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3lqg.pdb
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HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 09-FEB-10 3LQG
TITLE HUMAN ALDOSE REDUCTASE MUTANT T113A COMPLEXED WITH IDD388
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AR, ALDEHYDE REDUCTASE, ALDO-KETO REDUCTASE FAMILY 1 MEMBER
COMPND 5 B1;
COMPND 6 EC: 1.1.1.21;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALR2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS T113A MUTANT, OXIDOREDUCTASE, NADP, PHOSPHOPROTEIN, OXIDOREDUCTASE-
KEYWDS 2 OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KOCH,A.HEINE,G.KLEBE
REVDAT 2 24-AUG-11 3LQG 1 JRNL VERSN
REVDAT 1 15-DEC-10 3LQG 0
JRNL AUTH C.KOCH,A.HEINE,G.KLEBE
JRNL TITL TRACING THE DETAIL: HOW MUTATIONS AFFECT BINDING MODES AND
JRNL TITL 2 THERMODYNAMIC SIGNATURES OF CLOSELY RELATED ALDOSE REDUCTASE
JRNL TITL 3 INHIBITORS
JRNL REF J.MOL.BIOL. V. 406 700 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21185307
JRNL DOI 10.1016/J.JMB.2010.11.058
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.117
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.116
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.161
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3260
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 65145
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.107
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.106
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.146
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2804
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 56742
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2421
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 437
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2930.00
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2431.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 5
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 26572
REMARK 3 NUMBER OF RESTRAINTS : 32152
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 ANGLE DISTANCES (A) : 0.028
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.026
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.078
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.075
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.028
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.002
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.043
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.087
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 3 ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
REMARK 4
REMARK 4 3LQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057601.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : SILICON, RH-COATED
