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PROTEIN.pdb
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PROTEIN.pdb
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HEADER HYDROLASE/HYDROLASE INHIBITOR 31-JAN-11 3QK5
TITLE CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE WITH SMALL MOLECULE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY-ACID AMIDE HYDROLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 32-579;
COMPND 5 SYNONYM: ANANDAMIDE AMIDOHYDROLASE 1, OLEAMIDE HYDROLASE 1;
COMPND 6 EC: 3.5.1.99;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: FAAH, FAAH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCHISA
KEYWDS PROTEIN-INHIBITOR COMPLEX, FAAH, FATTY-ACID AMIDE HYDROLASE,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.MIN,N.P.C.WALKER,Z.WANG
REVDAT 3 13-SEP-23 3QK5 1 REMARK SEQADV
REVDAT 2 20-APR-11 3QK5 1 JRNL
REVDAT 1 06-APR-11 3QK5 0
JRNL AUTH D.J.GUSTIN,Z.MA,X.MIN,Y.LI,C.HEDBERG,C.GUIMARAES,A.C.PORTER,
JRNL AUTH 2 M.LINDSTROM,D.LESTER-ZEINER,G.XU,T.J.CARLSON,S.XIAO,
JRNL AUTH 3 C.MELEZA,R.CONNORS,Z.WANG,F.KAYSER
JRNL TITL IDENTIFICATION OF POTENT, NONCOVALENT FATTY ACID AMIDE
JRNL TITL 2 HYDROLASE (FAAH) INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 2492 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21392988
JRNL DOI 10.1016/J.BMCL.2011.02.052
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 72432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3648
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4954
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 259
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8438
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 881
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.868
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8864 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12026 ; 1.193 ; 2.004
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1133 ; 5.067 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 352 ;36.448 ;23.864
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1521 ;16.451 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;17.040 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1340 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6647 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5517 ; 0.325 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8908 ; 0.653 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3347 ; 1.108 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3098 ; 1.893 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3QK5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063746.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72512
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 85.589
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : 0.41000
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: MOLREP
REMARK 200 STARTING MODEL: 1MT5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, NH4F, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 45.71550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.29800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.35050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.29800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.71550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.35050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -7
REMARK 465 GLY A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 GLY A 3
REMARK 465 MET A 4
REMARK 465 ALA A 5
REMARK 465 SER A 6
REMARK 465 MET A 7
REMARK 465 THR A 8
REMARK 465 GLY A 9
REMARK 465 GLY A 10
REMARK 465 GLN A 11
REMARK 465 GLN A 12
REMARK 465 MET A 13
REMARK 465 GLY A 14
REMARK 465 ARG A 15
REMARK 465 ASP A 16
REMARK 465 LEU A 17
REMARK 465 TYR A 18
REMARK 465 ASP A 19
REMARK 465 ASP A 20
REMARK 465 ASP A 21
REMARK 465 ASP A 22
REMARK 465 LYS A 23
REMARK 465 ASP A 24
REMARK 465 ARG A 25
REMARK 465 TRP A 26
REMARK 465 GLY A 27
REMARK 465 SER A 28
REMARK 465 PRO A 578
REMARK 465 SER A 579
REMARK 465 MET B -7
REMARK 465 GLY B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 HIS B 2
REMARK 465 GLY B 3
REMARK 465 MET B 4
REMARK 465 ALA B 5
REMARK 465 SER B 6
REMARK 465 MET B 7
REMARK 465 THR B 8
REMARK 465 GLY B 9
REMARK 465 GLY B 10
REMARK 465 GLN B 11
REMARK 465 GLN B 12
