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83AH.pdb
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HEADER HYDROLASE 20-JAN-99 8A3H
TITLE CELLOBIOSE-DERIVED IMIDAZOLE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM
TITLE 2 BACILLUS AGARADHAERENS AT 0.97 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ENDOGLUCANASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC CORE DOMAIN;
COMPND 5 SYNONYM: CELLULASE;
COMPND 6 EC: 3.2.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AGARADHAERENS;
SOURCE 3 ORGANISM_TAXID: 76935;
SOURCE 4 STRAIN: AC13 (NCIMB 40482);
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: PL2306;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACILLUS, CELLULASE NEGATIVE STRAIN;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PMOL995;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: THERRAMYL-AMYLASE PROMOTER SYSTEM
KEYWDS CELLULOSE DEGRADATION, GLYCOSIDE HYDROLASE FAMILY 5, ENDOGLUCANASE,
KEYWDS 2 TRANSITION STATE ANALOGUE, LATERAL PROTONATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VARROT,M.SCHULEIN,M.PIPELIER,A.VASELLA,G.J.DAVIES
REVDAT 4 13-JUL-11 8A3H 1 VERSN
REVDAT 3 24-FEB-09 8A3H 1 VERSN
REVDAT 2 29-MAR-05 8A3H 1 JRNL
REVDAT 1 21-JAN-00 8A3H 0
JRNL AUTH A.VARROT,M.SCHULEIN,M.PIPELIER,A.VASELLA,G.J.DAVIES
JRNL TITL LATERAL PROTONATION OF A GLYCOSIDASE INHIBITOR. STRUCTURE OF
JRNL TITL 2 THE BACILLUS AGARADHAERENS CEL5A IN COMPLEX WITH A
JRNL TITL 3 CELLOBIOSE-DERIVED IMIDAZOLE AT 0.97 A RESOLUTION
JRNL REF J.AM.CHEM.SOC. V. 121 2621 1999
JRNL REFN ISSN 0002-7863
REMARK 2
REMARK 2 RESOLUTION. 0.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 152310
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.104
REMARK 3 FREE R VALUE : 0.118
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8085
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2377
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 499
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 6.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.017 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.033 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.043 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.034 ; 0.040
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.124 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.169 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.256 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.099 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 6.200 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 11.800; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 28.800; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.922 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.585 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.755 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.626 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8A3H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-99.
REMARK 100 THE RCSB ID CODE IS RCSB007240.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9076
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 : 149215
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.970
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : 0.03200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 44.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.32100
REMARK 200 R SYM FOR SHELL (I) : 0.32100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CONCENTRATION 20 MG/ML, 2 M
REMARK 280 AMMONIUM SULPHATE, 100 MM SODIUM CITRATE PH 5.5, 10% GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.22500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.66000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.94000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.66000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.22500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.94000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 400
REMARK 400 COMPOUND
REMARK 400 THE THREE FIRST RESIDUES ARE DISORDERED SO SEQUENCE STARTS
REMARK 400 AT RESIDUE SER A 4 . THIS IS THE NATURALLY OCCURING CORE
REMARK 400 DOMAIN AFTER LOSS OF THE CELLULOSE BINDING DOMAIN
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 ASN A 2
REMARK 465 ASP A 3
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 PRO A 276 CD PRO A 276 N 0.089