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65262
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG, 120MM AMMONIUM CITRATE, PH
REMARK 280 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 33.34500
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 0
REMARK 465 ALA A 1
REMARK 465 GLU A 313
REMARK 465 GLU A 314
REMARK 465 PHE A 315
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 11 CD CE NZ
REMARK 470 LYS A 85 CG CD CE NZ
REMARK 470 LYS A 119 CD CE NZ
REMARK 470 GLU A 126 CG CD OE1 OE2
REMARK 470 ASN A 136 CG OD1 ND2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 LYS A 221 CD CE NZ
REMARK 470 GLU A 229 CD OE1 OE2
REMARK 470 LYS A 234 CD CE NZ
REMARK 470 GLU A 267 CG CD OE1 OE2
REMARK 470 LYS A 274 CD CE NZ
REMARK 470 GLU A 279 CG CD OE1 OE2
REMARK 470 ARG A 293 CD NE CZ NH1 NH2
REMARK 470 LYS A 307 CG CD CE NZ
REMARK 470 HIS A 312 CA C O CB CG ND1 CD2
REMARK 470 HIS A 312 CE1 NE2
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 3 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 63 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 GLU A 64 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 GLU A 64 OE1 - CD - OE2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 TRP A 79 CG - CD1 - NE1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 PHE A 122 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 TYR A 189 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 GLU A 193 OE1 - CD - OE2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLU A 193 CG - CD - OE1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 TYR A 209 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 GLU A 271 OE1 - CD - OE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 LYS A 21 -0.12 80.51
REMARK 500 LEU A 300 114.87 -160.74
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 A1138 DISTANCE = 5.64 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 388 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LEP RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE MUTANT T113C COMPLEXED WITH IDD388
REMARK 900 RELATED ID: 2IKI RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE IN COMPLEX IDD388
REMARK 900 RELATED ID: 1US0 RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE IN COMPLEX WITH NADP+ AND THE
REMARK 900 INHIBITOR IDD594 AT 0.66 ANGSTROM
REMARK 900 RELATED ID: 3LQL RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE MUTANT T113A COMPLEXED WITH IDD 594
REMARK 900 RELATED ID: 3LBO RELATED DB: PDB
REMARK 900 RELATED ID: 3LD5 RELATED DB: PDB
REMARK 900 RELATED ID: 3LZ3 RELATED DB: PDB
REMARK 900 RELATED ID: 3M4H RELATED DB: PDB
REMARK 900 RELATED ID: 3LZ5 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE CONFLICT HAS BEEN DESCRIBED IN
REMARK 999 J BIOL CHEM 1989 SEP 5; 264(25): 14775-7 BY CHUNG S, ET AL.,