REMARK 465 MET B 13
REMARK 465 GLY B 14
REMARK 465 ARG B 15
REMARK 465 ASP B 16
REMARK 465 LEU B 17
REMARK 465 TYR B 18
REMARK 465 ASP B 19
REMARK 465 ASP B 20
REMARK 465 ASP B 21
REMARK 465 ASP B 22
REMARK 465 LYS B 23
REMARK 465 ASP B 24
REMARK 465 ARG B 25
REMARK 465 TRP B 26
REMARK 465 GLY B 27
REMARK 465 SER B 28
REMARK 465 GLU B 29
REMARK 465 LEU B 30
REMARK 465 GLU B 31
REMARK 465 PRO B 578
REMARK 465 SER B 579
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 190 -10.22 70.68
REMARK 500 SER A 190 -7.73 68.43
REMARK 500 MET A 191 -1.19 75.69
REMARK 500 ASP A 195 -165.74 -104.36
REMARK 500 CYS A 196 64.56 -152.25
REMARK 500 LYS A 209 117.48 -166.49
REMARK 500 SER A 218 46.07 -82.53
REMARK 500 GLN A 557 51.09 -103.44
REMARK 500 GLN A 557 47.09 -100.39
REMARK 500 SER B 190 -9.52 73.11
REMARK 500 SER B 190 -7.95 71.74
REMARK 500 SER B 193 148.30 -170.45
REMARK 500 ASP B 195 -165.97 -100.91
REMARK 500 CYS B 196 66.77 -154.12
REMARK 500 LYS B 209 117.48 -164.92
REMARK 500 SER B 218 45.81 -77.19
REMARK 500 TYR B 335 -57.80 -122.76
REMARK 500 GLN B 557 47.76 -104.77
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 QK5 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 580
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 581
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 582
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 586
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QK5 B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 581
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 586
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 587
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 588
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QJ8 RELATED DB: PDB
REMARK 900 RELATED ID: 3QJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 3QKV RELATED DB: PDB
DBREF 3QK5 A 32 579 UNP P97612 FAAH1_RAT 32 579
DBREF 3QK5 B 32 579 UNP P97612 FAAH1_RAT 32 579
SEQADV 3QK5 MET A -7 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A -6 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A -5 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 SER A -4 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS A -3 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS A -2 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS A -1 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS A 0 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS A 1 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS A 2 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A 3 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET A 4 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ALA A 5 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 SER A 6 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET A 7 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 THR A 8 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A 9 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A 10 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLN A 11 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLN A 12 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET A 13 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A 14 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ARG A 15 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP A 16 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 LEU A 17 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 TYR A 18 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP A 19 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP A 20 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP A 21 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP A 22 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 LYS A 23 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP A 24 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ARG A 25 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 TRP A 26 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY A 27 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 SER A 28 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLU A 29 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 LEU A 30 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLU A 31 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET