.735 8.587 1.00 15.43 C
ANISOU 70 CA PHE A 8 1457 2300 2105 -401 286 -428 C
ATOM 71 C PHE A 8 -6.845 28.861 7.651 1.00 17.31 C
ANISOU 71 C PHE A 8 1639 2662 2276 -409 284 -450 C
ATOM 72 O PHE A 8 -6.705 29.257 6.498 1.00 21.14 O
ANISOU 72 O PHE A 8 2086 3293 2652 -428 282 -504 O
ATOM 73 CB PHE A 8 -4.455 28.144 7.825 1.00 15.83 C
ANISOU 73 CB PHE A 8 1455 2345 2215 -428 276 -577 C
ATOM 74 CG PHE A 8 -3.159 28.224 8.591 1.00 15.48 C
ANISOU 74 CG PHE A 8 1455 2214 2212 -416 274 -538 C
ATOM 75 CD1 PHE A 8 -2.281 29.264 8.384 1.00 15.00 C
ANISOU 75 CD1 PHE A 8 1462 2216 2021 -410 296 -536 C
ATOM 76 CD2 PHE A 8 -2.843 27.253 9.557 1.00 15.89 C
ANISOU 76 CD2 PHE A 8 1459 2133 2445 -417 245 -472 C
ATOM 77 CE1 PHE A 8 -1.068 29.344 9.124 1.00 15.80 C
ANISOU 77 CE1 PHE A 8 1591 2263 2148 -409 292 -507 C
ATOM 78 CE2 PHE A 8 -1.654 27.324 10.284 1.00 15.83 C
ANISOU 78 CE2 PHE A 8 1466 2089 2459 -412 230 -406 C
ATOM 79 CZ PHE A 8 -0.772 28.360 10.073 1.00 15.23 C
ANISOU 79 CZ PHE A 8 1464 2090 2230 -410 255 -442 C
ATOM 80 H PHE A 8 -6.106 27.103 9.627 1.00 18.71 H
ATOM 81 HA PHE A 8 -5.402 29.630 8.869 1.00 18.51 H
ATOM 82 HB2 PHE A 8 -4.634 27.209 7.638 1.00 19.00 H
ATOM 83 HB3 PHE A 8 -4.341 28.632 6.995 1.00 19.00 H
ATOM 84 HD1 PHE A 8 -2.480 29.917 7.754 1.00 18.00 H
ATOM 85 HD2 PHE A 8 -3.432 26.549 9.709 1.00 19.07 H
ATOM 86 HE1 PHE A 8 -0.475 30.045 8.975 1.00 18.96 H
ATOM 87 HE2 PHE A 8 -1.457 26.670 10.915 1.00 18.99 H
ATOM 88 HZ PHE A 8 0.020 28.404 10.557 1.00 18.27 H
ATOM 89 N THR A 9 -8.035 28.552 8.145 1.00 21.85 N
ANISOU 89 N THR A 9 2190 3216 2896 -404 281 -390 N
ATOM 90 CA THR A 9 -9.191 28.522 7.246 1.00 27.23 C
ANISOU 90 CA THR A 9 2790 4034 3522 -422 269 -414 C
ATOM 91 C THR A 9 -9.616 29.918 6.795 1.00 28.84 C
ANISOU 91 C THR A 9 3015 4359 3584 -377 283 -289 C
ATOM 92 O THR A 9 -10.287 30.050 5.783 1.00 27.58 O
ANISOU 92 O THR A 9 2765 4378 3339 -398 261 -280 O
ATOM 93 CB THR A 9 -10.382 27.805 7.883 1.00 26.11 C
ANISOU 93 CB THR A 9 2604 3838 3480 -433 263 -379 C
ATOM 94 OG1 THR A 9 -10.595 28.317 9.195 1.00 23.82 O
ANISOU 94 OG1 THR A 9 2391 3469 3192 -393 291 -239 O
ATOM 95 CG2 THR A 9 -10.106 26.317 7.962 1.00 35.34 C
ANISOU 95 CG2 THR A 9 3693 4885 4849 -490 245 -496 C
ATOM 96 H THR A 9 -8.202 28.361 8.967 1.00 26.22 H
ATOM 97 HA THR A 9 -8.945 28.023 6.451 1.00 32.68 H
ATOM 98 HB THR A 9 -11.175 27.947 7.344 1.00 31.34 H
ATOM 99 HG1 THR A 9 -10.754 29.141 9.159 1.00 28.59 H
ATOM 100 HG21 THR A 9 -10.861 25.861 8.365 1.00 42.41 H
ATOM 101 HG22 THR A 9 -9.961 25.959 7.072 1.00 42.41 H
