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HEADER LIGASE 12-JAN-01 1HXD
TITLE CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND
TITLE 2 BIOTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIRA BIFUNCTIONAL PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BIOTIN REPRESSOR;
COMPND 5 EC: 6.3.4.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIGASE, REPRESSOR, BIOTIN, DNA-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KWON,E.D.STREAKER,S.RUPARELIA,D.BECKETT
REVDAT 2 24-FEB-09 1HXD 1 VERSN
REVDAT 1 30-MAY-01 1HXD 0
JRNL AUTH L.H.WEAVER,K.KWON,D.BECKETT,B.W.MATTHEWS
JRNL TITL COREPRESSOR-INDUCED ORGANIZATION AND ASSEMBLY OF
JRNL TITL 2 THE BIOTIN REPRESSOR: A MODEL FOR ALLOSTERIC
JRNL TITL 3 ACTIVATION OF A TRANSCRIPTIONAL REGULATOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 6045 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11353844
JRNL DOI 10.1073/PNAS.111128198
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.KWON,E.D.STREAKER,S.RUPARELIA,D.BECKETT
REMARK 1 TITL MULTIPLE DISORDERED LOOPS FUNCTION IN
REMARK 1 TITL 2 COREPRESOR-INDUCED DIMERIZATION OF THE BIOTIN
REMARK 1 TITL 3 REPRESSOR
REMARK 1 REF J.MOL.BIOL. V. 304 821 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.4249
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.P.WILSON,L.M.SHEWCHUK,R.G.BRENNAN,A.J.OTSUKA,
REMARK 1 AUTH 2 B.W.MATTHEWS
REMARK 1 TITL E. COLI BIOTIN HOLOENZYME SYNTHETASE/BIO REPRESSOR
REMARK 1 TITL 2 CRYSTAL STRUCTURE DELINEATES THE BIOTIN- AND
REMARK 1 TITL 3 DNA-BINDING DOMAINS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 9257 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 3 NUMBER OF REFLECTIONS : 26762
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1890
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 26762
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4712
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.018 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.800 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HXD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-01.
REMARK 100 THE RCSB ID CODE IS RCSB012656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : UCSD MARK II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26762
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 13.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1BIA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 71.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.60000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 52.45000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.45000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.45000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.45000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.60000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.45000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.45000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.60000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.45000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.45000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 MET A 1
REMARK 465 LYS A 2
REMARK 465 ASP A 3
REMARK 465 ARG A 212
REMARK 465 ARG A 213
REMARK 465 VAL A 214
REMARK 465 GLU A 215
REMARK 465 GLU A 216
REMARK 465 SER A 217
REMARK 465 VAL A 218
REMARK 465 VAL A 219
REMARK 465 ASN A 220
REMARK 465 SER A 318
REMARK 465 ALA A 319
REMARK 465 GLU A 320
REMARK 465 LYS A 321
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 ASP B 3
REMARK 465 ARG B 212
REMARK 465 ARG B 213
REMARK 465 VAL B 214
REMARK 465 GLU B 215
REMARK 465 GLU B 216
REMARK 465 SER B 217
REMARK 465 VAL B 218
REMARK 465 VAL B 219
REMARK 465 ASN B 220
REMARK 465 SER B 318
REMARK 465 ALA B 319
REMARK 465 GLU B 320
REMARK 465 LYS B 321
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 N PHE B 124 O HOH B 1604 2.16
REMARK 500 OD1 ASP A 269 O HOH A 606 2.18
REMARK 500 O ALA A 69 N LEU A 73 2.19
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 18 CD GLU A 18 OE2 0.068
REMARK 500 GLU A 23 CD GLU A 23 OE2 0.076
REMARK 500 GLU A 27 CD GLU A 27 OE2 0.082
REMARK 500 GLU A 62 CD GLU A 62 OE2 0.075
REMARK 500 ASP A 96 CG ASP A 96 OD2 0.151
REMARK 500 GLU A 100 CD GLU A 100 OE2 0.128
REMARK 500 GLU A 140 CD GLU A 140 OE2 0.071
REMARK 500 GLU A 159 CD GLU A 159 OE2 0.071
REMARK 500 GLU A 245 CD GLU A 245 OE2 0.070
REMARK 500 GLU A 251 CD GLU A 251 OE2 0.079
REMARK 500 GLU A 256 CD GLU A 256 OE2 0.079
REMARK 500 GLU A 266 CD GLU A 266 OE2 0.077
REMARK 500 GLU A 284 CD GLU A 284 OE2 0.068
REMARK 500 GLU A 313 CD GLU A 313 OE2 0.071
REMARK 500 GLU B 23 CD GLU B 23 OE2 0.078
REMARK 500 GLU B 27 CD GLU B 27 OE2 0.073
REMARK 500 GLU B 62 CD GLU B 62 OE2 0.077
REMARK 500 GLU B 100 CD GLU B 100 OE2 0.094
REMARK 500 GLU B 140 CD GLU B 140 OE2 0.074
REMARK 500 GLU B 245 CD GLU B 245 OE2 0.067
REMARK 500 GLU B 251 CD GLU B 251 OE2 0.074
REMARK 500 GLU B 254 CD GLU B 254 OE2 0.095
REMARK 500 GLU B 256 CD GLU B 256 OE2 0.080
REMARK 500 GLU B 284 CD GLU B 284 OE2 0.067
REMARK 500 GLU B 313 CD GLU B 313 OE2 0.077
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 23 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 GLU A 23 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 45 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 45 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 49 N - CA - CB ANGL. DEV. = 13.6 DEGREES
REMARK 500 LEU A 60 N - CA - CB ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP A 77 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 77 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PRO A 85 C - N - CD ANGL. DEV. = -29.5 DEGREES
REMARK 500 ASP A 88 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 THR A 90 CA - CB - CG2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG A 119 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASN A 175 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 ASP A 181 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 182 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASP A 197 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 LEU A 233 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TYR A 261 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 264 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 269 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 269 CB - CG - OD2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ASP A 293 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 303 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 303 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 317 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 49 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 49 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 VAL B 50 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 ASP B 77 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 PRO B 85 C - N - CD ANGL. DEV. = -17.8 DEGREES
REMARK 500 TYR B 93 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP B 96 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 96 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP B 105 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP B 105 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG B 118 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 118 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 121 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 PHE B 124 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU B 149 CB - CA - C ANGL. DEV. = -14.8 DEGREES
REMARK 500 ASP B 167 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 167 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASN B 175 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 ASP B 176 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 181 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 181 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR B 195 CA - CB - CG2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP B 197 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 58 ANGLE DEVIATIONS.
