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HEADER IMMUNE SYSTEM 24-JUN-13 4BV4
TITLE STRUCTURE AND ALLOSTERY IN TOLL-SPATZLE RECOGNITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA;
COMPND 3 CHAIN: R;
COMPND 4 FRAGMENT: PROTEIN TOLL, RESIDUES 28-397, VARIABLE LYMPHOCYTE
COMPND 5 RECEPTOR B, RESIDUES 133-201;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CHIMERIC PROTEIN, GLYCAN BOUND;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN SPAETZLE C-106;
COMPND 10 CHAIN: L, M;
COMPND 11 SYNONYM: PROTEIN SPAETZLE;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER, EPTATRETUS BURGERI;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY, INSHORE HAGFISH;
SOURCE 4 ORGANISM_TAXID: 7227, 7764;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 12 ORGANISM_COMMON: FRUIT FLY;
SOURCE 13 ORGANISM_TAXID: 7227;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1
KEYWDS CYTOKINE RECOGNITION, EMBRYONIC DEVELOPMENT, IMMUNE SYSTEM, INNATE
KEYWDS 2 IMMUNITY, LEUCINE-RICH REPEATS, CYSTINE-KNOT, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.LEWIS,C.J.ARNOT,H.BEESTON,A.MCCOY,A.E.ASHCROFT,N.J.GAY,
AUTHOR 2 M.GANGLOFF
REVDAT 3 08-JAN-14 4BV4 1 JRNL
REVDAT 2 11-DEC-13 4BV4 1 JRNL
REVDAT 1 04-DEC-13 4BV4 0
JRNL AUTH M.LEWIS,C.J.ARNOT,H.BEESTON,A.MCCOY,A.E.ASHCROFT,N.J.GAY,
JRNL AUTH 2 M.GANGLOFF
JRNL TITL CYTOKINE SPATZLE BINDS TO THE DROSOPHILA IMMUNORECEPTOR
JRNL TITL 2 TOLL WITH A NEUROTROPHIN-LIKE SPECIFICITY AND COUPLES
JRNL TITL 3 RECEPTOR ACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 20461 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 24282309
JRNL DOI 10.1073/PNAS.1317002110
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK;
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.74
REMARK 3 NUMBER OF REFLECTIONS : 24588
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1967
REMARK 3 R VALUE (WORKING SET) : 0.1950
REMARK 3 FREE R VALUE : 0.2271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.11
REMARK 3 FREE R VALUE TEST SET COUNT : 1256
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.45
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.74
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 938
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2159
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 885
REMARK 3 BIN R VALUE (WORKING SET) : 0.2122
REMARK 3 BIN FREE R VALUE : 0.2735
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.65
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 53
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 : 4570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 150
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.3453
REMARK 3 B22 (A**2) : 12.2952
REMARK 3 B33 (A**2) : -5.9499
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : -0.3304
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.343
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.465
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.254
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.482
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.260
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9245
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9032
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4840 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 6576 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 2305 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 130 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 678 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4840 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 683 ; 5.00 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5133 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.33
REMARK 3
REMARK 3 TLS DETAILS.
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN L
REMARK 3 ORIGIN FOR THE GROUP (A): 400.3477 -6.8524 117.5984
REMARK 3 T TENSOR
REMARK 3 T11: -0.2186 T22: 0.2390
REMARK 3 T33: -0.1616 T12: -0.0690
REMARK 3 T13: 0.0023 T23: -0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 2.1204 L22: 1.4244
REMARK 3 L33: 3.6694 L12: -0.9804
REMARK 3 L13: -2.4379 L23: 1.5945
REMARK 3 S TENSOR
REMARK 3 S11: 0.0101 S12: -0.2478 S13: 0.1726
REMARK 3 S21: 0.1074 S22: -0.0400 S23: 0.1217
REMARK 3 S31: -0.0465 S32: -0.0018 S33: 0.0298
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN M
REMARK 3 ORIGIN FOR THE GROUP (A): 410.9011 -3.1092 117.0293
REMARK 3 T TENSOR
REMARK 3 T11: -0.2603 T22: 0.1725
REMARK 3 T33: -0.1090 T12: -0.1111
REMARK 3 T13: -0.0241 T23: -0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 2.3158 L22: 4.8708
REMARK 3 L33: 4.6763 L12: -0.4951
REMARK 3 L13: 0.0580 L23: 2.7977
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.1225 S13: 0.3149
REMARK 3 S21: -0.0148 S22: 0.0433 S23: 0.0016
REMARK 3 S31: -0.0992 S32: 0.0192 S33: -0.0513
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN R
REMARK 3 ORIGIN FOR THE GROUP (A): 410.6345 -19.2876 104.1815
REMARK 3 T TENSOR
REMARK 3 T11: -0.2718 T22: -0.0530
REMARK 3 T33: -0.2971 T12: -0.0444
REMARK 3 T13: 0.0273 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 2.7177 L22: 0.6657
REMARK 3 L33: 1.7993 L12: -0.7093
REMARK 3 L13: 0.5863 L23: -0.1828
REMARK 3 S TENSOR
REMARK 3 S11: -0.0573 S12: -0.3010 S13: -0.2474
REMARK 3 S21: 0.1140 S22: 0.0820 S23: 0.0200
REMARK 3 S31: 0.1647 S32: 0.1882 S33: -0.0247
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 4BV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-13.