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 23 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 99 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 144 CB - CG - OD1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP A 144 CB - CG - OD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 GLU A 157 OE1 - CD - OE2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP A 181 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 255 CA - CB - CG ANGL. DEV. = -15.8 DEGREES
REMARK 500 ARG A 255 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 255 O - C - N ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO A 276 CA - C - N ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG A 301 NE - CZ - NH1 ANGL. DEV. = 3.0 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 SER A 68 -164.10 -100.45
REMARK 500 LEU A 103 -79.05 -159.86
REMARK 500 ALA A 137 96.16 -165.79
REMARK 500 ASN A 168 8.21 -158.86
REMARK 500 ASP A 237 -153.66 -134.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 62 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 831 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH A 962 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 968 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH A1055 DISTANCE = 6.17 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE IMIDAZOLE-DERIVED CELLOBIOSIDE IS
REMARK 600 BOUND IN THE -2 AND -1 SUBSITE. THE
REMARK 600 IMIDAZOLE RING SITE IN THE +1 SUBSITE
REMARK 600
REMARK 600 GLYCEROL MOLECULE COMING FROM THE
REMARK 600 CRYOPROTECTANT SOLUTION
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACI
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC ACID/BASE
REMARK 800
REMARK 800 SITE_IDENTIFIER: NUC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC NUCLEOPHILE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDC A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 606
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 26 RESIDUES IN THE DATABASE CORRESPONDS
REMARK 999 TO THE PROSEQUENCE. OUR NUMBERING BEGINS AT THE
REMARK 999 FIRST RESIDUE OBTAINED AFTER CLEAVAGE OF THE
REMARK 999 PROSEQUENCE
DBREF 8A3H A 1 303 UNP P06565 GUN2_BACS4 27 329
SEQADV 8A3H ASN A 2 UNP P06565 ASP 28 CONFLICT
SEQADV 8A3H ASP A 3 UNP P06565 TYR 29 CONFLICT
SEQRES 1 A 303 ASP ASN ASP SER VAL VAL GLU GLU HIS GLY GLN LEU SER
SEQRES 2 A 303 ILE SER ASN GLY GLU LEU VAL ASN GLU ARG GLY GLU GLN
SEQRES 3 A 303 VAL GLN LEU LYS GLY MET SER SER HIS GLY LEU GLN TRP
SEQRES 4 A 303 TYR GLY GLN PHE VAL ASN TYR GLU SER MET LYS TRP LEU
SEQRES 5 A 303 ARG ASP ASP TRP GLY ILE ASN VAL PHE ARG ALA ALA MET
SEQRES 6 A 303 TYR THR SER SER GLY GLY TYR ILE ASP ASP PRO SER VAL
SEQRES 7 A 303 LYS GLU LYS VAL LYS GLU ALA VAL GLU ALA ALA ILE ASP
SEQRES 8 A 303 LEU ASP ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU SER
SEQRES 9 A 303 ASP ASN ASP PRO ASN ILE TYR LYS GLU GLU ALA LYS ASP
SEQRES 10 A 303 PHE PHE ASP GLU MET SER GLU LEU TYR GLY ASP TYR PRO
SEQRES 11 A 303 ASN VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY SER
SEQRES 12 A 303 ASP VAL THR TRP GLY ASN GLN ILE LYS PRO TYR ALA GLU
SEQRES 13 A 303 GLU VAL ILE PRO ILE ILE ARG ASN ASN ASP PRO ASN ASN
SEQRES 14 A 303 ILE ILE ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL
SEQRES 15 A 303 HIS HIS ALA ALA ASP ASN GLN LEU ALA ASP PRO ASN VAL
SEQRES 16 A 303 MET TYR ALA PHE HIS PHE TYR ALA GLY THR HIS GLY GLN
SEQRES 17 A 303 ASN LEU ARG ASP GLN VAL ASP TYR ALA LEU ASP GLN GLY
SEQRES 18 A 303 ALA ALA ILE PHE VAL SER GLU TRP GLY THR SER ALA ALA
SEQRES 19 A 303 THR GLY ASP GLY GLY VAL PHE LEU ASP GLU ALA GLN VAL
SEQRES 20 A 303 TRP ILE ASP PHE MET ASP GLU ARG ASN LEU SER TRP ALA
SEQRES 21 A 303 ASN TRP SER LEU THR HIS LYS ASP GLU SER SER ALA ALA
SEQRES 22 A 303 LEU MET PRO GLY ALA ASN PRO THR GLY GLY TRP THR GLU
SEQRES 23 A 303 ALA GLU LEU SER PRO SER GLY THR PHE VAL ARG GLU LYS
SEQRES 24 A 303 ILE ARG GLU SER
HET SO4 A 607 5
HET ACT A 608 4
HET IDC A 500 25
HET GOL A 600 6
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 12
HET GOL A 604 6
HET GOL A 605 6
HET GOL A 606 12
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
HETNAM IDC 5-HYDROXYMETHYL-5,6,7,8-TETRAHYDRO-IMIDAZO[1,2-
HETNAM 2 IDC A]PYRIDIN-6YL-7,8-DIOL-GLUCOPYRANOSIDE
HETNAM GOL GLYCEROL
HETSYN IDC IMIDAZOLE-DERIVED CELLOBIOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 O4 S 2-
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 IDC C14 H22 N2 O9
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 12 HOH *499(H2 O)
HELIX 1 1 VAL A 5 HIS A 9 1 5
HELIX 2 2 LEU A 37 PHE A 43 1 7
HELIX 3 3 TYR A 46 ASP A 55 1 10
HELIX 4 4 PRO A 76 LEU A 92 5 17
HELIX 5 5 PRO A 108 TYR A 126 5 19
HELIX 6 6 ILE A 151 ASN A 165 1 15
HELIX 7 7 GLY A 176 SER A 179 1 4
HELIX 8 8 VAL A 182 ALA A 186 1 5
HELIX 9 9 GLN A 208 GLN A 220 1 13
HELIX 10 10 LEU A 242 GLU A 254 1 13