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 THR A 5 -85.45 -51.86
REMARK 500 VAL A 6 -49.14 -28.44
REMARK 500 LEU A 10 -72.12 -53.90
REMARK 500 ILE A 11 -39.48 -38.12
REMARK 500 PRO A 54 -97.30 32.55
REMARK 500 LYS A 56 -75.54 -94.14
REMARK 500 ALA A 69 -61.45 -29.39
REMARK 500 GLN A 75 -137.47 -53.54
REMARK 500 LEU A 76 -41.91 75.42
REMARK 500 ASP A 77 -154.56 85.12
REMARK 500 SER A 89 134.62 -179.28
REMARK 500 ASP A 96 -5.16 -57.51
REMARK 500 ARG A 97 28.22 -145.87
REMARK 500 ARG A 119 57.13 39.73
REMARK 500 PHE A 124 97.00 78.87
REMARK 500 ALA A 145 -125.84 148.23
REMARK 500 ALA A 146 -61.73 65.35
REMARK 500 ILE A 147 -79.75 -39.02
REMARK 500 ALA A 166 82.41 -25.06
REMARK 500 ASN A 175 41.29 -144.54
REMARK 500 ASP A 197 140.37 169.57
REMARK 500 MET A 209 -73.86 -90.22
REMARK 500 ALA A 259 -44.26 -28.27
REMARK 500 TYR A 261 -104.62 -88.11
REMARK 500 LEU A 262 -72.54 47.84
REMARK 500 LYS A 294 -9.42 -52.82
REMARK 500 ASP A 303 89.23 56.97
REMARK 500 MET A 310 46.43 -104.83
REMARK 500 VAL B 6 -70.30 -52.74
REMARK 500 ALA B 15 -16.61 -48.01
REMARK 500 GLU B 23 -71.41 -54.79
REMARK 500 PRO B 54 -64.92 -15.26
REMARK 500 ASP B 77 129.40 89.10
REMARK 500 ARG B 97 27.76 -142.92
REMARK 500 ARG B 121 133.24 -30.76
REMARK 500 TRP B 123 -75.55 -88.23
REMARK 500 PHE B 124 86.10 112.63
REMARK 500 ASN B 130 -161.74 -121.68
REMARK 500 PRO B 143 66.38 -41.53
REMARK 500 ALA B 144 110.51 -170.54
REMARK 500 ALA B 145 -79.58 167.67
REMARK 500 ALA B 146 -104.09 42.12
REMARK 500 LEU B 149 -69.95 -28.98
REMARK 500 ILE B 153 -76.96 -54.26
REMARK 500 ALA B 166 68.36 -104.23
REMARK 500 LYS B 194 -149.64 -121.54
REMARK 500 GLN B 255 -116.52 -76.59
REMARK 500 GLU B 256 -5.22 -38.15
REMARK 500 ALA B 259 -90.36 -35.29
REMARK 500 PRO B 260 -8.58 -46.42
REMARK 500 ASP B 269 118.73 -34.09
REMARK 500 ASP B 282 50.28 -162.66
REMARK 500 ASP B 303 69.58 29.76
REMARK 500 ILE B 314 -156.73 -74.20
REMARK 500 SER B 315 148.04 146.04
REMARK 500 LEU B 316 146.37 -28.07
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 RESIDUE BTN A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTN B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BIA RELATED DB: PDB
REMARK 900 BIRA BIFUNCTIONAL PROTEIN (ACTS AS BIOTIN OPERON REPRESSOR
REMARK 900 AND BIOTIN HOLOENZYME SYNTHETASE) (E.C.6.3.4.15)
REMARK 900 RELATED ID: 1BIB RELATED DB: PDB
REMARK 900 BIRA BIFUNCTIONAL PROTEIN (ACTS AS BIOTIN OPERON REPRESSOR
REMARK 900 AND BIOTIN HOLOENZYME SYNTHETASE) (E.C. 6.3.4.15) COMPLEX
REMARK 900 WITH BIOTINYLATED LYSINE
DBREF 1HXD A 1 321 UNP P06709 BIRA_ECOLI 1 321
DBREF 1HXD B 1 321 UNP P06709 BIRA_ECOLI 1 321
SEQRES 1 A 321 MET LYS ASP ASN THR VAL PRO LEU LYS LEU ILE ALA LEU
SEQRES 2 A 321 LEU ALA ASN GLY GLU PHE HIS SER GLY GLU GLN LEU GLY
SEQRES 3 A 321 GLU THR LEU GLY MET SER ARG ALA ALA ILE ASN LYS HIS
SEQRES 4 A 321 ILE GLN THR LEU ARG ASP TRP GLY VAL ASP VAL PHE THR
SEQRES 5 A 321 VAL PRO GLY LYS GLY TYR SER LEU PRO GLU PRO ILE GLN
SEQRES 6 A 321 LEU LEU ASN ALA LYS GLN ILE LEU GLY GLN LEU ASP GLY
SEQRES 7 A 321 GLY SER VAL ALA VAL LEU PRO VAL ILE ASP SER THR ASN
SEQRES 8 A 321 GLN TYR LEU LEU ASP ARG ILE GLY GLU LEU LYS SER GLY
SEQRES 9 A 321 ASP ALA CYS ILE ALA GLU TYR GLN GLN ALA GLY ARG GLY
SEQRES 10 A 321 ARG ARG GLY ARG LYS TRP PHE SER PRO PHE GLY ALA ASN
SEQRES 11 A 321 LEU TYR LEU SER MET PHE TRP ARG LEU GLU GLN GLY PRO
SEQRES 12 A 321 ALA ALA ALA ILE GLY LEU SER LEU VAL ILE GLY ILE VAL
SEQRES 13 A 321 MET ALA GLU VAL LEU ARG LYS LEU GLY ALA ASP LYS VAL
SEQRES 14 A 321 ARG VAL LYS TRP PRO ASN ASP LEU TYR LEU GLN ASP ARG
SEQRES 15 A 321 LYS LEU ALA GLY ILE LEU VAL GLU LEU THR GLY LYS THR
SEQRES 16 A 321 GLY ASP ALA ALA GLN ILE VAL ILE GLY ALA GLY ILE ASN
SEQRES 17 A 321 MET ALA MET ARG ARG VAL GLU GLU SER VAL VAL ASN GLN
SEQRES 18 A 321 GLY TRP ILE THR LEU GLN GLU ALA GLY ILE ASN LEU ASP
SEQRES 19 A 321 ARG ASN THR LEU ALA ALA MET LEU ILE ARG GLU LEU ARG
SEQRES 20 A 321 ALA ALA LEU GLU LEU PHE GLU GLN GLU GLY LEU ALA PRO
SEQRES 21 A 321 TYR LEU SER ARG TRP GLU LYS LEU ASP ASN PHE ILE ASN
SEQRES 22 A 321 ARG PRO VAL LYS LEU ILE ILE GLY ASP LYS GLU ILE PHE
SEQRES 23 A 321 GLY ILE SER ARG GLY ILE ASP LYS GLN GLY ALA LEU LEU
SEQRES 24 A 321 LEU GLU GLN ASP GLY ILE ILE LYS PRO TRP MET GLY GLY
SEQRES 25 A 321 GLU ILE SER LEU ARG SER ALA GLU LYS
