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AplysaACHBP_DMXBA0.pdb
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AplysaACHBP_DMXBA0.pdb
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HEADER RECEPTOR 07-JUL-09 2WN9
TITLE CRYSTAL STRUCTURE OF APLYSIA ACHBP IN COMPLEX WITH 4-0H-
TITLE 2 DMXBA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE ACETYLCHOLINE RECEPTOR;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: RESIDUES 18-236;
COMPND 5 SYNONYM: ACETYLCHOLINE BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: APLYSIA CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: CALIFORNIA SEA HARE;
SOURCE 4 ORGANISM_TAXID: 6500;
SOURCE 5 CELL: SENSORY CELL;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK-293
KEYWDS RECEPTOR, 4-0H-DMXBA, ACETYLCHOLINE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SULZENBACHER,R.HIBBS,J.SHI,T.TALLEY,S.CONROD,W.KEM,
AUTHOR 2 P.TAYLOR,P.MARCHOT,Y.BOURNE
REVDAT 2 03-NOV-09 2WN9 1 JRNL
REVDAT 1 01-SEP-09 2WN9 0
JRNL AUTH R.HIBBS,G.SULZENBACHER,J.SHI,T.TALLEY,S.CONROD,
JRNL AUTH 2 W.KEM,W.KEM,P.TAYLOR,P.MARCHOT,Y.BOURNE
JRNL TITL STRUCTURAL DETERMINANTS FOR INTERACTION OF PARTIAL
JRNL TITL 2 AGONISTS WITH ACETYLCHOLINE BINDING PROTEIN AND
JRNL TITL 3 NEURONAL ALPHA7 NICOTINIC ACETYLCHOLINE RECEPTOR.
JRNL REF EMBO J. V. 28 3040 2009
JRNL REFN ISSN 0261-4189
JRNL PMID 19696737
JRNL DOI 10.1038/EMBOJ.2009.227
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.91
REMARK 3 NUMBER OF REFLECTIONS : 125779
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) : 0.17131
REMARK 3 R VALUE (WORKING SET) : 0.16965
REMARK 3 FREE R VALUE : 0.20308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 6584
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.750
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.795
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9127
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.190
REMARK 3 BIN FREE R VALUE SET COUNT : 488
REMARK 3 BIN FREE R VALUE : 0.249
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8618
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 185
REMARK 3 SOLVENT ATOMS : 780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.431
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08
REMARK 3 B22 (A**2) : -0.73
REMARK 3 B33 (A**2) : -0.35
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.847
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9064 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7902 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12403 ; 1.489 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18487 ; 0.808 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1116 ; 6.110 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 435 ;35.140 ;24.345
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1483 ;14.029 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;20.581 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1381 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10051 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1846 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1511 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7815 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4443 ; 0.182 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5435 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 655 ; 0.147 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.091 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 40 ; 0.240 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.232 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5520 ; 2.036 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2134 ; 0.619 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8833 ; 2.828 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4070 ; 3.091 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3534 ; 4.548 ; 6.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6801 11.6187 59.3299
REMARK 3 T TENSOR
REMARK 3 T11: -.1155 T22: -.0491
REMARK 3 T33: -.0490 T12: -.0115
REMARK 3 T13: .0253 T23: .0113
REMARK 3 L TENSOR
REMARK 3 L11: .6051 L22: .6470
REMARK 3 L33: 1.5956 L12: -.1880
REMARK 3 L13: -.0741 L23: -.3421
REMARK 3 S TENSOR
REMARK 3 S11: .0423 S12: .0788 S13: .0525
REMARK 3 S21: -.0594 S22: -.0559 S23: -.1668
REMARK 3 S31: .0841 S32: .1663 S33: .0136
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -3 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): .1967 22.9481 60.3774
REMARK 3 T TENSOR
REMARK 3 T11: -.0828 T22: -.1165
REMARK 3 T33: -.0296 T12: .0142
REMARK 3 T13: -.0169 T23: -.0212
REMARK 3 L TENSOR
REMARK 3 L11: 1.3323 L22: 1.0862
REMARK 3 L33: 1.0710 L12: .2996
REMARK 3 L13: .3597 L23: -.1684
REMARK 3 S TENSOR
REMARK 3 S11: -.0472 S12: .1089 S13: .1367
REMARK 3 S21: -.1109 S22: .0080 S23: .1706
REMARK 3 S31: -.1133 S32: .0275 S33: .0392
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -5 C 208
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5499 3.3504 65.6533
REMARK 3 T TENSOR
REMARK 3 T11: -.1229 T22: -.0600
REMARK 3 T33: -.0428 T12: -.0179
REMARK 3 T13: -.0022 T23: .0102
REMARK 3 L TENSOR
REMARK 3 L11: .7432 L22: 1.5185
REMARK 3 L33: .4946 L12: .0957
REMARK 3 L13: .0337 L23: -.0520
REMARK 3 S TENSOR
REMARK 3 S11: .0173 S12: -.0046 S13: -.0303
REMARK 3 S21: -.1076 S22: .0768 S23: .2047
REMARK 3 S31: .0497 S32: -.1336 S33: -.0941
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -2 D 208
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1257 -19.6896 67.5374
REMARK 3 T TENSOR
REMARK 3 T11: -.0348 T22: -.1144
REMARK 3 T33: -.0674 T12: -.0339
REMARK 3 T13: -.0188 T23: .0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.2058 L22: 1.1690
REMARK 3 L33: .9789 L12: .2202
REMARK 3 L13: .2879 L23: .3229
REMARK 3 S TENSOR
REMARK 3 S11: .0262 S12: .0631 S13: -.1409
REMARK 3 S21: -.0935 S22: .0561 S23: .0074
REMARK 3 S31: .1186 S32: -.0223 S33: -.0824
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E -8 E 207
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8722 -13.9411 62.2797
REMARK 3 T TENSOR
REMARK 3 T11: -.0464 T22: -.0719
REMARK 3 T33: -.0602 T12: .0514
REMARK 3 T13: .0154 T23: -.0159
REMARK 3 L TENSOR
REMARK 3 L11: .7759 L22: .8026
REMARK 3 L33: .5312 L12: .3086
REMARK 3 L13: -.3719 L23: -.3865
REMARK 3 S TENSOR
REMARK 3 S11: -.0548 S12: .0670 S13: -.1070
REMARK 3 S21: -.1416 S22: .0143 S23: -.1371
REMARK 3 S31: .1686 S32: -.0075 S33: .0406
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. GLOBAL B-FACTORS, CONTAINING RESIDUAL
REMARK 3 AND TLS COMPONENT HAVE BEEN DEPOSITED
REMARK 4
REMARK 4 2WN9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-09.