REMARK 100 THE PDBE ID CODE IS EBI-57420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS, ANISOSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24588
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.35
REMARK 200 RESOLUTION RANGE LOW (A) : 49.12
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.6
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.8
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 32.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.9
REMARK 200 R MERGE FOR SHELL (I) : 0.78
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.60
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: PDB ENTRY 4ARN, 3E07
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 8000, 0.1M TRIS PH 7.5,
REMARK 280 0.1 M MGCL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 99.15500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 99.15500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.55500
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 32.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, R
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 L 0
REMARK 465 VAL L 1
REMARK 465 GLY L 2
REMARK 465 GLY L 3
REMARK 465 SER L 4
REMARK 465 ASP L 5
REMARK 465 GLU L 6
REMARK 465 LYS L 21
REMARK 465 GLY L 22
REMARK 465 LEU L 23
REMARK 465 ARG L 24
REMARK 465 ALA L 25
REMARK 465 ASP L 26
REMARK 465 ASP L 27
REMARK 465 THR L 28
REMARK 465 TRP L 29
REMARK 465 GLN L 30
REMARK 465 LEU L 31
REMARK 465 ILE L 32
REMARK 465 VAL L 33
REMARK 465 ASN L 34
REMARK 465 ASN L 35
REMARK 465 ASP L 36
REMARK 465 GLU L 37
REMARK 465 TYR L 38
REMARK 465 LYS L 39
REMARK 465 LEU L 77
REMARK 465 ALA L 78
REMARK 465 SER L 79
REMARK 465 ILE L 80
REMARK 465 LYS L 81
REMARK 465 SER L 82
REMARK 465 ASP L 83
REMARK 465 GLY L 84
REMARK 465 GLU L 85
REMARK 465 LEU L 86
REMARK 465 ASP L 87
REMARK 465 VAL L 88
REMARK 465 VAL L 89
REMARK 465 GLN L 90
REMARK 465 GLY L 106
REMARK 465 PRO M 19
REMARK 465 LYS M 20
REMARK 465 LYS M 21
REMARK 465 GLY M 22
REMARK 465 LEU M 23
REMARK 465 ARG M 24
REMARK 465 ALA M 25
REMARK 465 ASP M 26
REMARK 465 ASP M 27
REMARK 465 THR M 28
REMARK 465 TRP M 29
REMARK 465 GLN M 30
REMARK 465 LEU M 31
REMARK 465 ILE M 32
REMARK 465 VAL M 33
REMARK 465 ASN M 34
REMARK 465 ASN M 35
REMARK 465 ASP M 36
REMARK 465 GLU M 37
REMARK 465 TYR M 38
REMARK 465 LYS M 39
REMARK 465 GLN M 40
REMARK 465 LEU M 77
REMARK 465 ALA M 78
REMARK 465 SER M 79
REMARK 465 ILE M 80
REMARK 465 LYS M 81
REMARK 465 SER M 82
REMARK 465 ASP M 83
REMARK 465 GLY M 84
REMARK 465 GLU M 85
REMARK 465 LEU M 86
REMARK 465 ASP M 87
REMARK 465 VAL M 88
REMARK 465 VAL M 89
REMARK 465 GLN M 90
REMARK 465 ASN M 91
REMARK 465 SER M 92
REMARK 465 GLY M 106
REMARK 465 THR R 468
REMARK 465 GLY R 469
REMARK 465 GLU R 470
REMARK 465 ASN R 471
REMARK 465 LEU R 472
REMARK 465 TYR R 473
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 GLU M 48 69.47 -69.87
REMARK 500 ASN M 59 54.06 -116.47
REMARK 500 MET R 37 -118.08 -84.48
REMARK 500 SER R 38 -91.59 50.24
REMARK 500 MET R 49 -120.21 58.70
REMARK 500 ASN R 59 90.64 61.37
REMARK 500 ASN R 62 46.49 -144.32
REMARK 500 LYS R 72 -20.68 71.43
REMARK 500 ASP R 73 -73.76 -98.15
REMARK 500 LYS R 93 -106.98 65.14
REMARK 500 LEU R 94 123.79 57.37
REMARK 500 HIS R 112 54.41 -105.44
REMARK 500 ARG R 148 -41.66 73.60
REMARK 500 LEU R 149 48.63 -85.86
REMARK 500 ALA R 183 38.28 -143.15
REMARK 500 LEU R 196 42.39 -104.38
REMARK 500 ASN R 231 -160.16 -113.50
REMARK 500 ASN R 235 72.53 -117.07
REMARK 500 ALA R 244 41.06 -88.86
REMARK 500 ASN R 279 -169.38 -108.51
REMARK 500 HIS R 291 -16.85 79.88
REMARK 500 ASN R 292 63.47 -102.60
REMARK 500 ASN R 352 -156.61 -108.30
REMARK 500 CYS R 428 51.05 -92.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG R 501 BOUND TO ASN R 80
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG R 601 BOUND TO ASN R 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG R 901 BOUND TO ASN R 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG R1101 THROUGH MAN R1108 BOUND TO ASN R 346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG R1201 BOUND TO ASN R 391
DBREF 4BV4 L 1 106 UNP P48607 SPZ_DROME 221 326
DBREF 4BV4 M 1 106 UNP P48607 SPZ_DROME 221 326
DBREF 4BV4 R 28 397 UNP P08953 TOLL_DROME 28 397
DBREF 4BV4 R 400 468 UNP Q4G1L2 Q4G1L2_EPTBU 133 201
SEQADV 4BV4 GLY L 0 UNP P48607 EXPRESSION TAG
SEQADV 4BV4 GLY M 0 UNP P48607 EXPRESSION TAG
SEQADV 4BV4 ALA R 398 UNP P08953 LINKER
SEQADV 4BV4 SER R 399 UNP P08953 LINKER
SEQADV 4BV4 GLY R 469 UNP Q4G1L2 EXPRESSION TAG
SEQADV 4BV4 GLU R 470 UNP Q4G1L2 EXPRESSION TAG