ATOM 102 HG23 THR A 9 -9.315 26.154 8.500 1.00 42.41 H
ATOM 103 N GLY A 10 -9.230 30.943 7.545 1.00 23.64 N
ANISOU 103 N GLY A 10 2448 3611 2923 -325 324 -189 N
ATOM 104 CA GLY A 10 -9.578 32.310 7.199 1.00 25.42 C
ANISOU 104 CA GLY A 10 2671 3880 3108 -274 352 -55 C
ATOM 105 C GLY A 10 -8.340 33.182 7.076 1.00 26.09 C
ANISOU 105 C GLY A 10 2816 3924 3173 -267 379 -35 C
ATOM 106 O GLY A 10 -7.225 32.685 6.866 1.00 19.90 O
ANISOU 106 O GLY A 10 2058 3149 2355 -308 362 -135 O
ATOM 107 H GLY A 10 -8.763 30.871 8.264 1.00 28.37 H
ATOM 108 HA2 GLY A 10 -10.052 32.322 6.353 1.00 30.51 H
ATOM 109 HA3 GLY A 10 -10.154 32.684 7.884 1.00 30.51 H
ATOM 110 N VAL A 11 -8.536 34.487 7.218 1.00 17.94 N
ANISOU 110 N VAL A 11 1789 2828 2198 -215 430 87 N
ATOM 111 CA VAL A 11 -7.437 35.444 7.112 1.00 21.14 C
ANISOU 111 CA VAL A 11 2238 3170 2624 -213 468 120 C
ATOM 112 C VAL A 11 -6.775 35.535 8.492 1.00 22.02 C
ANISOU 112 C VAL A 11 2444 3132 2789 -220 524 2 C
ATOM 113 O VAL A 11 -7.463 35.711 9.478 1.00 16.51 O
ANISOU 113 O VAL A 11 1751 2364 2158 -200 573 -25 O
ATOM 114 CB VAL A 11 -7.946 36.824 6.695 1.00 21.80 C
ANISOU 114 CB VAL A 11 2253 3210 2821 -158 509 313 C
ATOM 115 CG1 VAL A 11 -6.808 37.853 6.705 1.00 19.85 C
ANISOU 115 CG1 VAL A 11 2042 2852 2649 -165 563 343 C
ATOM 116 CG2 VAL A 11 -8.580 36.774 5.296 1.00 24.91 C
ANISOU 116 CG2 VAL A 11 2518 3827 3122 -168 437 485 C
ATOM 117 H VAL A 11 -9.300 34.848 7.377 1.00 21.52 H
ATOM 118 HA VAL A 11 -6.784 35.135 6.465 1.00 25.37 H
ATOM 119 HB VAL A 11 -8.623 37.117 7.324 1.00 26.16 H
ATOM 120 HG11 VAL A 11 -7.161 38.715 6.437 1.00 23.82 H
ATOM 121 HG12 VAL A 11 -6.441 37.909 7.601 1.00 23.82 H
ATOM 122 HG13 VAL A 11 -6.121 37.568 6.082 1.00 23.82 H
ATOM 123 HG21 VAL A 11 -8.893 37.662 5.060 1.00 29.90 H
ATOM 124 HG22 VAL A 11 -7.913 36.477 4.658 1.00 29.90 H
ATOM 125 HG23 VAL A 11 -9.326 36.154 5.310 1.00 29.90 H
ATOM 126 N VAL A 12 -5.458 35.399 8.539 1.00 15.48 N
ANISOU 126 N VAL A 12 1669 2297 1914 -261 518 -73 N
ATOM 127 CA VAL A 12 -4.697 35.315 9.779 1.00 16.91 C
ANISOU 127 CA VAL A 12 1915 2410 2101 -291 549 -177 C
ATOM 128 C VAL A 12 -3.711 36.468 9.818 1.00 15.31 C
ANISOU 128 C VAL A 12 1742 2138 1938 -305 609 -192 C
ATOM 129 O VAL A 12 -2.975 36.692 8.855 1.00 15.45 O
ANISOU 129 O VAL A 12 1753 2189 1928 -317 589 -150 O
ATOM 130 CB VAL A 12 -3.885 33.996 9.836 1.00 14.40 C
ANISOU 130 CB VAL A 12 1605 2141 1724 -331 480 -246 C
ATOM 131 CG1 VAL A 12 -3.001 33.951 11.068 1.00 14.23 C
ANISOU 131 CG1 VAL A 12 1620 2098 1687 -370 496 -299 C
ATOM 132 CG2 VAL A 12 -4.839 32.773 9.809 1.00 14.82 C