REMARK 100 THE PDBE ID CODE IS EBI-40342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 132537
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 56.80
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.5
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.70
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) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.4
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2BYN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG400, 0.1 M HEPES, PH 7.5,
REMARK 280 0.2 M MGCL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 43.45450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.30350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.69700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.30350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.45450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.69700
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 GENERATING THE BIOMOLECULE
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.13 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, B, D, C
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 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 LYS A -1
REMARK 465 ALA A 209
REMARK 465 GLY A 210
REMARK 465 ASN A 211
REMARK 465 GLY A 212
REMARK 465 PHE A 213
REMARK 465 PHE A 214
REMARK 465 ARG A 215
REMARK 465 ASN A 216
REMARK 465 LEU A 217
REMARK 465 PHE A 218
REMARK 465 ASP A 219
REMARK 465 ASP B -8
REMARK 465 TYR B -7
REMARK 465 LYS B -6
REMARK 465 ASP B -5
REMARK 465 ASP B -4
REMARK 465 ARG B 208
REMARK 465 ALA B 209
REMARK 465 GLY B 210
REMARK 465 ASN B 211
REMARK 465 GLY B 212
REMARK 465 PHE B 213
REMARK 465 PHE B 214
REMARK 465 ARG B 215
REMARK 465 ASN B 216
REMARK 465 LEU B 217
REMARK 465 PHE B 218
REMARK 465 ASP B 219
REMARK 465 ASP C -8
REMARK 465 TYR C -7
REMARK 465 LYS C -6
REMARK 465 ALA C 209
REMARK 465 GLY C 210
REMARK 465 ASN C 211
REMARK 465 GLY C 212
REMARK 465 PHE C 213
REMARK 465 PHE C 214
REMARK 465 ARG C 215
REMARK 465 ASN C 216
REMARK 465 LEU C 217
REMARK 465 PHE C 218
REMARK 465 ASP C 219
REMARK 465 ASP D -8
REMARK 465 TYR D -7
REMARK 465 LYS D -6
REMARK 465 ASP D -5
REMARK 465 ASP D -4
REMARK 465 ASP D -3
REMARK 465 PRO D 18
REMARK 465 MET D 19
REMARK 465 TYR D 188
REMARK 465 SER D 189
REMARK 465 CYS D 190
REMARK 465 CYS D 191
REMARK 465 ALA D 209
REMARK 465 GLY D 210
REMARK 465 ASN D 211
REMARK 465 GLY D 212
REMARK 465 PHE D 213
REMARK 465 PHE D 214
REMARK 465 ARG D 215
REMARK 465 ASN D 216
REMARK 465 LEU D 217
REMARK 465 PHE D 218
REMARK 465 ASP D 219
REMARK 465 PRO E 18
REMARK 465 MET E 19
REMARK 465 ARG E 208
REMARK 465 ALA E 209
REMARK 465 GLY E 210
REMARK 465 ASN E 211
REMARK 465 GLY E 212
REMARK 465 PHE E 213
REMARK 465 PHE E 214
REMARK 465 ARG E 215
REMARK 465 ASN E 216
REMARK 465 LEU E 217
REMARK 465 PHE E 218
REMARK 465 ASP E 219
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 OE1 GLN D 121 - O HOH D 2092 2.03
REMARK 500 O HOH A 2104 - O HOH A 2106 2.09
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 CYS E 191 CB CYS E 191 SG 0.113
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 18 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 CYS B 140 CA - CB - SG ANGL. DEV. = -8.9 DEGREES
REMARK 500 CYS C 140 CA - CB - SG ANGL. DEV. = -7.1 DEGREES
REMARK 500 CYS E 140 CA - CB - SG ANGL. DEV. = -8.2 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 18 165.91 -49.38
REMARK 500 ASP A 89 50.25 -90.41
REMARK 500 ASP A 133 30.66 -95.64
REMARK 500 ASP B 89 46.96 -84.74