SEQADV 4BV4 ASN R 471 UNP Q4G1L2 EXPRESSION TAG
SEQADV 4BV4 LEU R 472 UNP Q4G1L2 EXPRESSION TAG
SEQADV 4BV4 TYR R 473 UNP Q4G1L2 EXPRESSION TAG
SEQRES 1 L 107 GLY VAL GLY GLY SER ASP GLU ARG PHE LEU CYS ARG SER
SEQRES 2 L 107 ILE ARG LYS LEU VAL TYR PRO LYS LYS GLY LEU ARG ALA
SEQRES 3 L 107 ASP ASP THR TRP GLN LEU ILE VAL ASN ASN ASP GLU TYR
SEQRES 4 L 107 LYS GLN ALA ILE GLN ILE GLU GLU CYS GLU GLY ALA ASP
SEQRES 5 L 107 GLN PRO CYS ASP PHE ALA ALA ASN PHE PRO GLN SER TYR
SEQRES 6 L 107 ASN PRO ILE CYS LYS GLN HIS TYR THR GLN GLN THR LEU
SEQRES 7 L 107 ALA SER ILE LYS SER ASP GLY GLU LEU ASP VAL VAL GLN
SEQRES 8 L 107 ASN SER PHE LYS ILE PRO SER CYS CYS LYS CYS ALA LEU
SEQRES 9 L 107 LYS THR GLY
SEQRES 1 M 107 GLY VAL GLY GLY SER ASP GLU ARG PHE LEU CYS ARG SER
SEQRES 2 M 107 ILE ARG LYS LEU VAL TYR PRO LYS LYS GLY LEU ARG ALA
SEQRES 3 M 107 ASP ASP THR TRP GLN LEU ILE VAL ASN ASN ASP GLU TYR
SEQRES 4 M 107 LYS GLN ALA ILE GLN ILE GLU GLU CYS GLU GLY ALA ASP
SEQRES 5 M 107 GLN PRO CYS ASP PHE ALA ALA ASN PHE PRO GLN SER TYR
SEQRES 6 M 107 ASN PRO ILE CYS LYS GLN HIS TYR THR GLN GLN THR LEU
SEQRES 7 M 107 ALA SER ILE LYS SER ASP GLY GLU LEU ASP VAL VAL GLN
SEQRES 8 M 107 ASN SER PHE LYS ILE PRO SER CYS CYS LYS CYS ALA LEU
SEQRES 9 M 107 LYS THR GLY
SEQRES 1 R 446 SER PHE GLY ARG ASP ALA CYS SER GLU MET SER ILE ASP
SEQRES 2 R 446 GLY LEU CYS GLN CYS ALA PRO ILE MET SER GLU TYR GLU
SEQRES 3 R 446 ILE ILE CYS PRO ALA ASN ALA GLU ASN PRO THR PHE ARG
SEQRES 4 R 446 LEU THR ILE GLN PRO LYS ASP TYR VAL GLN ILE MET CYS
SEQRES 5 R 446 ASN LEU THR ASP THR THR ASP TYR GLN GLN LEU PRO LYS
SEQRES 6 R 446 LYS LEU ARG ILE GLY GLU VAL ASP ARG VAL GLN MET ARG
SEQRES 7 R 446 ARG CYS MET LEU PRO GLY HIS THR PRO ILE ALA SER ILE
SEQRES 8 R 446 LEU ASP TYR LEU GLY ILE VAL SER PRO THR THR LEU ILE
SEQRES 9 R 446 PHE GLU SER ASP ASN LEU GLY MET ASN ILE THR ARG GLN
SEQRES 10 R 446 HIS LEU ASP ARG LEU HIS GLY LEU LYS ARG PHE ARG PHE
SEQRES 11 R 446 THR THR ARG ARG LEU THR HIS ILE PRO ALA ASN LEU LEU
SEQRES 12 R 446 THR ASP MET ARG ASN LEU SER HIS LEU GLU LEU ARG ALA
SEQRES 13 R 446 ASN ILE GLU GLU MET PRO SER HIS LEU PHE ASP ASP LEU
SEQRES 14 R 446 GLU ASN LEU GLU SER ILE GLU PHE GLY SER ASN LYS LEU
SEQRES 15 R 446 ARG GLN MET PRO ARG GLY ILE PHE GLY LYS MET PRO LYS
SEQRES 16 R 446 LEU LYS GLN LEU ASN LEU TRP SER ASN GLN LEU HIS ASN
SEQRES 17 R 446 LEU THR LYS HIS ASP PHE GLU GLY ALA THR SER VAL LEU
SEQRES 18 R 446 GLY ILE ASP ILE HIS ASP ASN GLY ILE GLU GLN LEU PRO
SEQRES 19 R 446 HIS ASP VAL PHE ALA HIS LEU THR ASN VAL THR ASP ILE
SEQRES 20 R 446 ASN LEU SER ALA ASN LEU PHE ARG SER LEU PRO GLN GLY
SEQRES 21 R 446 LEU PHE ASP HIS ASN LYS HIS LEU ASN GLU VAL ARG LEU
SEQRES 22 R 446 MET ASN ASN ARG VAL PRO LEU ALA THR LEU PRO SER ARG
SEQRES 23 R 446 LEU PHE ALA ASN GLN PRO GLU LEU GLN ILE LEU ARG LEU
SEQRES 24 R 446 ARG ALA GLU LEU GLN SER LEU PRO GLY ASP LEU PHE GLU
SEQRES 25 R 446 HIS SER THR GLN ILE THR ASN ILE SER LEU GLY ASP ASN
SEQRES 26 R 446 LEU LEU LYS THR LEU PRO ALA THR LEU LEU GLU HIS GLN
SEQRES 27 R 446 VAL ASN LEU LEU SER LEU ASP LEU SER ASN ASN ARG LEU
SEQRES 28 R 446 THR HIS LEU PRO ASP SER LEU PHE ALA HIS THR THR ASN
SEQRES 29 R 446 LEU THR ASP LEU ARG LEU ALA SER ASN GLN LEU LYS SER
SEQRES 30 R 446 VAL PRO ASP GLY ILE PHE ASP ARG LEU THR SER LEU GLN
SEQRES 31 R 446 LYS ILE TRP LEU HIS THR ASN PRO TRP ASP CYS SER CYS
SEQRES 32 R 446 PRO ARG ILE ASP TYR LEU SER ARG TRP LEU ASN LYS ASN
SEQRES 33 R 446 SER GLN LYS GLU GLN GLY SER ALA LYS CYS SER GLY SER
SEQRES 34 R 446 GLY LYS PRO VAL ARG SER ILE ILE CYS PRO THR THR GLY
SEQRES 35 R 446 GLU ASN LEU TYR
HET NAG R 501 14
HET NAG R 601 14
HET NAG R 901 14
HET NAG R1101 14
HET NAG R1102 14
HET BMA R1103 11
HET MAN R1104 11
HET BMA R1105 11
HET BMA R1106 11
HET MAN R1107 11
HET MAN R1108 11
HET NAG R1201 14
HETNAM BMA BETA-D-MANNOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
FORMUL 4 BMA 3(C6 H12 O6)
FORMUL 5 NAG 6(C8 H15 N O6)
FORMUL 6 MAN 3(C6 H12 O6)
FORMUL 7 HOH *104(H2 O)
HELIX 1 1 PHE L 56 PHE L 60 5 5
HELIX 2 2 GLY R 30 GLU R 36 1 7
HELIX 3 3 MET R 37 GLY R 41 5 5
HELIX 4 4 ASP R 83 LEU R 90 5 8
HELIX 5 5 ILE R 115 LEU R 122 1 8
HELIX 6 6 THR R 142 ASP R 147 5 6
HELIX 7 7 PRO R 189 ASP R 194 5 6
HELIX 8 8 GLY R 215 MET R 220 5 6
HELIX 9 9 THR R 237 GLU R 242 5 6
HELIX 10 10 ILE R 433 ASN R 443 1 11
HELIX 11 11 VAL R 460 ILE R 463 5 4
SHEET 1 LA 4 SER L 12 VAL L 17 0
SHEET 2 LA 4 ILE L 42 CYS L 47 -1 O ILE L 42 N VAL L 17
SHEET 3 LA 4 ASN M 65 GLN M 75 -1 O GLN M 74 N GLN L 43
SHEET 4 LA 4 LYS M 94 LYS M 104 -1 O ILE M 95 N THR M 73