REMARK 999 PUBMED ID 2504709
DBREF 3LQG A 0 315 UNP P15121 ALDR_HUMAN 1 316
SEQADV 3LQG ILE A 4 UNP P15121 LEU 5 SEE REMARK 999
SEQADV 3LQG ALA A 113 UNP P15121 THR 114 ENGINEERED MUTATION
SEQRES 1 A 316 MET ALA SER ARG ILE LEU LEU ASN ASN GLY ALA LYS MET
SEQRES 2 A 316 PRO ILE LEU GLY LEU GLY THR TRP LYS SER PRO PRO GLY
SEQRES 3 A 316 GLN VAL THR GLU ALA VAL LYS VAL ALA ILE ASP VAL GLY
SEQRES 4 A 316 TYR ARG HIS ILE ASP CYS ALA HIS VAL TYR GLN ASN GLU
SEQRES 5 A 316 ASN GLU VAL GLY VAL ALA ILE GLN GLU LYS LEU ARG GLU
SEQRES 6 A 316 GLN VAL VAL LYS ARG GLU GLU LEU PHE ILE VAL SER LYS
SEQRES 7 A 316 LEU TRP CYS THR TYR HIS GLU LYS GLY LEU VAL LYS GLY
SEQRES 8 A 316 ALA CYS GLN LYS THR LEU SER ASP LEU LYS LEU ASP TYR
SEQRES 9 A 316 LEU ASP LEU TYR LEU ILE HIS TRP PRO ALA GLY PHE LYS
SEQRES 10 A 316 PRO GLY LYS GLU PHE PHE PRO LEU ASP GLU SER GLY ASN
SEQRES 11 A 316 VAL VAL PRO SER ASP THR ASN ILE LEU ASP THR TRP ALA
SEQRES 12 A 316 ALA MET GLU GLU LEU VAL ASP GLU GLY LEU VAL LYS ALA
SEQRES 13 A 316 ILE GLY ILE SER ASN PHE ASN HIS LEU GLN VAL GLU MET
SEQRES 14 A 316 ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO ALA VAL
SEQRES 15 A 316 ASN GLN ILE GLU CYS HIS PRO TYR LEU THR GLN GLU LYS
SEQRES 16 A 316 LEU ILE GLN TYR CYS GLN SER LYS GLY ILE VAL VAL THR
SEQRES 17 A 316 ALA TYR SER PRO LEU GLY SER PRO ASP ARG PRO TRP ALA
SEQRES 18 A 316 LYS PRO GLU ASP PRO SER LEU LEU GLU ASP PRO ARG ILE
SEQRES 19 A 316 LYS ALA ILE ALA ALA LYS HIS ASN LYS THR THR ALA GLN
SEQRES 20 A 316 VAL LEU ILE ARG PHE PRO MET GLN ARG ASN LEU VAL VAL
SEQRES 21 A 316 ILE PRO LYS SER VAL THR PRO GLU ARG ILE ALA GLU ASN
SEQRES 22 A 316 PHE LYS VAL PHE ASP PHE GLU LEU SER SER GLN ASP MET
SEQRES 23 A 316 THR THR LEU LEU SER TYR ASN ARG ASN TRP ARG VAL CYS
SEQRES 24 A 316 ALA LEU LEU SER CYS THR SER HIS LYS ASP TYR PRO PHE
SEQRES 25 A 316 HIS GLU GLU PHE
HET NAP A 500 48
HET 388 A 600 24
HET BR A 700 1
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM 388 (2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-
HETNAM 2 388 CHLOROPHENOXY)ACETIC ACID
HETNAM BR BROMIDE ION
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN 388 IDD388
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 388 C16 H12 BR CL F N O4
FORMUL 4 BR BR 1-
FORMUL 5 HOH *437(H2 O)
HELIX 1 1 PRO A 23 GLY A 38 1 16
HELIX 2 2 ALA A 45 GLN A 49 5 5
HELIX 3 3 ASN A 50 GLU A 64 1 15
HELIX 4 4 LYS A 68 LEU A 72 5 5
HELIX 5 5 TRP A 79 HIS A 83 5 5
HELIX 6 6 GLU A 84 GLY A 86 5 3
HELIX 7 7 LEU A 87 LYS A 100 1 14
HELIX 8 8 ASN A 136 GLU A 150 1 15
HELIX 9 9 ASN A 162 ASN A 171 1 10
HELIX 10 10 GLN A 192 LYS A 202 1 11
HELIX 11 11 SER A 226 GLU A 229 5 4
HELIX 12 12 ASP A 230 ASN A 241 1 12
HELIX 13 13 THR A 243 ARG A 255 1 13
HELIX 14 14 THR A 265 LYS A 274 1 10