ANISOU 132 CG2 VAL A 12 1609 2225 1796 -329 428 -241 C
ATOM 133 H VAL A 12 -4.963 35.352 7.838 1.00 18.57 H
ATOM 134 HA VAL A 12 -5.288 35.367 10.546 1.00 20.30 H
ATOM 135 HB VAL A 12 -3.312 33.946 9.055 1.00 17.28 H
ATOM 136 HG11 VAL A 12 -2.508 33.116 11.073 1.00 17.07 H
ATOM 137 HG12 VAL A 12 -2.384 34.699 11.041 1.00 17.07 H
ATOM 138 HG13 VAL A 12 -3.559 34.011 11.859 1.00 17.07 H
ATOM 139 HG21 VAL A 12 -4.310 31.961 9.845 1.00 17.78 H
ATOM 140 HG22 VAL A 12 -5.431 32.818 10.576 1.00 17.78 H
ATOM 141 HG23 VAL A 12 -5.357 32.795 8.989 1.00 17.78 H
ATOM 142 N PRO A 13 -3.681 37.219 10.923 1.00 15.72 N
ANISOU 142 N PRO A 13 1808 2109 2055 -319 693 -271 N
ATOM 143 CA PRO A 13 -2.708 38.298 10.989 1.00 16.25 C
ANISOU 143 CA PRO A 13 1889 2094 2191 -349 760 -318 C
ATOM 144 C PRO A 13 -1.299 37.756 11.229 1.00 15.61 C
ANISOU 144 C PRO A 13 1852 2088 1991 -411 718 -396 C
ATOM 145 O PRO A 13 -1.111 36.719 11.876 1.00 15.58 O
ANISOU 145 O PRO A 13 1857 2175 1888 -437 663 -434 O
ATOM 146 CB PRO A 13 -3.202 39.136 12.186 1.00 17.21 C
ANISOU 146 CB PRO A 13 1983 2134 2424 -365 876 -448 C
ATOM 147 CG PRO A 13 -4.054 38.273 12.954 1.00 23.20 C
ANISOU 147 CG PRO A 13 2731 2995 3089 -369 851 -479 C
ATOM 148 CD PRO A 13 -4.620 37.248 12.058 1.00 16.09 C
ANISOU 148 CD PRO A 13 1833 2151 2129 -321 746 -337 C
ATOM 149 HA PRO A 13 -2.727 38.833 10.180 1.00 19.50 H
ATOM 150 HB2 PRO A 13 -2.442 39.423 12.715 1.00 20.66 H
ATOM 151 HB3 PRO A 13 -3.700 39.902 11.860 1.00 20.66 H
ATOM 152 HG2 PRO A 13 -3.529 37.851 13.652 1.00 27.84 H
ATOM 153 HG3 PRO A 13 -4.766 38.801 13.347 1.00 27.84 H
ATOM 154 HD2 PRO A 13 -4.639 36.386 12.501 1.00 19.31 H
ATOM 155 HD3 PRO A 13 -5.503 37.513 11.758 1.00 19.31 H
ATOM 156 N ILE A 14 -0.317 38.474 10.707 1.00 15.91 N
ANISOU 156 N ILE A 14 1898 2083 2064 -435 743 -392 N
ATOM 157 CA ILE A 14 1.062 38.055 10.753 1.00 15.46 C
ANISOU 157 CA ILE A 14 1866 2097 1910 -488 704 -454 C
ATOM 158 C ILE A 14 1.929 39.182 11.312 1.00 16.23 C
ANISOU 158 C ILE A 14 1968 2127 2074 -551 791 -555 C
ATOM 159 O ILE A 14 1.740 40.343 10.960 1.00 17.19 O
ANISOU 159 O ILE A 14 2064 2112 2354 -543 871 -523 O
ATOM 160 CB ILE A 14 1.584 37.742 9.323 1.00 15.25 C
ANISOU 160 CB ILE A 14 1826 2132 1837 -478 647 -368 C
ATOM 161 CG1 ILE A 14 0.793 36.587 8.710 1.00 14.81 C
ANISOU 161 CG1 ILE A 14 1742 2164 1723 -440 571 -328 C
ATOM 162 CG2 ILE A 14 3.084 37.397 9.343 1.00 14.98 C
ANISOU 162 CG2 ILE A 14 1801 2159 1733 -530 621 -448 C
ATOM 163 CD1 ILE A 14 1.087 36.367 7.221 1.00 15.12 C
