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3lii.pdb
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HEADER HYDROLASE 25-JAN-10 3LII
TITLE RECOMBINANT HUMAN ACETYLCHOLINESTERASE
CAVEAT 3LII NAG C 1 HAS WRONG CHIRALITY AT ATOM C1 NAG D 1 HAS WRONG
CAVEAT 2 3LII CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 35-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215
KEYWDS RECOMBINANT HUMAN ACETYLCHOLINESTERASE, BLOOD GROUP ANTIGEN, CELL
KEYWDS 2 JUNCTION, CELL MEMBRANE, DISULFIDE BOND, GLYCOPROTEIN, GPI-ANCHOR,
KEYWDS 3 HYDROLASE, LIPOPROTEIN, MEMBRANE, NEUROTRANSMITTER DEGRADATION,
KEYWDS 4 NUCLEUS, SECRETED, SERINE ESTERASE, SYNAPSE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DVIR,T.ROSENBERRY,M.HAREL,I.SILMAN,J.SUSSMAN
REVDAT 3 29-JUL-20 3LII 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 11-AUG-10 3LII 1 JRNL
REVDAT 1 16-MAR-10 3LII 0
JRNL AUTH H.DVIR,I.SILMAN,M.HAREL,T.L.ROSENBERRY,J.L.SUSSMAN
JRNL TITL ACETYLCHOLINESTERASE: FROM 3D STRUCTURE TO FUNCTION.
JRNL REF CHEM.BIOL.INTERACT V. 187 10 2010
JRNL REFN ISSN 0009-2797
JRNL PMID 20138030
JRNL DOI 10.1016/J.CBI.2010.01.042
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45505
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2470
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3233
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 101
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.18000
REMARK 3 B22 (A**2) : -4.18000
REMARK 3 B33 (A**2) : 6.27000
REMARK 3 B12 (A**2) : -2.09000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.488
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.308
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.231
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.813
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8646 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11832 ; 2.368 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1061 ; 8.531 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 393 ;35.726 ;22.621
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1221 ;23.478 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 75 ;24.406 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1265 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6807 ; 0.012 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 5320 ; 1.070 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8562 ; 2.101 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3326 ; 2.774 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3270 ; 4.924 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3LII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47979
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 31.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1B41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M LITHIUM SULFATE, 0.1M HEPES, PH
REMARK 280 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.42333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.84667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.63500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.05833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.21167
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -299.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLU A 4
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLU B 4
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ARG B 493
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 NH2 ARG B 417 O HOH B 649 1.91
REMARK 500 NH1 ARG B 417 O HOH B 649 2.02
REMARK 500 NH1 ARG A 224 O ALA A 484 2.09
REMARK 500 O ARG B 46 NH1 ARG B 274 2.17
REMARK 500 ND2 ASN B 350 O5 NAG D 1 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 51 CG GLU A 51 CD 0.096
REMARK 500 CYS A 529 CB CYS A 529 SG 0.176
REMARK 500 GLU B 81 CG GLU B 81 CD 0.092
REMARK 500 TRP B 286 CB TRP B 286 CG -0.109
REMARK 500 GLU B 376 CB GLU B 376 CG 0.192
REMARK 500 GLU B 376 CG GLU B 376 CD 0.169
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 ARG A 152 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 193 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 CYS A 257 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 PRO A 290 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 386 CA - CB - CG ANGL. DEV. = -15.6 DEGREES