HELIX 15 15 SER A 281 SER A 290 1 10
HELIX 16 16 LEU A 300 THR A 304 5 5
SHEET 1 A 2 ARG A 3 LEU A 5 0
SHEET 2 A 2 LYS A 11 PRO A 13 -1 O MET A 12 N ILE A 4
SHEET 1 B 8 LEU A 17 GLY A 18 0
SHEET 2 B 8 HIS A 41 ASP A 43 1 O ASP A 43 N LEU A 17
SHEET 3 B 8 PHE A 73 LEU A 78 1 O VAL A 75 N ILE A 42
SHEET 4 B 8 LEU A 106 ILE A 109 1 O LEU A 108 N LEU A 78
SHEET 5 B 8 ILE A 156 SER A 159 1 O GLY A 157 N ILE A 109
SHEET 6 B 8 VAL A 181 GLU A 185 1 O VAL A 181 N ILE A 158
SHEET 7 B 8 VAL A 205 TYR A 209 1 O THR A 207 N ILE A 184
SHEET 8 B 8 VAL A 258 VAL A 259 1 O VAL A 258 N ALA A 208
SITE 1 AC1 37 GLY A 18 THR A 19 TRP A 20 LYS A 21
SITE 2 AC1 37 ASP A 43 TYR A 48 HIS A 110 TRP A 111
SITE 3 AC1 37 SER A 159 ASN A 160 GLN A 183 TYR A 209
SITE 4 AC1 37 SER A 210 PRO A 211 LEU A 212 GLY A 213
SITE 5 AC1 37 SER A 214 PRO A 215 ASP A 216 LEU A 228
SITE 6 AC1 37 ALA A 245 ILE A 260 PRO A 261 LYS A 262
SITE 7 AC1 37 SER A 263 VAL A 264 THR A 265 ARG A 268
SITE 8 AC1 37 GLU A 271 ASN A 272 388 A 600 HOH A1027
SITE 9 AC1 37 HOH A1046 HOH A1068 HOH A1075 HOH A1152
SITE 10 AC1 37 HOH A1167
SITE 1 AC2 11 TRP A 20 VAL A 47 TYR A 48 HIS A 110
SITE 2 AC2 11 TRP A 111 PHE A 122 ALA A 299 LEU A 300
SITE 3 AC2 11 NAP A 500 BR A 700 HOH A1071
SITE 1 AC3 3 ALA A 113 PRO A 310 388 A 600
CRYST1 49.060 66.690 47.130 90.00 92.38 90.00 P 1 21 1 2
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 0.020382 0.000000 0.000847 0.00000
SCALE2 0.000000 0.014996 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021234 0.00000
ATOM 1 N SER A 2 13.842 7.699 38.784 1.00 42.29 N
ANISOU 1 N SER A 2 7623 4967 3478 4149 -3185 -949 N
ATOM 2 CA SER A 2 12.748 8.585 38.612 1.00 17.71 C
ANISOU 2 CA SER A 2 3441 1511 1776 497 -1457 -850 C
ATOM 3 C SER A 2 12.167 8.564 37.198 1.00 11.32 C
ANISOU 3 C SER A 2 1439 1576 1286 322 -380 -626 C
ATOM 4 O SER A 2 12.379 7.576 36.492 1.00 8.33 O
ANISOU 4 O SER A 2 1103 1283 778 119 -53 -183 O
ATOM 5 CB SER A 2 13.184 9.978 39.019 1.00 12.08 C
ATOM 6 OG SER A 2 14.226 10.525 38.205 1.00 29.19 O
ANISOU 6 OG SER A 2 4544 2930 3619 -1039 -2138 -762 O
ATOM 7 N ARG A 3 11.367 9.531 36.776 1.00 9.24 N
ANISOU 7 N ARG A 3 1489 929 1093 -162 -126 -203 N
ATOM 8 CA ARG A 3 10.533 9.469 35.589 1.00 9.39 C
ANISOU 8 CA ARG A 3 1555 1187 827 190 10 -194 C
ATOM 9 C ARG A 3 10.683 10.744 34.773 1.00 11.14 C
ANISOU 9 C ARG A 3 1981 1179 1073 -327 -330 -164 C
ATOM 10 O ARG A 3 10.991 11.798 35.340 1.00 13.55 O
ANISOU 10 O ARG A 3 2696 1289 1164 -333 22 -445 O
ATOM 11 CB ARG A 3 9.061 9.288 35.961 1.00 10.25 C
ANISOU 11 CB ARG A 3 1469 1107 1320 43 -228 -123 C
ATOM 12 CG ARG A 3 8.864 8.043 36.831 1.00 9.67 C
ANISOU 12 CG ARG A 3 1508 1202 962 208 41 -166 C
ATOM 13 CD ARG A 3 7.440 7.601 36.915 1.00 14.52 C
ANISOU 13 CD ARG A 3 1538 2161 1818 100 287 566 C