ANISOU 163 CD1 ILE A 14 1728 2326 1690 -453 533 -280 C
ATOM 164 H ILE A 14 -0.434 39.229 10.311 1.00 19.09 H
ATOM 165 HA ILE A 14 1.158 37.267 11.311 1.00 18.55 H
ATOM 166 HB ILE A 14 1.457 38.529 8.770 1.00 18.30 H
ATOM 167 HG12 ILE A 14 1.015 35.769 9.182 1.00 17.77 H
ATOM 168 HG13 ILE A 14 -0.155 36.773 8.802 1.00 17.77 H
ATOM 169 HG21 ILE A 14 3.377 37.207 8.438 1.00 17.98 H
ATOM 170 HG22 ILE A 14 3.577 38.153 9.699 1.00 17.98 H
ATOM 171 HG23 ILE A 14 3.221 36.618 9.905 1.00 17.98 H
ATOM 172 HD11 ILE A 14 0.553 35.623 6.901 1.00 18.14 H
ATOM 173 HD12 ILE A 14 0.859 37.173 6.732 1.00 18.14 H
ATOM 174 HD13 ILE A 14 2.030 36.169 7.112 1.00 18.14 H
ATOM 175 N LEU A 15 2.889 38.813 12.151 1.00 16.08 N
ANISOU 175 N LEU A 15 1955 2202 1954 -616 774 -664 N
ATOM 176 CA LEU A 15 3.971 39.699 12.575 1.00 16.84 C
ANISOU 176 CA LEU A 15 2042 2280 2076 -698 841 -783 C
ATOM 177 C LEU A 15 5.297 39.050 12.273 1.00 16.30 C
ANISOU 177 C LEU A 15 1978 2315 1899 -727 765 -772 C
ATOM 178 O LEU A 15 5.497 37.869 12.550 1.00 15.70 O
ANISOU 178 O LEU A 15 1891 2353 1723 -715 675 -742 O
ATOM 179 CB LEU A 15 3.901 39.970 14.092 1.00 17.71 C
ANISOU 179 CB LEU A 15 2115 2475 2138 -782 903 -962 C
ATOM 180 CG LEU A 15 2.725 40.790 14.579 1.00 18.74 C
ANISOU 180 CG LEU A 15 2211 2504 2406 -776 1015 -1056 C
ATOM 181 CD1 LEU A 15 2.729 40.816 16.144 1.00 22.96 C
ANISOU 181 CD1 LEU A 15 2680 3233 2810 -891 1069 -1268 C
ATOM 182 CD2 LEU A 15 2.784 42.211 14.035 1.00 22.26 C
ANISOU 182 CD2 LEU A 15 2631 2711 3118 -773 1133 -1096 C
ATOM 183 H LEU A 15 2.937 38.029 12.501 1.00 19.30 H
ATOM 184 HA LEU A 15 3.915 40.543 12.100 1.00 20.21 H
ATOM 185 HB2 LEU A 15 3.865 39.116 14.551 1.00 21.25 H
ATOM 186 HB3 LEU A 15 4.707 40.441 14.354 1.00 21.25 H
ATOM 187 HG LEU A 15 1.899 40.380 14.280 1.00 22.49 H
ATOM 188 HD11 LEU A 15 1.974 41.342 16.453 1.00 27.55 H
ATOM 189 HD12 LEU A 15 2.656 39.907 16.475 1.00 27.55 H
ATOM 190 HD13 LEU A 15 3.558 41.214 16.451 1.00 27.55 H
ATOM 191 HD21 LEU A 15 2.019 42.707 14.365 1.00 26.72 H
ATOM 192 HD22 LEU A 15 3.606 42.630 14.335 1.00 26.72 H
ATOM 193 HD23 LEU A 15 2.765 42.179 13.065 1.00 26.72 H
ATOM 194 N VAL A 16 6.207 39.826 11.711 1.00 16.74 N
ANISOU 194 N VAL A 16 2032 2320 2008 -765 805 -787 N
ATOM 195 CA VAL A 16 7.551 39.367 11.418 1.00 16.46 C
ANISOU 195 CA VAL A 16 1985 2382 1886 -799 751 -800 C
ATOM 196 C VAL A 16 8.562 40.315 12.066 1.00 17.42 C
ANISOU 196 C VAL A 16 2085 2505 2029 -903 822 -936 C
ATOM 197 O VAL A 16 8.412 41.536 11.998 1.00 18.41 O
ANISOU 197 O VAL A 16 2203 2487 2303 -939 926 -979 O