REMARK 500 LYS A 470 CD - CE - NZ ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG A 475 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU B 92 CB - CG - CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 LEU B 130 CB - CG - CD1 ANGL. DEV. = -11.8 DEGREES
REMARK 500 MET B 149 CG - SD - CE ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG B 152 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 VAL B 370 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG B 417 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 6 6.09 43.61
REMARK 500 PRO A 25 -46.55 -28.13
REMARK 500 PHE A 47 -7.40 78.28
REMARK 500 ASP A 61 99.51 -52.88
REMARK 500 ALA A 62 35.78 -98.06
REMARK 500 GLN A 66 -171.57 -69.90
REMARK 500 CYS A 96 -10.40 -146.28
REMARK 500 LEU A 97 78.86 -69.33
REMARK 500 ARG A 107 112.56 -38.98
REMARK 500 PRO A 111 80.15 -65.84
REMARK 500 GLU A 142 3.27 -154.30
REMARK 500 GLU A 185 3.14 -61.76
REMARK 500 ASN A 186 -15.99 -154.16
REMARK 500 ALA A 188 -64.41 -17.23
REMARK 500 ALA A 189 5.77 -64.96
REMARK 500 THR A 195 -148.57 -90.51
REMARK 500 SER A 196 78.83 5.35
REMARK 500 SER A 203 -117.09 35.29
REMARK 500 MET A 241 -41.78 -29.81
REMARK 500 CYS A 257 145.52 115.65
REMARK 500 ASN A 265 -150.56 -80.73
REMARK 500 ASP A 266 -90.55 52.18
REMARK 500 THR A 267 -45.39 -24.48
REMARK 500 ASP A 306 -81.44 -89.87
REMARK 500 SER A 309 -37.22 -36.69
REMARK 500 ASN A 317 -76.06 -51.71
REMARK 500 TYR A 341 36.05 -95.38
REMARK 500 ASN A 350 -149.36 -102.94
REMARK 500 SER A 352 46.48 27.93
REMARK 500 GLN A 369 81.91 43.11
REMARK 500 ASP A 404 -72.64 -46.97
REMARK 500 VAL A 407 -80.54 -114.76
REMARK 500 ASN A 464 73.22 -63.65
REMARK 500 ASP A 488 125.08 -174.96
REMARK 500 ASP A 494 66.73 170.32
REMARK 500 THR A 504 126.99 -171.15
REMARK 500 ASP A 514 -158.91 -151.30
REMARK 500 ARG A 525 59.54 38.18
REMARK 500 ALA B 6 -59.17 49.51
REMARK 500 ARG B 13 -7.89 -51.69
REMARK 500 PRO B 25 -8.40 -37.97
REMARK 500 PHE B 47 -0.94 85.03
REMARK 500 ALA B 62 40.33 -144.38
REMARK 500 TYR B 72 143.82 -37.05
REMARK 500 THR B 75 30.74 -81.63
REMARK 500 GLU B 81 -76.22 -46.89
REMARK 500 GLU B 91 137.69 -33.72
REMARK 500 ARG B 107 125.17 -38.13
REMARK 500 TYR B 133 49.25 -97.89
REMARK 500 ARG B 136 -68.85 -20.08
REMARK 500
REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 503 THR A 504 -149.13
REMARK 500 LEU B 22 LYS B 23 -146.90
REMARK 500 ASN B 490 GLU B 491 -147.25
REMARK 500 GLU B 491 PRO B 492 -146.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F8U RELATED DB: PDB
REMARK 900 MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1B41 RELATED DB: PDB
REMARK 900 RECOMBINANT NATIVE HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH SNAKE-
REMARK 900 VENOM TOXIN FASCICULIN-II
DBREF 3LII A 4 543 UNP P22303 ACES_HUMAN 35 574
DBREF 3LII B 4 543 UNP P22303 ACES_HUMAN 35 574
SEQRES 1 A 540 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 2 A 540 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 3 A 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 4 A 540 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 5 A 540 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 6 A 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 A 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 A 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 A 540 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 A 540 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 11 A 540 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 12 A 540 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 A 540 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 16 A 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 A 540 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 18 A 540 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 19 A 540 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 20 A 540 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 21 A 540 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 22 A 540 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 23 A 540 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 A 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 A 540 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 26 A 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 A 540 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 A 540 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 29 A 540 