REMARK 500 ARG D 16 43.77 -85.79
REMARK 500 ASP D 89 49.10 -88.90
REMARK 500 ASP D 133 31.37 -96.13
REMARK 500 ASP E 133 40.94 -95.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZY5 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZY5 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZY5 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZY5 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZY5 E 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2W8F RELATED DB: PDB
REMARK 900 APLYSIA CALIFORNICA ACHBP BOUND TO IN SILICO
REMARK 900 COMPOUND 31
REMARK 900 RELATED ID: 2BR8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINE-BINDING
REMARK 900 PROTEIN (ACHBP) FROM APLYSIA CALIFORNICA IN
REMARK 900 COMPLEX WITH AN ALPHA-CONOTOXIN PNIA VARIANT
REMARK 900 RELATED ID: 2BR7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINE-BINDING
REMARK 900 PROTEIN (ACHBP) FROM APLYSIA CALIFORNICA IN
REMARK 900 COMPLEX WITH HEPES
REMARK 900 RELATED ID: 2BYR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA
REMARK 900 CALIFORNICA IN COMPLEX WITH METHYLLYCACONITINE
REMARK 900 RELATED ID: 2BYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APLYSIA CALIFORNICA ACHBP
REMARK 900 IN COMPLEX WITH ALPHA-CONOTOXIN IMI
REMARK 900 RELATED ID: 2C9T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINE BINDING
REMARK 900 PROTEIN (ACHBP) FROM APLYSIA CALIFORNICA IN
REMARK 900 COMPLEX WITH ALPHA-CONOTOXIN IMI
REMARK 900 RELATED ID: 2BYN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO ACHBP FROM APLYSIA
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 2BYS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA
REMARK 900 CALIFORNICA IN COMPLEX WITH LOBELINE
REMARK 900 RELATED ID: 2BYQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APLYSIA CALIFORNICA ACHBP
REMARK 900 IN COMPLEX WITH EPIBATIDINE
REMARK 900 RELATED ID: 2W8E RELATED DB: PDB
REMARK 900 APLYSIA CALIFORNICA ACHBP IN APO STATE
REMARK 900 RELATED ID: 2W8G RELATED DB: PDB
REMARK 900 APLYSIA CALIFORNICA ACHBP BOUND TO IN SILICO
REMARK 900 COMPOUND 35
REMARK 900 RELATED ID: 2UZ6 RELATED DB: PDB
REMARK 900 ACHBP-TARGETED A-CONOTOXIN CORRELATES DISTINCT
REMARK 900 BINDING ORIENTATIONS WITH NACHR SUBTYPE
REMARK 900 SELECTIVITY.
DBREF 2WN9 A -8 0 PDB 2WN9 2WN9 -8 0
DBREF 2WN9 A 1 219 UNP Q8WSF8 Q8WSF8_APLCA 18 236
DBREF 2WN9 B -8 0 PDB 2WN9 2WN9 -8 0
DBREF 2WN9 B 1 219 UNP Q8WSF8 Q8WSF8_APLCA 18 236
DBREF 2WN9 C -8 0 PDB 2WN9 2WN9 -8 0
DBREF 2WN9 C 1 219 UNP Q8WSF8 Q8WSF8_APLCA 18 236
DBREF 2WN9 D -8 0 PDB 2WN9 2WN9 -8 0
DBREF 2WN9 D 1 219 UNP Q8WSF8 Q8WSF8_APLCA 18 236
DBREF 2WN9 E -8 0 PDB 2WN9 2WN9 -8 0
DBREF 2WN9 E 1 219 UNP Q8WSF8 Q8WSF8_APLCA 18 236
SEQRES 1 A 228 ASP TYR LYS ASP ASP ASP ASP LYS LEU HIS SER GLN ALA
SEQRES 2 A 228 ASN LEU MET ARG LEU LYS SER ASP LEU PHE ASN ARG SER
SEQRES 3 A 228 PRO MET TYR PRO GLY PRO THR LYS ASP ASP PRO LEU THR
SEQRES 4 A 228 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 A 228 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 A 228 GLN GLN ARG TRP LYS LEU ASN SER LEU MET TRP ASP PRO
SEQRES 7 A 228 ASN GLU TYR GLY ASN ILE THR ASP PHE ARG THR SER ALA
SEQRES 8 A 228 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 A 228 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 A 228 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 A 228 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 A 228 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 A 228 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 A 228 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 A 228 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 A 228 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 A 228 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 A 228 PHE PHE ARG ASN LEU PHE ASP