HELIX 11 11 GLU A 286 GLU A 288 5 3
HELIX 12 12 PRO A 291 ARG A 301 1 11
SHEET 1 A 2 SER A 13 SER A 15 0
SHEET 2 A 2 GLU A 18 VAL A 20 -1 N VAL A 20 O SER A 13
SHEET 1 B 5 TRP A 259 ASN A 261 0
SHEET 2 B 5 LYS A 30 SER A 33 1 N GLY A 31 O TRP A 259
SHEET 3 B 5 VAL A 60 TYR A 66 1 N VAL A 60 O MET A 32
SHEET 4 B 5 TYR A 95 HIS A 101 1 N TYR A 95 O PHE A 61
SHEET 5 B 5 VAL A 132 GLU A 135 1 N ILE A 133 O VAL A 96
SHEET 1 C 2 ILE A 171 VAL A 173 0
SHEET 2 C 2 VAL A 195 TYR A 197 1 N MET A 196 O ILE A 171
SHEET 1 D 2 HIS A 200 TYR A 202 0
SHEET 2 D 2 GLU A 228 GLY A 230 1 N GLU A 228 O PHE A 201
CISPEP 1 TRP A 262 SER A 263 0 3.34
SITE 1 ACI 1 GLU A 139
SITE 1 NUC 1 GLU A 228
SITE 1 AC1 3 ARG A 53 HOH A 887 HOH A 926
SITE 1 AC2 2 ARG A 297 ARG A 301
SITE 1 AC3 19 HIS A 35 TRP A 39 TYR A 66 HIS A 101
SITE 2 AC3 19 LEU A 103 ASN A 138 GLU A 139 TYR A 202
SITE 3 AC3 19 GLU A 228 ALA A 234 THR A 235 GLY A 236
SITE 4 AC3 19 TRP A 262 LYS A 267 GLU A 269 HOH A 749
SITE 5 AC3 19 HOH A 786 HOH A 891 HOH A 948
SITE 1 AC4 8 SER A 69 GLY A 70 VAL A 240 PRO A 291
SITE 2 AC4 8 HOH A 727 HOH A 818 HOH A 965 HOH A1019
SITE 1 AC5 9 GLU A 80 LYS A 83 GLU A 84 GLU A 87
SITE 2 AC5 9 LYS A 152 GLU A 156 GLN A 189 HOH A 678
SITE 3 AC5 9 HOH A 692
SITE 1 AC6 4 TYR A 72 ILE A 73 PRO A 76 HOH A 908
SITE 1 AC7 11 GLN A 11 SER A 13 ASN A 168 GLY A 204
SITE 2 AC7 11 PHE A 241 HOH A 642 HOH A 689 HOH A 697
SITE 3 AC7 11 HOH A 698 HOH A 751 HOH A 858
SITE 1 AC8 10 LYS A 116 ASP A 117 ASP A 120 ASN A 279
SITE 2 AC8 10 HOH A 676 HOH A 769 HOH A 816 HOH A 845
SITE 3 AC8 10 HOH A 877 HOH A 905
SITE 1 AC9 7 GLU A 87 ASP A 91 HOH A 681 HOH A 719
SITE 2 AC9 7 HOH A 809 HOH A 854 HOH A1103
SITE 1 BC1 13 THR A 146 TRP A 147 GLY A 148 ASN A 149
SITE 2 BC1 13 HIS A 184 ASN A 188 HOH A 668 HOH A 669
SITE 3 BC1 13 HOH A 679 HOH A 950 HOH A1012 HOH A1068
SITE 4 BC1 13 HOH A1105
CRYST1 54.450 69.880 77.320 90.00 90.00 90.00 P 21 21 21 4
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 0.018365 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012933 0.00000
ATOM 1 N SER A 4 72.462 44.225 7.583 1.00 21.76 N
ANISOU 1 N SER A 4 2533 2231 3506 -149 362 406 N
ATOM 2 CA SER A 4 73.547 43.253 7.543 1.00 17.29 C
ANISOU 2 CA SER A 4 2778 1894 1897 -128 547 -50 C
ATOM 3 C SER A 4 73.369 42.004 8.410 1.00 13.03 C
ANISOU 3 C SER A 4 1633 1845 1474 -383 290 -77 C
ATOM 4 O SER A 4 73.551 40.891 7.911 1.00 14.70 O
ANISOU 4 O SER A 4 1972 1858 1754 -253 400 -30 O
ATOM 5 CB SER A 4 74.916 43.855 7.751 1.00 25.38 C
ANISOU 5 CB SER A 4 3196 3806 2642 -958 215 35 C
ATOM 6 OG SER A 4 74.830 44.589 8.958 1.00 27.81 O
ANISOU 6 OG SER A 4 3825 3755 2986 -436 157 -135 O
ATOM 7 N VAL A 5 72.917 42.175 9.638 1.00 12.77 N
ANISOU 7 N VAL A 5 1830 1557 1464 -170 341 -32 N
ATOM 8 CA VAL A 5 72.814 40.998 10.564 1.00 12.92 C
ANISOU 8 CA VAL A 5 1593 1833 1482 -245 99 47 C
ATOM 9 C VAL A 5 71.812 39.970 10.097 1.00 10.16 C
ANISOU 9 C VAL A 5 1096 1470 1295 47 -26 11 C
ATOM 10 O VAL A 5 72.125 38.754 9.984 1.00 10.95 O
ANISOU 10 O VAL A 5 1216 1471 1473 106 90 -58 O
ATOM 11 CB VAL A 5 72.434 41.527 11.970 1.00 14.12 C
ANISOU 11 CB VAL A 5 2015 1921 1431 -502 67 74 C
ATOM 12 CG1 VAL A 5 71.991 40.406 12.892 1.00 18.79 C
ANISOU 12 CG1 VAL A 5 3314 2441 1385 -941 -161 317 C
ATOM 13 CG2 VAL A 5 73.586 42.323 12.578 1.00 15.24 C
ANISOU 13 CG2 VAL A 5 2233 1885 1672 -473 -190 78 C
ATOM 14 N VAL A 6 70.586 40.378 9.838 1.00 10.23 N
ANISOU 14 N VAL A 6 1134 1414 1340 158 138 55 N
ATOM 15 CA VAL A 6 69.535 39.460 9.439 1.00 9.49 C
ANISOU 15 CA VAL A 6 1073 1345 1190 127 213 12 C
ATOM 16 C VAL A 6 69.778 38.949 8.007 1.00 9.76 C
ANISOU 16 C VAL A 6 1250 1347 1112 86 256 118 C
ATOM 17 O VAL A 6 69.511 37.770 7.714 1.00 10.46 O
ANISOU 17 O VAL A 6 1351 1433 1188 222 175 34 O
ATOM 18 CB VAL A 6 68.164 40.067 9.652 1.00 9.33 C
ANISOU 18 CB VAL A 6 1049 1367 1127 249 179 49 C
ATOM 19 CG1 VAL A 6 67.059 39.142 9.101 1.00 10.88 C
ANISOU 19 CG1 VAL A 6 1075 1789 1270 172 67 -177 C
ATOM 20 CG2 VAL A 6 67.924 40.271 11.163 1.00 9.04 C
ANISOU 20 CG2 VAL A 6 985 1376 1075 167 138 34 C
ATOM 21 N GLU A 7 70.297 39.786 7.109 1.00 10.76 N
ANISOU 21 N GLU A 7 1428 1452 1209 207 337 118 N
ATOM 22 CA GLU A 7 70.612 39.262 5.761 1.00 11.42 C
ANISOU 22 CA GLU A 7 1590 1637 1113 229 255 64 C
ATOM 23 C GLU A 7 71.667 38.168 5.833 1.00 10.50 C
ANISOU 23 C GLU A 7 1437 1426 1129 50 154 77 C
ATOM 24 O GLU A 7 71.600 37.138 5.163 1.00 12.22 O
ANISOU 24 O GLU A 7 1805 1618 1220 337 207 -29 O
ATOM 25 CB GLU A 7 71.149 40.426 4.897 1.00 14.04 C
ANISOU 25 CB GLU A 7 2262 1830 1242 462 548 424 C
ATOM 26 CG AGLU A 7 71.073 40.080 3.406 0.45 13.76 C