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 A 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 31 A 540 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 32 A 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 A 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 34 A 540 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 35 A 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 36 A 540 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 37 A 540 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 38 A 540 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 39 A 540 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 40 A 540 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 A 540 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 A 540 PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 540 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 2 B 540 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 3 B 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 4 B 540 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 5 B 540 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 6 B 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 B 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 B 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 B 540 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 B 540 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 11 B 540 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 12 B 540 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 B 540 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 16 B 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 B 540 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 18 B 540 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 19 B 540 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 20 B 540 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 21 B 540 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 22 B 540 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 23 B 540 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 B 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 B 540 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 26 B 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 B 540 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 B 540 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 29 B 540 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 B 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 31 B 540 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 32 B 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 B 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 34 B 540 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 35 B 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 36 B 540 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 37 B 540 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 38 B 540 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 39 B 540 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 40 B 540 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 B 540 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 B 540 PRO LYS LEU LEU SER ALA THR
MODRES 3LII ASN A 350 ASN GLYCOSYLATION SITE
MODRES 3LII ASN B 350 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET SO4 A1005 5
HET SO4 A1010 5
HET SO4 A1012 5
HET SO4 A1011 5
HET SO4 A1013 5
HET SO4 A1017 5
HET SO4 B1014 5
HET SO4 B1015 5
HET SO4 B1016 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 SO4 9(O4 S 2-)
FORMUL 14 HOH *54(H2 O)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 ALA A 141 1 7
HELIX 5 5 GLY A 154 LEU A 159 1 6
HELIX 6 6 ASN A 170 ALA A 188 1 19
HELIX 7 7 ALA A 189 GLY A 191 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 215 GLY A 220 1 6
HELIX 10 10 MET A 241 VAL A 255 1 15
HELIX 11 11 ASP A 266 CYS A 272 1 7
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 TRP A 286 LEU A 289 5 4
HELIX 14 14 THR A 311 ALA A 318 1 8
HELIX 15 15 GLY A 335 VAL A 340 1 6
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 ALA A 420 1 14
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 THR A 466 GLY A 487 1 22
HELIX 23 23 ARG A 525 ARG A 534 1 10
HELIX 24 24 ARG A 534 SER A 541 1 8
HELIX 25 25 MET B 42 ARG B 46 5 5
HELIX 26 26 PHE B 80 MET B 85 1 6
HELIX 27 27 LEU B 130 TYR B 133 5 4