SEQRES 1 B 228 ASP TYR LYS ASP ASP ASP ASP LYS LEU HIS SER GLN ALA
SEQRES 2 B 228 ASN LEU MET ARG LEU LYS SER ASP LEU PHE ASN ARG SER
SEQRES 3 B 228 PRO MET TYR PRO GLY PRO THR LYS ASP ASP PRO LEU THR
SEQRES 4 B 228 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 B 228 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 B 228 GLN GLN ARG TRP LYS LEU ASN SER LEU MET TRP ASP PRO
SEQRES 7 B 228 ASN GLU TYR GLY ASN ILE THR ASP PHE ARG THR SER ALA
SEQRES 8 B 228 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 B 228 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 B 228 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 B 228 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 B 228 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 B 228 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 B 228 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 B 228 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 B 228 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 B 228 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 B 228 PHE PHE ARG ASN LEU PHE ASP
SEQRES 1 C 228 ASP TYR LYS ASP ASP ASP ASP LYS LEU HIS SER GLN ALA
SEQRES 2 C 228 ASN LEU MET ARG LEU LYS SER ASP LEU PHE ASN ARG SER
SEQRES 3 C 228 PRO MET TYR PRO GLY PRO THR LYS ASP ASP PRO LEU THR
SEQRES 4 C 228 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 C 228 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 C 228 GLN GLN ARG TRP LYS LEU ASN SER LEU MET TRP ASP PRO
SEQRES 7 C 228 ASN GLU TYR GLY ASN ILE THR ASP PHE ARG THR SER ALA
SEQRES 8 C 228 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 C 228 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 C 228 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 C 228 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 C 228 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 C 228 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 C 228 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 C 228 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 C 228 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 C 228 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 C 228 PHE PHE ARG ASN LEU PHE ASP
SEQRES 1 D 228 ASP TYR LYS ASP ASP ASP ASP LYS LEU HIS SER GLN ALA
SEQRES 2 D 228 ASN LEU MET ARG LEU LYS SER ASP LEU PHE ASN ARG SER
SEQRES 3 D 228 PRO MET TYR PRO GLY PRO THR LYS ASP ASP PRO LEU THR
SEQRES 4 D 228 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 D 228 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 D 228 GLN GLN ARG TRP LYS LEU ASN SER LEU MET TRP ASP PRO
SEQRES 7 D 228 ASN GLU TYR GLY ASN ILE THR ASP PHE ARG THR SER ALA
SEQRES 8 D 228 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 D 228 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 D 228 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 D 228 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 D 228 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 D 228 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 D 228 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 D 228 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 D 228 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 D 228 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 D 228 PHE PHE ARG ASN LEU PHE ASP