ATOM 198 CB VAL A 16 7.799 39.343 9.911 1.00 16.28 C
ANISOU 198 CB VAL A 16 1959 2349 1876 -766 730 -689 C
ATOM 199 CG1 VAL A 16 9.166 38.779 9.593 1.00 16.12 C
ANISOU 199 CG1 VAL A 16 1909 2440 1775 -799 682 -732 C
ATOM 200 CG2 VAL A 16 6.693 38.517 9.189 1.00 15.69 C
ANISOU 200 CG2 VAL A 16 1884 2299 1779 -685 673 -590 C
ATOM 201 H VAL A 16 6.066 40.643 11.484 1.00 20.08 H
ATOM 202 HA VAL A 16 7.682 38.474 11.774 1.00 19.75 H
ATOM 203 HB VAL A 16 7.764 40.251 9.571 1.00 19.53 H
ATOM 204 HG11 VAL A 16 9.291 38.777 8.631 1.00 19.34 H
ATOM 205 HG12 VAL A 16 9.842 39.333 10.014 1.00 19.34 H
ATOM 206 HG13 VAL A 16 9.220 37.873 9.935 1.00 19.34 H
ATOM 207 HG21 VAL A 16 6.872 38.516 8.236 1.00 18.83 H
ATOM 208 HG22 VAL A 16 6.706 37.608 9.529 1.00 18.83 H
ATOM 209 HG23 VAL A 16 5.831 38.924 9.364 1.00 18.83 H
ATOM 210 N GLU A 17 9.595 39.732 12.671 1.00 18.42 N
ANISOU 210 N GLU A 17 2178 2785 2035 -954 767 -995 N
ATOM 211 CA GLU A 17 10.673 40.491 13.276 1.00 18.40 C
ANISOU 211 CA GLU A 17 2136 2837 2018 -1069 821 -1137 C
ATOM 212 C GLU A 17 11.973 39.835 12.881 1.00 18.08 C
ANISOU 212 C GLU A 17 2063 2908 1900 -1076 743 -1100 C
ATOM 213 O GLU A 17 12.101 38.609 12.958 1.00 17.55 O
ANISOU 213 O GLU A 17 1966 2939 1764 -1021 641 -1020 O
ATOM 214 CB GLU A 17 10.509 40.475 14.785 1.00 19.23 C
ANISOU 214 CB GLU A 17 2186 3098 2024 -1150 829 -1259 C
ATOM 215 CG GLU A 17 9.211 41.107 15.230 1.00 22.51 C
ANISOU 215 CG GLU A 17 2608 3413 2534 -1145 914 -1327 C
ATOM 216 CD GLU A 17 9.212 42.599 15.067 1.00 27.80 C
ANISOU 216 CD GLU A 17 3263 3887 3413 -1201 1065 -1473 C
ATOM 217 OE1 GLU A 17 10.301 43.186 14.850 1.00 23.48 O
ANISOU 217 OE1 GLU A 17 2690 3321 2912 -1267 1100 -1529 O
ATOM 218 OE2 GLU A 17 8.115 43.179 15.199 1.00 38.66 O
ANISOU 218 OE2 GLU A 17 4633 5120 4935 -1177 1156 -1532 O
ATOM 219 H GLU A 17 9.691 38.881 12.742 1.00 22.11 H
ATOM 220 HA GLU A 17 10.663 41.408 12.959 1.00 22.08 H
ATOM 221 HB2 GLU A 17 10.519 39.556 15.095 1.00 23.08 H
ATOM 222 HB3 GLU A 17 11.239 40.971 15.188 1.00 23.08 H
ATOM 223 HG2 GLU A 17 8.485 40.747 14.698 1.00 27.02 H
ATOM 224 HG3 GLU A 17 9.067 40.907 16.168 1.00 27.02 H
ATOM 225 N ALEU A 18 12.929 40.652 12.460 0.40 18.70 N
ANISOU 225 N ALEU A 18 2127 2953 2024 -1144 798 -1157 N
ATOM 226 N BLEU A 18 12.935 40.641 12.445 0.60 18.69 N
ANISOU 226 N BLEU A 18 2126 2952 2022 -1143 797 -1155 N
ATOM 227 CA ALEU A 18 14.222 40.167 12.025 0.40 18.61 C
ANISOU 227 CA ALEU A 18 2071 3046 1953 -1157 741 -1143 C
ATOM 228 CA BLEU A 18 14.225 40.145 11.992 0.60 18.58 C
ANISOU 228 CA BLEU A 18 2068 3043 1950 -1155 740 -1139 C