SHEET 1 LB 3 ASN L 65 GLN L 75 0
SHEET 2 LB 3 PHE L 93 LYS L 104 -1 O PHE L 93 N GLN L 75
SHEET 3 LB 3 GLU M 6 PHE M 8 -1 O ARG M 7 N LEU L 103
SHEET 1 MA 2 SER M 12 VAL M 17 0
SHEET 2 MA 2 ILE M 42 CYS M 47 -1 O ILE M 42 N VAL M 17
SHEET 1 RA19 GLN R 44 ILE R 48 0
SHEET 2 RA19 GLU R 51 CYS R 56 -1 O GLU R 51 N ILE R 48
SHEET 3 RA19 PHE R 65 GLN R 70 -1 O PHE R 65 N CYS R 56
SHEET 4 RA19 TYR R 74 CYS R 79 -1 O TYR R 74 N GLN R 70
SHEET 5 RA19 ARG R 101 ARG R 105 1 O ARG R 101 N VAL R 75
SHEET 6 RA19 THR R 129 GLU R 133 1 O THR R 129 N VAL R 102
SHEET 7 RA19 ARG R 154 THR R 158 1 O ARG R 154 N LEU R 130
SHEET 8 RA19 HIS R 178 ARG R 182 1 O HIS R 178 N PHE R 155
SHEET 9 RA19 SER R 201 GLU R 203 1 O SER R 201 N LEU R 179
SHEET 10 RA19 GLN R 225 ASN R 227 1 O GLN R 225 N ILE R 202
SHEET 11 RA19 GLY R 249 ASP R 251 1 O GLY R 249 N LEU R 226
SHEET 12 RA19 ASP R 273 ASN R 275 1 O ASP R 273 N ILE R 250
SHEET 13 RA19 GLU R 297 LEU R 300 1 O GLU R 297 N ILE R 274
SHEET 14 RA19 ILE R 323 LEU R 326 1 O ILE R 323 N VAL R 298
SHEET 15 RA19 ASN R 346 SER R 348 1 O ASN R 346 N LEU R 324
SHEET 16 RA19 SER R 370 ASP R 372 1 O SER R 370 N ILE R 347
SHEET 17 RA19 ASP R 394 ARG R 396 1 O ASP R 394 N LEU R 371
SHEET 18 RA19 LYS R 418 TRP R 420 1 O LYS R 418 N LEU R 395
SHEET 19 RA19 GLU R 447 GLN R 448 1 N GLN R 448 O ILE R 419
SHEET 1 RB 2 GLY R 97 GLU R 98 0
SHEET 2 RB 2 ILE R 124 VAL R 125 1 N VAL R 125 O GLY R 97
SSBOND 1 CYS L 10 CYS L 68 1555 1555 2.05
SSBOND 2 CYS L 47 CYS L 99 1555 1555 2.04
SSBOND 3 CYS L 54 CYS L 101 1555 1555 2.04
SSBOND 4 CYS L 98 CYS M 98 1555 1555 2.03
SSBOND 5 CYS M 10 CYS M 68 1555 1555 2.03
SSBOND 6 CYS M 47 CYS M 99 1555 1555 2.05
SSBOND 7 CYS M 54 CYS M 101 1555 1555 2.04
SSBOND 8 CYS R 43 CYS R 56 1555 1555 2.04
SSBOND 9 CYS R 79 CYS R 107 1555 1555 2.04
SSBOND 10 CYS R 428 CYS R 453 1555 1555 2.03
SSBOND 11 CYS R 430 CYS R 465 1555 1555 2.04
LINK ND2 ASN R 80 C1 NAG R 501 1555 1555 1.43
LINK ND2 ASN R 140 C1 NAG R 601 1555 1555 1.44
LINK ND2 ASN R 270 C1 NAG R 901 1555 1555 1.43
LINK ND2 ASN R 346 C1 NAG R1101 1555 1555 1.43
LINK ND2 ASN R 391 C1 NAG R1201 1555 1555 1.43
LINK O4 NAG R1101 C1 NAG R1102 1555 1555 1.41
LINK O4 NAG R1102 C1 BMA R1103 1555 1555 1.41
LINK O6 BMA R1103 C1 BMA R1105 1555 1555 1.38
LINK O3 BMA R1103 C1 MAN R1104 1555 1555 1.43
LINK O2 MAN R1104 C1 MAN R1108 1555 1555 1.44
LINK O6 BMA R1105 C1 BMA R1106 1555 1555 1.40
LINK O3 BMA R1105 C1 MAN R1107 1555 1555 1.43
CISPEP 1 ALA M 50 ASP M 51 0 0.58
CISPEP 2 CYS R 56 PRO R 57 0 -1.46
CISPEP 3 ARG R 327 ALA R 328 0 8.81
CISPEP 4 CYS R 430 PRO R 431 0 9.03
SITE 1 AC1 2 ASN R 80 ARG R 106
SITE 1 AC2 4 MET R 139 ASN R 140 LEU R 162 HIS R 164
SITE 1 AC3 5 THR R 245 SER R 246 THR R 269 ASN R 270
SITE 2 AC3 5 HIS R 294
SITE 1 AC4 8 GLN L 52 ARG R 325 ASN R 346 SER R 370
SITE 2 AC4 8 THR R 393 ASP R 394 GLN R 417 HOH R2062
SITE 1 AC5 4 VAL R 366 ASN R 367 THR R 390 ASN R 391
CRYST1 198.310 57.110 70.500 90.00 97.76 90.00 C 1 2 1 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 0.005043 0.000000 0.000687 0.00000
SCALE2 0.000000 0.017510 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014315 0.00000
ATOM 1 N ARG L 7 404.609 0.843 105.104 1.00 62.41 N
ANISOU 1 N ARG L 7 7384 9367 6961 -54 768 -120 N
ATOM 2 CA ARG L 7 403.847 -0.409 105.068 1.00 60.23 C
ANISOU 2 CA ARG L 7 6919 9345 6619 -1 517 -97 C
ATOM 3 C ARG L 7 404.425 -1.448 106.048 1.00 60.18 C
ANISOU 3 C ARG L 7 6721 9475 6668 -233 398 -201 C
ATOM 4 O ARG L 7 405.635 -1.663 106.105 1.00 58.82 O
ANISOU 4 O ARG L 7 6537 9268 6545 -395 438 -251 O
ATOM 5 CB ARG L 7 403.792 -0.983 103.629 1.00 60.19 C
ANISOU 5 CB ARG L 7 6952 9395 6522 141 449 11 C
ATOM 6 CG ARG L 7 403.116 -2.355 103.472 1.00 66.53 C
ANISOU 6 CG ARG L 7 7560 10452 7266 154 226 -1 C
ATOM 7 CD ARG L 7 401.600 -2.274 103.459 1.00 81.06 C
ANISOU 7 CD ARG L 7 9329 12452 9019 357 137 1 C
ATOM 8 NE ARG L 7 400.971 -3.589 103.309 1.00 89.68 N
ANISOU 8 NE ARG L 7 10224 13780 10069 323 -37 -56 N
ATOM 9 CZ ARG L 7 400.727 -4.184 102.142 1.00 98.12 C
ANISOU 9 CZ ARG L 7 11258 14978 11045 424 -117 -35 C
ATOM 10 NH1 ARG L 7 401.082 -3.598 101.003 1.00 81.13 N
ANISOU 10 NH1 ARG L 7 9264 12747 8815 590 -53 68 N
ATOM 11 NH2 ARG L 7 400.147 -5.376 102.107 1.00 78.85 N
ANISOU 11 NH2 ARG L 7 8635 12740 8585 351 -239 -125 N
ATOM 12 N PHE L 8 403.533 -2.087 106.805 1.00 55.28 N
ANISOU 12 N PHE L 8 5956 9019 6027 -227 263 -234 N
ATOM 13 CA PHE L 8 403.848 -3.121 107.783 1.00 53.09 C
ANISOU 13 CA PHE L 8 5526 8876 5770 -385 162 -305 C
ATOM 14 C PHE L 8 403.217 -4.443 107.342 1.00 54.00 C