HELIX 28 28 ASP B 134 ARG B 143 1 10
HELIX 29 29 VAL B 153 LEU B 159 1 7
HELIX 30 30 ASN B 170 ALA B 188 1 19
HELIX 31 31 SER B 203 SER B 215 1 13
HELIX 32 32 SER B 215 GLY B 220 1 6
HELIX 33 33 MET B 241 LEU B 254 1 14
HELIX 34 34 ASP B 266 THR B 275 1 10
HELIX 35 35 PRO B 277 GLU B 285 1 9
HELIX 36 36 TRP B 286 VAL B 288 5 3
HELIX 37 37 THR B 311 ALA B 318 1 8
HELIX 38 38 GLY B 335 LEU B 339 5 5
HELIX 39 39 SER B 355 VAL B 367 1 13
HELIX 40 40 SER B 371 THR B 383 1 13
HELIX 41 41 ASP B 390 VAL B 407 1 18
HELIX 42 42 VAL B 407 ALA B 420 1 14
HELIX 43 43 PRO B 440 GLY B 444 5 5
HELIX 44 44 GLU B 450 PHE B 455 1 6
HELIX 45 45 GLY B 456 ASP B 460 5 5
HELIX 46 46 GLU B 468 GLY B 487 1 20
HELIX 47 47 ARG B 525 ARG B 534 1 10
HELIX 48 48 ARG B 534 SER B 541 1 8
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 A 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 B 9 ILE A 20 THR A 24 0
SHEET 2 B 9 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 B 9 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 B 9 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 B 9 VAL A 114 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 B 9 VAL A 197 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 B 9 ARG A 224 GLN A 228 1 O VAL A 226 N LEU A 199
SHEET 8 B 9 GLN A 325 VAL A 331 1 O LEU A 327 N ALA A 225
SHEET 9 B 9 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 1 C 2 VAL A 68 CYS A 69 0
SHEET 2 C 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 D 2 VAL A 239 GLY A 240 0
SHEET 2 D 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 E 2 GLN A 509 SER A 512 0
SHEET 2 E 2 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 F 3 LEU B 9 VAL B 12 0
SHEET 2 F 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 F 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 18
SHEET 1 G11 ILE B 20 THR B 24 0
SHEET 2 G11 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 G11 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 G11 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 G11 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 G11 GLY B 192 GLU B 202 1 O THR B 198 N VAL B 114
SHEET 7 G11 ARG B 224 GLN B 228 1 O VAL B 226 N LEU B 199
SHEET 8 G11 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 G11 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 326
SHEET 10 G11 GLN B 509 LEU B 513 1 O VAL B 511 N VAL B 429
SHEET 11 G11 VAL B 520 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 H 2 VAL B 68 CYS B 69 0
SHEET 2 H 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 I 2 VAL B 239 GLY B 240 0
SHEET 2 I 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.08
SSBOND 2 CYS A 409 CYS A 529 1555 1555 2.11
SSBOND 3 CYS B 69 CYS B 96 1555 1555 2.11
SSBOND 4 CYS B 409 CYS B 529 1555 1555 2.10
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG D 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.48
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.49
CISPEP 1 CYS A 257 PRO A 258 0 6.15
CISPEP 2 TYR B 105 PRO B 106 0 -2.71
CISPEP 3 CYS B 257 PRO B 258 0 8.04
CRYST1 210.900 210.900 115.270 90.00 90.00 120.00 P 61 12
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 0.004742 0.002738 0.000000 0.00000
SCALE2 0.000000 0.005475 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008675 0.00000
ATOM 1 N ASP A 5 95.646 113.367 -35.564 1.00108.79 N
ATOM 2 CA ASP A 5 94.198 113.086 -35.332 1.00109.26 C
ATOM 3 C ASP A 5 93.473 114.130 -34.445 1.00109.03 C
ATOM 4 O ASP A 5 92.232 114.261 -34.510 1.00109.21 O
ATOM 5 CB ASP A 5 93.978 111.665 -34.788 1.00109.35 C
ATOM 6 CG ASP A 5 92.464 111.306 -34.636 1.00111.00 C
ATOM 7 OD1 ASP A 5 91.705 111.939 -33.834 1.00111.16 O
ATOM 8 OD2 ASP A 5 92.029 110.359 -35.322 1.00112.37 O
ATOM 9 N ALA A 6 94.218 114.865 -33.618 1.00108.53 N
ATOM 10 CA ALA A 6 93.641 115.995 -32.809 1.00107.63 C
ATOM 11 C ALA A 6 92.271 115.764 -32.100 1.00106.45 C
ATOM 12 O ALA A 6 91.695 116.697 -31.524 1.00106.10 O
ATOM 13 CB ALA A 6 93.645 117.347 -33.622 1.00107.73 C
ATOM 14 N GLU A 7 91.777 114.522 -32.169 1.00105.27 N
ATOM 15 CA GLU A 7 90.709 114.009 -31.300 1.00104.49 C
ATOM 16 C GLU A 7 91.398 113.430 -30.071 1.00102.77 C
ATOM 17 O GLU A 7 90.816 113.288 -28.992 1.00102.57 O
ATOM 18 CB GLU A 7 89.932 112.875 -31.999 1.00104.99 C
ATOM 19 CG GLU A 7 88.734 113.303 -32.861 1.00108.28 C
ATOM 20 CD GLU A 7 87.617 114.016 -32.048 1.00112.47 C