SEQRES 1 E 228 ASP TYR LYS ASP ASP ASP ASP LYS LEU HIS SER GLN ALA
SEQRES 2 E 228 ASN LEU MET ARG LEU LYS SER ASP LEU PHE ASN ARG SER
SEQRES 3 E 228 PRO MET TYR PRO GLY PRO THR LYS ASP ASP PRO LEU THR
SEQRES 4 E 228 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 E 228 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 E 228 GLN GLN ARG TRP LYS LEU ASN SER LEU MET TRP ASP PRO
SEQRES 7 E 228 ASN GLU TYR GLY ASN ILE THR ASP PHE ARG THR SER ALA
SEQRES 8 E 228 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 E 228 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 E 228 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 E 228 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 E 228 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 E 228 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 E 228 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 E 228 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 E 228 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 E 228 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 E 228 PHE PHE ARG ASN LEU PHE ASP
HET ZY5 A 301 22
HET NAG A 401 14
HET NAG A 402 14
HET BMA A 403 11
HET MAN A 404 11
HET MAN A 405 11
HET ZY5 B 301 22
HET NAG B 401 14
HET ZY5 C 301 22
HET ZY5 D 301 22
HET ZY5 E 301 22
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM ZY5 4-[(E)-5,6-DIHYDRO-2,3'-BIPYRIDIN-3(4H)-
HETNAM 2 ZY5 YLIDENEMETHYL]-3-METHOXYPHENOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 6 BMA C6 H12 O6
FORMUL 7 MAN 2(C6 H12 O6)
FORMUL 8 ZY5 5(C18 H18 N2 O2)
FORMUL 9 NAG 3(C8 H15 N O6)
FORMUL 10 HOH *780(H2 O1)
HELIX 1 1 LEU A 0 ASN A 15 1 16
HELIX 2 2 LEU A 62 MET A 66 5 5
HELIX 3 3 ASP A 68 TYR A 72 5 5
HELIX 4 4 ALA A 83 ILE A 85 5 3
HELIX 5 5 ASP B -3 ASN B 15 1 19
HELIX 6 6 LEU B 62 MET B 66 5 5
HELIX 7 7 ASP B 68 TYR B 72 5 5
HELIX 8 8 ALA B 83 ILE B 85 5 3
HELIX 9 9 ASP C -5 ASN C 15 1 21
HELIX 10 10 LEU C 62 MET C 66 5 5
HELIX 11 11 ASP C 68 TYR C 72 5 5
HELIX 12 12 ALA C 83 ILE C 85 5 3
HELIX 13 13 ASP D -2 ASN D 15 1 18
HELIX 14 14 LEU D 62 MET D 66 5 5
HELIX 15 15 ASP D 68 TYR D 72 5 5
HELIX 16 16 ALA D 83 ILE D 85 5 3
HELIX 17 17 ASP E -8 ASN E 15 1 24
HELIX 18 18 LEU E 62 MET E 66 5 5
HELIX 19 19 ASP E 68 TYR E 72 5 5
HELIX 20 20 ALA E 83 ILE E 85 5 3
SHEET 1 AA 2 LEU A 29 THR A 32 0
SHEET 2 AA 2 ILE A 154 LYS A 157 1 O ASP A 155 N VAL A 31
SHEET 1 AB 4 THR A 36 ASP A 44 0
SHEET 2 AB 4 GLU A 49 TYR A 55 -1 O GLU A 49 N ASP A 44
SHEET 3 AB 4 ALA A 120 MET A 126 -1 O GLN A 121 N TYR A 54
SHEET 4 AB 4 GLN A 100 VAL A 101 -1 O GLN A 100 N ARG A 122
SHEET 1 AC 4 GLN A 58 TRP A 60 0
SHEET 2 AC 4 VAL A 115 PHE A 117 -1 O VAL A 115 N TRP A 60
SHEET 3 AC 4 ILE A 106 THR A 110 -1 O VAL A 108 N MET A 116
SHEET 4 AC 4 ASP A 77 SER A 81 -1 O PHE A 78 N VAL A 109
SHEET 1 AD 3 THR A 139 PHE A 144 0
SHEET 2 AD 3 TYR A 195 GLU A 206 -1 O VAL A 198 N PHE A 144
SHEET 3 AD 3 TYR A 174 GLN A 186 -1 O GLU A 175 N ARG A 205
SHEET 1 BA 2 LEU B 29 THR B 32 0
SHEET 2 BA 2 ILE B 154 LYS B 157 1 O ASP B 155 N VAL B 31
SHEET 1 BB 4 THR B 36 ASP B 44 0
SHEET 2 BB 4 GLU B 49 TYR B 55 -1 O GLU B 49 N ASP B 44
SHEET 3 BB 4 ALA B 120 MET B 126 -1 O GLN B 121 N TYR B 54
SHEET 4 BB 4 GLN B 100 VAL B 101 -1 O GLN B 100 N ARG B 122
SHEET 1 BC 4 GLN B 58 TRP B 60 0
SHEET 2 BC 4 VAL B 115 PHE B 117 -1 O VAL B 115 N TRP B 60
SHEET 3 BC 4 ILE B 106 THR B 110 -1 O VAL B 108 N MET B 116
SHEET 4 BC 4 ASP B 77 SER B 81 -1 O PHE B 78 N VAL B 109
SHEET 1 BD 3 THR B 139 PHE B 144 0