ANISOU 14 C PHE L 8 5540 9145 5831 -346 21 -269 C
ATOM 15 O PHE L 8 402.265 -4.452 106.551 1.00 54.47 O
ANISOU 15 O PHE L 8 5601 9257 5837 -201 -19 -230 O
ATOM 16 CB PHE L 8 403.377 -2.701 109.192 1.00 55.14 C
ANISOU 16 CB PHE L 8 5730 9166 6056 -434 178 -391 C
ATOM 17 CG PHE L 8 404.095 -1.481 109.727 1.00 57.70 C
ANISOU 17 CG PHE L 8 6133 9349 6440 -519 334 -471 C
ATOM 18 CD1 PHE L 8 405.302 -1.606 110.406 1.00 60.49 C
ANISOU 18 CD1 PHE L 8 6423 9737 6823 -695 358 -577 C
ATOM 19 CD2 PHE L 8 403.575 -0.206 109.534 1.00 61.08 C
ANISOU 19 CD2 PHE L 8 6698 9621 6888 -418 474 -456 C
ATOM 20 CE1 PHE L 8 405.976 -0.476 110.887 1.00 62.43 C
ANISOU 20 CE1 PHE L 8 6717 9874 7129 -808 522 -701 C
ATOM 21 CE2 PHE L 8 404.254 0.923 110.006 1.00 65.08 C
ANISOU 21 CE2 PHE L 8 7293 9971 7463 -527 664 -555 C
ATOM 22 CZ PHE L 8 405.451 0.780 110.679 1.00 62.85 C
ANISOU 22 CZ PHE L 8 6923 9736 7221 -741 687 -694 C
ATOM 23 N LEU L 9 403.763 -5.554 107.849 1.00 47.62 N
ANISOU 23 N LEU L 9 4648 8418 5029 -466 -36 -294 N
ATOM 24 CA LEU L 9 403.367 -6.922 107.513 1.00 45.93 C
ANISOU 24 CA LEU L 9 4360 8312 4780 -474 -118 -278 C
ATOM 25 C LEU L 9 402.058 -7.329 108.159 1.00 50.26 C
ANISOU 25 C LEU L 9 4820 8963 5314 -459 -154 -328 C
ATOM 26 O LEU L 9 401.400 -8.266 107.692 1.00 49.71 O
ANISOU 26 O LEU L 9 4688 8980 5219 -458 -191 -346 O
ATOM 27 CB LEU L 9 404.485 -7.891 107.934 1.00 44.78 C
ANISOU 27 CB LEU L 9 4190 8187 4636 -582 -125 -275 C
ATOM 28 CG LEU L 9 405.756 -7.832 107.084 1.00 47.47 C
ANISOU 28 CG LEU L 9 4585 8463 4987 -606 -101 -240 C
ATOM 29 CD1 LEU L 9 406.918 -8.361 107.840 1.00 47.13 C
ANISOU 29 CD1 LEU L 9 4502 8467 4939 -685 -99 -266 C
ATOM 30 CD2 LEU L 9 405.590 -8.597 105.794 1.00 47.55 C
ANISOU 30 CD2 LEU L 9 4612 8484 4971 -565 -135 -184 C
ATOM 31 N CYS L 10 401.671 -6.609 109.225 1.00 46.91 N
ANISOU 31 N CYS L 10 4385 8530 4909 -461 -125 -372 N
ATOM 32 CA CYS L 10 400.450 -6.859 109.972 1.00 45.34 C
ANISOU 32 CA CYS L 10 4104 8419 4704 -454 -138 -432 C
ATOM 33 C CYS L 10 399.563 -5.645 110.000 1.00 48.02 C
ANISOU 33 C CYS L 10 4453 8749 5044 -337 -120 -452 C
ATOM 34 O CYS L 10 400.009 -4.543 110.324 1.00 48.23 O
ANISOU 34 O CYS L 10 4561 8669 5096 -319 -58 -443 O
ATOM 35 CB CYS L 10 400.787 -7.356 111.373 1.00 44.96 C
ANISOU 35 CB CYS L 10 4035 8387 4659 -558 -113 -462 C
ATOM 36 SG CYS L 10 401.414 -9.051 111.380 1.00 48.21 S
ANISOU 36 SG CYS L 10 4447 8829 5041 -637 -109 -426 S
ATOM 37 N ARG L 11 398.303 -5.861 109.597 1.00 44.65 N
ANISOU 37 N ARG L 11 3937 8443 4584 -251 -162 -495 N
ATOM 38 CA ARG L 11 397.256 -4.848 109.599 1.00 45.37 C
ANISOU 38 CA ARG L 11 4012 8574 4653 -95 -155 -519 C
ATOM 39 C ARG L 11 396.896 -4.544 111.055 1.00 49.98 C
ANISOU 39 C ARG L 11 4569 9142 5279 -166 -111 -578 C
ATOM 40 O ARG L 11 396.581 -5.455 111.848 1.00 48.90 O
ANISOU 40 O ARG L 11 4349 9074 5155 -286 -115 -641 O
ATOM 41 CB ARG L 11 396.038 -5.288 108.770 1.00 45.30 C
ANISOU 41 CB ARG L 11 3868 8765 4578 17 -227 -584 C
ATOM 42 CG ARG L 11 396.239 -5.060 107.265 1.00 63.04 C
ANISOU 42 CG ARG L 11 6166 11039 6748 178 -266 -516 C
ATOM 43 CD ARG L 11 394.941 -5.050 106.456 1.00 81.29 C
ANISOU 43 CD ARG L 11 8336 13595 8954 371 -343 -594 C
ATOM 44 NE ARG L 11 394.073 -3.909 106.777 1.00 94.63 N
ANISOU 44 NE ARG L 11 10030 15321 10604 578 -324 -594 N
ATOM 45 CZ ARG L 11 392.970 -3.585 106.105 1.00113.31 C
ANISOU 45 CZ ARG L 11 12289 17914 12849 827 -387 -644 C
ATOM 46 NH1 ARG L 11 392.584 -4.306 105.059 1.00102.31 N
ANISOU 46 NH1 ARG L 11 10762 16751 11361 884 -481 -720 N
ATOM 47 NH2 ARG L 11 392.243 -2.539 106.476 1.00102.43 N
ANISOU 47 NH2 ARG L 11 10932 16554 11434 1031 -355 -631 N
ATOM 48 N SER L 12 397.021 -3.264 111.412 1.00 46.94 N
ANISOU 48 N SER L 12 4277 8645 4913 -95 -44 -558 N
ATOM 49 CA SER L 12 396.768 -2.797 112.762 1.00 46.93 C
ANISOU 49 CA SER L 12 4266 8618 4948 -155 8 -618 C
ATOM 50 C SER L 12 395.881 -1.552 112.796 1.00 50.83 C
ANISOU 50 C SER L 12 4796 9084 5434 18 63 -625 C
ATOM 51 O SER L 12 395.741 -0.854 111.792 1.00 50.56 O
ANISOU 51 O SER L 12 4841 9007 5361 199 85 -558 O
ATOM 52 CB SER L 12 398.093 -2.502 113.455 1.00 48.96 C
ANISOU 52 CB SER L 12 4604 8755 5242 -295 68 -620 C
ATOM 53 OG SER L 12 398.606 -1.251 113.027 1.00 57.79 O
ANISOU 53 OG SER L 12 5855 9716 6385 -237 166 -592 O
ATOM 54 N ILE L 13 395.326 -1.259 113.976 1.00 48.37 N
ANISOU 54 N ILE L 13 4443 8788 5148 -23 98 -696 N
ATOM 55 CA ILE L 13 394.490 -0.088 114.203 1.00 50.03 C
ANISOU 55 CA ILE L 13 4689 8963 5356 135 167 -710 C
ATOM 56 C ILE L 13 394.909 0.631 115.517 1.00 53.31 C
ANISOU 56 C ILE L 13 5169 9257 5828 14 270 -767 C