ATOM 21 OE1 GLU A 7 86.831 113.360 -31.326 1.00112.53 O
ATOM 22 OE2 GLU A 7 87.512 115.259 -32.139 1.00116.04 O
ATOM 23 N LEU A 8 92.666 113.098 -30.285 1.00100.59 N
ATOM 24 CA LEU A 8 93.484 112.389 -29.349 1.00 98.15 C
ATOM 25 C LEU A 8 94.349 113.290 -28.485 1.00 97.50 C
ATOM 26 O LEU A 8 94.982 112.780 -27.572 1.00 98.33 O
ATOM 27 CB LEU A 8 94.371 111.391 -30.101 1.00 97.31 C
ATOM 28 CG LEU A 8 93.551 110.423 -30.941 1.00 95.23 C
ATOM 29 CD1 LEU A 8 94.308 109.130 -31.091 1.00 92.09 C
ATOM 30 CD2 LEU A 8 92.177 110.170 -30.241 1.00 94.46 C
ATOM 31 N LEU A 9 94.412 114.601 -28.754 1.00 96.15 N
ATOM 32 CA LEU A 9 95.268 115.519 -27.950 1.00 94.49 C
ATOM 33 C LEU A 9 94.279 116.130 -26.988 1.00 93.11 C
ATOM 34 O LEU A 9 93.118 116.240 -27.347 1.00 93.21 O
ATOM 35 CB LEU A 9 96.034 116.537 -28.832 1.00 94.44 C
ATOM 36 CG LEU A 9 96.976 116.100 -30.043 1.00 95.39 C
ATOM 37 CD1 LEU A 9 98.505 116.332 -29.888 1.00 93.57 C
ATOM 38 CD2 LEU A 9 96.765 114.704 -30.721 1.00 95.26 C
ATOM 39 N VAL A 10 94.681 116.396 -25.743 1.00 91.69 N
ATOM 40 CA VAL A 10 93.765 116.942 -24.702 1.00 90.23 C
ATOM 41 C VAL A 10 94.544 117.633 -23.628 1.00 89.47 C
ATOM 42 O VAL A 10 95.600 117.160 -23.217 1.00 88.93 O
ATOM 43 CB VAL A 10 92.953 115.863 -23.955 1.00 90.00 C
ATOM 44 CG1 VAL A 10 92.053 116.483 -22.881 1.00 89.02 C
ATOM 45 CG2 VAL A 10 92.109 115.135 -24.887 1.00 90.51 C
ATOM 46 N THR A 11 94.004 118.728 -23.134 1.00 88.53 N
ATOM 47 CA THR A 11 94.709 119.424 -22.102 1.00 88.30 C
ATOM 48 C THR A 11 94.013 119.403 -20.775 1.00 87.80 C
ATOM 49 O THR A 11 92.896 119.858 -20.602 1.00 87.91 O
ATOM 50 CB THR A 11 95.068 120.833 -22.541 1.00 88.89 C
ATOM 51 OG1 THR A 11 96.053 120.736 -23.586 1.00 89.33 O
ATOM 52 CG2 THR A 11 95.594 121.677 -21.349 1.00 87.94 C
ATOM 53 N VAL A 12 94.736 118.869 -19.825 1.00 87.62 N
ATOM 54 CA VAL A 12 94.235 118.586 -18.508 1.00 87.67 C
ATOM 55 C VAL A 12 94.941 119.579 -17.590 1.00 87.69 C
ATOM 56 O VAL A 12 95.984 120.121 -17.966 1.00 87.96 O
ATOM 57 CB VAL A 12 94.605 117.116 -18.188 1.00 87.62 C
ATOM 58 CG1 VAL A 12 95.068 116.943 -16.756 1.00 88.77 C
ATOM 59 CG2 VAL A 12 93.470 116.157 -18.575 1.00 86.69 C
ATOM 60 N ARG A 13 94.421 119.805 -16.391 1.00 87.62 N
ATOM 61 CA ARG A 13 95.052 120.763 -15.488 1.00 88.35 C
ATOM 62 C ARG A 13 96.546 120.620 -15.243 1.00 88.33 C
ATOM 63 O ARG A 13 97.144 121.513 -14.688 1.00 89.21 O
ATOM 64 CB ARG A 13 94.330 120.818 -14.168 1.00 88.19 C
ATOM 65 CG ARG A 13 93.051 121.595 -14.309 1.00 93.74 C
ATOM 66 CD ARG A 13 92.380 121.896 -12.985 1.00102.03 C
ATOM 67 NE ARG A 13 93.329 122.487 -12.038 1.00108.04 N
ATOM 68 CZ ARG A 13 93.019 122.857 -10.794 1.00110.69 C
ATOM 69 NH1 ARG A 13 91.762 122.707 -10.350 1.00112.12 N
ATOM 70 NH2 ARG A 13 93.965 123.374 -10.004 1.00110.84 N
ATOM 71 N GLY A 14 97.159 119.513 -15.637 1.00 88.12 N
ATOM 72 CA GLY A 14 98.560 119.311 -15.366 1.00 87.22 C
ATOM 73 C GLY A 14 99.401 119.524 -16.593 1.00 87.49 C
ATOM 74 O GLY A 14 100.609 119.690 -16.498 1.00 88.28 O
ATOM 75 N GLY A 15 98.790 119.518 -17.765 1.00 87.49 N
ATOM 76 CA GLY A 15 99.579 119.513 -18.999 1.00 87.96 C
ATOM 77 C GLY A 15 98.864 118.777 -20.108 1.00 88.41 C
ATOM 78 O GLY A 15 97.649 118.619 -20.064 1.00 87.99 O
ATOM 79 N ARG A 16 99.620 118.318 -21.097 1.00 89.34 N
ATOM 80 CA ARG A 16 99.036 117.796 -22.346 1.00 90.76 C
ATOM 81 C ARG A 16 99.176 116.252 -22.481 1.00 90.86 C
ATOM 82 O ARG A 16 100.178 115.691 -22.017 1.00 91.72 O
ATOM 83 CB ARG A 16 99.647 118.547 -23.574 1.00 91.49 C
ATOM 84 CG ARG A 16 99.215 120.062 -23.752 1.00 93.29 C
ATOM 85 CD ARG A 16 99.863 120.790 -24.949 1.00 95.93 C
ATOM 86 NE ARG A 16 101.189 121.355 -24.644 1.00 99.69 N
ATOM 87 CZ ARG A 16 102.330 121.050 -25.289 1.00100.92 C
ATOM 88 NH1 ARG A 16 102.304 120.179 -26.305 1.00100.73 N
ATOM 89 NH2 ARG A 16 103.504 121.617 -24.928 1.00 99.06 N
ATOM 90 N LEU A 17 98.199 115.574 -23.115 1.00 90.38 N
ATOM 91 CA LEU A 17 98.184 114.091 -23.212 1.00 89.18 C
ATOM 92 C LEU A 17 97.899 113.623 -24.620 1.00 89.03 C
ATOM 93 O LEU A 17 96.961 114.086 -25.198 1.00 88.89 O
ATOM 94 CB LEU A 17 97.080 113.511 -22.307 1.00 88.78 C
ATOM 95 CG LEU A 17 96.656 114.104 -20.950 1.00 87.04 C
ATOM 96 CD1 LEU A 17 95.300 113.663 -20.519 1.00 85.52 C
ATOM 97 CD2 LEU A 17 97.602 113.744 -19.888 1.00 86.59 C
ATOM 98 N ARG A 18 98.695 112.723 -25.175 1.00 89.50 N