B -7 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B -6 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B -5 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 SER B -4 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS B -3 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS B -2 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS B -1 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS B 0 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS B 1 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 HIS B 2 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B 3 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET B 4 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ALA B 5 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 SER B 6 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET B 7 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 THR B 8 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B 9 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B 10 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLN B 11 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLN B 12 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 MET B 13 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B 14 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ARG B 15 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP B 16 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 LEU B 17 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 TYR B 18 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP B 19 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP B 20 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP B 21 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP B 22 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 LYS B 23 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ASP B 24 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 ARG B 25 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 TRP B 26 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLY B 27 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 SER B 28 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLU B 29 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 LEU B 30 UNP P97612 EXPRESSION TAG
SEQADV 3QK5 GLU B 31 UNP P97612 EXPRESSION TAG
SEQRES 1 A 587 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 587 SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR
SEQRES 3 A 587 ASP ASP ASP ASP LYS ASP ARG TRP GLY SER GLU LEU GLU
SEQRES 4 A 587 THR GLY ARG GLN LYS ALA ARG GLY ALA ALA THR ARG ALA
SEQRES 5 A 587 ARG GLN LYS GLN ARG ALA SER LEU GLU THR MET ASP LYS
SEQRES 6 A 587 ALA VAL GLN ARG PHE ARG LEU GLN ASN PRO ASP LEU ASP
SEQRES 7 A 587 SER GLU ALA LEU LEU THR LEU PRO LEU LEU GLN LEU VAL
SEQRES 8 A 587 GLN LYS LEU GLN SER GLY GLU LEU SER PRO GLU ALA VAL
SEQRES 9 A 587 PHE PHE THR TYR LEU GLY LYS ALA TRP GLU VAL ASN LYS
SEQRES 10 A 587 GLY THR ASN CYS VAL THR SER TYR LEU THR ASP CYS GLU
SEQRES 11 A 587 THR GLN LEU SER GLN ALA PRO ARG GLN GLY LEU LEU TYR
SEQRES 12 A 587 GLY VAL PRO VAL SER LEU LYS GLU CYS PHE SER TYR LYS
SEQRES 13 A 587 GLY HIS ASP SER THR LEU GLY LEU SER LEU ASN GLU GLY
SEQRES 14 A 587 MET PRO SER GLU SER ASP CYS VAL VAL VAL GLN VAL LEU
SEQRES 15 A 587 LYS LEU GLN GLY ALA VAL PRO PHE VAL HIS THR ASN VAL
SEQRES 16 A 587 PRO GLN SER MET LEU SER PHE ASP CYS SER ASN PRO LEU
SEQRES 17 A 587 PHE GLY GLN THR MET ASN PRO TRP LYS SER SER LYS SER
SEQRES 18 A 587 PRO GLY GLY SER SER GLY GLY GLU GLY ALA LEU ILE GLY
SEQRES 19 A 587 SER GLY GLY SER PRO LEU GLY LEU GLY THR ASP ILE GLY
SEQRES 20 A 587 GLY SER ILE ARG PHE PRO SER ALA PHE CYS GLY ILE CYS
SEQRES 21 A 587 GLY LEU LYS PRO THR GLY ASN ARG LEU SER LYS SER GLY
SEQRES 22 A 587 LEU LYS GLY CYS VAL TYR GLY GLN THR ALA VAL GLN LEU
SEQRES 23 A 587 SER LEU GLY PRO MET ALA ARG ASP VAL GLU SER LEU ALA
SEQRES 24 A 587 LEU CYS LEU LYS ALA LEU LEU CYS GLU HIS LEU PHE THR
SEQRES 25 A 587 LEU ASP PRO THR VAL PRO PRO LEU PRO PHE ARG GLU GLU
SEQRES 26 A 587 VAL TYR ARG SER SER ARG PRO LEU ARG VAL GLY TYR TYR
SEQRES 27 A 587 GLU THR ASP ASN TYR THR MET PRO SER PRO ALA MET ARG
SEQRES 28 A 587 ARG ALA LEU ILE GLU THR LYS GLN ARG LEU GLU ALA ALA
SEQRES 29 A 587 GLY HIS THR LEU ILE PRO PHE LEU PRO ASN ASN ILE PRO