ATOM 57 O ILE L 13 395.213 -0.011 116.531 1.00 51.98 O
ANISOU 57 O ILE L 13 4938 9138 5674 -160 248 -827 O
ATOM 58 CB ILE L 13 392.974 -0.448 114.156 1.00 54.21 C
ANISOU 58 CB ILE L 13 5053 9701 5843 251 96 -776 C
ATOM 59 CG1 ILE L 13 392.111 0.807 113.876 1.00 56.83 C
ANISOU 59 CG1 ILE L 13 5433 10024 6135 518 152 -755 C
ATOM 60 CG2 ILE L 13 392.504 -1.258 115.382 1.00 54.35 C
ANISOU 60 CG2 ILE L 13 4945 9812 5893 74 85 -881 C
ATOM 61 CD1 ILE L 13 390.686 0.556 113.383 1.00 68.63 C
ANISOU 61 CD1 ILE L 13 6747 11779 7550 712 63 -818 C
ATOM 62 N ARG L 14 394.971 1.969 115.460 1.00 50.21 N
ANISOU 62 N ARG L 14 4918 8701 5457 116 401 -748 N
ATOM 63 CA ARG L 14 395.292 2.774 116.628 1.00 50.07 C
ANISOU 63 CA ARG L 14 4961 8571 5494 4 522 -830 C
ATOM 64 C ARG L 14 394.011 3.046 117.382 1.00 53.03 C
ANISOU 64 C ARG L 14 5263 9025 5862 92 527 -883 C
ATOM 65 O ARG L 14 393.043 3.545 116.804 1.00 53.75 O
ANISOU 65 O ARG L 14 5368 9136 5920 322 541 -838 O
ATOM 66 CB ARG L 14 396.012 4.078 116.260 1.00 52.92 C
ANISOU 66 CB ARG L 14 5527 8685 5897 33 713 -812 C
ATOM 67 CG ARG L 14 397.504 3.905 116.049 1.00 65.48 C
ANISOU 67 CG ARG L 14 7163 10197 7519 -155 747 -835 C
ATOM 68 CD ARG L 14 398.286 4.950 116.813 1.00 82.71 C
ANISOU 68 CD ARG L 14 9444 12211 9770 -310 943 -960 C
ATOM 69 NE ARG L 14 399.725 4.706 116.744 1.00 95.69 N
ANISOU 69 NE ARG L 14 11075 13843 11440 -514 962 -1032 N
ATOM 70 CZ ARG L 14 400.453 4.194 117.731 1.00115.91 C
ANISOU 70 CZ ARG L 14 13500 16550 13991 -711 895 -1163 C
ATOM 71 NH1 ARG L 14 399.886 3.878 118.890 1.00102.85 N
ANISOU 71 NH1 ARG L 14 11736 15041 12303 -738 817 -1225 N
ATOM 72 NH2 ARG L 14 401.756 4.004 117.572 1.00109.42 N
ANISOU 72 NH2 ARG L 14 12649 15746 13178 -867 911 -1238 N
ATOM 73 N LYS L 15 393.984 2.645 118.656 1.00 47.46 N
ANISOU 73 N LYS L 15 4470 8392 5170 -71 508 -977 N
ATOM 74 CA LYS L 15 392.853 2.828 119.554 1.00 46.69 C
ANISOU 74 CA LYS L 15 4297 8370 5073 -32 523 -1046 C
ATOM 75 C LYS L 15 393.340 3.168 120.966 1.00 49.97 C
ANISOU 75 C LYS L 15 4732 8742 5512 -207 597 -1150 C
ATOM 76 O LYS L 15 394.515 2.993 121.305 1.00 49.61 O
ANISOU 76 O LYS L 15 4711 8673 5465 -366 602 -1183 O
ATOM 77 CB LYS L 15 391.910 1.598 119.559 1.00 48.30 C
ANISOU 77 CB LYS L 15 4324 8785 5241 -29 400 -1066 C
ATOM 78 CG LYS L 15 392.532 0.283 120.039 1.00 57.45 C
ANISOU 78 CG LYS L 15 5423 10021 6383 -224 334 -1079 C
ATOM 79 CD LYS L 15 391.478 -0.787 120.341 1.00 64.66 C
ANISOU 79 CD LYS L 15 6192 11096 7279 -256 293 -1135 C
ATOM 80 CE LYS L 15 391.069 -0.818 121.799 1.00 70.08 C
ANISOU 80 CE LYS L 15 6856 11806 7965 -348 356 -1214 C
ATOM 81 NZ LYS L 15 390.693 -2.184 122.256 1.00 71.12 N
ANISOU 81 NZ LYS L 15 6912 12036 8073 -461 359 -1248 N
ATOM 82 N LEU L 16 392.423 3.699 121.767 1.00 46.90 N
ANISOU 82 N LEU L 16 4320 8365 5134 -161 656 -1213 N
ATOM 83 CA LEU L 16 392.638 4.093 123.148 1.00 47.23 C
ANISOU 83 CA LEU L 16 4370 8391 5186 -299 731 -1326 C
ATOM 84 C LEU L 16 392.171 2.991 124.086 1.00 50.41 C
ANISOU 84 C LEU L 16 4643 8970 5540 -385 647 -1366 C
ATOM 85 O LEU L 16 391.078 2.458 123.902 1.00 50.02 O
ANISOU 85 O LEU L 16 4502 9020 5484 -305 599 -1350 O
ATOM 86 CB LEU L 16 391.877 5.403 123.469 1.00 48.92 C
ANISOU 86 CB LEU L 16 4660 8487 5440 -185 876 -1370 C
ATOM 87 CG LEU L 16 392.368 6.698 122.827 1.00 54.96 C
ANISOU 87 CG LEU L 16 5612 9016 6255 -108 1044 -1346 C
ATOM 88 CD1 LEU L 16 391.399 7.828 123.116 1.00 56.32 C
ANISOU 88 CD1 LEU L 16 5863 9083 6453 59 1190 -1362 C
ATOM 89 CD2 LEU L 16 393.749 7.080 123.329 1.00 57.03 C
ANISOU 89 CD2 LEU L 16 5943 9178 6548 -336 1142 -1454 C
ATOM 90 N VAL L 17 392.998 2.644 125.085 1.00 46.72 N
ANISOU 90 N VAL L 17 4170 8554 5029 -542 643 -1430 N
ATOM 91 CA VAL L 17 392.655 1.636 126.101 1.00 45.67 C
ANISOU 91 CA VAL L 17 3962 8563 4828 -608 604 -1455 C
ATOM 92 C VAL L 17 392.635 2.334 127.466 1.00 50.32 C
ANISOU 92 C VAL L 17 4565 9161 5392 -672 686 -1574 C
ATOM 93 O VAL L 17 393.359 3.321 127.668 1.00 50.41 O
ANISOU 93 O VAL L 17 4633 9099 5423 -724 754 -1654 O
ATOM 94 CB VAL L 17 393.534 0.348 126.086 1.00 47.71 C
ANISOU 94 CB VAL L 17 4206 8914 5009 -678 520 -1397 C
ATOM 95 CG1 VAL L 17 393.315 -0.450 124.804 1.00 46.27 C
ANISOU 95 CG1 VAL L 17 3998 8729 4854 -624 453 -1297 C
ATOM 96 CG2 VAL L 17 395.017 0.656 126.278 1.00 47.20 C
ANISOU 96 CG2 VAL L 17 4176 8855 4902 -756 510 -1438 C
ATOM 97 N TYR L 18 391.781 1.857 128.376 1.00 46.52 N
ANISOU 97 N TYR L 18 4037 8767 4872 -677 703 -1603 N
ATOM 98 CA TYR L 18 391.611 2.509 129.667 1.00 47.14 C
ANISOU 98 CA TYR L 18 4127 8863 4921 -724 783 -1718 C