SEQRES 1 B 321 MET LYS ASP ASN THR VAL PRO LEU LYS LEU ILE ALA LEU
SEQRES 2 B 321 LEU ALA ASN GLY GLU PHE HIS SER GLY GLU GLN LEU GLY
SEQRES 3 B 321 GLU THR LEU GLY MET SER ARG ALA ALA ILE ASN LYS HIS
SEQRES 4 B 321 ILE GLN THR LEU ARG ASP TRP GLY VAL ASP VAL PHE THR
SEQRES 5 B 321 VAL PRO GLY LYS GLY TYR SER LEU PRO GLU PRO ILE GLN
SEQRES 6 B 321 LEU LEU ASN ALA LYS GLN ILE LEU GLY GLN LEU ASP GLY
SEQRES 7 B 321 GLY SER VAL ALA VAL LEU PRO VAL ILE ASP SER THR ASN
SEQRES 8 B 321 GLN TYR LEU LEU ASP ARG ILE GLY GLU LEU LYS SER GLY
SEQRES 9 B 321 ASP ALA CYS ILE ALA GLU TYR GLN GLN ALA GLY ARG GLY
SEQRES 10 B 321 ARG ARG GLY ARG LYS TRP PHE SER PRO PHE GLY ALA ASN
SEQRES 11 B 321 LEU TYR LEU SER MET PHE TRP ARG LEU GLU GLN GLY PRO
SEQRES 12 B 321 ALA ALA ALA ILE GLY LEU SER LEU VAL ILE GLY ILE VAL
SEQRES 13 B 321 MET ALA GLU VAL LEU ARG LYS LEU GLY ALA ASP LYS VAL
SEQRES 14 B 321 ARG VAL LYS TRP PRO ASN ASP LEU TYR LEU GLN ASP ARG
SEQRES 15 B 321 LYS LEU ALA GLY ILE LEU VAL GLU LEU THR GLY LYS THR
SEQRES 16 B 321 GLY ASP ALA ALA GLN ILE VAL ILE GLY ALA GLY ILE ASN
SEQRES 17 B 321 MET ALA MET ARG ARG VAL GLU GLU SER VAL VAL ASN GLN
SEQRES 18 B 321 GLY TRP ILE THR LEU GLN GLU ALA GLY ILE ASN LEU ASP
SEQRES 19 B 321 ARG ASN THR LEU ALA ALA MET LEU ILE ARG GLU LEU ARG
SEQRES 20 B 321 ALA ALA LEU GLU LEU PHE GLU GLN GLU GLY LEU ALA PRO
SEQRES 21 B 321 TYR LEU SER ARG TRP GLU LYS LEU ASP ASN PHE ILE ASN
SEQRES 22 B 321 ARG PRO VAL LYS LEU ILE ILE GLY ASP LYS GLU ILE PHE
SEQRES 23 B 321 GLY ILE SER ARG GLY ILE ASP LYS GLN GLY ALA LEU LEU
SEQRES 24 B 321 LEU GLU GLN ASP GLY ILE ILE LYS PRO TRP MET GLY GLY
SEQRES 25 B 321 GLU ILE SER LEU ARG SER ALA GLU LYS
HET BTN A 500 16
HET BTN B 501 16
HETNAM BTN BIOTIN
FORMUL 3 BTN 2(C10 H16 N2 O3 S)
FORMUL 5 HOH *59(H2 O)
HELIX 1 1 ASN A 4 ALA A 15 1 12
HELIX 2 2 GLY A 22 LEU A 29 1 8
HELIX 3 3 SER A 32 ASP A 45 1 14
HELIX 4 4 ASN A 68 GLN A 75 1 8
HELIX 5 5 SER A 89 ASP A 96 1 8
HELIX 6 6 ALA A 146 GLY A 165 1 20
HELIX 7 7 LEU A 226 GLY A 230 5 5
HELIX 8 8 ASP A 234 GLY A 257 1 24
HELIX 9 9 LEU A 262 ASP A 269 1 8
HELIX 10 10 VAL B 6 ALA B 15 1 10
HELIX 11 11 GLY B 22 GLY B 30 1 9
HELIX 12 12 SER B 32 TRP B 46 1 15
HELIX 13 13 ASN B 68 GLN B 75 1 8
HELIX 14 14 SER B 89 ASP B 96 1 8
HELIX 15 15 ARG B 97 LEU B 101 5 5
HELIX 16 16 GLY B 117 ARG B 121 5 5
HELIX 17 17 ALA B 146 LEU B 164 1 19
HELIX 18 18 ASP B 234 GLN B 255 1 22
HELIX 19 19 LEU B 258 PRO B 260 5 3
HELIX 20 20 TYR B 261 ASP B 269 1 9
SHEET 1 A 3 HIS A 20 SER A 21 0
SHEET 2 A 3 GLY A 57 SER A 59 -1 N TYR A 58 O HIS A 20
SHEET 3 A 3 PHE A 51 VAL A 53 -1 N PHE A 51 O SER A 59
SHEET 1 B 7 VAL A 81 VAL A 83 0
SHEET 2 B 7 ALA A 106 ILE A 108 1 O ALA A 106 N ALA A 82
SHEET 3 B 7 LEU A 131 LEU A 139 -1 O SER A 134 N CYS A 107
SHEET 4 B 7 ALA A 199 ILE A 207 -1 O ALA A 199 N LEU A 139
SHEET 5 B 7 ARG A 182 THR A 192 -1 N GLY A 186 O GLY A 206
SHEET 6 B 7 ASP A 176 LEU A 179 -1 O LEU A 177 N LEU A 184
SHEET 7 B 7 ARG A 170 LYS A 172 -1 O ARG A 170 N TYR A 178
SHEET 1 C 5 ILE A 306 TRP A 309 0
SHEET 2 C 5 ALA A 297 GLU A 301 -1 N LEU A 298 O TRP A 309
SHEET 3 C 5 LYS A 283 ASP A 293 -1 O ILE A 288 N GLU A 301
SHEET 4 C 5 PRO A 275 ILE A 280 -1 N VAL A 276 O GLY A 287
SHEET 5 C 5 GLU A 313 LEU A 316 -1 O GLU A 313 N ILE A 279
SHEET 1 D 3 HIS B 20 SER B 21 0
SHEET 2 D 3 GLY B 57 SER B 59 -1 O TYR B 58 N HIS B 20
SHEET 3 D 3 PHE B 51 VAL B 53 -1 N PHE B 51 O SER B 59
SHEET 1 E 7 VAL B 81 ILE B 87 0
SHEET 2 E 7 ALA B 106 GLN B 112 1 O ALA B 106 N ALA B 82
SHEET 3 E 7 LEU B 131 LEU B 139 -1 O TYR B 132 N ALA B 109
SHEET 4 E 7 ALA B 199 ILE B 207 -1 O ALA B 199 N LEU B 139
SHEET 5 E 7 ARG B 182 THR B 192 -1 O GLY B 186 N GLY B 206
SHEET 6 E 7 ASP B 176 LEU B 179 -1 O LEU B 177 N LEU B 184
SHEET 7 E 7 ARG B 170 LYS B 172 -1 N ARG B 170 O TYR B 178
SHEET 1 F 5 ILE B 305 TRP B 309 0
SHEET 2 F 5 LEU B 298 GLN B 302 -1 N LEU B 298 O TRP B 309
SHEET 3 F 5 LYS B 283 ILE B 292 -1 O ILE B 288 N GLU B 301
SHEET 4 F 5 PRO B 275 ILE B 280 -1 N VAL B 276 O GLY B 287
SHEET 5 F 5 SER B 315 LEU B 316 -1 O SER B 315 N LYS B 277
CISPEP 1 TRP A 173 PRO A 174 0 6.58
CISPEP 2 TRP B 173 PRO B 174 0 1.86
SITE 1 AC1 17 SER A 89 THR A 90 ASN A 91 GLN A 112
SITE 2 AC1 17 ARG A 116 GLY A 117 ARG A 118 TRP A 123