SEQRES 30 A 587 TYR ALA LEU GLU VAL LEU SER ALA GLY GLY LEU PHE SER
SEQRES 31 A 587 ASP GLY GLY ARG SER PHE LEU GLN ASN PHE LYS GLY ASP
SEQRES 32 A 587 PHE VAL ASP PRO CYS LEU GLY ASP LEU ILE LEU ILE LEU
SEQRES 33 A 587 ARG LEU PRO SER TRP PHE LYS ARG LEU LEU SER LEU LEU
SEQRES 34 A 587 LEU LYS PRO LEU PHE PRO ARG LEU ALA ALA PHE LEU ASN
SEQRES 35 A 587 SER MET ARG PRO ARG SER ALA GLU LYS LEU TRP LYS LEU
SEQRES 36 A 587 GLN HIS GLU ILE GLU MET TYR ARG GLN SER VAL ILE ALA
SEQRES 37 A 587 GLN TRP LYS ALA MET ASN LEU ASP VAL LEU LEU THR PRO
SEQRES 38 A 587 MET LEU GLY PRO ALA LEU ASP LEU ASN THR PRO GLY ARG
SEQRES 39 A 587 ALA THR GLY ALA ILE SER TYR THR VAL LEU TYR ASN CYS
SEQRES 40 A 587 LEU ASP PHE PRO ALA GLY VAL VAL PRO VAL THR THR VAL
SEQRES 41 A 587 THR ALA GLU ASP ASP ALA GLN MET GLU LEU TYR LYS GLY
SEQRES 42 A 587 TYR PHE GLY ASP ILE TRP ASP ILE ILE LEU LYS LYS ALA
SEQRES 43 A 587 MET LYS ASN SER VAL GLY LEU PRO VAL ALA VAL GLN CYS
SEQRES 44 A 587 VAL ALA LEU PRO TRP GLN GLU GLU LEU CYS LEU ARG PHE
SEQRES 45 A 587 MET ARG GLU VAL GLU GLN LEU MET THR PRO GLN LYS GLN
SEQRES 46 A 587 PRO SER
SEQRES 1 B 587 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 B 587 SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR
SEQRES 3 B 587 ASP ASP ASP ASP LYS ASP ARG TRP GLY SER GLU LEU GLU
SEQRES 4 B 587 THR GLY ARG GLN LYS ALA ARG GLY ALA ALA THR ARG ALA
SEQRES 5 B 587 ARG GLN LYS GLN ARG ALA SER LEU GLU THR MET ASP LYS
SEQRES 6 B 587 ALA VAL GLN ARG PHE ARG LEU GLN ASN PRO ASP LEU ASP
SEQRES 7 B 587 SER GLU ALA LEU LEU THR LEU PRO LEU LEU GLN LEU VAL
SEQRES 8 B 587 GLN LYS LEU GLN SER GLY GLU LEU SER PRO GLU ALA VAL
SEQRES 9 B 587 PHE PHE THR TYR LEU GLY LYS ALA TRP GLU VAL ASN LYS
SEQRES 10 B 587 GLY THR ASN CYS VAL THR SER TYR LEU THR ASP CYS GLU
SEQRES 11 B 587 THR GLN LEU SER GLN ALA PRO ARG GLN GLY LEU LEU TYR
SEQRES 12 B 587 GLY VAL PRO VAL SER LEU LYS GLU CYS PHE SER TYR LYS
SEQRES 13 B 587 GLY HIS ASP SER THR LEU GLY LEU SER LEU ASN GLU GLY
SEQRES 14 B 587 MET PRO SER GLU SER ASP CYS VAL VAL VAL GLN VAL LEU
SEQRES 15 B 587 LYS LEU GLN GLY ALA VAL PRO PHE VAL HIS THR ASN VAL
SEQRES 16 B 587 PRO GLN SER MET LEU SER PHE ASP CYS SER ASN PRO LEU
SEQRES 17 B 587 PHE GLY GLN THR MET ASN PRO TRP LYS SER SER LYS SER
SEQRES 18 B 587 PRO GLY GLY SER SER GLY GLY GLU GLY ALA LEU ILE GLY
SEQRES 19 B 587 SER GLY GLY SER PRO LEU GLY LEU GLY THR ASP ILE GLY
SEQRES 20 B 587 GLY SER ILE ARG PHE PRO SER ALA PHE CYS GLY ILE CYS
SEQRES 21 B 587 GLY LEU LYS PRO THR GLY ASN ARG LEU SER LYS SER GLY
SEQRES 22 B 587 LEU LYS GLY CYS VAL TYR GLY GLN THR ALA VAL GLN LEU
SEQRES 23 B 587 SER LEU GLY PRO MET ALA ARG ASP VAL GLU SER LEU ALA
SEQRES 24 B 587 LEU CYS LEU LYS ALA LEU LEU CYS GLU HIS LEU PHE THR
SEQRES 25 B 587 LEU ASP PRO THR VAL PRO PRO LEU PRO PHE ARG GLU GLU
SEQRES 26 B 587 VAL TYR ARG SER SER ARG PRO LEU ARG VAL GLY TYR TYR
SEQRES 27 B 587 GLU THR ASP ASN TYR THR MET PRO SER PRO ALA MET ARG
SEQRES 28 B 587 ARG ALA LEU ILE GLU THR LYS GLN ARG LEU GLU ALA ALA
SEQRES 29 B 587 GLY HIS THR LEU ILE PRO PHE LEU PRO ASN ASN ILE PRO
SEQRES 30 B 587 TYR ALA LEU GLU VAL LEU SER ALA GLY GLY LEU PHE SER
SEQRES 31 B 587 ASP GLY GLY ARG SER PHE LEU GLN ASN PHE LYS GLY ASP
SEQRES 32 B 587 PHE VAL ASP PRO CYS LEU GLY ASP LEU ILE LEU ILE LEU
SEQRES 33 B 587 ARG LEU PRO SER TRP PHE LYS ARG LEU LEU SER LEU LEU
SEQRES 34 B 587 LEU LYS PRO LEU PHE PRO ARG LEU ALA ALA PHE LEU ASN
SEQRES 35 B 587 SER MET ARG PRO ARG SER ALA GLU LYS LEU TRP LYS LEU
SEQRES 36 B 587 GLN HIS GLU ILE GLU MET TYR ARG GLN SER VAL ILE ALA
SEQRES 37 B 587 GLN TRP LYS ALA MET ASN LEU ASP VAL LEU LEU THR PRO
SEQRES 38 B 587 MET LEU GLY PRO ALA LEU ASP LEU ASN THR PRO GLY ARG
SEQRES 39 B 587 ALA THR GLY ALA ILE SER TYR THR VAL LEU TYR ASN CYS
SEQRES 40 B 587 LEU ASP PHE PRO ALA GLY VAL VAL PRO VAL THR THR VAL
SEQRES 41 B 587 THR ALA GLU ASP ASP ALA GLN MET GLU LEU TYR LYS GLY
SEQRES 42 B 587 TYR PHE GLY ASP ILE TRP ASP ILE ILE LEU LYS LYS ALA
SEQRES 43 B 587 MET LYS ASN SER VAL GLY LEU PRO VAL ALA VAL GLN CYS
SEQRES 44 B 587 VAL ALA LEU PRO TRP GLN GLU GLU LEU CYS LEU ARG PHE
SEQRES 45 B 587 MET ARG GLU VAL GLU GLN LEU MET THR PRO GLN LYS GLN
SEQRES 46 B 587 PRO SER
HET QK5 A 600 34
HET EDO A 580 4
HET EDO A 581 4
HET EDO A 582 4
HET GOL A 583 6
HET EDO A 584 4
HET EDO A 585 4
HET EDO A 586 4