ATOM 14 NE ARG A 3 6.578 8.469 37.662 1.00 18.70 N
ANISOU 14 NE ARG A 3 1587 2619 2898 512 525 526 N
ATOM 15 CZ ARG A 3 5.244 8.357 37.645 1.00 21.14 C
ANISOU 15 CZ ARG A 3 1565 2485 3981 612 275 809 C
ATOM 16 NH1 ARG A 3 4.666 7.415 36.908 1.00 37.22 N
ANISOU 16 NH1 ARG A 3 2708 6347 5085 -1781 1438 -1208 N
ATOM 17 NH2 ARG A 3 4.563 9.219 38.385 1.00 27.50 N
ANISOU 17 NH2 ARG A 3 2076 3751 4623 709 1590 746 N
ATOM 18 N ILE A 4 10.463 10.600 33.483 1.00 8.64 N
ANISOU 18 N ILE A 4 1484 704 1096 -81 -341 -87 N
ATOM 19 CA ILE A 4 10.508 11.689 32.525 1.00 9.20 C
ANISOU 19 CA ILE A 4 1288 909 1299 -249 -55 87 C
ATOM 20 C ILE A 4 9.114 11.890 31.932 1.00 8.80 C
ANISOU 20 C ILE A 4 1376 826 1140 -176 -56 332 C
ATOM 21 O ILE A 4 8.387 10.932 31.674 1.00 8.63 O
ANISOU 21 O ILE A 4 994 854 1431 -41 139 99 O
ATOM 22 CB ILE A 4 11.572 11.410 31.421 1.00 10.76 C
ANISOU 22 CB ILE A 4 1482 1052 1557 -90 105 14 C
ATOM 23 CG1 ILE A 4 11.847 12.629 30.530 1.00 15.50 C
ANISOU 23 CG1 ILE A 4 2565 1688 1638 19 643 430 C
ATOM 24 CG2 ILE A 4 11.225 10.183 30.614 1.00 15.91 C
ANISOU 24 CG2 ILE A 4 3104 1296 1643 585 -552 -389 C
ATOM 25 CD1 ILE A 4 13.080 12.385 29.645 1.00 17.12 C
ANISOU 25 CD1 ILE A 4 1618 2782 2105 -165 289 713 C
ATOM 26 N LEU A 5 8.733 13.154 31.773 1.00 10.59 N
ANISOU 26 N LEU A 5 2043 829 1151 47 -361 -32 N
ATOM 27 CA LEU A 5 7.420 13.470 31.233 1.00 11.30 C
ANISOU 27 CA LEU A 5 2195 654 1444 89 -504 166 C
ATOM 28 C LEU A 5 7.428 13.328 29.731 1.00 11.68 C
ANISOU 28 C LEU A 5 1793 1243 1400 -89 -432 358 C
ATOM 29 O LEU A 5 8.206 13.957 29.021 1.00 13.31 O
ANISOU 29 O LEU A 5 1882 1504 1671 -382 -353 246 O
ATOM 30 CB LEU A 5 7.029 14.888 31.669 1.00 15.22 C
ANISOU 30 CB LEU A 5 2774 705 2304 319 -493 72 C
ATOM 31 CG LEU A 5 5.668 15.407 31.190 1.00 15.56 C
ANISOU 31 CG LEU A 5 2483 1207 2221 553 -260 -882 C
ATOM 32 CD1 LEU A 5 4.549 14.560 31.797 1.00 18.64 C
ANISOU 32 CD1 LEU A 5 2687 1923 2472 627 -255 92 C
ATOM 33 CD2 LEU A 5 5.558 16.898 31.527 1.00 22.15 C
ANISOU 33 CD2 LEU A 5 3742 1122 3553 995 -1069 -792 C
ATOM 34 N LEU A 6 6.496 12.522 29.221 1.00 9.04 N
ANISOU 34 N LEU A 6 1623 784 1029 119 -46 220 N
ATOM 35 CA LEU A 6 6.274 12.359 27.809 1.00 9.55 C
ANISOU 35 CA LEU A 6 1775 821 1032 310 -59 167 C
ATOM 36 C LEU A 6 5.283 13.388 27.263 1.00 10.55 C
ANISOU 36 C LEU A 6 1969 1039 1001 610 -347 -301 C
ATOM 37 O LEU A 6 4.485 13.983 28.008 1.00 11.24 O
ANISOU 37 O LEU A 6 2179 872 1220 503 -76 -249 O
ATOM 38 CB LEU A 6 5.689 10.989 27.539 1.00 10.15 C
ANISOU 38 CB LEU A 6 1377 985 1496 336 -205 -125 C
ATOM 39 CG LEU A 6 6.530 9.783 27.984 1.00 8.39 C
ANISOU 39 CG LEU A 6 1385 787 1016 150 -84 -8 C
ATOM 40 CD1 LEU A 6 5.793 8.494 27.605 1.00 10.28 C
ANISOU 40 CD1 LEU A 6 1432 965 1510 159 -450 -230 C
ATOM 41 CD2 LEU A 6 7.931 9.812 27.402 1.00 9.89 C