ANISOU 26 CG AGLU A 7 2380 1580 1269 791 461 184 C
ATOM 27 CG BGLU A 7 71.375 39.972 3.446 0.55 17.08 C
ANISOU 27 CG BGLU A 7 2320 2802 1366 333 500 123 C
ATOM 28 CD AGLU A 7 71.775 41.173 2.627 0.45 17.75 C
ANISOU 28 CD AGLU A 7 2818 2023 1902 725 700 596 C
ATOM 29 CD BGLU A 7 71.016 41.096 2.527 0.55 23.33 C
ANISOU 29 CD BGLU A 7 3645 2873 2347 952 -724 -65 C
ATOM 30 OE1AGLU A 7 72.022 42.290 3.129 0.45 29.61 O
ANISOU 30 OE1AGLU A 7 4685 2810 3754 -1709 514 509 O
ATOM 31 OE1BGLU A 7 70.930 42.291 2.838 0.55 24.98 O
ANISOU 31 OE1BGLU A 7 3985 2212 3296 868 255 1145 O
ATOM 32 OE2AGLU A 7 72.135 40.957 1.487 0.45 18.62 O
ANISOU 32 OE2AGLU A 7 3214 2064 1796 -658 489 105 O
ATOM 33 OE2BGLU A 7 70.711 40.899 1.366 0.55 23.18 O
ANISOU 33 OE2BGLU A 7 4081 2784 1943 253 -54 371 O
ATOM 34 N GLU A 8 72.684 38.383 6.702 1.00 10.64 N
ANISOU 34 N GLU A 8 1270 1511 1261 24 316 23 N
ATOM 35 CA GLU A 8 73.731 37.384 6.833 1.00 11.11 C
ANISOU 35 CA GLU A 8 1380 1582 1258 102 239 0 C
ATOM 36 C GLU A 8 73.282 36.116 7.516 1.00 10.86 C
ANISOU 36 C GLU A 8 1269 1527 1331 340 390 124 C
ATOM 37 O GLU A 8 73.537 35.004 6.989 1.00 14.47 O
ANISOU 37 O GLU A 8 2366 1718 1414 594 575 71 O
ATOM 38 CB GLU A 8 74.898 37.970 7.606 1.00 12.64 C
ANISOU 38 CB GLU A 8 1397 1827 1579 127 309 103 C
ATOM 39 CG GLU A 8 75.972 36.929 7.906 1.00 19.13 C
ANISOU 39 CG GLU A 8 2193 2208 2867 416 -201 -1 C
ATOM 40 CD GLU A 8 77.211 37.426 8.552 1.00 21.93 C
ANISOU 40 CD GLU A 8 2870 2697 2765 69 -504 -164 C
ATOM 41 OE1 GLU A 8 77.411 38.659 8.716 1.00 22.25 O
ANISOU 41 OE1 GLU A 8 2414 2975 3064 -174 -180 -389 O
ATOM 42 OE2 GLU A 8 78.080 36.566 8.885 1.00 33.92 O
ANISOU 42 OE2 GLU A 8 3051 4090 5746 454 -1017 1034 O
ATOM 43 N HIS A 9 72.671 36.210 8.703 1.00 10.05 N
ANISOU 43 N HIS A 9 1142 1450 1225 -8 282 97 N
ATOM 44 CA HIS A 9 72.349 35.002 9.457 1.00 9.75 C
ANISOU 44 CA HIS A 9 1216 1332 1157 21 217 124 C
ATOM 45 C HIS A 9 71.028 34.391 9.051 1.00 9.59 C
ANISOU 45 C HIS A 9 1154 1428 1060 128 191 20 C
ATOM 46 O HIS A 9 70.843 33.166 9.191 1.00 10.35 O
ANISOU 46 O HIS A 9 1362 1364 1209 28 19 60 O
ATOM 47 CB HIS A 9 72.372 35.325 10.966 1.00 10.17 C
ANISOU 47 CB HIS A 9 1257 1443 1164 99 75 93 C
ATOM 48 CG HIS A 9 73.766 35.621 11.397 1.00 11.92 C
ANISOU 48 CG HIS A 9 1391 1637 1501 32 -30 198 C
ATOM 49 ND1 HIS A 9 74.756 34.647 11.393 1.00 13.73 N
ANISOU 49 ND1 HIS A 9 1504 1671 2043 -12 -63 174 N
ATOM 50 CD2 HIS A 9 74.312 36.792 11.767 1.00 15.13 C
ANISOU 50 CD2 HIS A 9 1976 1791 1980 33 -334 -5 C
ATOM 51 CE1 HIS A 9 75.868 35.245 11.815 1.00 17.21 C
ANISOU 51 CE1 HIS A 9 1847 1922 2770 -117 -631 260 C
ATOM 52 NE2 HIS A 9 75.634 36.546 12.074 1.00 17.75 N
ANISOU 52 NE2 HIS A 9 1999 1963 2782 -264 -587 120 N
ATOM 53 N GLY A 10 70.074 35.221 8.591 1.00 10.23 N
ANISOU 53 N GLY A 10 1273 1485 1129 126 182 190 N
ATOM 54 CA GLY A 10 68.810 34.740 8.061 1.00 11.34 C
ANISOU 54 CA GLY A 10 1486 1715 1109 -37 91 85 C
ATOM 55 C GLY A 10 67.966 34.012 9.100 1.00 10.04 C
ANISOU 55 C GLY A 10 1351 1499 964 74 148 112 C
ATOM 56 O GLY A 10 67.735 34.509 10.225 1.00 10.09 O
ANISOU 56 O GLY A 10 1228 1518 1088 59 161 -23 O
ATOM 57 N GLN A 11 67.441 32.890 8.677 1.00 9.83 N
ANISOU 57 N GLN A 11 1131 1616 989 46 95 -45 N
ATOM 58 CA GLN A 11 66.504 32.122 9.477 1.00 9.77 C
ANISOU 58 CA GLN A 11 1038 1596 1081 175 44 -10 C
ATOM 59 C GLN A 11 67.188 31.480 10.673 1.00 10.09 C
ANISOU 59 C GLN A 11 1184 1615 1034 339 226 -23 C
ATOM 60 O GLN A 11 68.125 30.671 10.506 1.00 13.17 O
ANISOU 60 O GLN A 11 1521 2385 1097 715 284 143 O
ATOM 61 CB GLN A 11 65.923 31.049 8.542 1.00 9.79 C
ANISOU 61 CB GLN A 11 1280 1378 1062 111 156 -1 C
ATOM 62 CG GLN A 11 64.717 30.373 9.116 1.00 10.12 C
ANISOU 62 CG GLN A 11 1310 1395 1140 118 308 -41 C
ATOM 63 CD GLN A 11 63.585 31.367 9.291 1.00 10.27 C
ANISOU 63 CD GLN A 11 1326 1364 1211 -28 170 -161 C
ATOM 64 OE1 GLN A 11 63.411 32.300 8.500 1.00 10.96 O
ANISOU 64 OE1 GLN A 11 1410 1585 1167 185 -18 -173 O
ATOM 65 NE2 GLN A 11 62.815 31.177 10.357 1.00 10.72 N
ANISOU 65 NE2 GLN A 11 1134 1488 1452 -43 267 -49 N
ATOM 66 N LEU A 12 66.760 31.832 11.882 1.00 8.39 N
ANISOU 66 N LEU A 12 985 1273 930 127 118 16 N
ATOM 67 CA LEU A 12 67.309 31.254 13.102 1.00 9.07 C
ANISOU 67 CA LEU A 12 1179 1207 1059 201 120 43 C
ATOM 68 C LEU A 12 66.586 29.959 13.421 1.00 8.94 C
ANISOU 68 C LEU A 12 937 1288 1173 -23 22 6 C
ATOM 69 O LEU A 12 65.371 29.846 13.111 1.00 11.31 O
ANISOU 69 O LEU A 12 1153 1468 1677 9 -5 293 O
ATOM 70 CB LEU A 12 67.178 32.208 14.288 1.00 9.87 C
ANISOU 70 CB LEU A 12 1486 1275 988 139 -12 -14 C