SITE 3 AC1 17 LEU A 133 SER A 134 LYS A 183 GLY A 186
SITE 4 AC1 17 ILE A 187 LEU A 188 GLY A 204 ALA A 205
SITE 5 AC1 17 GLY A 206
SITE 1 AC2 16 SER B 89 THR B 90 GLN B 112 GLY B 115
SITE 2 AC2 16 ARG B 116 GLY B 117 ARG B 118 ARG B 121
SITE 3 AC2 16 TRP B 123 TYR B 132 LYS B 183 GLY B 186
SITE 4 AC2 16 ILE B 187 LEU B 188 ALA B 205 GLY B 206
CRYST1 104.900 108.900 143.200 90.00 90.00 90.00 C 2 2 21 16
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 0.009533 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009183 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006983 0.00000
ATOM 1 N ASN A 4 66.039 30.785 50.117 1.00 88.31 N
ATOM 2 CA ASN A 4 66.049 29.799 51.200 1.00 85.31 C
ATOM 3 C ASN A 4 67.440 29.525 51.712 1.00 73.80 C
ATOM 4 O ASN A 4 67.713 28.613 52.474 1.00 78.35 O
ATOM 5 CB ASN A 4 65.401 28.459 50.827 1.00 85.69 C
ATOM 6 CG ASN A 4 64.012 28.337 51.410 1.00100.00 C
ATOM 7 OD1 ASN A 4 63.343 27.285 51.281 1.00100.00 O
ATOM 8 ND2 ASN A 4 63.571 29.431 52.045 1.00100.00 N
ATOM 9 N THR A 5 68.304 30.361 51.263 1.00 55.01 N
ATOM 10 CA THR A 5 69.682 30.333 51.596 1.00 50.44 C
ATOM 11 C THR A 5 70.020 30.292 53.044 1.00 43.26 C
ATOM 12 O THR A 5 70.346 29.238 53.578 1.00 48.03 O
ATOM 13 CB THR A 5 70.243 31.639 51.096 1.00 85.46 C
ATOM 14 OG1 THR A 5 69.127 32.511 50.888 1.00100.00 O
ATOM 15 CG2 THR A 5 71.040 31.370 49.828 1.00 59.92 C
ATOM 16 N VAL A 6 70.056 31.527 53.590 1.00 41.42 N
ATOM 17 CA VAL A 6 70.399 31.900 54.973 1.00 39.17 C
ATOM 18 C VAL A 6 70.097 30.846 55.984 1.00 32.61 C
ATOM 19 O VAL A 6 70.935 30.535 56.858 1.00 31.19 O
ATOM 20 CB VAL A 6 69.670 33.126 55.508 1.00 42.04 C
ATOM 21 CG1 VAL A 6 70.438 33.687 56.690 1.00 37.94 C
ATOM 22 CG2 VAL A 6 69.525 34.160 54.399 1.00 44.74 C
ATOM 23 N PRO A 7 68.837 30.356 55.854 1.00 26.59 N
ATOM 24 CA PRO A 7 68.359 29.306 56.720 1.00 17.87 C
ATOM 25 C PRO A 7 69.413 28.212 56.653 1.00 29.46 C
ATOM 26 O PRO A 7 70.124 27.890 57.627 1.00 34.51 O
ATOM 27 CB PRO A 7 66.928 29.038 56.241 1.00 19.78 C
ATOM 28 CG PRO A 7 66.482 30.238 55.414 1.00 27.85 C
ATOM 29 CD PRO A 7 67.738 30.937 54.983 1.00 23.14 C
ATOM 30 N LEU A 8 69.612 27.766 55.432 1.00 30.17 N
ATOM 31 CA LEU A 8 70.555 26.734 55.141 1.00 33.33 C
ATOM 32 C LEU A 8 71.934 27.051 55.691 1.00 34.71 C
ATOM 33 O LEU A 8 72.656 26.126 56.092 1.00 24.53 O
ATOM 34 CB LEU A 8 70.422 26.374 53.646 1.00 37.58 C
ATOM 35 CG LEU A 8 69.060 25.700 53.305 1.00 45.17 C
ATOM 36 CD1 LEU A 8 68.623 25.981 51.869 1.00 49.62 C
ATOM 37 CD2 LEU A 8 69.098 24.175 53.392 1.00 44.22 C
ATOM 38 N LYS A 9 72.281 28.354 55.792 1.00 38.71 N
ATOM 39 CA LYS A 9 73.573 28.776 56.388 1.00 40.89 C
ATOM 40 C LYS A 9 73.571 28.708 57.909 1.00 33.38 C
ATOM 41 O LYS A 9 74.512 28.227 58.596 1.00 28.54 O
ATOM 42 CB LYS A 9 73.966 30.204 56.041 1.00 53.62 C
ATOM 43 CG LYS A 9 74.529 30.442 54.622 1.00100.00 C
ATOM 44 CD LYS A 9 75.859 31.243 54.596 1.00100.00 C
ATOM 45 CE LYS A 9 75.976 32.414 53.588 1.00100.00 C
ATOM 46 NZ LYS A 9 77.219 33.238 53.708 1.00 73.35 N
ATOM 47 N LEU A 10 72.467 29.220 58.424 1.00 23.92 N
ATOM 48 CA LEU A 10 72.276 29.204 59.831 1.00 24.72 C
ATOM 49 C LEU A 10 72.426 27.870 60.329 1.00 25.92 C
ATOM 50 O LEU A 10 73.412 27.525 60.897 1.00 30.21 O
ATOM 51 CB LEU A 10 70.882 29.554 60.172 1.00 29.50 C
ATOM 52 CG LEU A 10 70.784 31.036 60.114 1.00 38.99 C
ATOM 53 CD1 LEU A 10 69.302 31.335 60.345 1.00 38.07 C
ATOM 54 CD2 LEU A 10 71.795 31.510 61.169 1.00 33.35 C
ATOM 55 N ILE A 11 71.412 27.147 59.984 1.00 22.15 N
ATOM 56 CA ILE A 11 71.311 25.756 60.261 1.00 23.58 C
ATOM 57 C ILE A 11 72.671 25.093 60.097 1.00 27.97 C
ATOM 58 O ILE A 11 73.154 24.285 60.910 1.00 25.70 O
ATOM 59 CB ILE A 11 70.267 25.246 59.304 1.00 29.19 C
ATOM 60 CG1 ILE A 11 69.836 23.846 59.648 1.00 38.84 C
ATOM 61 CG2 ILE A 11 70.826 25.197 57.905 1.00 30.11 C
ATOM 62 CD1 ILE A 11 70.414 23.363 60.974 1.00 63.06 C
ATOM 63 N ALA A 12 73.343 25.559 59.072 1.00 29.02 N
ATOM 64 CA ALA A 12 74.648 25.050 58.751 1.00 27.56 C
ATOM 65 C ALA A 12 75.609 25.341 59.883 1.00 35.50 C
ATOM 66 O ALA A 12 76.537 24.581 60.149 1.00 39.77 O
ATOM 67 CB ALA A 12 75.071 25.580 57.400 1.00 27.43 C
ATOM 68 N LEU A 13 75.382 26.403 60.625 1.00 30.48 N
ATOM 69 CA LEU A 13 76.286 26.613 61.762 1.00 27.84 C
ATOM 70 C LEU A 13 75.756 26.218 63.082 1.00 18.22 C