ATOM 99 C TYR L 18 391.877 1.580 130.860 1.00 50.71 C
ANISOU 99 C TYR L 18 4567 9461 5241 -788 768 -1737 C
ATOM 100 O TYR L 18 391.007 0.791 131.235 1.00 49.86 O
ANISOU 100 O TYR L 18 4436 9400 5108 -771 789 -1706 O
ATOM 101 CB TYR L 18 390.191 3.115 129.769 1.00 49.03 C
ANISOU 101 CB TYR L 18 4340 9057 5233 -639 857 -1750 C
ATOM 102 CG TYR L 18 389.832 4.031 128.613 1.00 50.38 C
ANISOU 102 CG TYR L 18 4541 9102 5499 -510 884 -1710 C
ATOM 103 CD1 TYR L 18 389.273 3.524 127.442 1.00 51.46 C
ANISOU 103 CD1 TYR L 18 4623 9268 5660 -398 812 -1621 C
ATOM 104 CD2 TYR L 18 390.045 5.407 128.693 1.00 51.71 C
ANISOU 104 CD2 TYR L 18 4805 9124 5720 -486 1000 -1769 C
ATOM 105 CE1 TYR L 18 388.941 4.360 126.378 1.00 51.40 C
ANISOU 105 CE1 TYR L 18 4655 9171 5704 -229 836 -1572 C
ATOM 106 CE2 TYR L 18 389.708 6.254 127.641 1.00 52.70 C
ANISOU 106 CE2 TYR L 18 4999 9114 5910 -325 1057 -1708 C
ATOM 107 CZ TYR L 18 389.155 5.727 126.486 1.00 57.75 C
ANISOU 107 CZ TYR L 18 5584 9809 6550 -177 965 -1600 C
ATOM 108 OH TYR L 18 388.818 6.564 125.448 1.00 57.23 O
ANISOU 108 OH TYR L 18 5597 9634 6513 30 1021 -1528 O
ATOM 109 N PRO L 19 393.069 1.690 131.497 1.00 48.14 N
ANISOU 109 N PRO L 19 4255 9218 4817 -852 748 -1802 N
ATOM 110 CA PRO L 19 393.327 0.896 132.710 1.00 48.20 C
ANISOU 110 CA PRO L 19 4266 9389 4659 -858 740 -1816 C
ATOM 111 C PRO L 19 392.490 1.452 133.860 1.00 52.35 C
ANISOU 111 C PRO L 19 4793 9931 5168 -870 833 -1915 C
ATOM 112 O PRO L 19 392.437 2.673 134.036 1.00 52.56 O
ANISOU 112 O PRO L 19 4813 9894 5263 -911 892 -2035 O
ATOM 113 CB PRO L 19 394.842 1.074 132.950 1.00 50.13 C
ANISOU 113 CB PRO L 19 4489 9759 4798 -900 683 -1896 C
ATOM 114 CG PRO L 19 395.354 1.853 131.794 1.00 53.69 C
ANISOU 114 CG PRO L 19 4936 10081 5383 -945 677 -1915 C
ATOM 115 CD PRO L 19 394.209 2.577 131.195 1.00 49.51 C
ANISOU 115 CD PRO L 19 4438 9360 5013 -915 751 -1890 C
ATOM 116 N LYS L 20 391.785 0.566 134.593 1.00 48.53 N
ANISOU 116 N LYS L 20 4331 9505 4603 -837 874 -1865 N
ATOM 117 CA LYS L 20 390.887 0.930 135.694 1.00 50.31 C
ANISOU 117 CA LYS L 20 4562 9748 4807 -845 972 -1947 C
ATOM 118 C LYS L 20 391.392 0.358 137.011 1.00 83.07 C
ANISOU 118 C LYS L 20 8758 14065 8739 -821 987 -1963 C
ATOM 119 O LYS L 20 391.596 -0.852 137.109 1.00 50.93 O
ANISOU 119 O LYS L 20 4747 10049 4556 -762 984 -1845 O
ATOM 120 CB LYS L 20 389.459 0.424 135.412 1.00 51.88 C
ANISOU 120 CB LYS L 20 4744 9867 5102 -826 1043 -1893 C
ATOM 121 CG LYS L 20 388.803 1.010 134.162 1.00 64.02 C
ANISOU 121 CG LYS L 20 6215 11289 6820 -801 1024 -1889 C
ATOM 122 CD LYS L 20 388.001 2.280 134.438 1.00 74.24 C
ANISOU 122 CD LYS L 20 7482 12524 8202 -780 1097 -1995 C
ATOM 123 CE LYS L 20 386.590 2.009 134.896 1.00 82.21 C
ANISOU 123 CE LYS L 20 8437 13555 9244 -766 1186 -2032 C
ATOM 124 NZ LYS L 20 385.843 3.271 135.117 1.00 95.48 N
ANISOU 124 NZ LYS L 20 10091 15180 11007 -718 1255 -2127 N
ATOM 125 N GLN L 40 393.765 6.763 133.563 1.00 78.98 N
ANISOU 125 N GLN L 40 8243 12887 8878 -1132 1186 -2448 N
ATOM 126 CA GLN L 40 393.900 7.646 132.402 1.00 78.79 C
ANISOU 126 CA GLN L 40 8310 12626 9002 -1120 1288 -2424 C
ATOM 127 C GLN L 40 394.210 6.835 131.111 1.00 79.80 C
ANISOU 127 C GLN L 40 8438 12735 9147 -1046 1169 -2244 C
ATOM 128 O GLN L 40 394.861 5.792 131.177 1.00 79.54 O
ANISOU 128 O GLN L 40 8334 12874 9015 -1071 1032 -2205 O
ATOM 129 CB GLN L 40 394.978 8.717 132.658 1.00 81.83 C
ANISOU 129 CB GLN L 40 8721 12954 9415 -1294 1435 -2648 C
ATOM 130 CG GLN L 40 394.611 9.717 133.764 1.00 94.74 C
ANISOU 130 CG GLN L 40 10377 14559 11062 -1375 1595 -2844 C
ATOM 131 CD GLN L 40 395.636 10.820 133.964 1.00112.86 C
ANISOU 131 CD GLN L 40 12696 16783 13403 -1580 1782 -3106 C
ATOM 132 OE1 GLN L 40 395.365 12.002 133.723 1.00107.24 O
ANISOU 132 OE1 GLN L 40 12121 15801 12823 -1605 2016 -3172 O
ATOM 133 NE2 GLN L 40 396.820 10.474 134.456 1.00105.48 N
ANISOU 133 NE2 GLN L 40 11627 16099 12352 -1728 1703 -3282 N
ATOM 134 N ALA L 41 393.750 7.351 129.949 1.00 73.40 N
ANISOU 134 N ALA L 41 7718 11720 8450 -935 1233 -2136 N
ATOM 135 CA ALA L 41 393.820 6.793 128.589 1.00 70.40 C
ANISOU 135 CA ALA L 41 7355 11294 8098 -834 1145 -1965 C
ATOM 136 C ALA L 41 395.238 6.586 128.045 1.00 71.32 C
ANISOU 136 C ALA L 41 7474 11421 8202 -944 1115 -1987 C
ATOM 137 O ALA L 41 396.133 7.365 128.358 1.00 72.95 O
ANISOU 137 O ALA L 41 7710 11579 8430 -1086 1233 -2149 O
ATOM 138 CB ALA L 41 393.074 7.712 127.651 1.00 71.78 C
ANISOU 138 CB ALA L 41 7648 11255 8371 -670 1263 -1883 C
ATOM 139 N ILE L 42 395.420 5.552 127.174 1.00 62.99 N