ATOM 99 CA ARG A 18 98.332 112.045 -26.437 1.00 90.77 C
ATOM 100 C ARG A 18 97.611 110.752 -26.144 1.00 89.98 C
ATOM 101 O ARG A 18 98.154 109.901 -25.466 1.00 90.56 O
ATOM 102 CB ARG A 18 99.558 111.641 -27.259 1.00 91.61 C
ATOM 103 CG ARG A 18 99.786 112.353 -28.605 1.00 97.53 C
ATOM 104 CD ARG A 18 100.850 111.613 -29.513 1.00107.18 C
ATOM 105 NE ARG A 18 101.847 110.835 -28.743 1.00113.76 N
ATOM 106 CZ ARG A 18 102.948 111.349 -28.173 1.00117.01 C
ATOM 107 NH1 ARG A 18 103.234 112.659 -28.283 1.00117.63 N
ATOM 108 NH2 ARG A 18 103.762 110.550 -27.481 1.00116.89 N
ATOM 109 N GLY A 19 96.422 110.568 -26.702 1.00 89.24 N
ATOM 110 CA GLY A 19 95.662 109.334 -26.516 1.00 87.49 C
ATOM 111 C GLY A 19 95.862 108.316 -27.593 1.00 86.59 C
ATOM 112 O GLY A 19 96.782 108.407 -28.373 1.00 86.32 O
ATOM 113 N ILE A 20 94.995 107.330 -27.615 1.00 86.81 N
ATOM 114 CA ILE A 20 95.044 106.334 -28.646 1.00 88.11 C
ATOM 115 C ILE A 20 93.609 105.989 -29.087 1.00 90.12 C
ATOM 116 O ILE A 20 92.657 106.159 -28.281 1.00 90.24 O
ATOM 117 CB ILE A 20 95.735 105.097 -28.142 1.00 87.49 C
ATOM 118 CG1 ILE A 20 96.281 104.290 -29.327 1.00 87.03 C
ATOM 119 CG2 ILE A 20 94.803 104.353 -27.181 1.00 86.41 C
ATOM 120 CD1 ILE A 20 96.360 102.769 -29.124 1.00 84.56 C
ATOM 121 N ARG A 21 93.469 105.515 -30.349 1.00 91.72 N
ATOM 122 CA ARG A 21 92.173 105.126 -30.968 1.00 93.17 C
ATOM 123 C ARG A 21 91.989 103.606 -30.902 1.00 92.79 C
ATOM 124 O ARG A 21 92.906 102.860 -31.277 1.00 93.07 O
ATOM 125 CB ARG A 21 92.157 105.578 -32.434 1.00 94.36 C
ATOM 126 CG ARG A 21 90.766 105.862 -33.073 1.00 99.34 C
ATOM 127 CD ARG A 21 90.914 106.237 -34.593 1.00107.93 C
ATOM 128 NE ARG A 21 90.694 105.090 -35.490 1.00114.86 N
ATOM 129 CZ ARG A 21 89.742 105.026 -36.436 1.00119.16 C
ATOM 130 NH1 ARG A 21 88.926 106.068 -36.641 1.00121.13 N
ATOM 131 NH2 ARG A 21 89.609 103.927 -37.196 1.00119.29 N
ATOM 132 N LEU A 22 90.831 103.128 -30.424 1.00 92.54 N
ATOM 133 CA LEU A 22 90.622 101.662 -30.254 1.00 91.89 C
ATOM 134 C LEU A 22 89.427 101.195 -31.049 1.00 92.32 C
ATOM 135 O LEU A 22 88.357 101.823 -30.985 1.00 91.99 O
ATOM 136 CB LEU A 22 90.405 101.271 -28.784 1.00 91.20 C
ATOM 137 CG LEU A 22 91.394 101.750 -27.731 1.00 88.69 C
ATOM 138 CD1 LEU A 22 90.826 101.523 -26.368 1.00 86.76 C
ATOM 139 CD2 LEU A 22 92.743 101.075 -27.919 1.00 85.55 C
ATOM 140 N LYS A 23 89.616 100.096 -31.786 1.00 92.67 N
ATOM 141 CA LYS A 23 88.554 99.495 -32.594 1.00 93.09 C
ATOM 142 C LYS A 23 87.454 98.838 -31.746 1.00 92.92 C
ATOM 143 O LYS A 23 87.667 98.427 -30.632 1.00 92.80 O
ATOM 144 CB LYS A 23 89.147 98.513 -33.610 1.00 93.27 C
ATOM 145 CG LYS A 23 89.781 99.172 -34.889 1.00 96.71 C
ATOM 146 CD LYS A 23 91.355 99.437 -34.829 1.00101.77 C
ATOM 147 CE LYS A 23 92.043 99.672 -36.237 1.00103.15 C
ATOM 148 NZ LYS A 23 91.202 100.489 -37.219 1.00104.71 N
ATOM 149 N THR A 24 86.253 98.793 -32.282 1.00 93.75 N
ATOM 150 CA THR A 24 85.124 98.068 -31.710 1.00 93.97 C
ATOM 151 C THR A 24 84.416 97.522 -32.922 1.00 95.35 C
ATOM 152 O THR A 24 84.155 98.279 -33.864 1.00 96.03 O
ATOM 153 CB THR A 24 84.114 99.020 -31.048 1.00 93.32 C
ATOM 154 OG1 THR A 24 84.748 99.676 -29.962 1.00 93.01 O
ATOM 155 CG2 THR A 24 82.881 98.280 -30.545 1.00 91.50 C
ATOM 156 N PRO A 25 84.064 96.235 -32.918 1.00 96.18 N
ATOM 157 CA PRO A 25 82.987 95.840 -33.850 1.00 96.75 C
ATOM 158 C PRO A 25 81.959 96.990 -34.189 1.00 96.48 C
ATOM 159 O PRO A 25 81.646 97.216 -35.353 1.00 96.50 O
ATOM 160 CB PRO A 25 82.276 94.709 -33.079 1.00 96.82 C
ATOM 161 CG PRO A 25 82.694 94.944 -31.615 1.00 96.81 C
ATOM 162 CD PRO A 25 84.151 95.295 -31.801 1.00 96.61 C
ATOM 163 N GLY A 26 81.466 97.721 -33.197 1.00 95.95 N
ATOM 164 CA GLY A 26 80.493 98.734 -33.494 1.00 95.23 C
ATOM 165 C GLY A 26 80.971 100.150 -33.363 1.00 94.97 C
ATOM 166 O GLY A 26 80.225 100.978 -32.864 1.00 95.03 O
ATOM 167 N GLY A 27 82.188 100.461 -33.803 1.00 94.62 N
ATOM 168 CA GLY A 27 82.666 101.856 -33.675 1.00 94.24 C
ATOM 169 C GLY A 27 84.133 102.122 -33.346 1.00 93.52 C
ATOM 170 O GLY A 27 84.992 101.259 -33.577 1.00 93.08 O
ATOM 171 N PRO A 28 84.456 103.372 -32.918 1.00 92.99 N
ATOM 172 CA PRO A 28 85.791 103.522 -32.337 1.00 91.92 C
ATOM 173 C PRO A 28 85.682 104.356 -31.031 1.00 90.35 C
ATOM 174 O PRO A 28 84.666 105.069 -30.829 1.00 89.75 O
ATOM 175 CB PRO A 28 86.582 104.242 -33.472 1.00 91.59 C