ATOM 71 O LEU A 13 76.443 26.026 64.036 1.00 24.01 O
ATOM 72 CB LEU A 13 76.677 28.041 61.988 1.00 30.66 C
ATOM 73 CG LEU A 13 75.916 28.853 61.010 1.00 43.27 C
ATOM 74 CD1 LEU A 13 74.887 29.649 61.820 1.00 56.96 C
ATOM 75 CD2 LEU A 13 76.964 29.673 60.301 1.00 39.02 C
ATOM 76 N LEU A 14 74.504 26.152 63.203 1.00 24.18 N
ATOM 77 CA LEU A 14 74.096 25.748 64.490 1.00 27.24 C
ATOM 78 C LEU A 14 74.318 24.286 64.647 1.00 29.39 C
ATOM 79 O LEU A 14 74.293 23.747 65.741 1.00 33.33 O
ATOM 80 CB LEU A 14 72.637 26.118 64.683 1.00 28.58 C
ATOM 81 CG LEU A 14 72.511 27.583 64.412 1.00 36.67 C
ATOM 82 CD1 LEU A 14 71.032 27.884 64.455 1.00 38.54 C
ATOM 83 CD2 LEU A 14 73.320 28.356 65.473 1.00 28.59 C
ATOM 84 N ALA A 15 74.472 23.646 63.517 1.00 31.04 N
ATOM 85 CA ALA A 15 74.608 22.202 63.434 1.00 31.74 C
ATOM 86 C ALA A 15 75.469 21.561 64.521 1.00 38.34 C
ATOM 87 O ALA A 15 75.256 20.420 64.914 1.00 33.37 O
ATOM 88 CB ALA A 15 75.094 21.889 62.045 1.00 34.31 C
ATOM 89 N ASN A 16 76.439 22.312 65.055 1.00 44.04 N
ATOM 90 CA ASN A 16 77.318 21.768 66.087 1.00 42.33 C
ATOM 91 C ASN A 16 76.649 21.486 67.404 1.00 54.59 C
ATOM 92 O ASN A 16 77.162 20.714 68.197 1.00 60.12 O
ATOM 93 CB ASN A 16 78.534 22.644 66.419 1.00 38.89 C
ATOM 94 CG ASN A 16 78.169 24.097 66.487 1.00 48.56 C
ATOM 95 OD1 ASN A 16 78.351 24.829 65.509 1.00 65.50 O
ATOM 96 ND2 ASN A 16 77.550 24.485 67.599 1.00 19.02 N
ATOM 97 N GLY A 17 75.507 22.115 67.653 1.00 51.10 N
ATOM 98 CA GLY A 17 74.804 21.873 68.899 1.00 46.86 C
ATOM 99 C GLY A 17 75.252 22.848 69.966 1.00 46.10 C
ATOM 100 O GLY A 17 74.783 22.791 71.105 1.00 45.88 O
ATOM 101 N GLU A 18 76.187 23.725 69.565 1.00 36.49 N
ATOM 102 CA GLU A 18 76.688 24.787 70.417 1.00 31.96 C
ATOM 103 C GLU A 18 75.883 26.084 70.303 1.00 53.77 C
ATOM 104 O GLU A 18 75.053 26.249 69.408 1.00 60.74 O
ATOM 105 CB GLU A 18 78.144 25.294 70.171 1.00 29.40 C
ATOM 106 CG GLU A 18 79.215 24.258 69.820 1.00 61.40 C
ATOM 107 CD GLU A 18 80.131 24.828 68.778 1.00100.00 C
ATOM 108 OE1 GLU A 18 80.935 24.157 68.149 1.00 98.14 O
ATOM 109 OE2 GLU A 18 79.942 26.122 68.602 1.00100.00 O
ATOM 110 N PHE A 19 76.240 27.035 71.173 1.00 50.02 N
ATOM 111 CA PHE A 19 75.707 28.388 71.230 1.00 45.28 C
ATOM 112 C PHE A 19 76.350 29.329 70.210 1.00 39.50 C
ATOM 113 O PHE A 19 77.556 29.313 69.906 1.00 41.30 O
ATOM 114 CB PHE A 19 75.867 29.060 72.638 1.00 46.52 C
ATOM 115 CG PHE A 19 74.682 29.924 73.049 1.00 43.21 C
ATOM 116 CD1 PHE A 19 74.723 31.310 72.866 1.00 40.77 C
ATOM 117 CD2 PHE A 19 73.523 29.347 73.585 1.00 39.97 C
ATOM 118 CE1 PHE A 19 73.613 32.103 73.169 1.00 36.37 C
ATOM 119 CE2 PHE A 19 72.417 30.123 73.935 1.00 38.11 C
ATOM 120 CZ PHE A 19 72.482 31.504 73.736 1.00 35.32 C
ATOM 121 N HIS A 20 75.506 30.153 69.673 1.00 21.25 N
ATOM 122 CA HIS A 20 75.934 31.118 68.771 1.00 21.78 C
ATOM 123 C HIS A 20 75.106 32.239 69.156 1.00 27.75 C
ATOM 124 O HIS A 20 73.914 32.063 69.394 1.00 30.30 O
ATOM 125 CB HIS A 20 75.803 30.622 67.324 1.00 29.69 C
ATOM 126 CG HIS A 20 76.521 29.303 67.079 1.00 37.74 C
ATOM 127 ND1 HIS A 20 76.151 28.115 67.727 1.00 39.83 N
ATOM 128 CD2 HIS A 20 77.562 29.008 66.241 1.00 39.74 C
ATOM 129 CE1 HIS A 20 76.957 27.161 67.296 1.00 39.49 C
ATOM 130 NE2 HIS A 20 77.805 27.657 66.394 1.00 40.74 N
ATOM 131 N SER A 21 75.747 33.334 69.356 1.00 28.70 N
ATOM 132 CA SER A 21 75.049 34.529 69.727 1.00 31.54 C
ATOM 133 C SER A 21 74.576 35.111 68.427 1.00 36.25 C
ATOM 134 O SER A 21 75.246 34.875 67.439 1.00 33.51 O
ATOM 135 CB SER A 21 76.036 35.400 70.435 1.00 47.43 C
ATOM 136 OG SER A 21 77.090 35.610 69.510 1.00 61.42 O
ATOM 137 N GLY A 22 73.457 35.837 68.412 1.00 37.74 N
ATOM 138 CA GLY A 22 72.949 36.419 67.174 1.00 41.62 C
ATOM 139 C GLY A 22 73.926 37.450 66.615 1.00 50.46 C
ATOM 140 O GLY A 22 73.889 37.935 65.464 1.00 44.03 O
ATOM 141 N GLU A 23 74.818 37.710 67.512 1.00 49.78 N
ATOM 142 CA GLU A 23 75.905 38.605 67.426 1.00 55.28 C
ATOM 143 C GLU A 23 76.959 37.993 66.518 1.00 49.55 C
ATOM 144 O GLU A 23 77.188 38.516 65.442 1.00 45.07 O
ATOM 145 CB GLU A 23 76.143 38.859 68.922 1.00 63.59 C
ATOM 146 CG GLU A 23 75.031 38.097 69.741 1.00100.00 C
ATOM 147 CD GLU A 23 73.937 38.894 70.449 1.00100.00 C
ATOM 148 OE1 GLU A 23 72.844 39.188 69.933 1.00 84.26 O