ATOM 229 C ALEU A 18 15.316 41.042 12.588 0.40 19.78 C
ANISOU 229 C ALEU A 18 2169 3253 2092 -1289 798 -1283 C
ATOM 230 C BLEU A 18 15.329 41.026 12.541 0.60 19.75 C
ANISOU 230 C BLEU A 18 2166 3248 2090 -1287 797 -1278 C
ATOM 231 O ALEU A 18 15.244 42.259 12.489 0.40 20.65 O
ANISOU 231 O ALEU A 18 2292 3230 2323 -1358 908 -1357 O
ATOM 232 O BLEU A 18 15.263 42.236 12.404 0.60 20.60 O
ANISOU 232 O BLEU A 18 2287 3221 2318 -1353 905 -1347 O
ATOM 233 CB ALEU A 18 14.305 40.200 10.500 0.40 18.24 C
ANISOU 233 CB ALEU A 18 2044 2928 1958 -1108 749 -1044 C
ATOM 234 CB BLEU A 18 14.287 40.165 10.455 0.60 18.20 C
ANISOU 234 CB BLEU A 18 2040 2924 1953 -1104 747 -1039 C
ATOM 235 CG ALEU A 18 15.643 39.742 9.921 0.40 18.36 C
ANISOU 235 CG ALEU A 18 1994 3058 1922 -1127 712 -1060 C
ATOM 236 CG BLEU A 18 15.672 39.985 9.820 0.60 18.48 C
ANISOU 236 CG BLEU A 18 2015 3059 1949 -1141 729 -1059 C
ATOM 237 CD1ALEU A 18 15.381 39.130 8.572 0.40 17.93 C
ANISOU 237 CD1ALEU A 18 1931 3023 1858 -1058 688 -983 C
ATOM 238 CD1BLEU A 18 16.228 38.592 10.049 0.60 18.11 C
ANISOU 238 CD1BLEU A 18 1899 3134 1847 -1085 629 -1070 C
ATOM 239 CD2ALEU A 18 16.666 40.884 9.791 0.40 19.38 C
ANISOU 239 CD2ALEU A 18 2099 3180 2083 -1242 789 -1119 C
ATOM 240 CD2BLEU A 18 15.630 40.302 8.321 0.60 18.63 C
ANISOU 240 CD2BLEU A 18 2034 3059 1987 -1133 763 -965 C
ATOM 241 H ALEU A 18 12.847 41.507 12.417 0.40 22.44 H
ATOM 242 H BLEU A 18 12.861 41.497 12.402 0.60 22.42 H
ATOM 243 HA ALEU A 18 14.355 39.256 12.331 0.40 22.33 H
ATOM 244 HA BLEU A 18 14.360 39.236 12.303 0.60 22.30 H
ATOM 245 HB2ALEU A 18 13.617 39.619 10.140 0.40 21.89 H
ATOM 246 HB2BLEU A 18 13.722 39.451 10.120 0.60 21.84 H
ATOM 247 HB3ALEU A 18 14.153 41.110 10.201 0.40 21.89 H
ATOM 248 HB3BLEU A 18 13.940 41.018 10.149 0.60 21.84 H
ATOM 249 HG ALEU A 18 16.023 39.059 10.495 0.40 22.03 H
ATOM 250 HG BLEU A 18 16.283 40.614 10.233 0.60 22.18 H
ATOM 251 HD11ALEU A 18 16.222 38.834 8.191 0.40 21.52 H
ATOM 252 HD11BLEU A 18 17.101 38.529 9.630 0.60 21.73 H
ATOM 253 HD12ALEU A 18 14.782 38.375 8.680 0.40 21.52 H
ATOM 254 HD12BLEU A 18 16.307 38.437 11.003 0.60 21.73 H
ATOM 255 HD13ALEU A 18 14.973 39.797 7.998 0.40 21.52 H
ATOM 256 HD13BLEU A 18 15.625 37.943 9.656 0.60 21.73 H
ATOM 257 HD21ALEU A 18 17.489 40.529 9.420 0.40 23.25 H
ATOM 258 HD21BLEU A 18 16.516 40.180 7.948 0.60 22.36 H
ATOM 259 HD22ALEU A 18 16.305 41.566 9.204 0.40 23.25 H
ATOM 260 HD22BLEU A 18 15.002 39.701 7.889 0.60 22.36 H
ATOM 261 HD23ALEU A 18 16.834 41.258 10.670 0.40 23.25 H