ATOM 176 CG PRO A 28 85.470 105.083 -34.197 1.00 92.43 C
ATOM 177 CD PRO A 28 84.082 104.646 -33.570 1.00 92.98 C
ATOM 178 N VAL A 29 86.676 104.202 -30.141 1.00 88.52 N
ATOM 179 CA VAL A 29 86.712 104.953 -28.876 1.00 86.50 C
ATOM 180 C VAL A 29 88.084 105.509 -28.685 1.00 85.76 C
ATOM 181 O VAL A 29 89.058 104.895 -29.119 1.00 85.33 O
ATOM 182 CB VAL A 29 86.353 104.136 -27.594 1.00 86.20 C
ATOM 183 CG1 VAL A 29 85.804 105.067 -26.545 1.00 84.46 C
ATOM 184 CG2 VAL A 29 85.349 103.048 -27.855 1.00 84.44 C
ATOM 185 N SER A 30 88.129 106.678 -28.044 1.00 85.25 N
ATOM 186 CA SER A 30 89.369 107.382 -27.725 1.00 85.64 C
ATOM 187 C SER A 30 89.726 107.109 -26.269 1.00 84.98 C
ATOM 188 O SER A 30 88.940 107.432 -25.322 1.00 84.79 O
ATOM 189 CB SER A 30 89.265 108.907 -27.906 1.00 86.37 C
ATOM 190 OG SER A 30 88.381 109.301 -28.940 1.00 88.79 O
ATOM 191 N ALA A 31 90.929 106.539 -26.114 1.00 83.36 N
ATOM 192 CA ALA A 31 91.436 106.070 -24.847 1.00 81.20 C
ATOM 193 C ALA A 31 92.664 106.883 -24.372 1.00 79.73 C
ATOM 194 O ALA A 31 93.564 107.197 -25.147 1.00 79.52 O
ATOM 195 CB ALA A 31 91.761 104.623 -24.986 1.00 81.09 C
ATOM 196 N PHE A 32 92.666 107.215 -23.086 1.00 77.92 N
ATOM 197 CA PHE A 32 93.774 107.897 -22.417 1.00 76.12 C
ATOM 198 C PHE A 32 94.353 107.142 -21.246 1.00 73.89 C
ATOM 199 O PHE A 32 93.924 107.310 -20.098 1.00 73.89 O
ATOM 200 CB PHE A 32 93.319 109.274 -21.991 1.00 76.76 C
ATOM 201 CG PHE A 32 93.097 110.152 -23.154 1.00 79.38 C
ATOM 202 CD1 PHE A 32 94.128 110.371 -24.055 1.00 80.28 C
ATOM 203 CD2 PHE A 32 91.862 110.688 -23.412 1.00 81.76 C
ATOM 204 CE1 PHE A 32 93.948 111.139 -25.133 1.00 79.05 C
ATOM 205 CE2 PHE A 32 91.672 111.454 -24.511 1.00 81.09 C
ATOM 206 CZ PHE A 32 92.721 111.675 -25.375 1.00 80.72 C
ATOM 207 N LEU A 33 95.345 106.331 -21.563 1.00 70.70 N
ATOM 208 CA LEU A 33 95.808 105.326 -20.669 1.00 68.19 C
ATOM 209 C LEU A 33 97.040 105.736 -19.878 1.00 67.55 C
ATOM 210 O LEU A 33 98.099 106.079 -20.412 1.00 67.22 O
ATOM 211 CB LEU A 33 96.060 104.056 -21.450 1.00 67.56 C
ATOM 212 CG LEU A 33 94.852 103.583 -22.259 1.00 66.23 C
ATOM 213 CD1 LEU A 33 95.058 102.186 -22.838 1.00 64.52 C
ATOM 214 CD2 LEU A 33 93.616 103.594 -21.421 1.00 65.30 C
ATOM 215 N GLY A 34 96.897 105.705 -18.571 1.00 66.50 N
ATOM 216 CA GLY A 34 98.046 105.927 -17.749 1.00 65.05 C
ATOM 217 C GLY A 34 98.355 107.385 -17.642 1.00 63.63 C
ATOM 218 O GLY A 34 99.490 107.785 -17.735 1.00 63.50 O
ATOM 219 N ILE A 35 97.333 108.181 -17.429 1.00 62.93 N
ATOM 220 CA ILE A 35 97.560 109.519 -16.933 1.00 62.80 C
ATOM 221 C ILE A 35 98.036 109.492 -15.467 1.00 62.36 C
ATOM 222 O ILE A 35 97.361 108.905 -14.595 1.00 62.99 O
ATOM 223 CB ILE A 35 96.273 110.316 -16.976 1.00 63.17 C
ATOM 224 CG1 ILE A 35 95.741 110.368 -18.417 1.00 63.23 C
ATOM 225 CG2 ILE A 35 96.466 111.704 -16.282 1.00 62.97 C
ATOM 226 CD1 ILE A 35 94.245 110.648 -18.500 1.00 63.85 C
ATOM 227 N PRO A 36 99.190 110.120 -15.186 1.00 61.09 N
ATOM 228 CA PRO A 36 99.681 110.318 -13.837 1.00 60.60 C
ATOM 229 C PRO A 36 98.736 111.137 -13.015 1.00 60.32 C
ATOM 230 O PRO A 36 98.362 112.199 -13.448 1.00 60.59 O
ATOM 231 CB PRO A 36 100.928 111.166 -14.050 1.00 60.71 C
ATOM 232 CG PRO A 36 100.907 111.567 -15.418 1.00 60.42 C
ATOM 233 CD PRO A 36 100.189 110.526 -16.166 1.00 60.47 C
ATOM 234 N PHE A 37 98.373 110.672 -11.830 1.00 60.21 N
ATOM 235 CA PHE A 37 97.528 111.470 -10.968 1.00 60.12 C
ATOM 236 C PHE A 37 98.064 111.775 -9.566 1.00 61.47 C
ATOM 237 O PHE A 37 97.395 112.436 -8.762 1.00 61.87 O
ATOM 238 CB PHE A 37 96.141 110.847 -10.908 1.00 59.77 C
ATOM 239 CG PHE A 37 96.004 109.644 -9.997 1.00 56.58 C
ATOM 240 CD1 PHE A 37 95.704 109.816 -8.611 1.00 53.92 C
ATOM 241 CD2 PHE A 37 96.058 108.358 -10.534 1.00 54.08 C
ATOM 242 CE1 PHE A 37 95.529 108.714 -7.748 1.00 53.56 C
ATOM 243 CE2 PHE A 37 95.886 107.233 -9.706 1.00 54.82 C
ATOM 244 CZ PHE A 37 95.626 107.410 -8.283 1.00 54.84 C
ATOM 245 N ALA A 38 99.252 111.261 -9.269 1.00 62.68 N
ATOM 246 CA ALA A 38 99.953 111.534 -8.019 1.00 63.78 C
ATOM 247 C ALA A 38 101.467 111.465 -8.260 1.00 64.75 C
ATOM 248 O ALA A 38 101.921 110.847 -9.234 1.00 65.20 O
ATOM 249 CB ALA A 38 99.544 110.552 -6.932 1.00 63.63 C
ATOM 250 N GLU A 39 102.239 112.124 -7.389 1.00 65.15 N
ATOM 251 CA GLU A 39 103.690 112.006 -7.392 1.00 64.90 C
ATOM 252 C GLU A 39 104.008 110.582 -6.915 1.00 63.43 C