HET QK5 B 600 34
HET EDO B 580 4
HET EDO B 581 4
HET EDO B 582 4
HET EDO B 583 4
HET EDO B 584 4
HET EDO B 585 4
HET EDO B 586 4
HET EDO B 587 4
HET EDO B 588 4
HETNAM QK5 (3-{(3R)-1-[4-(1-BENZOTHIOPHEN-2-YL)PYRIMIDIN-2-
HETNAM 2 QK5 YL]PIPERIDIN-3-YL}-2-METHYL-1H-PYRROLO[2,3-B]PYRIDIN-
HETNAM 3 QK5 1-YL)ACETONITRILE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 QK5 2(C27 H24 N6 S)
FORMUL 4 EDO 15(C2 H6 O2)
FORMUL 7 GOL C3 H8 O3
FORMUL 21 HOH *881(H2 O)
HELIX 1 1 ARG A 34 ASN A 66 1 33
HELIX 2 2 ASP A 70 THR A 76 1 7
HELIX 3 3 PRO A 78 GLY A 89 1 12
HELIX 4 4 SER A 92 ASN A 112 1 21
HELIX 5 5 ASP A 120 ALA A 128 1 9
HELIX 6 6 LEU A 156 GLU A 160 5 5
HELIX 7 7 CYS A 168 GLN A 177 1 10
HELIX 8 8 PRO A 188 LEU A 192 5 5
HELIX 9 9 SER A 218 SER A 227 1 10
HELIX 10 10 ILE A 242 GLY A 250 1 9
HELIX 11 11 ASP A 286 LEU A 298 1 13
HELIX 12 12 CYS A 299 ASP A 306 1 8
HELIX 13 13 ARG A 315 SER A 321 1 7
HELIX 14 14 SER A 339 ALA A 356 1 18
HELIX 15 15 ASN A 367 VAL A 374 1 8
HELIX 16 16 VAL A 374 PHE A 381 1 8
HELIX 17 17 GLY A 385 GLN A 390 1 6
HELIX 18 18 ASN A 391 LYS A 393 5 3
HELIX 19 19 ASP A 398 GLY A 402 5 5
HELIX 20 20 ASP A 403 LEU A 410 1 8
HELIX 21 21 PRO A 411 LYS A 423 1 13
HELIX 22 22 PHE A 426 SER A 435 1 10
HELIX 23 23 SER A 440 MET A 465 1 26
HELIX 24 24 THR A 483 ALA A 490 5 8
HELIX 25 25 ILE A 491 ASP A 501 1 11
HELIX 26 26 THR A 513 GLN A 519 1 7
HELIX 27 27 MET A 520 TYR A 523 5 4
HELIX 28 28 ASP A 529 MET A 539 1 11
HELIX 29 29 GLN A 557 THR A 573 1 17
HELIX 30 30 PRO A 574 GLN A 577 5 4
HELIX 31 31 ARG B 34 ASN B 66 1 33
HELIX 32 32 ASP B 70 LEU B 77 1 8
HELIX 33 33 PRO B 78 GLY B 89 1 12
HELIX 34 34 SER B 92 ASN B 112 1 21
HELIX 35 35 ASP B 120 ALA B 128 1 9
HELIX 36 36 LEU B 156 GLU B 160 5 5
HELIX 37 37 CYS B 168 GLN B 177 1 10
HELIX 38 38 PRO B 188 LEU B 192 5 5
HELIX 39 39 SER B 218 SER B 227 1 10
HELIX 40 40 ILE B 242 GLY B 250 1 9
HELIX 41 41 ASP B 286 LEU B 298 1 13
HELIX 42 42 CYS B 299 ASP B 306 1 8
HELIX 43 43 ARG B 315 ARG B 320 1 6
HELIX 44 44 SER B 339 ALA B 356 1 18
HELIX 45 45 ASN B 367 VAL B 374 1 8
HELIX 46 46 VAL B 374 PHE B 381 1 8
HELIX 47 47 GLY B 385 ASN B 391 1 7
HELIX 48 48 ASP B 398 GLY B 402 5 5
HELIX 49 49 ASP B 403 LEU B 410 1 8
HELIX 50 50 PRO B 411 LYS B 423 1 13
HELIX 51 51 PHE B 426 MET B 436 1 11
HELIX 52 52 SER B 440 MET B 465 1 26
HELIX 53 53 THR B 483 ALA B 490 5 8
HELIX 54 54 ILE B 491 LEU B 500 1 10
HELIX 55 55 THR B 513 GLN B 519 1 7
HELIX 56 56 MET B 520 TYR B 523 5 4
HELIX 57 57 ASP B 529 MET B 539 1 11
HELIX 58 58 GLN B 557 THR B 573 1 17
HELIX 59 59 PRO B 574 GLN B 577 5 4
SHEET 1 A11 VAL A 114 TYR A 117 0
SHEET 2 A11 VAL A 180 THR A 185 -1 O HIS A 184 N THR A 115
SHEET 3 A11 PRO A 138 LYS A 142 1 N LEU A 141 O THR A 185
SHEET 4 A11 LEU A 232 ASP A 237 1 O LEU A 232 N SER A 140
SHEET 5 A11 SER A 279 ALA A 284 -1 O MET A 283 N GLY A 233
SHEET 6 A11 CYS A 252 LYS A 255 -1 N CYS A 252 O ALA A 284
SHEET 7 A11 ALA A 504 THR A 511 -1 O ALA A 504 N LYS A 255
SHEET 8 A11 PRO A 546 VAL A 552 -1 O CYS A 551 N GLY A 505
SHEET 9 A11 VAL A 469 PRO A 473 -1 N THR A 472 O GLN A 550
SHEET 10 A11 ARG A 326 TYR A 329 1 N GLY A 328 O LEU A 471
SHEET 11 A11 THR A 359 PRO A 362 1 O ILE A 361 N VAL A 327
SHEET 1 B 2 SER A 197 ASN A 198 0
SHEET 2 B 2 GLY A 202 GLN A 203 -1 O GLY A 202 N ASN A 198
SHEET 1 C11 VAL B 114 TYR B 117 0
SHEET 2 C11 VAL B 180 THR B 185 -1 O HIS B 184 N THR B 115
SHEET 3 C11 PRO B 138 LYS B 142 1 N LEU B 141 O VAL B 183
SHEET 4 C11 LEU B 232 ASP B 237 1 O LEU B 232 N SER B 140
SHEET 5 C11 SER B 279 ALA B 284 -1 O SER B 279 N ASP B 237
SHEET 6 C11 CYS B 252 LYS B 255 -1 N CYS B 252 O ALA B 284
SHEET 7 C11 ALA B 504 THR B 511 -1 O ALA B 504 N LYS B 255
SHEET 8 C11 PRO B 546 VAL B 552 -1 O CYS B 551 N GLY B 505
SHEET 9 C11 VAL B 469 PRO B 473 -1 N THR B 472 O GLN B 550
SHEET 10 C11 ARG B 326 TYR B 329 1 N GLY B 328 O LEU B 471
SHEET 11 C11 THR B 359 PRO B 362 1 O THR B 359 N VAL B 327
SHEET 1 D 2 SER B 197 ASN B 198 0
SHEET 2 D 2 GLY B 202 GLN B 203 -1 O GLY B 202 N ASN B 198
CISPEP 1 GLY A 216 SER A 217 0 6.29
CISPEP 2 GLY A 476 PRO A 477 0 -1.58
CISPEP 3 GLY B 216 SER B 217 0 4.06
CISPEP 4 GLY B 476 PRO B 477 0 -2.24
SITE 1 AC1 17 MET A 191 LEU A 192 SER A 193 PHE A 194
SITE 2 AC1 17 ILE A 238 GLY A 239 GLY A 240 SER A 241
SITE 3 AC1 17 PHE A 244 PHE A 381 LEU A 404 ILE A 407