SHEET 2 BD 3 CYS B 191 GLU B 206 -1 O VAL B 198 N PHE B 144
SHEET 3 BD 3 TYR B 174 TYR B 188 -1 O GLU B 175 N ARG B 205
SHEET 1 CA 2 LEU C 29 THR C 32 0
SHEET 2 CA 2 ILE C 154 LYS C 157 1 O ASP C 155 N VAL C 31
SHEET 1 CB 4 THR C 36 ASP C 44 0
SHEET 2 CB 4 GLU C 49 TYR C 55 -1 O GLU C 49 N ASP C 44
SHEET 3 CB 4 ALA C 120 MET C 126 -1 O GLN C 121 N TYR C 54
SHEET 4 CB 4 GLN C 100 VAL C 101 -1 O GLN C 100 N ARG C 122
SHEET 1 CC 4 GLN C 58 TRP C 60 0
SHEET 2 CC 4 VAL C 115 PHE C 117 -1 O VAL C 115 N TRP C 60
SHEET 3 CC 4 ILE C 106 THR C 110 -1 O VAL C 108 N MET C 116
SHEET 4 CC 4 ASP C 77 SER C 81 -1 O PHE C 78 N VAL C 109
SHEET 1 CD 3 THR C 139 PHE C 144 0
SHEET 2 CD 3 TYR C 195 GLU C 206 -1 O VAL C 198 N PHE C 144
SHEET 3 CD 3 TYR C 174 GLN C 186 -1 O GLU C 175 N ARG C 205
SHEET 1 DA 2 LEU D 29 THR D 32 0
SHEET 2 DA 2 ILE D 154 LYS D 157 1 O ASP D 155 N VAL D 31
SHEET 1 DB 4 THR D 36 ASP D 44 0
SHEET 2 DB 4 GLU D 49 TYR D 55 -1 O GLU D 49 N ASP D 44
SHEET 3 DB 4 ALA D 120 MET D 126 -1 O GLN D 121 N TYR D 54
SHEET 4 DB 4 GLN D 100 VAL D 101 -1 O GLN D 100 N ARG D 122
SHEET 1 DC 4 GLN D 58 TRP D 60 0
SHEET 2 DC 4 VAL D 115 PHE D 117 -1 O VAL D 115 N TRP D 60
SHEET 3 DC 4 ILE D 106 THR D 110 -1 O VAL D 108 N MET D 116
SHEET 4 DC 4 ASP D 77 SER D 81 -1 O PHE D 78 N VAL D 109
SHEET 1 DD 3 THR D 139 PHE D 144 0
SHEET 2 DD 3 TYR D 195 GLU D 206 -1 O VAL D 198 N PHE D 144
SHEET 3 DD 3 TYR D 174 GLN D 186 -1 O GLU D 175 N ARG D 205
SHEET 1 EA 2 LEU E 29 THR E 32 0
SHEET 2 EA 2 ILE E 154 LYS E 157 1 O ASP E 155 N VAL E 31
SHEET 1 EB 4 THR E 36 ASP E 44 0
SHEET 2 EB 4 GLU E 49 TYR E 55 -1 O GLU E 49 N ASP E 44
SHEET 3 EB 4 ALA E 120 MET E 126 -1 O GLN E 121 N TYR E 54
SHEET 4 EB 4 GLN E 100 VAL E 101 -1 O GLN E 100 N ARG E 122
SHEET 1 EC 4 GLN E 58 TRP E 60 0
SHEET 2 EC 4 VAL E 115 PHE E 117 -1 O VAL E 115 N TRP E 60
SHEET 3 EC 4 ILE E 106 THR E 110 -1 O VAL E 108 N MET E 116
SHEET 4 EC 4 ASP E 77 SER E 81 -1 O PHE E 78 N VAL E 109
SHEET 1 ED 3 THR E 139 PHE E 144 0
SHEET 2 ED 3 CYS E 191 GLU E 206 -1 O VAL E 198 N PHE E 144
SHEET 3 ED 3 TYR E 174 TYR E 188 -1 O GLU E 175 N ARG E 205
SSBOND 1 CYS A 127 CYS A 140 1555 1555 1.92
SSBOND 2 CYS A 190 CYS A 191 1555 1555 2.05
SSBOND 3 CYS B 127 CYS B 140 1555 1555 1.92
SSBOND 4 CYS B 190 CYS B 191 1555 1555 2.06
SSBOND 5 CYS C 127 CYS C 140 1555 1555 1.92
SSBOND 6 CYS C 190 CYS C 191 1555 1555 2.10
SSBOND 7 CYS D 127 CYS D 140 1555 1555 1.97
SSBOND 8 CYS E 127 CYS E 140 1555 1555 1.91
SSBOND 9 CYS E 190 CYS E 191 1555 1555 2.06
LINK ND2 ASN A 74 C1 NAG A 401 1555 1555 1.37
LINK O4 NAG A 401 C1 NAG A 402 1555 1555 1.43
LINK O4 NAG A 402 C1 BMA A 403 1555 1555 1.43
LINK O3 BMA A 403 C1 MAN A 404 1555 1555 1.42
LINK O6 BMA A 403 C1 MAN A 405 1555 1555 1.43
LINK ND2 ASN B 74 C1 NAG B 401 1555 1555 1.36
SITE 1 AC1 9 TYR A 93 TRP A 147 THR E 36 TYR E 55
SITE 2 AC1 9 ILE E 118 ASP E 164 SER E 166 SER E 167
SITE 3 AC1 9 HOH E2032
SITE 1 AC2 2 ASN A 74 NAG A 402
SITE 1 AC3 4 NAG A 401 BMA A 403 MAN A 405 HOH A2179
SITE 1 AC4 5 NAG A 402 MAN A 404 MAN A 405 HOH A2178
SITE 2 AC4 5 ASN C 70
SITE 1 AC5 5 BMA A 403 HOH A2179 ARG C 8 GLU C 71
SITE 2 AC5 5 GLU C 135
SITE 1 AC6 2 NAG A 402 BMA A 403
SITE 1 AC7 9 THR A 36 ILE A 118 ASP A 164 SER A 166
SITE 2 AC7 9 SER A 167 HOH A2053 HOH A2125 TYR B 93
SITE 3 AC7 9 TRP B 147
SITE 1 AC8 1 ASN B 74
SITE 1 AC9 11 THR B 36 ILE B 118 ASP B 164 SER B 166
SITE 2 AC9 11 SER B 167 HOH B2100 TYR C 93 TRP C 147
SITE 3 AC9 11 TYR C 188 CYS C 190 TYR C 195
SITE 1 BC1 11 THR C 36 TYR C 55 GLN C 57 ILE C 118