ATOM 149 OE2 GLU A 23 74.235 39.086 71.729 1.00 68.92 O
ATOM 150 N GLN A 24 77.565 36.858 66.898 1.00 44.60 N
ATOM 151 CA GLN A 24 78.528 36.245 66.012 1.00 39.31 C
ATOM 152 C GLN A 24 77.817 35.926 64.688 1.00 44.51 C
ATOM 153 O GLN A 24 78.225 36.397 63.626 1.00 51.12 O
ATOM 154 CB GLN A 24 79.266 35.087 66.718 1.00 41.27 C
ATOM 155 CG GLN A 24 79.038 33.710 66.059 1.00 74.76 C
ATOM 156 CD GLN A 24 79.443 32.532 66.939 1.00100.00 C
ATOM 157 OE1 GLN A 24 79.006 32.430 68.103 1.00100.00 O
ATOM 158 NE2 GLN A 24 80.255 31.620 66.383 1.00100.00 N
ATOM 159 N LEU A 25 76.669 35.244 64.738 1.00 37.33 N
ATOM 160 CA LEU A 25 75.902 34.908 63.515 1.00 35.40 C
ATOM 161 C LEU A 25 75.652 36.031 62.480 1.00 38.04 C
ATOM 162 O LEU A 25 75.694 35.862 61.245 1.00 30.32 O
ATOM 163 CB LEU A 25 74.491 34.328 63.812 1.00 33.38 C
ATOM 164 CG LEU A 25 74.527 33.239 64.858 1.00 39.46 C
ATOM 165 CD1 LEU A 25 73.114 32.957 65.349 1.00 41.06 C
ATOM 166 CD2 LEU A 25 75.151 31.980 64.272 1.00 32.91 C
ATOM 167 N GLY A 26 75.259 37.188 62.955 1.00 46.97 N
ATOM 168 CA GLY A 26 74.943 38.237 62.007 1.00 50.78 C
ATOM 169 C GLY A 26 76.152 38.836 61.297 1.00 53.67 C
ATOM 170 O GLY A 26 76.046 39.332 60.166 1.00 44.13 O
ATOM 171 N GLU A 27 77.289 38.830 61.993 1.00 52.45 N
ATOM 172 CA GLU A 27 78.473 39.407 61.416 1.00 55.79 C
ATOM 173 C GLU A 27 78.977 38.459 60.319 1.00 71.97 C
ATOM 174 O GLU A 27 79.249 38.857 59.163 1.00 74.73 O
ATOM 175 CB GLU A 27 79.461 39.800 62.537 1.00 54.65 C
ATOM 176 CG GLU A 27 80.339 38.631 63.031 1.00 57.79 C
ATOM 177 CD GLU A 27 81.376 39.033 64.077 1.00100.00 C
ATOM 178 OE1 GLU A 27 82.137 40.010 63.958 1.00100.00 O
ATOM 179 OE2 GLU A 27 81.364 38.224 65.137 1.00100.00 O
ATOM 180 N THR A 28 79.062 37.180 60.707 1.00 65.52 N
ATOM 181 CA THR A 28 79.459 36.101 59.816 1.00 60.15 C
ATOM 182 C THR A 28 78.570 36.147 58.596 1.00 55.70 C
ATOM 183 O THR A 28 79.005 36.168 57.441 1.00 67.08 O
ATOM 184 CB THR A 28 79.325 34.671 60.463 1.00 72.21 C
ATOM 185 OG1 THR A 28 79.990 34.533 61.715 1.00 87.32 O
ATOM 186 CG2 THR A 28 79.877 33.622 59.506 1.00 57.97 C
ATOM 187 N LEU A 29 77.295 36.253 58.896 1.00 35.45 N
ATOM 188 CA LEU A 29 76.320 36.223 57.870 1.00 39.86 C
ATOM 189 C LEU A 29 76.220 37.532 57.195 1.00 48.84 C
ATOM 190 O LEU A 29 75.559 37.663 56.173 1.00 45.35 O
ATOM 191 CB LEU A 29 74.986 35.754 58.446 1.00 42.38 C
ATOM 192 CG LEU A 29 74.659 34.410 57.862 1.00 43.12 C
ATOM 193 CD1 LEU A 29 75.136 34.485 56.424 1.00 44.97 C
ATOM 194 CD2 LEU A 29 75.387 33.310 58.646 1.00 31.47 C
ATOM 195 N GLY A 30 76.879 38.490 57.827 1.00 59.22 N
ATOM 196 CA GLY A 30 76.882 39.861 57.372 1.00 63.82 C
ATOM 197 C GLY A 30 75.475 40.432 57.378 1.00 74.91 C
ATOM 198 O GLY A 30 75.039 41.092 56.425 1.00 80.46 O
ATOM 199 N MET A 31 74.749 40.156 58.457 1.00 73.86 N
ATOM 200 CA MET A 31 73.373 40.652 58.583 1.00 77.69 C
ATOM 201 C MET A 31 72.959 40.914 60.051 1.00 82.09 C
ATOM 202 O MET A 31 73.642 40.472 60.980 1.00 87.10 O
ATOM 203 CB MET A 31 72.336 39.758 57.854 1.00 79.12 C
ATOM 204 CG MET A 31 72.805 38.327 57.619 1.00 80.51 C
ATOM 205 SD MET A 31 71.438 37.288 57.075 1.00 83.15 S
ATOM 206 CE MET A 31 70.493 38.499 56.111 1.00 78.80 C
ATOM 207 N SER A 32 71.848 41.666 60.251 1.00 64.10 N
ATOM 208 CA SER A 32 71.355 42.010 61.576 1.00 56.33 C
ATOM 209 C SER A 32 70.836 40.840 62.358 1.00 46.04 C
ATOM 210 O SER A 32 70.358 39.819 61.817 1.00 33.62 O
ATOM 211 CB SER A 32 70.224 43.010 61.584 1.00 60.40 C
ATOM 212 OG SER A 32 69.044 42.341 61.180 1.00 61.89 O
ATOM 213 N ARG A 33 70.834 41.067 63.671 1.00 41.60 N
ATOM 214 CA ARG A 33 70.380 40.077 64.615 1.00 35.25 C
ATOM 215 C ARG A 33 68.972 39.920 64.281 1.00 33.31 C
ATOM 216 O ARG A 33 68.336 38.867 64.393 1.00 36.97 O
ATOM 217 CB ARG A 33 70.668 40.581 66.012 1.00 48.42 C
ATOM 218 CG ARG A 33 71.954 41.404 66.051 1.00 65.46 C
ATOM 219 CD ARG A 33 72.570 41.524 67.434 1.00 60.29 C
ATOM 220 NE ARG A 33 72.525 42.907 67.883 1.00 89.80 N
ATOM 221 CZ ARG A 33 71.935 43.302 69.013 1.00100.00 C
ATOM 222 NH1 ARG A 33 71.342 42.431 69.854 1.00100.00 N
ATOM 223 NH2 ARG A 33 71.958 44.607 69.317 1.00100.00 N
ATOM 224 N ALA A 34 68.550 41.052 63.782 1.00 22.66 N
ATOM 225 CA ALA A 34 67.209 41.247 63.369 1.00 24.44 C
ATOM 226 C ALA A 34 66.868 40.324 62.251 1.00 40.89 C