ANISOU 139 N ILE L 42 6384 10429 7121 -884 972 -1840 N
ATOM 140 CA ILE L 42 396.696 5.202 126.523 1.00 60.05 C
ANISOU 140 CA ILE L 42 6004 10078 6734 -962 925 -1834 C
ATOM 141 C ILE L 42 396.460 4.829 125.036 1.00 61.26 C
ANISOU 141 C ILE L 42 6208 10137 6932 -832 872 -1652 C
ATOM 142 O ILE L 42 395.740 3.860 124.772 1.00 60.84 O
ANISOU 142 O ILE L 42 6098 10173 6845 -736 752 -1534 O
ATOM 143 CB ILE L 42 397.466 4.057 127.258 1.00 61.35 C
ANISOU 143 CB ILE L 42 6050 10494 6766 -1034 781 -1866 C
ATOM 144 CG1 ILE L 42 397.617 4.321 128.776 1.00 62.52 C
ANISOU 144 CG1 ILE L 42 6136 10792 6827 -1123 811 -2042 C
ATOM 145 CG2 ILE L 42 398.830 3.830 126.604 1.00 60.65 C
ANISOU 145 CG2 ILE L 42 5940 10439 6664 -1109 745 -1886 C
ATOM 146 CD1 ILE L 42 398.095 3.138 129.612 1.00 66.70 C
ANISOU 146 CD1 ILE L 42 6572 11586 7185 -1115 677 -2039 C
ATOM 147 N GLN L 43 397.080 5.568 124.076 1.00 55.21 N
ANISOU 147 N GLN L 43 5548 9194 6236 -836 977 -1642 N
ATOM 148 CA GLN L 43 396.935 5.254 122.648 1.00 53.84 C
ANISOU 148 CA GLN L 43 5429 8944 6083 -701 931 -1474 C
ATOM 149 C GLN L 43 397.856 4.077 122.298 1.00 54.36 C
ANISOU 149 C GLN L 43 5411 9149 6095 -774 783 -1433 C
ATOM 150 O GLN L 43 399.074 4.125 122.491 1.00 53.84 O
ANISOU 150 O GLN L 43 5322 9115 6019 -919 804 -1534 O
ATOM 151 CB GLN L 43 397.168 6.466 121.729 1.00 56.80 C
ANISOU 151 CB GLN L 43 5986 9058 6537 -643 1127 -1454 C
ATOM 152 CG GLN L 43 396.667 6.216 120.299 1.00 72.04 C
ANISOU 152 CG GLN L 43 7982 10932 8458 -431 1077 -1263 C
ATOM 153 CD GLN L 43 396.780 7.419 119.397 1.00 93.49 C
ANISOU 153 CD GLN L 43 10919 13378 11226 -318 1298 -1212 C
ATOM 154 OE1 GLN L 43 397.877 7.904 119.096 1.00 88.85 O
ANISOU 154 OE1 GLN L 43 10433 12639 10688 -451 1446 -1274 O
ATOM 155 NE2 GLN L 43 395.644 7.893 118.900 1.00 86.43 N
ANISOU 155 NE2 GLN L 43 10106 12422 10310 -52 1337 -1098 N
ATOM 156 N ILE L 44 397.235 3.029 121.772 1.00 47.85 N
ANISOU 156 N ILE L 44 4531 8416 5234 -670 643 -1301 N
ATOM 157 CA ILE L 44 397.798 1.720 121.514 1.00 44.88 C
ANISOU 157 CA ILE L 44 4080 8173 4799 -708 506 -1241 C
ATOM 158 C ILE L 44 397.646 1.288 120.053 1.00 45.43 C
ANISOU 158 C ILE L 44 4179 8197 4886 -604 451 -1105 C
ATOM 159 O ILE L 44 396.940 1.933 119.281 1.00 45.03 O
ANISOU 159 O ILE L 44 4192 8046 4870 -469 499 -1049 O
ATOM 160 CB ILE L 44 396.974 0.813 122.502 1.00 47.64 C
ANISOU 160 CB ILE L 44 4340 8676 5085 -702 434 -1242 C
ATOM 161 CG1 ILE L 44 397.828 0.146 123.529 1.00 47.90 C
ANISOU 161 CG1 ILE L 44 4320 8855 5024 -798 391 -1301 C
ATOM 162 CG2 ILE L 44 395.847 -0.089 121.908 1.00 46.67 C
ANISOU 162 CG2 ILE L 44 4170 8601 4960 -604 364 -1145 C
ATOM 163 CD1 ILE L 44 398.360 1.069 124.504 1.00 59.90 C
ANISOU 163 CD1 ILE L 44 5835 10394 6530 -887 465 -1455 C
ATOM 164 N GLU L 45 398.303 0.176 119.698 1.00 40.00 N
ANISOU 164 N GLU L 45 3446 7597 4157 -646 352 -1053 N
ATOM 165 CA GLU L 45 398.205 -0.451 118.391 1.00 38.94 C
ANISOU 165 CA GLU L 45 3320 7452 4024 -568 288 -940 C
ATOM 166 C GLU L 45 397.695 -1.878 118.576 1.00 42.04 C
ANISOU 166 C GLU L 45 3625 7982 4368 -573 192 -901 C
ATOM 167 O GLU L 45 398.306 -2.678 119.286 1.00 39.04 O
ANISOU 167 O GLU L 45 3216 7683 3934 -652 164 -913 O
ATOM 168 CB GLU L 45 399.543 -0.412 117.659 1.00 40.07 C
ANISOU 168 CB GLU L 45 3512 7534 4177 -627 299 -922 C
ATOM 169 CG GLU L 45 399.468 -1.011 116.274 1.00 49.93 C
ANISOU 169 CG GLU L 45 4779 8771 5422 -544 237 -807 C
ATOM 170 CD GLU L 45 400.807 -1.348 115.649 1.00 69.49 C
ANISOU 170 CD GLU L 45 7280 11225 7898 -616 227 -786 C
ATOM 171 OE1 GLU L 45 401.647 -0.428 115.519 1.00 62.10 O
ANISOU 171 OE1 GLU L 45 6414 10178 7003 -673 332 -840 O
ATOM 172 OE2 GLU L 45 400.998 -2.522 115.251 1.00 52.38 O
ANISOU 172 OE2 GLU L 45 5066 9141 5694 -621 136 -727 O
ATOM 173 N GLU L 46 396.537 -2.168 117.981 1.00 42.17 N
ANISOU 173 N GLU L 46 3598 8032 4391 -481 164 -871 N
ATOM 174 CA GLU L 46 395.889 -3.466 118.063 1.00 42.89 C
ANISOU 174 CA GLU L 46 3608 8233 4455 -509 121 -868 C
ATOM 175 C GLU L 46 395.845 -4.136 116.697 1.00 49.73 C
ANISOU 175 C GLU L 46 4452 9125 5319 -467 64 -814 C
ATOM 176 O GLU L 46 395.690 -3.454 115.684 1.00 49.50 O
ANISOU 176 O GLU L 46 4444 9064 5299 -355 47 -783 O
ATOM 177 CB GLU L 46 394.475 -3.302 118.626 1.00 45.27 C
ANISOU 177 CB GLU L 46 3834 8599 4768 -470 150 -939 C
ATOM 178 CG GLU L 46 393.844 -4.603 119.095 1.00 61.54 C
ANISOU 178 CG GLU L 46 5826 10749 6808 -553 168 -976 C
ATOM 179 CD GLU L 46 392.889 -4.480 120.263 1.00 85.16 C
ANISOU 179 CD GLU L 46 8772 13783 9801 -577 235 -1059 C
ATOM 180 OE1 GLU L 46 391.693 -4.201 120.018 1.00 77.10 O