SITE 2 BC1 11 ASP C 164 SER C 166 SER C 167 HOH C2025
SITE 3 BC1 11 HOH C2091 TYR D 93 TRP D 147
SITE 1 BC2 10 THR D 36 GLN D 57 ILE D 118 ASP D 164
SITE 2 BC2 10 SER D 166 SER D 167 HOH D2090 TYR E 93
SITE 3 BC2 10 TRP E 147 TYR E 195
CRYST1 86.909 115.394 130.607 90.00 90.00 90.00 P 21 21 21 20
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 0.011506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007657 0.00000
ATOM 1 N LEU A 0 4.981 27.871 36.194 1.00 59.41 N
ATOM 2 CA LEU A 0 4.562 26.730 35.319 1.00 58.95 C
ATOM 3 C LEU A 0 5.726 26.160 34.500 1.00 56.39 C
ATOM 4 O LEU A 0 5.946 24.954 34.531 1.00 52.73 O
ATOM 5 CB LEU A 0 3.400 27.123 34.393 1.00 61.76 C
ATOM 6 CG LEU A 0 2.088 27.495 35.088 1.00 65.36 C
ATOM 7 CD1 LEU A 0 1.019 27.799 34.047 1.00 67.28 C
ATOM 8 CD2 LEU A 0 1.610 26.400 36.067 1.00 65.66 C
ATOM 9 N HIS A 1 6.451 27.004 33.758 1.00 54.78 N
ATOM 10 CA HIS A 1 7.711 26.552 33.128 1.00 53.64 C
ATOM 11 C HIS A 1 8.790 26.199 34.161 1.00 48.04 C
ATOM 12 O HIS A 1 9.582 25.315 33.912 1.00 43.83 O
ATOM 13 CB HIS A 1 8.298 27.571 32.150 1.00 57.26 C
ATOM 14 CG HIS A 1 7.571 27.650 30.845 1.00 62.06 C
ATOM 15 ND1 HIS A 1 7.655 28.748 30.014 1.00 66.66 N
ATOM 16 CD2 HIS A 1 6.735 26.777 30.231 1.00 64.92 C
ATOM 17 CE1 HIS A 1 6.916 28.542 28.938 1.00 66.99 C
ATOM 18 NE2 HIS A 1 6.342 27.357 29.048 1.00 66.84 N
ATOM 19 N SER A 2 8.842 26.899 35.294 1.00 45.19 N
ATOM 20 CA SER A 2 9.777 26.519 36.360 1.00 41.47 C
ATOM 21 C SER A 2 9.381 25.161 36.920 1.00 37.00 C
ATOM 22 O SER A 2 10.250 24.304 37.153 1.00 36.58 O
ATOM 23 CB SER A 2 9.829 27.563 37.472 1.00 42.16 C
ATOM 24 OG SER A 2 8.616 27.570 38.205 1.00 46.91 O
ATOM 25 N GLN A 3 8.083 24.948 37.121 1.00 33.01 N
ATOM 26 CA GLN A 3 7.588 23.653 37.603 1.00 35.61 C
ATOM 27 C GLN A 3 7.890 22.535 36.595 1.00 32.47 C
ATOM 28 O GLN A 3 8.290 21.431 36.989 1.00 30.77 O
ATOM 29 CB GLN A 3 6.087 23.663 37.903 1.00 35.90 C
ATOM 30 CG GLN A 3 5.737 23.950 39.321 1.00 40.78 C
ATOM 31 CD GLN A 3 4.241 23.887 39.573 1.00 47.07 C
ATOM 32 OE1 GLN A 3 3.626 24.900 39.887 1.00 53.29 O
ATOM 33 NE2 GLN A 3 3.650 22.700 39.422 1.00 48.59 N
ATOM 34 N ALA A 4 7.633 22.824 35.329 1.00 33.76 N
ATOM 35 CA ALA A 4 7.888 21.878 34.242 1.00 32.40 C
ATOM 36 C ALA A 4 9.380 21.527 34.178 1.00 31.90 C
ATOM 37 O ALA A 4 9.742 20.352 34.039 1.00 30.88 O
ATOM 38 CB ALA A 4 7.419 22.438 32.928 1.00 34.62 C
ATOM 39 N ASN A 5 10.233 22.541 34.296 1.00 29.00 N
ATOM 40 CA ASN A 5 11.684 22.310 34.303 1.00 30.22 C
ATOM 41 C ASN A 5 12.127 21.381 35.424 1.00 29.13 C
ATOM 42 O ASN A 5 12.975 20.510 35.212 1.00 29.42 O
ATOM 43 CB ASN A 5 12.449 23.623 34.379 1.00 30.86 C
ATOM 44 CG ASN A 5 12.416 24.391 33.069 1.00 36.45 C
ATOM 45 OD1 ASN A 5 12.282 23.807 31.993 1.00 37.25 O
ATOM 46 ND2 ASN A 5 12.546 25.704 33.153 1.00 36.99 N
ATOM 47 N LEU A 6 11.573 21.563 36.616 1.00 27.43 N
ATOM 48 CA LEU A 6 11.937 20.732 37.742 1.00 26.17 C
ATOM 49 C LEU A 6 11.406 19.320 37.584 1.00 24.97 C
ATOM 50 O LEU A 6 12.104 18.350 37.874 1.00 25.15 O
ATOM 51 CB LEU A 6 11.422 21.360 39.065 1.00 26.58 C
ATOM 52 CG LEU A 6 11.822 20.602 40.316 1.00 27.57 C
ATOM 53 CD1 LEU A 6 13.294 20.340 40.385 1.00 27.37 C
ATOM 54 CD2 LEU A 6 11.355 21.388 41.562 1.00 29.21 C
ATOM 55 N MET A 7 10.167 19.180 37.120 1.00 25.97 N
ATOM 56 CA MET A 7 9.597 17.838 36.902 1.00 30.48 C
ATOM 57 C MET A 7 10.418 17.100 35.835 1.00 27.34 C
ATOM 58 O MET A 7 10.705 15.905 35.990 1.00 28.73 O
ATOM 59 CB MET A 7 8.114 17.921 36.500 1.00 31.60 C
ATOM 60 CG MET A 7 7.230 18.386 37.661 1.00 36.90 C