ATOM 227 O ALA A 34 65.861 39.615 62.307 1.00 41.93 O
ATOM 228 CB ALA A 34 67.022 42.724 63.053 1.00 26.65 C
ATOM 229 N ALA A 35 67.703 40.343 61.206 1.00 41.54 N
ATOM 230 CA ALA A 35 67.412 39.472 60.088 1.00 35.75 C
ATOM 231 C ALA A 35 67.443 38.032 60.582 1.00 38.66 C
ATOM 232 O ALA A 35 66.506 37.248 60.426 1.00 35.66 O
ATOM 233 CB ALA A 35 68.354 39.793 58.961 1.00 34.26 C
ATOM 234 N ILE A 36 68.514 37.730 61.293 1.00 34.43 N
ATOM 235 CA ILE A 36 68.708 36.420 61.837 1.00 27.46 C
ATOM 236 C ILE A 36 67.509 35.855 62.572 1.00 35.85 C
ATOM 237 O ILE A 36 67.326 34.644 62.530 1.00 43.34 O
ATOM 238 CB ILE A 36 69.965 36.404 62.675 1.00 26.92 C
ATOM 239 CG1 ILE A 36 71.115 36.284 61.707 1.00 18.44 C
ATOM 240 CG2 ILE A 36 69.942 35.234 63.643 1.00 30.44 C
ATOM 241 CD1 ILE A 36 72.111 37.371 61.996 1.00 52.09 C
ATOM 242 N ASN A 37 66.671 36.678 63.235 1.00 25.27 N
ATOM 243 CA ASN A 37 65.600 36.019 63.935 1.00 19.00 C
ATOM 244 C ASN A 37 64.583 35.457 63.010 1.00 41.92 C
ATOM 245 O ASN A 37 64.035 34.416 63.363 1.00 50.94 O
ATOM 246 CB ASN A 37 64.885 36.788 65.065 1.00 12.85 C
ATOM 247 CG ASN A 37 64.403 35.883 66.200 1.00 45.95 C
ATOM 248 OD1 ASN A 37 64.969 34.816 66.512 1.00 74.39 O
ATOM 249 ND2 ASN A 37 63.337 36.302 66.837 1.00 29.65 N
ATOM 250 N LYS A 38 64.337 36.113 61.835 1.00 46.41 N
ATOM 251 CA LYS A 38 63.354 35.587 60.826 1.00 43.74 C
ATOM 252 C LYS A 38 63.752 34.210 60.272 1.00 35.36 C
ATOM 253 O LYS A 38 62.952 33.291 60.170 1.00 27.29 O
ATOM 254 CB LYS A 38 63.080 36.479 59.607 1.00 43.72 C
ATOM 255 CG LYS A 38 61.600 36.650 59.240 1.00 81.61 C
ATOM 256 CD LYS A 38 60.954 37.921 59.825 1.00100.00 C
ATOM 257 CE LYS A 38 59.422 37.925 59.839 1.00100.00 C
ATOM 258 NZ LYS A 38 58.854 38.794 60.883 1.00100.00 N
ATOM 259 N HIS A 39 65.033 34.066 59.952 1.00 30.42 N
ATOM 260 CA HIS A 39 65.487 32.820 59.432 1.00 35.21 C
ATOM 261 C HIS A 39 65.239 31.752 60.434 1.00 41.87 C
ATOM 262 O HIS A 39 64.685 30.707 60.099 1.00 46.74 O
ATOM 263 CB HIS A 39 66.900 32.980 58.919 1.00 43.02 C
ATOM 264 CG HIS A 39 66.855 33.920 57.759 1.00 48.47 C
ATOM 265 ND1 HIS A 39 65.794 33.874 56.859 1.00 49.81 N
ATOM 266 CD2 HIS A 39 67.697 34.940 57.414 1.00 52.36 C
ATOM 267 CE1 HIS A 39 66.006 34.861 56.008 1.00 52.55 C
ATOM 268 NE2 HIS A 39 67.142 35.519 56.308 1.00 52.93 N
ATOM 269 N ILE A 40 65.551 32.101 61.667 1.00 37.33 N
ATOM 270 CA ILE A 40 65.317 31.245 62.796 1.00 33.87 C
ATOM 271 C ILE A 40 63.906 30.640 62.707 1.00 42.15 C
ATOM 272 O ILE A 40 63.707 29.427 62.869 1.00 46.45 O
ATOM 273 CB ILE A 40 65.584 32.021 64.087 1.00 29.65 C
ATOM 274 CG1 ILE A 40 67.056 32.360 64.165 1.00 29.38 C
ATOM 275 CG2 ILE A 40 65.248 31.207 65.323 1.00 16.72 C
ATOM 276 CD1 ILE A 40 67.905 31.119 64.379 1.00 31.74 C
ATOM 277 N GLN A 41 62.928 31.463 62.354 1.00 41.42 N
ATOM 278 CA GLN A 41 61.581 30.921 62.299 1.00 46.21 C
ATOM 279 C GLN A 41 61.482 29.837 61.279 1.00 36.53 C
ATOM 280 O GLN A 41 61.112 28.716 61.617 1.00 36.82 O
ATOM 281 CB GLN A 41 60.412 31.923 62.099 1.00 49.69 C
ATOM 282 CG GLN A 41 60.832 33.392 61.905 1.00 98.22 C
ATOM 283 CD GLN A 41 60.220 34.054 60.660 1.00100.00 C
ATOM 284 OE1 GLN A 41 59.135 34.676 60.740 1.00100.00 O
ATOM 285 NE2 GLN A 41 60.916 33.968 59.512 1.00 77.20 N
ATOM 286 N THR A 42 61.882 30.205 60.083 1.00 23.83 N
ATOM 287 CA THR A 42 61.878 29.292 58.984 1.00 30.28 C
ATOM 288 C THR A 42 62.379 27.909 59.374 1.00 30.74 C
ATOM 289 O THR A 42 61.823 26.886 58.994 1.00 27.92 O
ATOM 290 CB THR A 42 62.647 29.904 57.816 1.00 35.30 C
ATOM 291 OG1 THR A 42 62.265 31.250 57.628 1.00 33.54 O
ATOM 292 CG2 THR A 42 62.274 29.104 56.598 1.00 39.72 C
ATOM 293 N LEU A 43 63.363 27.938 60.249 1.00 27.81 N
ATOM 294 CA LEU A 43 64.017 26.776 60.777 1.00 25.02 C
ATOM 295 C LEU A 43 63.112 25.997 61.669 1.00 26.43 C
ATOM 296 O LEU A 43 62.934 24.798 61.508 1.00 18.00 O
ATOM 297 CB LEU A 43 65.323 27.147 61.528 1.00 25.10 C
ATOM 298 CG LEU A 43 66.573 27.324 60.628 1.00 29.04 C
ATOM 299 CD1 LEU A 43 67.893 27.193 61.396 1.00 17.83 C
ATOM 300 CD2 LEU A 43 66.626 26.282 59.516 1.00 44.41 C
ATOM 301 N ARG A 44 62.550 26.718 62.625 1.00 33.82 N
ATOM 302 CA ARG A 44 61.658 26.109 63.585 1.00 39.16 C
ATOM 303 C ARG A 44 60.606 25.367 62.795 1.00 45.21 C
ATOM 304 O ARG A 44 60.121 24.303 63.159 1.00 47.66 O