ATOM 71 CG LEU A 12 67.850 33.579 14.104 1.00 11.19 C
ANISOU 71 CG LEU A 12 1817 1199 1238 211 -315 55 C
ATOM 72 CD1 LEU A 12 67.698 34.428 15.350 1.00 16.22 C
ANISOU 72 CD1 LEU A 12 3723 1239 1200 99 -572 -1 C
ATOM 73 CD2 LEU A 12 69.333 33.423 13.691 1.00 14.58 C
ANISOU 73 CD2 LEU A 12 1514 1294 2730 -19 -685 295 C
ATOM 74 N SER A 13 67.230 29.024 14.091 1.00 8.74 N
ANISOU 74 N SER A 13 1075 1217 1029 124 63 -37 N
ATOM 75 CA SER A 13 66.600 27.795 14.539 1.00 8.97 C
ANISOU 75 CA SER A 13 1160 1124 1125 62 91 -18 C
ATOM 76 C SER A 13 67.409 27.280 15.737 1.00 8.08 C
ANISOU 76 C SER A 13 1008 1076 985 81 120 -152 C
ATOM 77 O SER A 13 68.470 27.796 16.079 1.00 8.59 O
ANISOU 77 O SER A 13 983 1221 1059 26 80 -56 O
ATOM 78 CB SER A 13 66.503 26.735 13.445 1.00 9.86 C
ANISOU 78 CB SER A 13 1262 1395 1089 37 46 -118 C
ATOM 79 OG SER A 13 67.795 26.338 13.090 1.00 12.11 O
ANISOU 79 OG SER A 13 1366 1804 1431 162 61 -426 O
ATOM 80 N ILE A 14 66.851 26.208 16.349 1.00 8.53 N
ANISOU 80 N ILE A 14 1101 1118 1022 18 29 -87 N
ATOM 81 CA ILE A 14 67.561 25.508 17.414 1.00 8.61 C
ANISOU 81 CA ILE A 14 1080 1123 1070 48 32 -44 C
ATOM 82 C ILE A 14 68.089 24.185 16.897 1.00 8.81 C
ANISOU 82 C ILE A 14 1116 1101 1131 119 -11 -73 C
ATOM 83 O ILE A 14 67.365 23.381 16.315 1.00 10.44 O
ANISOU 83 O ILE A 14 1310 1186 1472 147 -74 -160 O
ATOM 84 CB ILE A 14 66.654 25.280 18.649 1.00 8.68 C
ANISOU 84 CB ILE A 14 1054 1223 1021 -41 66 -51 C
ATOM 85 CG1 ILE A 14 66.070 26.606 19.172 1.00 8.80 C
ANISOU 85 CG1 ILE A 14 1020 1290 1033 4 98 -61 C
ATOM 86 CG2 ILE A 14 67.395 24.499 19.720 1.00 9.97 C
ANISOU 86 CG2 ILE A 14 1213 1402 1175 -21 -17 61 C
ATOM 87 CD1 ILE A 14 67.131 27.632 19.543 1.00 9.36 C
ANISOU 87 CD1 ILE A 14 1105 1316 1135 -31 166 -163 C
ATOM 88 N SER A 15 69.399 23.939 17.113 1.00 9.25 N
ANISOU 88 N SER A 15 1180 1141 1193 210 121 -108 N
ATOM 89 CA SER A 15 70.049 22.689 16.725 1.00 10.31 C
ANISOU 89 CA SER A 15 1334 1210 1372 212 109 -145 C
ATOM 90 C SER A 15 70.849 22.213 17.912 1.00 10.59 C
ANISOU 90 C SER A 15 1381 1243 1399 321 119 -165 C
ATOM 91 O SER A 15 71.731 22.923 18.418 1.00 11.42 O
ANISOU 91 O SER A 15 1300 1525 1515 202 88 -169 O
ATOM 92 CB SER A 15 70.980 22.914 15.549 1.00 13.01 C
ANISOU 92 CB SER A 15 1834 1618 1490 405 368 -141 C
ATOM 93 OG SER A 15 71.645 21.721 15.216 1.00 20.22 O
ANISOU 93 OG SER A 15 3351 2156 2176 1054 771 -233 O
ATOM 94 N ASN A 16 70.550 20.995 18.414 1.00 11.71 N
ANISOU 94 N ASN A 16 1600 1267 1581 246 -27 -66 N
ATOM 95 CA ASN A 16 71.277 20.440 19.546 1.00 14.16 C
ANISOU 95 CA ASN A 16 2054 1468 1859 751 -114 -62 C
ATOM 96 C ASN A 16 71.331 21.390 20.719 1.00 11.70 C
ANISOU 96 C ASN A 16 1575 1239 1631 311 -124 40 C
ATOM 97 O ASN A 16 72.349 21.582 21.380 1.00 13.31 O
ANISOU 97 O ASN A 16 1639 1647 1772 435 -124 -110 O
ATOM 98 CB ASN A 16 72.672 19.970 19.141 1.00 19.04 C
ANISOU 98 CB ASN A 16 2408 2331 2496 1265 75 -411 C
ATOM 99 CG AASN A 16 72.547 18.844 18.115 0.50 20.16 C
ANISOU 99 CG AASN A 16 2869 2307 2482 580 -235 -196 C
ATOM 100 CG BASN A 16 73.406 19.136 20.154 0.50 21.17 C
ANISOU 100 CG BASN A 16 2845 2680 2519 682 8 85 C
ATOM 101 OD1AASN A 16 71.754 17.915 18.272 0.50 25.24 O
ANISOU 101 OD1AASN A 16 3867 1886 3837 376 217 -751 O
ATOM 102 OD1BASN A 16 72.731 18.319 20.782 0.50 25.13 O
ANISOU 102 OD1BASN A 16 3856 2454 3240 967 737 391 O
ATOM 103 ND2AASN A 16 73.268 18.994 17.021 0.50 29.97 N
ANISOU 103 ND2AASN A 16 3949 4436 3000 846 640 -634 N
ATOM 104 ND2BASN A 16 74.704 19.389 20.262 0.50 28.30 N
ANISOU 104 ND2BASN A 16 3018 3739 3997 235 261 -586 N
ATOM 105 N GLY A 17 70.204 22.078 20.977 1.00 10.38 N
ANISOU 105 N GLY A 17 1426 1124 1394 141 -50 69 N
ATOM 106 CA GLY A 17 70.118 22.950 22.151 1.00 10.12 C
ANISOU 106 CA GLY A 17 1324 1261 1261 151 44 123 C
ATOM 107 C GLY A 17 70.733 24.308 22.026 1.00 9.01 C
ANISOU 107 C GLY A 17 942 1250 1232 200 21 94 C
ATOM 108 O GLY A 17 70.868 25.009 23.032 1.00 10.00 O
ANISOU 108 O GLY A 17 1152 1442 1204 86 78 -68 O
ATOM 109 N GLU A 18 71.168 24.684 20.804 1.00 9.23 N
ANISOU 109 N GLU A 18 1164 1174 1171 124 49 65 N
ATOM 110 CA GLU A 18 71.867 25.937 20.531 1.00 9.20 C
ANISOU 110 CA GLU A 18 961 1348 1187 152 55 23 C
ATOM 111 C GLU A 18 71.119 26.762 19.497 1.00 8.46 C
ANISOU 111 C GLU A 18 907 1224 1085 135 111 -21 C
ATOM 112 O GLU A 18 70.632 26.227 18.499 1.00 9.11 O
ANISOU 112 O GLU A 18 1111 1202 1149 154 69 1 O
ATOM 113 CB GLU A 18 73.260 25.619 19.941 1.00 10.75 C
ANISOU 113 CB GLU A 18 991 1442 1652 139 -27 48 C
ATOM 114 CG GLU A 18 74.203 24.857 20.851 1.00 14.10 C
ANISOU 114 CG GLU A 18 1248 1770 2339 498 -261 -98 C