SITE 4 AC1 17 LEU A 429 GLY A 485 THR A 488 TRP A 531
SITE 5 AC1 17 HOH A 594
SITE 1 AC2 2 ARG A 34 VAL A 397
SITE 1 AC3 2 THR A 32 HOH A 680
SITE 1 AC4 3 ASN A 334 TYR A 526 HOH A 758
SITE 1 AC5 3 VAL A 509 THR A 510 LEU B 64
SITE 1 AC6 6 GLU A 288 LEU A 292 LYS A 295 PHE A 314
SITE 2 AC6 6 GLU A 316 ARG A 320
SITE 1 AC7 4 ARG A 437 PRO A 438 ARG A 439 LYS A 443
SITE 1 AC8 5 GLY A 250 ILE A 251 ARG A 285 HOH A 611
SITE 2 AC8 5 HOH A 828
SITE 1 AC9 16 LEU B 192 SER B 193 ILE B 238 GLY B 239
SITE 2 AC9 16 GLY B 240 SER B 241 PHE B 244 LEU B 380
SITE 3 AC9 16 PHE B 381 LEU B 404 ILE B 407 LEU B 429
SITE 4 AC9 16 GLY B 485 THR B 488 HOH B 590 HOH B 924
SITE 1 BC1 2 ARG B 439 HOH B 754
SITE 1 BC2 3 ASN B 334 TYR B 526 HOH B 619
SITE 1 BC3 1 ARG B 285
SITE 1 BC4 6 SER B 321 SER B 322 ARG B 563 ARG B 566
SITE 2 BC4 6 GLU B 567 HOH B 902
SITE 1 BC5 1 SER B 146
SITE 1 BC6 5 LEU B 80 GLN B 81 GLU B 288 HOH B 629
SITE 2 BC6 5 HOH B 862
SITE 1 BC7 8 ASN A 366 HOH A 746 HOH A 906 ASP B 517
SITE 2 BC7 8 LYS B 540 ASN B 541 HOH B 643 HOH B 861
CRYST1 91.431 104.701 148.596 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010937 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006730 0.00000
ATOM 1 N GLU A 29 -35.491 -14.738 -9.513 1.00 32.42 N
ATOM 2 CA GLU A 29 -35.249 -15.961 -8.683 1.00 32.39 C
ATOM 3 C GLU A 29 -35.954 -15.873 -7.328 1.00 31.94 C
ATOM 4 O GLU A 29 -35.983 -14.813 -6.702 1.00 31.94 O
ATOM 5 CB GLU A 29 -33.750 -16.204 -8.489 1.00 32.46 C
ATOM 6 CG GLU A 29 -33.386 -17.675 -8.349 1.00 33.71 C
ATOM 7 CD GLU A 29 -31.909 -17.908 -8.061 1.00 35.39 C
ATOM 8 OE1 GLU A 29 -31.511 -17.824 -6.878 1.00 36.09 O
ATOM 9 OE2 GLU A 29 -31.149 -18.203 -9.012 1.00 35.92 O
ATOM 10 N LEU A 30 -36.516 -16.999 -6.893 1.00 31.56 N
ATOM 11 CA LEU A 30 -37.280 -17.094 -5.644 1.00 31.06 C
ATOM 12 C LEU A 30 -36.437 -16.784 -4.400 1.00 30.62 C
ATOM 13 O LEU A 30 -35.309 -17.269 -4.271 1.00 30.53 O
ATOM 14 CB LEU A 30 -37.886 -18.498 -5.526 1.00 31.21 C
ATOM 15 CG LEU A 30 -38.838 -18.845 -4.378 1.00 31.64 C
ATOM 16 CD1 LEU A 30 -40.179 -18.109 -4.516 1.00 31.54 C
ATOM 17 CD2 LEU A 30 -39.050 -20.355 -4.327 1.00 31.58 C
ATOM 18 N GLU A 31 -36.998 -15.986 -3.490 1.00 29.91 N
ATOM 19 CA GLU A 31 -36.336 -15.648 -2.229 1.00 29.39 C
ATOM 20 C GLU A 31 -36.239 -16.863 -1.300 1.00 28.68 C
ATOM 21 O GLU A 31 -37.253 -17.470 -0.942 1.00 28.67 O
ATOM 22 CB GLU A 31 -37.047 -14.483 -1.527 1.00 29.62 C
ATOM 23 CG GLU A 31 -36.412 -14.061 -0.190 1.00 30.74 C
ATOM 24 CD GLU A 31 -34.985 -13.540 -0.340 1.00 32.58 C
ATOM 25 OE1 GLU A 31 -34.767 -12.592 -1.130 1.00 33.67 O
ATOM 26 OE2 GLU A 31 -34.080 -14.075 0.339 1.00 32.90 O
ATOM 27 N THR A 32 -35.009 -17.201 -0.917 1.00 27.70 N
ATOM 28 CA THR A 32 -34.737 -18.397 -0.113 1.00 26.81 C
ATOM 29 C THR A 32 -34.501 -18.095 1.373 1.00 26.20 C
ATOM 30 O THR A 32 -34.396 -19.013 2.184 1.00 26.02 O
ATOM 31 CB THR A 32 -33.539 -19.215 -0.680 1.00 26.84 C
ATOM 32 OG1 THR A 32 -32.338 -18.433 -0.613 1.00 27.14 O
ATOM 33 CG2 THR A 32 -33.792 -19.634 -2.127 1.00 26.53 C
ATOM 34 N GLY A 33 -34.421 -16.812 1.723 1.00 25.49 N
ATOM 35 CA GLY A 33 -34.241 -16.402 3.113 1.00 24.63 C
ATOM 36 C GLY A 33 -32.829 -16.627 3.620 1.00 24.19 C
ATOM 37 O GLY A 33 -31.884 -16.742 2.831 1.00 24.04 O
ATOM 38 N ARG A 34 -32.691 -16.714 4.941 1.00 23.72 N
ATOM 39 CA ARG A 34 -31.375 -16.710 5.581 1.00 23.22 C
ATOM 40 C ARG A 34 -31.119 -17.867 6.549 1.00 23.10 C
ATOM 41 O ARG A 34 -30.145 -17.830 7.311 1.00 23.16 O
ATOM 42 CB ARG A 34 -31.164 -15.381 6.322 1.00 23.18 C
ATOM 43 CG ARG A 34 -31.242 -14.120 5.464 1.00 23.03 C
ATOM 44 CD ARG A 34 -29.984 -13.908 4.612 1.00 22.45 C
ATOM 45 NE ARG A 34 -30.102 -12.704 3.793 1.00 21.56 N
ATOM 46 CZ ARG A 34 -30.694 -12.656 2.602 1.00 21.71 C
ATOM 47 NH1 ARG A 34 -31.221 -13.751 2.064 1.00 21.66 N
ATOM 48 NH2 ARG A 34 -30.756 -11.509 1.942 1.00 21.11 N
ATOM 49 N GLN A 35 -31.972 -18.891 6.522 1.00 22.81 N
ATOM 50 CA GLN A 35 -31.883 -19.978 7.507 1.00 22.71 C
ATOM 51 C GLN A 35 -30.642 -20.858 7.337 1.00 22.43 C
ATOM 52 O GLN A 35 -30.038 -21.280 8.324 1.00 22.27 O
ATOM 53 CB GLN A 35 -33.164 -20.820 7.541 1.00 22.75 C
ATOM 54 CG GLN A 35 -34.406 -20.059 8.042 1.00 23.88 C
ATOM 55 CD GLN A 35 -34.182 -19.333 9.365 1.00 25.12 C
ATOM 56 OE1 GLN A 35 -34.280 -18.106 9.433 1.00 27.17 O