ATOM 253 O GLU A 39 103.299 110.020 -6.061 1.00 62.84 O
ATOM 254 CB GLU A 39 104.353 113.115 -6.534 1.00 65.73 C
ATOM 255 CG GLU A 39 104.375 114.506 -7.206 1.00 70.75 C
ATOM 256 CD GLU A 39 105.117 114.542 -8.601 1.00 81.76 C
ATOM 257 OE1 GLU A 39 105.969 113.663 -8.944 1.00 87.31 O
ATOM 258 OE2 GLU A 39 104.867 115.482 -9.396 1.00 86.36 O
ATOM 259 N PRO A 40 105.021 109.959 -7.524 1.00 62.24 N
ATOM 260 CA PRO A 40 105.376 108.607 -7.129 1.00 62.01 C
ATOM 261 C PRO A 40 105.522 108.421 -5.621 1.00 61.60 C
ATOM 262 O PRO A 40 106.254 109.154 -4.953 1.00 62.21 O
ATOM 263 CB PRO A 40 106.683 108.392 -7.867 1.00 61.97 C
ATOM 264 CG PRO A 40 106.432 109.143 -9.172 1.00 61.27 C
ATOM 265 CD PRO A 40 105.702 110.363 -8.768 1.00 61.58 C
ATOM 266 N PRO A 41 104.805 107.465 -5.084 1.00 61.16 N
ATOM 267 CA PRO A 41 104.823 107.193 -3.673 1.00 62.35 C
ATOM 268 C PRO A 41 106.002 106.305 -3.333 1.00 63.49 C
ATOM 269 O PRO A 41 105.826 105.143 -2.906 1.00 63.86 O
ATOM 270 CB PRO A 41 103.517 106.451 -3.454 1.00 62.72 C
ATOM 271 CG PRO A 41 103.251 105.798 -4.738 1.00 62.00 C
ATOM 272 CD PRO A 41 103.969 106.533 -5.827 1.00 61.06 C
ATOM 273 N MET A 42 107.196 106.862 -3.532 1.00 64.48 N
ATOM 274 CA MET A 42 108.449 106.119 -3.464 1.00 64.48 C
ATOM 275 C MET A 42 109.375 106.702 -2.414 1.00 65.18 C
ATOM 276 O MET A 42 109.230 107.860 -2.006 1.00 65.32 O
ATOM 277 CB MET A 42 109.148 106.158 -4.800 1.00 63.92 C
ATOM 278 CG MET A 42 108.301 105.785 -5.925 1.00 63.00 C
ATOM 279 SD MET A 42 109.257 104.662 -6.947 1.00 65.86 S
ATOM 280 CE MET A 42 109.999 105.790 -8.262 1.00 69.22 C
ATOM 281 N GLY A 43 110.327 105.870 -1.991 1.00 66.33 N
ATOM 282 CA GLY A 43 111.320 106.234 -0.988 1.00 66.66 C
ATOM 283 C GLY A 43 110.679 106.617 0.316 1.00 66.59 C
ATOM 284 O GLY A 43 110.044 105.762 0.962 1.00 67.73 O
ATOM 285 N PRO A 44 110.823 107.898 0.695 1.00 65.95 N
ATOM 286 CA PRO A 44 110.333 108.404 1.936 1.00 65.77 C
ATOM 287 C PRO A 44 108.865 108.505 1.844 1.00 66.16 C
ATOM 288 O PRO A 44 108.273 109.072 2.728 1.00 67.76 O
ATOM 289 CB PRO A 44 110.856 109.842 1.960 1.00 65.56 C
ATOM 290 CG PRO A 44 110.806 110.260 0.577 1.00 66.56 C
ATOM 291 CD PRO A 44 111.300 108.991 -0.166 1.00 66.36 C
ATOM 292 N ARG A 45 108.253 108.042 0.763 1.00 66.14 N
ATOM 293 CA ARG A 45 106.809 108.218 0.631 1.00 65.51 C
ATOM 294 C ARG A 45 106.049 106.935 0.695 1.00 63.65 C
ATOM 295 O ARG A 45 104.855 106.949 0.891 1.00 63.57 O
ATOM 296 CB ARG A 45 106.457 108.973 -0.617 1.00 66.06 C
ATOM 297 CG ARG A 45 106.415 110.390 -0.331 1.00 70.13 C
ATOM 298 CD ARG A 45 107.031 111.024 -1.501 1.00 81.11 C
ATOM 299 NE ARG A 45 106.392 112.302 -1.804 1.00 90.04 N
ATOM 300 CZ ARG A 45 106.675 113.027 -2.887 1.00 95.87 C
ATOM 301 NH1 ARG A 45 106.040 114.177 -3.102 1.00 97.81 N
ATOM 302 NH2 ARG A 45 107.589 112.593 -3.773 1.00 99.12 N
ATOM 303 N ARG A 46 106.742 105.829 0.532 1.00 61.69 N
ATOM 304 CA ARG A 46 106.148 104.568 0.831 1.00 60.91 C
ATOM 305 C ARG A 46 105.331 104.699 2.139 1.00 60.93 C
ATOM 306 O ARG A 46 105.828 105.272 3.071 1.00 62.01 O
ATOM 307 CB ARG A 46 107.243 103.530 0.984 1.00 60.07 C
ATOM 308 CG ARG A 46 106.666 102.234 1.319 1.00 58.37 C
ATOM 309 CD ARG A 46 107.670 101.237 1.419 1.00 55.81 C
ATOM 310 NE ARG A 46 108.479 101.093 0.231 1.00 57.65 N
ATOM 311 CZ ARG A 46 109.381 100.126 0.150 1.00 59.62 C
ATOM 312 NH1 ARG A 46 109.535 99.301 1.171 1.00 60.59 N
ATOM 313 NH2 ARG A 46 110.131 99.961 -0.906 1.00 59.81 N
ATOM 314 N PHE A 47 104.092 104.192 2.193 1.00 60.38 N
ATOM 315 CA PHE A 47 103.183 104.279 3.364 1.00 58.97 C
ATOM 316 C PHE A 47 102.436 105.564 3.644 1.00 58.97 C
ATOM 317 O PHE A 47 101.573 105.606 4.512 1.00 58.21 O
ATOM 318 CB PHE A 47 103.892 103.848 4.612 1.00 58.35 C
ATOM 319 CG PHE A 47 104.581 102.596 4.452 1.00 57.79 C
ATOM 320 CD1 PHE A 47 103.917 101.502 3.981 1.00 58.87 C
ATOM 321 CD2 PHE A 47 105.891 102.484 4.759 1.00 58.43 C
ATOM 322 CE1 PHE A 47 104.560 100.287 3.839 1.00 59.97 C
ATOM 323 CE2 PHE A 47 106.538 101.272 4.610 1.00 59.51 C
ATOM 324 CZ PHE A 47 105.875 100.178 4.128 1.00 58.87 C
ATOM 325 N LEU A 48 102.761 106.594 2.897 1.00 60.09 N
ATOM 326 CA LEU A 48 102.305 107.948 3.172 1.00 62.47 C
ATOM 327 C LEU A 48 101.113 108.243 2.311 1.00 63.49 C
ATOM 328 O LEU A 48 100.946 107.568 1.326 1.00 64.64 O
ATOM 329 CB LEU A 48 103.443 108.938 2.819 1.00 63.14 C
ATOM 330 CG LEU A 48 104.227 109.599 3.952 1.00 62.92 C