ATOM 115 CD GLU A 18 74.630 25.621 22.058 1.00 17.15 C
ANISOU 115 CD GLU A 18 2025 1942 2549 184 -594 -87 C
ATOM 116 OE1 GLU A 18 74.471 26.848 22.172 1.00 15.65 O
ANISOU 116 OE1 GLU A 18 1797 2019 2130 78 -284 -212 O
ATOM 117 OE2 GLU A 18 75.181 24.956 22.993 1.00 29.54 O
ANISOU 117 OE2 GLU A 18 4944 2273 4008 65 -2231 415 O
ATOM 118 N LEU A 19 71.158 28.088 19.686 1.00 7.91 N
ANISOU 118 N LEU A 19 776 1218 1011 54 57 47 N
ATOM 119 CA LEU A 19 70.688 29.006 18.642 1.00 7.90 C
ANISOU 119 CA LEU A 19 840 1164 998 106 71 5 C
ATOM 120 C LEU A 19 71.701 29.024 17.500 1.00 7.76 C
ANISOU 120 C LEU A 19 741 1191 1018 42 13 23 C
ATOM 121 O LEU A 19 72.897 29.307 17.724 1.00 8.84 O
ANISOU 121 O LEU A 19 850 1394 1117 46 62 27 O
ATOM 122 CB LEU A 19 70.502 30.411 19.220 1.00 8.51 C
ANISOU 122 CB LEU A 19 956 1224 1053 59 15 -42 C
ATOM 123 CG LEU A 19 69.815 31.427 18.291 1.00 8.03 C
ANISOU 123 CG LEU A 19 896 1174 982 47 63 12 C
ATOM 124 CD1 LEU A 19 68.394 31.043 17.959 1.00 8.38 C
ANISOU 124 CD1 LEU A 19 822 1279 1085 4 33 -21 C
ATOM 125 CD2 LEU A 19 69.893 32.817 18.931 1.00 9.29 C
ANISOU 125 CD2 LEU A 19 1020 1279 1230 67 -101 -78 C
ATOM 126 N VAL A 20 71.197 28.753 16.275 1.00 8.19 N
ANISOU 126 N VAL A 20 837 1218 1058 98 117 49 N
ATOM 127 CA VAL A 20 72.060 28.725 15.088 1.00 8.27 C
ANISOU 127 CA VAL A 20 763 1317 1062 160 132 13 C
ATOM 128 C VAL A 20 71.389 29.534 13.974 1.00 8.37 C
ANISOU 128 C VAL A 20 885 1247 1049 141 147 -28 C
ATOM 129 O VAL A 20 70.168 29.764 13.949 1.00 8.73 O
ANISOU 129 O VAL A 20 973 1292 1053 90 105 4 O
ATOM 130 CB VAL A 20 72.349 27.281 14.609 1.00 9.64 C
ANISOU 130 CB VAL A 20 1182 1315 1165 239 334 63 C
ATOM 131 CG1 VAL A 20 73.115 26.500 15.683 1.00 10.71 C
ANISOU 131 CG1 VAL A 20 1332 1343 1396 357 224 1 C
ATOM 132 CG2 VAL A 20 71.091 26.541 14.153 1.00 10.23 C
ANISOU 132 CG2 VAL A 20 1421 1255 1210 170 329 -30 C
ATOM 133 N ASN A 21 72.216 29.901 12.990 1.00 9.13 N
ANISOU 133 N ASN A 21 1086 1314 1067 202 251 55 N
ATOM 134 CA ASN A 21 71.737 30.581 11.779 1.00 9.00 C
ANISOU 134 CA ASN A 21 1101 1237 1081 175 124 0 C
ATOM 135 C ASN A 21 71.369 29.577 10.707 1.00 9.60 C
ANISOU 135 C ASN A 21 1204 1261 1181 28 405 4 C
ATOM 136 O ASN A 21 71.356 28.349 10.911 1.00 10.71 O
ANISOU 136 O ASN A 21 1477 1378 1215 113 404 -72 O
ATOM 137 CB ASN A 21 72.792 31.582 11.307 1.00 9.62 C
ANISOU 137 CB ASN A 21 1249 1301 1106 173 210 -2 C
ATOM 138 CG ASN A 21 74.037 30.959 10.750 1.00 9.73 C
ANISOU 138 CG ASN A 21 1033 1430 1234 107 244 66 C
ATOM 139 OD1 ASN A 21 74.117 29.775 10.449 1.00 10.82 O
ANISOU 139 OD1 ASN A 21 1356 1450 1303 290 327 -11 O
ATOM 140 ND2 ASN A 21 75.065 31.794 10.622 1.00 11.91 N
ANISOU 140 ND2 ASN A 21 1376 1533 1617 103 355 111 N
ATOM 141 N GLU A 22 71.066 30.071 9.503 1.00 9.65 N
ANISOU 141 N GLU A 22 1239 1346 1084 57 264 -107 N
ATOM 142 CA GLU A 22 70.540 29.219 8.428 1.00 10.95 C
ANISOU 142 CA GLU A 22 1486 1512 1163 -108 214 -201 C
ATOM 143 C GLU A 22 71.575 28.328 7.795 1.00 10.80 C
ANISOU 143 C GLU A 22 1556 1398 1151 10 256 -70 C
ATOM 144 O GLU A 22 71.207 27.446 6.978 1.00 12.80 O
ANISOU 144 O GLU A 22 1931 1580 1353 22 227 -270 O
ATOM 145 CB GLU A 22 69.820 30.064 7.375 1.00 10.98 C
ANISOU 145 CB GLU A 22 1158 1732 1282 -80 176 -272 C
ATOM 146 CG GLU A 22 70.657 31.024 6.598 1.00 11.17 C
ANISOU 146 CG GLU A 22 1448 1652 1145 -3 23 -89 C
ATOM 147 CD GLU A 22 69.777 31.971 5.778 1.00 12.90 C
ANISOU 147 CD GLU A 22 1357 2330 1213 -75 -38 61 C
ATOM 148 OE1 GLU A 22 68.568 32.168 6.041 1.00 13.56 O
ANISOU 148 OE1 GLU A 22 1524 2316 1313 415 -173 -204 O
ATOM 149 OE2 GLU A 22 70.350 32.539 4.832 1.00 24.64 O
ANISOU 149 OE2 GLU A 22 1974 4934 2454 -91 -292 1990 O
ATOM 150 N ARG A 23 72.833 28.486 8.154 1.00 10.98 N
ANISOU 150 N ARG A 23 1342 1515 1317 207 249 -254 N
ATOM 151 CA ARG A 23 73.908 27.579 7.788 1.00 12.00 C
ANISOU 151 CA ARG A 23 1418 1667 1475 232 459 -197 C
ATOM 152 C ARG A 23 74.211 26.596 8.893 1.00 14.60 C
ANISOU 152 C ARG A 23 2334 1529 1686 581 642 -182 C
ATOM 153 O ARG A 23 75.150 25.793 8.767 1.00 18.07 O
ANISOU 153 O ARG A 23 2893 1900 2072 942 817 -141 O
ATOM 154 CB ARG A 23 75.144 28.335 7.330 1.00 13.18 C
ANISOU 154 CB ARG A 23 1452 1773 1783 191 433 -164 C
ATOM 155 CG ARG A 23 74.938 29.073 6.032 1.00 16.07 C
ANISOU 155 CG ARG A 23 2259 2118 1731 -260 677 -40 C
ATOM 156 CD ARG A 23 76.130 29.942 5.672 1.00 17.76 C
ANISOU 156 CD ARG A 23 2227 2094 2427 -217 959 -234 C
ATOM 157 NE ARG A 23 76.320 31.043 6.606 1.00 15.13 N
ANISOU 157 NE ARG A 23 1680 1834 2236 131 249 151 N
ATOM 158 CZ ARG A 23 75.469 32.083 6.569 1.00 17.24 C
ANISOU 158 CZ ARG A 23 2464 1918 2167 209 464 362 C