ATOM 262 HD23BLEU A 18 15.344 41.221 8.202 0.60 22.36 H
ATOM 263 N ASP A 19 16.329 40.408 13.170 1.00 20.05 N
ANISOU 263 N ASP A 19 2122 3475 2020 -1314 725 -1292 N
ATOM 264 CA ASP A 19 17.578 41.091 13.554 1.00 21.22 C
ANISOU 264 CA ASP A 19 2203 3710 2148 -1398 770 -1372 C
ATOM 265 C ASP A 19 18.665 40.532 12.666 1.00 22.77 C
ANISOU 265 C ASP A 19 2368 3957 2327 -1375 714 -1328 C
ATOM 266 O ASP A 19 18.895 39.309 12.651 1.00 20.44 O
ANISOU 266 O ASP A 19 2017 3759 1992 -1316 608 -1261 O
ATOM 267 CB ASP A 19 17.976 40.790 15.003 1.00 22.21 C
ANISOU 267 CB ASP A 19 2228 4069 2144 -1450 729 -1396 C
ATOM 268 CG ASP A 19 17.168 41.573 16.016 1.00 35.56 C
ANISOU 268 CG ASP A 19 3896 5766 3849 -1514 812 -1494 C
ATOM 269 OD1 ASP A 19 16.575 42.613 15.638 1.00 23.46 O
ANISOU 269 OD1 ASP A 19 2422 4028 2464 -1523 927 -1578 O
ATOM 270 OD2 ASP A 19 17.155 41.154 17.202 1.00 36.38 O
ANISOU 270 OD2 ASP A 19 3904 6100 3817 -1565 767 -1490 O
ATOM 271 H AASP A 19 16.323 39.569 13.359 0.40 24.06 H
ATOM 272 H BASP A 19 16.311 39.577 13.392 0.60 24.06 H
ATOM 273 HA ASP A 19 17.504 42.049 13.423 1.00 25.46 H
ATOM 274 HB2 ASP A 19 17.839 39.845 15.177 1.00 26.66 H
ATOM 275 HB3 ASP A 19 18.911 41.017 15.126 1.00 26.66 H
ATOM 276 N GLY A 20 19.329 41.417 11.925 1.00 25.73 N
ANISOU 276 N GLY A 20 2760 4260 2757 -1424 787 -1370 N
ATOM 277 CA GLY A 20 20.388 41.017 11.017 1.00 23.03 C
ANISOU 277 CA GLY A 20 2372 3981 2398 -1413 752 -1342 C
ATOM 278 C GLY A 20 21.732 41.678 11.300 1.00 23.54 C
ANISOU 278 C GLY A 20 2391 4121 2431 -1485 784 -1418 C
ATOM 279 O GLY A 20 21.810 42.748 11.938 1.00 23.72 O
ANISOU 279 O GLY A 20 2429 4102 2482 -1558 864 -1507 O
ATOM 280 H GLY A 20 19.179 42.264 11.933 1.00 30.88 H
ATOM 281 HA2 GLY A 20 20.507 40.056 11.073 1.00 27.64 H
ATOM 282 HA3 GLY A 20 20.128 41.238 10.109 1.00 27.64 H
ATOM 283 N ASP A 21 22.780 41.008 10.820 1.00 22.63 N
ANISOU 283 N ASP A 21 2204 4117 2278 -1460 730 -1402 N
ATOM 284 CA ASP A 21 24.172 41.428 10.912 1.00 23.74 C
ANISOU 284 CA ASP A 21 2287 4350 2383 -1518 744 -1462 C
ATOM 285 C ASP A 21 24.884 40.835 9.680 1.00 23.60 C
ANISOU 285 C ASP A 21 2218 4373 2374 -1479 717 -1435 C
ATOM 286 O ASP A 21 25.142 39.633 9.632 1.00 23.34 O
ANISOU 286 O ASP A 21 2102 4419 2347 -1396 643 -1415 O
ATOM 287 CB ASP A 21 24.816 40.878 12.192 1.00 24.43 C
ANISOU 287 CB ASP A 21 2280 4621 2381 -1521 676 -1474 C
ATOM 288 CG ASP A 21 26.275 41.282 12.348 1.00 39.60 C
ANISOU 288 CG ASP A 21 4130 6660 4255 -1586 687 -1537 C
ATOM 289 OD1 ASP A 21 26.914 41.624 11.335 1.00 35.23 O
ANISOU 289 OD1 ASP A 21 3583 6060 3742 -1602 723 -1557 O