ANISOU 41 CD2 LEU A 6 1381 949 1426 311 -2 53 C
ATOM 42 N ASN A 7 5.349 13.543 25.939 1.00 10.65 N
ANISOU 42 N ASN A 7 2064 983 1001 589 -306 -106 N
ATOM 43 CA ASN A 7 4.440 14.464 25.268 1.00 10.64 C
ANISOU 43 CA ASN A 7 1863 959 1220 545 13 157 C
ATOM 44 C ASN A 7 2.996 13.989 25.140 1.00 11.72 C
ANISOU 44 C ASN A 7 1713 1082 1657 723 143 -105 C
ATOM 45 O ASN A 7 2.158 14.663 24.505 1.00 13.55 O
ANISOU 45 O ASN A 7 2034 1068 2046 407 -414 77 O
ATOM 46 CB ASN A 7 4.961 14.863 23.862 1.00 10.56 C
ANISOU 46 CB ASN A 7 2154 858 1000 112 -249 10 C
ATOM 47 CG ASN A 7 5.091 13.688 22.937 1.00 10.77 C
ANISOU 47 CG ASN A 7 2195 886 1013 9 -376 -35 C
ATOM 48 OD1 ASN A 7 4.555 12.634 23.216 1.00 10.34 O
ANISOU 48 OD1 ASN A 7 1458 764 1706 316 -288 4 O
ATOM 49 ND2 ASN A 7 5.773 13.861 21.793 1.00 10.33 N
ANISOU 49 ND2 ASN A 7 1717 937 1272 364 -226 -100 N
ATOM 50 N ASN A 8 2.659 12.872 25.777 1.00 11.17 N
ANISOU 50 N ASN A 8 1628 1457 1159 220 -632 30 N
ATOM 51 CA ASN A 8 1.281 12.484 25.989 1.00 10.90 C
ANISOU 51 CA ASN A 8 1569 1104 1470 394 -651 -10 C
ATOM 52 C ASN A 8 0.836 12.815 27.398 1.00 10.86 C
ANISOU 52 C ASN A 8 1536 891 1701 347 -422 -128 C
ATOM 53 O ASN A 8 -0.311 12.498 27.718 1.00 12.65 O
ANISOU 53 O ASN A 8 1494 1394 1919 264 -453 -247 O
ATOM 54 CB ASN A 8 1.067 10.990 25.659 1.00 11.13 C
ANISOU 54 CB ASN A 8 1668 1151 1411 410 -551 -139 C
ATOM 55 CG ASN A 8 1.566 10.104 26.784 1.00 11.62 C
ANISOU 55 CG ASN A 8 1481 1090 1843 344 -632 81 C
ATOM 56 OD1 ASN A 8 2.481 10.477 27.522 1.00 10.51 O
ANISOU 56 OD1 ASN A 8 1688 1007 1296 217 -466 19 O
ATOM 57 ND2 ASN A 8 1.003 8.914 26.947 1.00 9.89 N
ANISOU 57 ND2 ASN A 8 1238 1177 1343 282 -130 -178 N
ATOM 58 N GLY A 9 1.644 13.428 28.245 1.00 10.15 N
ANISOU 58 N GLY A 9 1517 820 1521 278 -178 -220 N
ATOM 59 CA GLY A 9 1.193 13.768 29.569 1.00 10.98 C
ANISOU 59 CA GLY A 9 1624 892 1657 330 16 -228 C
ATOM 60 C GLY A 9 1.483 12.685 30.591 1.00 10.68 C
ANISOU 60 C GLY A 9 1636 983 1440 332 -51 -318 C
ATOM 61 O GLY A 9 1.239 12.947 31.766 1.00 15.25 O
ANISOU 61 O GLY A 9 3037 1239 1519 438 357 -353 O
ATOM 62 N ALA A 10 1.972 11.534 30.227 1.00 9.36 N
ANISOU 62 N ALA A 10 1303 889 1365 217 -83 -225 N
ATOM 63 CA ALA A 10 2.295 10.470 31.167 1.00 9.08 C
ANISOU 63 CA ALA A 10 1252 1066 1133 306 85 -196 C
ATOM 64 C ALA A 10 3.765 10.519 31.556 1.00 9.06 C
ANISOU 64 C ALA A 10 1289 913 1242 244 56 -144 C
ATOM 65 O ALA A 10 4.578 11.039 30.805 1.00 10.69 O
ANISOU 65 O ALA A 10 1355 1443 1265 -25 -54 0 O
ATOM 66 CB ALA A 10 1.938 9.142 30.517 1.00 11.04 C
ANISOU 66 CB ALA A 10 1696 922 1576 163 -350 1 C
ATOM 67 N LYS A 11 4.133 9.936 32.686 1.00 9.95 N
ANISOU 67 N LYS A 11 1203 1284 1294 151 5 -16 N
ATOM 68 CA LYS A 11 5.517 9.861 33.145 1.00 9.64 C
ANISOU 68 CA LYS A 11 1196 1114 1351 232 0 -272 C