ATOM 57 NE2 GLN A 35 -33.871 -20.085 10.414 1.00 24.71 N
ATOM 58 N LYS A 36 -30.271 -21.129 6.090 1.00 22.14 N
ATOM 59 CA LYS A 36 -29.024 -21.828 5.797 1.00 22.25 C
ATOM 60 C LYS A 36 -27.823 -20.979 6.248 1.00 21.77 C
ATOM 61 O LYS A 36 -26.910 -21.490 6.894 1.00 21.54 O
ATOM 62 CB LYS A 36 -28.941 -22.168 4.307 1.00 22.53 C
ATOM 63 CG LYS A 36 -27.975 -23.296 3.957 1.00 24.24 C
ATOM 64 CD LYS A 36 -28.076 -23.670 2.477 1.00 26.00 C
ATOM 65 CE LYS A 36 -26.885 -24.518 2.027 1.00 28.84 C
ATOM 66 NZ LYS A 36 -25.612 -23.722 1.939 1.00 30.34 N
ATOM 67 N ALA A 37 -27.861 -19.682 5.933 1.00 21.28 N
ATOM 68 CA ALA A 37 -26.805 -18.733 6.307 1.00 21.01 C
ATOM 69 C ALA A 37 -26.622 -18.611 7.820 1.00 20.78 C
ATOM 70 O ALA A 37 -25.493 -18.509 8.309 1.00 20.88 O
ATOM 71 CB ALA A 37 -27.080 -17.361 5.693 1.00 20.73 C
ATOM 72 N ARG A 38 -27.734 -18.627 8.554 1.00 20.60 N
ATOM 73 CA ARG A 38 -27.696 -18.571 10.013 1.00 20.45 C
ATOM 74 C ARG A 38 -27.096 -19.833 10.609 1.00 20.19 C
ATOM 75 O ARG A 38 -26.313 -19.752 11.561 1.00 20.10 O
ATOM 76 CB ARG A 38 -29.085 -18.315 10.596 1.00 20.61 C
ATOM 77 CG ARG A 38 -29.603 -16.909 10.355 1.00 21.86 C
ATOM 78 CD ARG A 38 -30.962 -16.701 11.001 1.00 23.84 C
ATOM 79 NE ARG A 38 -30.871 -16.714 12.457 1.00 25.30 N
ATOM 80 CZ ARG A 38 -31.918 -16.697 13.277 1.00 27.57 C
ATOM 81 NH1 ARG A 38 -31.728 -16.714 14.590 1.00 27.12 N
ATOM 82 NH2 ARG A 38 -33.154 -16.671 12.788 1.00 28.44 N
ATOM 83 N GLY A 39 -27.458 -20.987 10.041 1.00 19.74 N
ATOM 84 CA GLY A 39 -26.897 -22.277 10.442 1.00 19.40 C
ATOM 85 C GLY A 39 -25.396 -22.341 10.208 1.00 19.37 C
ATOM 86 O GLY A 39 -24.639 -22.805 11.069 1.00 19.11 O
ATOM 87 N ALA A 40 -24.964 -21.858 9.044 1.00 19.24 N
ATOM 88 CA ALA A 40 -23.535 -21.773 8.721 1.00 19.41 C
ATOM 89 C ALA A 40 -22.779 -20.915 9.741 1.00 19.37 C
ATOM 90 O ALA A 40 -21.671 -21.260 10.153 1.00 19.62 O
ATOM 91 CB ALA A 40 -23.344 -21.223 7.316 1.00 19.03 C
ATOM 92 N ALA A 41 -23.391 -19.809 10.153 1.00 19.51 N
ATOM 93 CA ALA A 41 -22.777 -18.891 11.114 1.00 19.84 C
ATOM 94 C ALA A 41 -22.608 -19.497 12.509 1.00 20.07 C
ATOM 95 O ALA A 41 -21.581 -19.271 13.163 1.00 20.23 O
ATOM 96 CB ALA A 41 -23.562 -17.589 11.186 1.00 19.55 C
ATOM 97 N THR A 42 -23.601 -20.263 12.963 1.00 19.94 N
ATOM 98 CA THR A 42 -23.498 -20.912 14.270 1.00 20.23 C
ATOM 99 C THR A 42 -22.463 -22.033 14.217 1.00 19.97 C
ATOM 100 O THR A 42 -21.654 -22.171 15.132 1.00 19.95 O
ATOM 101 CB THR A 42 -24.857 -21.435 14.822 1.00 20.42 C
ATOM 102 OG1 THR A 42 -25.094 -22.778 14.386 1.00 22.02 O
ATOM 103 CG2 THR A 42 -25.999 -20.549 14.391 1.00 19.71 C
ATOM 104 N ARG A 43 -22.485 -22.808 13.134 1.00 19.97 N
ATOM 105 CA ARG A 43 -21.465 -23.841 12.889 1.00 20.16 C
ATOM 106 C ARG A 43 -20.044 -23.269 12.847 1.00 19.64 C
ATOM 107 O ARG A 43 -19.142 -23.827 13.464 1.00 19.80 O
ATOM 108 CB ARG A 43 -21.757 -24.620 11.603 1.00 20.27 C
ATOM 109 CG ARG A 43 -22.678 -25.813 11.784 1.00 21.36 C
ATOM 110 CD ARG A 43 -22.933 -26.527 10.459 1.00 23.91 C
ATOM 111 NE ARG A 43 -24.268 -26.235 9.934 1.00 26.44 N
ATOM 112 CZ ARG A 43 -24.525 -25.685 8.751 1.00 27.48 C
ATOM 113 NH1 ARG A 43 -25.781 -25.466 8.394 1.00 29.34 N
ATOM 114 NH2 ARG A 43 -23.543 -25.359 7.922 1.00 27.62 N
ATOM 115 N ALA A 44 -19.862 -22.154 12.140 1.00 19.27 N
ATOM 116 CA ALA A 44 -18.539 -21.527 11.977 1.00 18.96 C
ATOM 117 C ALA A 44 -17.995 -20.964 13.283 1.00 18.92 C
ATOM 118 O ALA A 44 -16.804 -21.086 13.572 1.00 18.40 O
ATOM 119 CB ALA A 44 -18.579 -20.441 10.920 1.00 18.56 C
ATOM 120 N ARG A 45 -18.870 -20.341 14.067 1.00 19.22 N
ATOM 121 CA ARG A 45 -18.461 -19.773 15.342 1.00 19.43 C
ATOM 122 C ARG A 45 -18.124 -20.850 16.354 1.00 19.36 C
ATOM 123 O ARG A 45 -17.278 -20.640 17.223 1.00 19.71 O
ATOM 124 CB ARG A 45 -19.489 -18.768 15.881 1.00 19.67 C
ATOM 125 CG ARG A 45 -19.658 -17.572 14.950 1.00 21.17 C
ATOM 126 CD ARG A 45 -19.506 -16.223 15.626 1.00 23.49 C
ATOM 127 NE ARG A 45 -18.121 -15.913 15.968 1.00 26.01 N
ATOM 128 CZ ARG A 45 -17.641 -14.683 16.170 1.00 26.39 C
ATOM 129 NH1 ARG A 45 -16.363 -14.518 16.492 1.00 24.57 N
ATOM 130 NH2 ARG A 45 -18.428 -13.618 16.044 1.00 26.33 N
ATOM 131 N GLN A 46 -18.758 -22.013 16.224 1.00 19.21 N
ATOM 132 CA GLN A 46 -18.400 -23.162 17.058 1.00 19.24 C
ATOM 133 C GLN A 46 -17.018 -23.707 16.714 1.00 19.48 C