ATOM 290 OD2 ASP A 21 26.793 41.252 13.496 1.00 38.18 O
ANISOU 290 OD2 ASP A 21 3876 6650 3982 -1630 656 -1561 O
ATOM 291 H ASP A 21 22.696 40.256 10.410 1.00 27.16 H
ATOM 292 HA ASP A 21 24.242 42.395 10.898 1.00 28.49 H
ATOM 293 HB2 ASP A 21 24.329 41.215 12.960 1.00 29.32 H
ATOM 294 HB3 ASP A 21 24.775 39.909 12.174 1.00 29.32 H
ATOM 295 N VAL A 22 25.170 41.670 8.687 1.00 24.07 N
ANISOU 295 N VAL A 22 2309 4378 2459 -1538 779 -1429 N
ATOM 296 CA VAL A 22 25.845 41.220 7.455 1.00 24.30 C
ANISOU 296 CA VAL A 22 2279 4490 2465 -1519 767 -1417 C
ATOM 297 C VAL A 22 27.187 41.932 7.335 1.00 25.57 C
ANISOU 297 C VAL A 22 2397 4714 2605 -1602 799 -1461 C
ATOM 298 O VAL A 22 27.246 43.156 7.313 1.00 26.35 O
ANISOU 298 O VAL A 22 2538 4723 2751 -1694 865 -1439 O
ATOM 299 CB VAL A 22 24.972 41.484 6.207 1.00 24.09 C
ANISOU 299 CB VAL A 22 2295 4410 2448 -1520 799 -1317 C
ATOM 300 CG1 VAL A 22 25.709 41.086 4.917 1.00 24.79 C
ANISOU 300 CG1 VAL A 22 2306 4643 2470 -1520 791 -1326 C
ATOM 301 CG2 VAL A 22 23.638 40.702 6.308 1.00 22.89 C
ANISOU 301 CG2 VAL A 22 2177 4207 2312 -1434 767 -1285 C
ATOM 302 H VAL A 22 24.985 42.510 8.695 1.00 28.88 H
ATOM 303 HA VAL A 22 26.011 40.267 7.512 1.00 29.16 H
ATOM 304 HB VAL A 22 24.765 42.430 6.157 1.00 28.91 H
ATOM 305 HG11 VAL A 22 25.133 41.264 4.157 1.00 29.75 H
ATOM 306 HG12 VAL A 22 26.524 41.608 4.845 1.00 29.75 H
ATOM 307 HG13 VAL A 22 25.924 40.141 4.955 1.00 29.75 H
ATOM 308 HG21 VAL A 22 23.107 40.881 5.516 1.00 27.46 H
ATOM 309 HG22 VAL A 22 23.832 39.754 6.369 1.00 27.46 H
ATOM 310 HG23 VAL A 22 23.161 40.994 7.100 1.00 27.46 H
ATOM 311 N ASN A 23 28.262 41.154 7.282 1.00 26.93 N
ANISOU 311 N ASN A 23 2468 5022 2741 -1566 758 -1520 N
ATOM 312 CA ASN A 23 29.615 41.710 7.332 1.00 27.26 C
ANISOU 312 CA ASN A 23 2455 5145 2756 -1641 780 -1572 C
ATOM 313 C ASN A 23 29.732 42.771 8.448 1.00 27.89 C
ANISOU 313 C ASN A 23 2577 5176 2844 -1730 819 -1607 C
ATOM 314 O ASN A 23 30.338 43.849 8.274 1.00 29.03 O
ANISOU 314 O ASN A 23 2728 5288 3014 -1832 881 -1630 O
ATOM 315 CB ASN A 23 30.008 42.268 5.970 1.00 28.02 C
ANISOU 315 CB ASN A 23 2546 5266 2836 -1704 827 -1538 C
ATOM 316 CG ASN A 23 30.533 41.189 5.033 1.00 28.25 C
ANISOU 316 CG ASN A 23 2479 5432 2824 -1639 797 -1592 C
ATOM 317 OD1 ASN A 23 30.050 40.054 5.031 1.00 27.55 O
ANISOU 317 OD1 ASN A 23 2357 5347 2764 -1533 755 -1628 O
ATOM 318 ND2 ASN A 23 31.529 41.538 4.239 1.00 29.50 N
ANISOU 318 ND2 ASN A 23 2579 5695 2934 -1704 825 -1612 N
ATOM 319 H ASN A 23 28.238 40.297 7.216 1.00 32.31 H