ATOM 305 CB ARG A 44 61.120 27.140 64.594 1.00 40.68 C
ATOM 306 CG ARG A 44 62.154 27.606 65.650 1.00 48.46 C
ATOM 307 CD ARG A 44 61.741 28.820 66.551 1.00 84.98 C
ATOM 308 NE ARG A 44 61.513 30.142 65.881 1.00100.00 N
ATOM 309 CZ ARG A 44 62.102 31.370 66.102 1.00100.00 C
ATOM 310 NH1 ARG A 44 63.065 31.590 67.017 1.00 77.85 N
ATOM 311 NH2 ARG A 44 61.707 32.432 65.355 1.00 46.48 N
ATOM 312 N ASP A 45 60.368 25.895 61.627 1.00 46.24 N
ATOM 313 CA ASP A 45 59.418 25.300 60.735 1.00 53.50 C
ATOM 314 C ASP A 45 59.866 24.024 60.072 1.00 57.31 C
ATOM 315 O ASP A 45 59.027 23.276 59.623 1.00 60.44 O
ATOM 316 CB ASP A 45 58.970 26.183 59.556 1.00 60.72 C
ATOM 317 CG ASP A 45 58.532 27.569 59.947 1.00100.00 C
ATOM 318 OD1 ASP A 45 58.467 27.967 61.112 1.00100.00 O
ATOM 319 OD2 ASP A 45 58.228 28.297 58.889 1.00100.00 O
ATOM 320 N TRP A 46 61.154 23.762 59.935 1.00 42.84 N
ATOM 321 CA TRP A 46 61.476 22.517 59.265 1.00 32.78 C
ATOM 322 C TRP A 46 61.677 21.370 60.209 1.00 46.07 C
ATOM 323 O TRP A 46 62.421 20.428 59.942 1.00 46.98 O
ATOM 324 CB TRP A 46 62.677 22.652 58.364 1.00 27.28 C
ATOM 325 CG TRP A 46 62.385 23.658 57.311 1.00 27.97 C
ATOM 326 CD1 TRP A 46 61.159 24.071 56.867 1.00 31.10 C
ATOM 327 CD2 TRP A 46 63.341 24.427 56.611 1.00 26.22 C
ATOM 328 NE1 TRP A 46 61.293 24.977 55.849 1.00 26.93 N
ATOM 329 CE2 TRP A 46 62.627 25.238 55.701 1.00 27.03 C
ATOM 330 CE3 TRP A 46 64.742 24.472 56.662 1.00 25.80 C
ATOM 331 CZ2 TRP A 46 63.299 26.095 54.841 1.00 26.80 C
ATOM 332 CZ3 TRP A 46 65.392 25.281 55.776 1.00 24.72 C
ATOM 333 CH2 TRP A 46 64.684 26.095 54.891 1.00 24.56 C
ATOM 334 N GLY A 47 60.977 21.454 61.322 1.00 50.97 N
ATOM 335 CA GLY A 47 61.088 20.433 62.335 1.00 52.07 C
ATOM 336 C GLY A 47 62.303 20.701 63.182 1.00 56.75 C
ATOM 337 O GLY A 47 62.613 19.978 64.147 1.00 64.52 O
ATOM 338 N VAL A 48 62.978 21.779 62.813 1.00 45.79 N
ATOM 339 CA VAL A 48 64.169 22.152 63.522 1.00 45.00 C
ATOM 340 C VAL A 48 63.834 22.729 64.874 1.00 46.91 C
ATOM 341 O VAL A 48 63.061 23.714 64.932 1.00 45.53 O
ATOM 342 CB VAL A 48 65.038 23.064 62.674 1.00 50.58 C
ATOM 343 CG1 VAL A 48 66.496 22.946 63.120 1.00 46.93 C
ATOM 344 CG2 VAL A 48 64.912 22.642 61.207 1.00 53.60 C
ATOM 345 N ASP A 49 64.368 22.093 65.956 1.00 43.13 N
ATOM 346 CA ASP A 49 64.113 22.680 67.263 1.00 47.47 C
ATOM 347 C ASP A 49 65.218 23.600 67.719 1.00 55.29 C
ATOM 348 O ASP A 49 66.264 23.193 68.209 1.00 56.72 O
ATOM 349 CB ASP A 49 63.785 21.864 68.532 1.00 52.37 C
ATOM 350 CG ASP A 49 63.077 22.753 69.594 1.00 99.90 C
ATOM 351 OD1 ASP A 49 61.854 22.909 69.648 1.00100.00 O
ATOM 352 OD2 ASP A 49 63.896 23.392 70.433 1.00100.00 O
ATOM 353 N VAL A 50 64.901 24.868 67.550 1.00 46.50 N
ATOM 354 CA VAL A 50 65.723 25.959 67.905 1.00 40.23 C
ATOM 355 C VAL A 50 65.352 26.399 69.303 1.00 47.62 C
ATOM 356 O VAL A 50 64.190 26.519 69.635 1.00 51.07 O
ATOM 357 CB VAL A 50 65.574 27.061 66.859 1.00 39.14 C
ATOM 358 CG1 VAL A 50 66.337 28.315 67.281 1.00 41.03 C
ATOM 359 CG2 VAL A 50 66.128 26.568 65.524 1.00 32.92 C
ATOM 360 N PHE A 51 66.369 26.610 70.114 1.00 42.71 N
ATOM 361 CA PHE A 51 66.229 27.068 71.453 1.00 34.27 C
ATOM 362 C PHE A 51 66.726 28.539 71.470 1.00 20.57 C
ATOM 363 O PHE A 51 67.857 28.858 71.120 1.00 16.53 O
ATOM 364 CB PHE A 51 66.879 25.989 72.325 1.00 38.44 C
ATOM 365 CG PHE A 51 67.401 26.653 73.508 1.00 46.56 C
ATOM 366 CD1 PHE A 51 66.602 26.755 74.642 1.00 59.99 C
ATOM 367 CD2 PHE A 51 68.609 27.341 73.456 1.00 58.16 C
ATOM 368 CE1 PHE A 51 67.038 27.468 75.755 1.00 63.11 C
ATOM 369 CE2 PHE A 51 69.062 28.066 74.556 1.00 64.22 C
ATOM 370 CZ PHE A 51 68.274 28.114 75.706 1.00 62.16 C
ATOM 371 N THR A 52 65.827 29.473 71.747 1.00 21.93 N
ATOM 372 CA THR A 52 66.152 30.892 71.763 1.00 22.35 C
ATOM 373 C THR A 52 66.343 31.413 73.191 1.00 23.07 C
ATOM 374 O THR A 52 65.852 30.895 74.166 1.00 21.64 O
ATOM 375 CB THR A 52 65.159 31.748 70.919 1.00 27.21 C
ATOM 376 OG1 THR A 52 65.361 31.469 69.553 1.00 34.87 O
ATOM 377 CG2 THR A 52 65.354 33.257 71.053 1.00 24.94 C
ATOM 378 N VAL A 53 67.141 32.433 73.302 1.00 22.52 N
ATOM 379 CA VAL A 53 67.456 33.040 74.562 1.00 22.78 C
ATOM 380 C VAL A 53 67.413 34.503 74.303 1.00 29.50 C
ATOM 381 O VAL A 53 68.394 35.230 74.372 1.00 39.91 O
ATOM 382 CB VAL A 53 68.736 32.514 75.215 1.00 18.11 C