ATOM 159 NH1 ARG A 23 74.591 32.125 5.528 1.00 20.04 N
ANISOU 159 NH1 ARG A 23 1862 2442 3310 110 87 620 N
ATOM 160 NH2 ARG A 23 75.569 33.067 7.397 1.00 21.51 N
ANISOU 160 NH2 ARG A 23 3587 1703 2881 114 1312 133 N
ATOM 161 N GLY A 24 73.511 26.666 10.045 1.00 13.46 N
ANISOU 161 N GLY A 24 2157 1420 1536 410 582 -53 N
ATOM 162 CA GLY A 24 73.771 25.783 11.158 1.00 14.22 C
ANISOU 162 CA GLY A 24 2308 1385 1712 450 323 -112 C
ATOM 163 C GLY A 24 74.892 26.226 12.072 1.00 13.53 C
ANISOU 163 C GLY A 24 1894 1609 1638 503 487 59 C
ATOM 164 O GLY A 24 75.314 25.462 12.952 1.00 16.38 O
ANISOU 164 O GLY A 24 2463 1879 1881 806 573 280 O
ATOM 165 N GLU A 25 75.372 27.463 11.901 1.00 12.63 N
ANISOU 165 N GLU A 25 1667 1656 1476 458 457 87 N
ATOM 166 CA GLU A 25 76.442 27.994 12.714 1.00 13.04 C
ANISOU 166 CA GLU A 25 1608 1787 1561 602 536 168 C
ATOM 167 C GLU A 25 75.905 28.670 13.993 1.00 11.67 C
ANISOU 167 C GLU A 25 1250 1643 1542 405 406 203 C
ATOM 168 O GLU A 25 74.868 29.374 13.889 1.00 10.95 O
ANISOU 168 O GLU A 25 1084 1667 1411 298 254 44 O
ATOM 169 CB GLU A 25 77.224 29.033 11.912 1.00 14.59 C
ANISOU 169 CB GLU A 25 1583 2221 1740 426 634 259 C
ATOM 170 CG GLU A 25 77.792 28.474 10.637 1.00 16.69 C
ANISOU 170 CG GLU A 25 1992 2586 1761 562 850 248 C
ATOM 171 CD GLU A 25 78.158 29.464 9.575 1.00 22.04 C
ANISOU 171 CD GLU A 25 2925 3161 2289 1040 1161 866 C
ATOM 172 OE1 GLU A 25 77.667 30.609 9.531 1.00 20.78 O
ANISOU 172 OE1 GLU A 25 2375 2955 2565 655 1217 983 O
ATOM 173 OE2 GLU A 25 78.977 29.016 8.709 1.00 26.81 O
ANISOU 173 OE2 GLU A 25 3423 4079 2683 1369 1710 1177 O
ATOM 174 N GLN A 26 76.533 28.511 15.132 1.00 11.99 N
ANISOU 174 N GLN A 26 1125 1826 1603 456 295 152 N
ATOM 175 CA GLN A 26 76.073 29.202 16.341 1.00 10.74 C
ANISOU 175 CA GLN A 26 874 1773 1433 256 138 47 C
ATOM 176 C GLN A 26 76.056 30.698 16.148 1.00 11.23 C
ANISOU 176 C GLN A 26 1017 1781 1469 9 298 -5 C
ATOM 177 O GLN A 26 76.986 31.270 15.561 1.00 13.84 O
ANISOU 177 O GLN A 26 1294 2016 1950 -100 463 84 O
ATOM 178 CB GLN A 26 76.978 28.843 17.543 1.00 13.57 C
ANISOU 178 CB GLN A 26 1277 2134 1746 237 57 129 C
ATOM 179 CG AGLN A 26 76.811 27.424 18.054 0.65 14.10 C
ANISOU 179 CG AGLN A 26 1494 2211 1654 707 173 325 C
ATOM 180 CG BGLN A 26 76.800 27.352 17.877 0.35 15.21 C
ANISOU 180 CG BGLN A 26 1648 2116 2016 623 80 372 C
ATOM 181 CD AGLN A 26 77.631 27.150 19.310 0.65 15.82 C
ANISOU 181 CD AGLN A 26 1693 2297 2022 680 -116 76 C
ATOM 182 CD BGLN A 26 77.527 27.011 19.164 0.35 18.19 C
ANISOU 182 CD BGLN A 26 2785 2245 1880 670 0 404 C
ATOM 183 OE1AGLN A 26 78.251 27.987 19.975 0.65 17.86 O
ANISOU 183 OE1AGLN A 26 2077 2449 2259 589 -196 -90 O
ATOM 184 OE1BGLN A 26 78.634 26.477 19.116 0.35 22.64 O
ANISOU 184 OE1BGLN A 26 3142 2700 2762 1200 -160 496 O
ATOM 185 NE2AGLN A 26 77.657 25.859 19.647 0.65 22.14 N
ANISOU 185 NE2AGLN A 26 3115 2768 2531 676 37 1030 N
ATOM 186 NE2BGLN A 26 76.915 27.343 20.294 0.35 17.69 N
ANISOU 186 NE2BGLN A 26 3112 1762 1848 611 -33 203 N
ATOM 187 N VAL A 27 75.040 31.354 16.686 1.00 9.98 N
ANISOU 187 N VAL A 27 1051 1471 1272 125 165 34 N
ATOM 188 CA VAL A 27 74.930 32.802 16.684 1.00 10.93 C
ANISOU 188 CA VAL A 27 1298 1546 1311 39 95 79 C
ATOM 189 C VAL A 27 74.517 33.263 18.096 1.00 10.46 C
ANISOU 189 C VAL A 27 1150 1534 1291 37 178 98 C
ATOM 190 O VAL A 27 73.743 32.548 18.770 1.00 12.89 O
ANISOU 190 O VAL A 27 1567 1800 1532 -417 338 -231 O
ATOM 191 CB VAL A 27 74.051 33.340 15.596 1.00 13.97 C
ANISOU 191 CB VAL A 27 1675 1814 1820 393 -35 136 C
ATOM 192 CG1AVAL A 27 74.525 33.082 14.229 0.60 21.96 C
ANISOU 192 CG1AVAL A 27 4917 2206 1220 699 -479 -210 C
ATOM 193 CG1BVAL A 27 72.599 33.062 15.896 0.40 15.01 C
ANISOU 193 CG1BVAL A 27 1836 1560 2306 -271 -93 198 C
ATOM 194 CG2AVAL A 27 72.679 32.710 15.730 0.60 13.29 C
ANISOU 194 CG2AVAL A 27 1514 1984 1550 587 461 -40 C
ATOM 195 CG2BVAL A 27 74.230 34.828 15.350 0.40 13.94 C
ANISOU 195 CG2BVAL A 27 1694 2000 1603 428 223 674 C
ATOM 196 N GLN A 28 75.042 34.394 18.486 1.00 10.18 N
ANISOU 196 N GLN A 28 995 1348 1526 106 303 11 N
ATOM 197 CA GLN A 28 74.745 34.991 19.792 1.00 9.23 C
ANISOU 197 CA GLN A 28 790 1283 1434 73 125 -15 C
ATOM 198 C GLN A 28 74.212 36.402 19.572 1.00 9.07 C
ANISOU 198 C GLN A 28 917 1279 1252 28 194 -16 C
ATOM 199 O GLN A 28 74.865 37.265 18.966 1.00 11.15 O
ANISOU 199 O GLN A 28 1069 1377 1792 6 372 197 O
ATOM 200 CB GLN A 28 76.013 35.017 20.668 1.00 10.42 C
ANISOU 200 CB GLN A 28 845 1421 1695 62 -50 122 C
ATOM 201 CG GLN A 28 75.754 35.473 22.071 1.00 10.50 C
ANISOU 201 CG GLN A 28 928 1529 1534 102 -26 83 C