ATOM 61 SD MET A 7 5.471 18.490 37.269 1.00 48.15 S
ATOM 62 CE MET A 7 5.506 19.699 35.951 1.00 41.80 C
ATOM 63 N ARG A 8 10.863 17.835 34.831 1.00 28.73 N
ATOM 64 CA ARG A 8 11.680 17.247 33.751 1.00 28.07 C
ATOM 65 C ARG A 8 13.034 16.801 34.268 1.00 26.99 C
ATOM 66 O ARG A 8 13.506 15.696 33.954 1.00 27.61 O
ATOM 67 CB ARG A 8 11.813 18.210 32.583 1.00 29.36 C
ATOM 68 CG ARG A 8 12.706 17.700 31.415 1.00 29.88 C
ATOM 69 CD ARG A 8 12.649 18.606 30.170 1.00 31.85 C
ATOM 70 NE ARG A 8 12.882 20.023 30.465 1.00 31.73 N
ATOM 71 CZ ARG A 8 14.053 20.643 30.448 1.00 33.87 C
ATOM 72 NH1 ARG A 8 15.172 20.017 30.124 1.00 37.23 N
ATOM 73 NH2 ARG A 8 14.090 21.925 30.761 1.00 35.48 N
ATOM 74 N LEU A 9 13.682 17.655 35.051 1.00 25.50 N
ATOM 75 CA LEU A 9 14.948 17.270 35.699 1.00 23.98 C
ATOM 76 C LEU A 9 14.803 16.008 36.529 1.00 24.88 C
ATOM 77 O LEU A 9 15.589 15.075 36.402 1.00 26.82 O
ATOM 78 CB LEU A 9 15.459 18.414 36.560 1.00 24.06 C
ATOM 79 CG LEU A 9 16.730 18.166 37.356 1.00 23.15 C
ATOM 80 CD1 LEU A 9 17.898 17.818 36.434 1.00 25.67 C
ATOM 81 CD2 LEU A 9 17.033 19.386 38.157 1.00 23.96 C
ATOM 82 N LYS A 10 13.795 15.966 37.410 1.00 23.90 N
ATOM 83 CA LYS A 10 13.628 14.819 38.244 1.00 24.25 C
ATOM 84 C LYS A 10 13.357 13.547 37.415 1.00 24.09 C
ATOM 85 O LYS A 10 13.919 12.492 37.724 1.00 26.72 O
ATOM 86 CB LYS A 10 12.537 15.071 39.297 1.00 25.17 C
ATOM 87 CG LYS A 10 12.967 16.113 40.310 1.00 26.10 C
ATOM 88 CD LYS A 10 11.891 16.347 41.357 1.00 28.48 C
ATOM 89 CE LYS A 10 11.955 15.297 42.446 1.00 34.61 C
ATOM 90 NZ LYS A 10 10.887 15.449 43.485 1.00 34.87 N
ATOM 91 N SER A 11 12.517 13.658 36.401 1.00 27.81 N
ATOM 92 CA SER A 11 12.215 12.538 35.520 1.00 29.03 C
ATOM 93 C SER A 11 13.471 12.083 34.783 1.00 30.79 C
ATOM 94 O SER A 11 13.738 10.891 34.690 1.00 33.32 O
ATOM 95 CB SER A 11 11.125 12.935 34.527 1.00 33.02 C
ATOM 96 OG SER A 11 10.942 11.931 33.534 1.00 37.26 O
ATOM 97 N ASP A 12 14.251 13.032 34.284 1.00 29.59 N
ATOM 98 CA ASP A 12 15.520 12.676 33.598 1.00 29.91 C
ATOM 99 C ASP A 12 16.480 11.935 34.544 1.00 30.93 C
ATOM 100 O ASP A 12 17.098 10.932 34.158 1.00 30.81 O
ATOM 101 CB ASP A 12 16.203 13.910 33.026 1.00 30.29 C
ATOM 102 CG ASP A 12 15.517 14.464 31.791 1.00 29.65 C
ATOM 103 OD1 ASP A 12 14.646 13.806 31.197 1.00 31.84 O
ATOM 104 OD2 ASP A 12 15.831 15.609 31.415 1.00 29.16 O
ATOM 105 N LEU A 13 16.608 12.411 35.780 1.00 26.45 N
ATOM 106 CA LEU A 13 17.547 11.819 36.720 1.00 27.61 C
ATOM 107 C LEU A 13 17.057 10.479 37.214 1.00 31.80 C
ATOM 108 O LEU A 13 17.852 9.564 37.359 1.00 33.31 O
ATOM 109 CB LEU A 13 17.794 12.720 37.914 1.00 27.92 C
ATOM 110 CG LEU A 13 18.614 13.980 37.624 1.00 27.77 C
ATOM 111 CD1 LEU A 13 18.702 14.816 38.890 1.00 30.21 C
ATOM 112 CD2 LEU A 13 19.995 13.641 37.103 1.00 31.47 C
ATOM 113 N PHE A 14 15.750 10.390 37.469 1.00 33.12 N
ATOM 114 CA PHE A 14 15.170 9.226 38.151 1.00 37.07 C
ATOM 115 C PHE A 14 14.539 8.191 37.214 1.00 41.75 C
ATOM 116 O PHE A 14 14.431 7.035 37.603 1.00 41.92 O
ATOM 117 CB PHE A 14 14.136 9.670 39.194 1.00 37.54 C
ATOM 118 CG PHE A 14 14.695 10.551 40.294 1.00 36.24 C
ATOM 119 CD1 PHE A 14 13.880 11.454 40.939 1.00 40.70 C
ATOM 120 CD2 PHE A 14 16.016 10.488 40.677 1.00 39.15 C
ATOM 121 CE1 PHE A 14 14.378 12.263 41.946 1.00 40.03 C
ATOM 122 CE2 PHE A 14 16.519 11.315 41.676 1.00 39.09 C
ATOM 123 CZ PHE A 14 15.695 12.189 42.303 1.00 37.92 C
ATOM 124 N ASN A 15 14.119 8.586 36.008 1.00 44.26 N
ATOM 125 CA ASN A 15 13.523 7.635 35.036 1.00 47.54 C