ATOM 134 O GLN A 46 -16.245 -24.032 17.613 1.00 19.58 O
ATOM 135 CB GLN A 46 -19.443 -24.279 16.962 1.00 18.84 C
ATOM 136 CG GLN A 46 -19.124 -25.521 17.816 1.00 17.77 C
ATOM 137 CD GLN A 46 -18.956 -25.211 19.307 1.00 16.19 C
ATOM 138 OE1 GLN A 46 -19.436 -24.191 19.808 1.00 13.29 O
ATOM 139 NE2 GLN A 46 -18.261 -26.096 20.016 1.00 15.94 N
ATOM 140 N LYS A 47 -16.720 -23.805 15.419 1.00 19.79 N
ATOM 141 CA LYS A 47 -15.414 -24.276 14.958 1.00 20.47 C
ATOM 142 C LYS A 47 -14.299 -23.355 15.424 1.00 20.39 C
ATOM 143 O LYS A 47 -13.236 -23.826 15.840 1.00 20.35 O
ATOM 144 CB LYS A 47 -15.380 -24.408 13.436 1.00 20.74 C
ATOM 145 CG LYS A 47 -16.258 -25.517 12.899 1.00 22.75 C
ATOM 146 CD LYS A 47 -16.150 -25.615 11.394 1.00 25.67 C
ATOM 147 CE LYS A 47 -17.280 -26.453 10.819 1.00 27.47 C
ATOM 148 NZ LYS A 47 -17.348 -26.298 9.330 1.00 29.08 N
ATOM 149 N GLN A 48 -14.550 -22.048 15.352 1.00 20.40 N
ATOM 150 CA GLN A 48 -13.632 -21.037 15.877 1.00 20.60 C
ATOM 151 C GLN A 48 -13.468 -21.174 17.399 1.00 20.85 C
ATOM 152 O GLN A 48 -12.347 -21.162 17.920 1.00 20.95 O
ATOM 153 CB GLN A 48 -14.134 -19.637 15.501 1.00 20.57 C
ATOM 154 CG GLN A 48 -13.319 -18.473 16.068 1.00 20.75 C
ATOM 155 CD GLN A 48 -13.978 -17.128 15.819 1.00 21.25 C
ATOM 156 OE1 GLN A 48 -15.167 -16.946 16.090 1.00 22.49 O
ATOM 157 NE2 GLN A 48 -13.208 -16.176 15.305 1.00 20.82 N
ATOM 158 N ARG A 49 -14.596 -21.304 18.095 1.00 20.96 N
ATOM 159 CA ARG A 49 -14.634 -21.492 19.546 1.00 21.46 C
ATOM 160 C ARG A 49 -13.849 -22.737 19.972 1.00 21.85 C
ATOM 161 O ARG A 49 -12.983 -22.659 20.844 1.00 22.00 O
ATOM 162 CB ARG A 49 -16.095 -21.588 19.999 1.00 21.36 C
ATOM 163 CG ARG A 49 -16.332 -21.655 21.490 1.00 21.56 C
ATOM 164 CD ARG A 49 -17.836 -21.643 21.787 1.00 19.89 C
ATOM 165 NE ARG A 49 -18.462 -20.387 21.365 1.00 19.20 N
ATOM 166 CZ ARG A 49 -19.348 -20.264 20.377 1.00 19.07 C
ATOM 167 NH1 ARG A 49 -19.843 -19.068 20.087 1.00 18.56 N
ATOM 168 NH2 ARG A 49 -19.753 -21.324 19.685 1.00 18.74 N
ATOM 169 N ALA A 50 -14.149 -23.873 19.342 1.00 22.29 N
ATOM 170 CA ALA A 50 -13.451 -25.136 19.601 1.00 22.99 C
ATOM 171 C ALA A 50 -11.954 -25.067 19.289 1.00 23.62 C
ATOM 172 O ALA A 50 -11.138 -25.621 20.035 1.00 23.96 O
ATOM 173 CB ALA A 50 -14.099 -26.272 18.821 1.00 23.06 C
ATOM 174 N SER A 51 -11.608 -24.395 18.189 1.00 24.09 N
ATOM 175 CA SER A 51 -10.213 -24.165 17.784 1.00 24.61 C
ATOM 176 C SER A 51 -9.391 -23.503 18.879 1.00 24.98 C
ATOM 177 O SER A 51 -8.323 -23.994 19.244 1.00 25.21 O
ATOM 178 CB SER A 51 -10.146 -23.289 16.527 1.00 24.17 C
ATOM 179 OG SER A 51 -10.423 -24.042 15.365 1.00 24.27 O
ATOM 180 N LEU A 52 -9.897 -22.382 19.384 1.00 25.38 N
ATOM 181 CA LEU A 52 -9.208 -21.598 20.403 1.00 25.89 C
ATOM 182 C LEU A 52 -9.069 -22.333 21.744 1.00 26.42 C
ATOM 183 O LEU A 52 -8.077 -22.145 22.456 1.00 26.13 O
ATOM 184 CB LEU A 52 -9.905 -20.245 20.589 1.00 25.76 C
ATOM 185 CG LEU A 52 -9.924 -19.299 19.377 1.00 25.90 C
ATOM 186 CD1 LEU A 52 -11.014 -18.239 19.513 1.00 25.05 C
ATOM 187 CD2 LEU A 52 -8.559 -18.657 19.126 1.00 25.73 C
ATOM 188 N GLU A 53 -10.059 -23.165 22.074 1.00 26.96 N
ATOM 189 CA GLU A 53 -10.009 -24.003 23.270 1.00 27.80 C
ATOM 190 C GLU A 53 -8.913 -25.046 23.152 1.00 27.77 C
ATOM 191 O GLU A 53 -8.145 -25.256 24.091 1.00 27.83 O
ATOM 192 CB GLU A 53 -11.348 -24.701 23.511 1.00 27.93 C
ATOM 193 CG GLU A 53 -12.378 -23.832 24.188 1.00 30.22 C
ATOM 194 CD GLU A 53 -13.643 -24.588 24.543 1.00 32.35 C
ATOM 195 OE1 GLU A 53 -13.544 -25.774 24.933 1.00 33.30 O
ATOM 196 OE2 GLU A 53 -14.736 -23.987 24.438 1.00 32.93 O
ATOM 197 N THR A 54 -8.866 -25.700 21.994 1.00 28.01 N
ATOM 198 CA THR A 54 -7.828 -26.677 21.664 1.00 28.43 C
ATOM 199 C THR A 54 -6.438 -26.033 21.720 1.00 28.57 C
ATOM 200 O THR A 54 -5.488 -26.638 22.225 1.00 28.68 O
ATOM 201 CB THR A 54 -8.081 -27.306 20.269 1.00 28.47 C
ATOM 202 OG1 THR A 54 -9.424 -27.803 20.206 1.00 28.40 O
ATOM 203 CG2 THR A 54 -7.113 -28.453 19.992 1.00 28.36 C
ATOM 204 N MET A 55 -6.337 -24.806 21.207 1.00 28.64 N
ATOM 205 CA MET A 55 -5.108 -24.018 21.280 1.00 28.83 C
ATOM 206 C MET A 55 -4.692 -23.786 22.729 1.00 29.22 C
ATOM 207 O MET A 55 -3.570 -24.115 23.120 1.00 28.91 O
ATOM 208 CB MET A 55 -5.285 -22.677 20.566 1.00 28.62 C
ATOM 209 CG MET A 55 -5.264 -22.786 19.058 1.00 28.49 C