ATOM 202 CD GLN A 28 77.022 35.540 22.871 1.00 12.85 C
ANISOU 202 CD GLN A 28 1106 1971 1805 -110 -170 267 C
ATOM 203 OE1 GLN A 28 78.148 35.699 22.327 1.00 16.27 O
ANISOU 203 OE1 GLN A 28 1306 2743 2132 -123 -82 1 O
ATOM 204 NE2 GLN A 28 76.917 35.438 24.175 1.00 13.50 N
ANISOU 204 NE2 GLN A 28 1338 2162 1630 -356 -325 441 N
ATOM 205 N LEU A 29 72.982 36.621 20.049 1.00 7.78 N
ANISOU 205 N LEU A 29 828 1092 1036 104 53 -7 N
ATOM 206 CA LEU A 29 72.339 37.934 20.001 1.00 8.02 C
ANISOU 206 CA LEU A 29 865 1107 1075 15 37 53 C
ATOM 207 C LEU A 29 72.630 38.698 21.299 1.00 7.95 C
ANISOU 207 C LEU A 29 822 1149 1050 -23 10 36 C
ATOM 208 O LEU A 29 72.574 38.084 22.375 1.00 8.22 O
ANISOU 208 O LEU A 29 983 1142 998 16 34 14 O
ATOM 209 CB LEU A 29 70.831 37.812 19.731 1.00 8.26 C
ANISOU 209 CB LEU A 29 899 1129 1112 104 -56 -18 C
ATOM 210 CG LEU A 29 70.451 36.973 18.501 1.00 8.42 C
ANISOU 210 CG LEU A 29 899 1159 1140 82 -91 32 C
ATOM 211 CD1 LEU A 29 68.940 36.955 18.349 1.00 8.79 C
ANISOU 211 CD1 LEU A 29 862 1198 1279 47 -89 -20 C
ATOM 212 CD2 LEU A 29 71.116 37.519 17.235 1.00 10.14 C
ANISOU 212 CD2 LEU A 29 1115 1630 1109 1 -87 -22 C
ATOM 213 N LYS A 30 72.886 39.998 21.177 1.00 7.84 N
ANISOU 213 N LYS A 30 765 1138 1076 1 -10 0 N
ATOM 214 CA LYS A 30 73.087 40.881 22.349 1.00 7.90 C
ANISOU 214 CA LYS A 30 776 1161 1065 -63 95 27 C
ATOM 215 C LYS A 30 72.384 42.193 22.035 1.00 7.67 C
ANISOU 215 C LYS A 30 873 1070 971 -171 1 25 C
ATOM 216 O LYS A 30 72.641 42.831 20.993 1.00 8.62 O
ANISOU 216 O LYS A 30 1011 1142 1124 -32 137 92 O
ATOM 217 CB LYS A 30 74.549 41.126 22.686 1.00 8.63 C
ANISOU 217 CB LYS A 30 827 1246 1207 -124 -88 69 C
ATOM 218 CG LYS A 30 75.349 39.872 22.960 1.00 9.90 C
ANISOU 218 CG LYS A 30 1045 1502 1216 80 -93 66 C
ATOM 219 CD LYS A 30 76.824 40.153 23.252 1.00 11.44 C
ANISOU 219 CD LYS A 30 1091 1718 1538 113 -230 116 C
ATOM 220 CE LYS A 30 77.516 38.832 23.514 1.00 13.31 C
ANISOU 220 CE LYS A 30 1335 1858 1864 210 -292 -24 C
ATOM 221 NZ LYS A 30 78.972 39.043 23.788 1.00 14.30 N
ANISOU 221 NZ LYS A 30 1143 2315 1976 150 43 335 N
ATOM 222 N GLY A 31 71.526 42.639 22.939 1.00 7.68 N
ANISOU 222 N GLY A 31 803 1057 1058 16 -16 44 N
ATOM 223 CA GLY A 31 70.825 43.896 22.695 1.00 7.99 C
ANISOU 223 CA GLY A 31 855 1134 1048 -48 46 54 C
ATOM 224 C GLY A 31 70.157 44.448 23.946 1.00 7.47 C
ANISOU 224 C GLY A 31 732 1005 1101 -136 -47 83 C
ATOM 225 O GLY A 31 70.518 44.102 25.079 1.00 7.68 O
ANISOU 225 O GLY A 31 807 1052 1059 -19 -57 52 O
ATOM 226 N MET A 32 69.230 45.357 23.693 1.00 7.80 N
ANISOU 226 N MET A 32 768 1123 1073 -32 -43 50 N
ATOM 227 CA MET A 32 68.497 46.067 24.729 1.00 7.23 C
ANISOU 227 CA MET A 32 691 1008 1049 -95 -70 32 C
ATOM 228 C MET A 32 67.043 45.687 24.727 1.00 7.11 C
ANISOU 228 C MET A 32 724 926 1051 -93 -66 24 C
ATOM 229 O MET A 32 66.419 45.471 23.656 1.00 7.43 O
ANISOU 229 O MET A 32 735 1105 983 -66 -65 10 O
ATOM 230 CB MET A 32 68.597 47.608 24.560 1.00 7.50 C
ANISOU 230 CB MET A 32 747 1003 1100 -83 -47 50 C
ATOM 231 CG MET A 32 69.939 48.164 24.943 1.00 8.81 C
ANISOU 231 CG MET A 32 964 1139 1244 -135 -275 69 C
ATOM 232 SD MET A 32 70.420 47.875 26.666 1.00 8.36 S
ANISOU 232 SD MET A 32 863 1059 1255 -132 -255 70 S
ATOM 233 CE MET A 32 69.126 48.752 27.541 1.00 9.23 C
ANISOU 233 CE MET A 32 1068 1123 1315 -153 -156 -16 C
ATOM 234 N SER A 33 66.440 45.677 25.934 1.00 7.13 N
ANISOU 234 N SER A 33 712 962 1036 74 -59 -3 N
ATOM 235 CA SER A 33 65.006 45.718 26.122 1.00 6.97 C
ANISOU 235 CA SER A 33 699 958 991 -20 -63 -51 C
ATOM 236 C SER A 33 64.539 47.145 26.372 1.00 7.01 C
ANISOU 236 C SER A 33 780 919 966 -49 -38 0 C
ATOM 237 O SER A 33 65.195 47.907 27.095 1.00 7.79 O
ANISOU 237 O SER A 33 927 953 1079 -10 -63 -84 O
ATOM 238 CB SER A 33 64.620 44.857 27.350 1.00 7.12 C
ANISOU 238 CB SER A 33 708 921 1076 -57 -76 -49 C
ATOM 239 OG SER A 33 63.206 44.708 27.481 1.00 7.26 O
ANISOU 239 OG SER A 33 771 956 1033 -41 -2 -22 O
ATOM 240 N SER A 34 63.368 47.464 25.817 1.00 7.23 N
ANISOU 240 N SER A 34 836 952 960 35 8 -32 N
ATOM 241 CA SER A 34 62.641 48.635 26.279 1.00 7.32 C
ANISOU 241 CA SER A 34 825 900 1056 31 21 5 C
ATOM 242 C SER A 34 62.259 48.399 27.760 1.00 7.27 C
ANISOU 242 C SER A 34 751 960 1050 5 -51 -76 C
ATOM 243 O SER A 34 62.284 47.289 28.290 1.00 7.78 O
ANISOU 243 O SER A 34 980 947 1029 12 8 2 O
ATOM 244 CB SER A 34 61.371 48.842 25.463 1.00 7.67 C
ANISOU 244 CB SER A 34 925 873 1115 12 -20 -4 C
ATOM 245 OG SER A 34 60.356 47.869 25.728 1.00 7.56 O
ANISOU 245 OG SER A 34 778 1006 1089 -50 -14 -39 O
ATOM 246 N HIS A 35 61.893 49.531 28.424 1.00 8.01 N