ATOM 69 C LYS A 11 6.066 8.435 32.941 1.00 8.68 C
ANISOU 69 C LYS A 11 1202 954 1143 41 33 -233 C
ATOM 70 O LYS A 11 5.412 7.414 33.199 1.00 12.06 O
ANISOU 70 O LYS A 11 1497 1134 1950 14 607 3 O
ATOM 71 CB LYS A 11 5.608 10.283 34.613 1.00 10.78 C
ANISOU 71 CB LYS A 11 1434 1234 1427 468 -125 -427 C
ATOM 72 CG LYS A 11 5.245 11.741 34.822 1.00 17.36 C
ANISOU 72 CG LYS A 11 3183 1417 1996 929 -799 -762 C
ATOM 73 N MET A 12 7.285 8.383 32.418 1.00 7.31 N
ANISOU 73 N MET A 12 1004 603 1170 37 -193 -147 N
ATOM 74 CA MET A 12 7.970 7.170 32.035 1.00 6.80 C
ANISOU 74 CA MET A 12 1095 607 883 36 -192 -121 C
ATOM 75 C MET A 12 9.197 6.944 32.904 1.00 6.21 C
ANISOU 75 C MET A 12 976 553 831 14 -118 -170 C
ATOM 76 O MET A 12 10.058 7.836 32.953 1.00 7.65 O
ANISOU 76 O MET A 12 1244 711 952 -200 -176 -103 O
ATOM 77 CB MET A 12 8.381 7.232 30.563 1.00 7.84 C
ANISOU 77 CB MET A 12 1229 876 875 67 -186 -36 C
ATOM 78 CG MET A 12 9.034 5.979 30.016 1.00 8.04 C
ANISOU 78 CG MET A 12 872 1119 1065 219 334 183 C
ATOM 79 SD MET A 12 9.241 6.105 28.244 1.00 8.08 S
ANISOU 79 SD MET A 12 1034 1064 973 46 -36 -63 S
ATOM 80 CE MET A 12 9.902 4.531 27.782 1.00 9.04 C
ANISOU 80 CE MET A 12 1151 1274 1010 263 -415 -309 C
ATOM 81 N PRO A 13 9.311 5.797 33.581 1.00 6.25 N
ANISOU 81 N PRO A 13 741 678 954 18 -57 -44 N
ATOM 82 CA PRO A 13 10.544 5.551 34.379 1.00 6.61 C
ANISOU 82 CA PRO A 13 797 790 925 113 -40 -99 C
ATOM 83 C PRO A 13 11.775 5.511 33.469 1.00 6.10 C
ANISOU 83 C PRO A 13 730 864 722 114 -186 -200 C
ATOM 84 O PRO A 13 11.812 4.847 32.425 1.00 7.19 O
ANISOU 84 O PRO A 13 982 1022 726 -285 15 -218 O
ATOM 85 CB PRO A 13 10.275 4.207 35.037 1.00 6.53 C
ANISOU 85 CB PRO A 13 938 725 819 80 -171 -163 C
ATOM 86 CG PRO A 13 8.777 4.064 34.984 1.00 7.28 C
ANISOU 86 CG PRO A 13 939 785 1043 30 -118 75 C
ATOM 87 CD PRO A 13 8.379 4.661 33.653 1.00 6.96 C
ANISOU 87 CD PRO A 13 695 767 1184 53 -20 261 C
ATOM 88 N ILE A 14 12.798 6.247 33.880 1.00 6.03 N
ANISOU 88 N ILE A 14 858 747 685 18 -175 -94 N
ATOM 89 CA ILE A 14 14.012 6.381 33.073 1.00 6.65 C
ANISOU 89 CA ILE A 14 1016 634 877 -90 -25 88 C
ATOM 90 C ILE A 14 14.858 5.131 33.056 1.00 7.52 C
ANISOU 90 C ILE A 14 821 607 1427 -176 229 118 C
ATOM 91 O ILE A 14 15.733 5.024 32.191 1.00 7.96 O
ANISOU 91 O ILE A 14 973 978 1073 -85 121 18 O
ATOM 92 CB ILE A 14 14.822 7.642 33.457 1.00 7.63 C
ANISOU 92 CB ILE A 14 959 628 1312 -6 -108 -36 C
ATOM 93 CG1 ILE A 14 15.442 7.545 34.843 1.00 10.52 C
ANISOU 93 CG1 ILE A 14 1365 1055 1578 -23 -502 -197 C
ATOM 94 CG2 ILE A 14 13.978 8.882 33.272 1.00 8.53 C
ANISOU 94 CG2 ILE A 14 1149 700 1391 146 -42 -208 C
ATOM 95 CD1 ILE A 14 16.324 8.727 35.204 1.00 13.80 C
ANISOU 95 CD1 ILE A 14 1471 1924 1847 -578 -102 -699 C
ATOM 96 N LEU A 15 14.635 4.180 33.959 1.00 6.02 N
ANISOU 96 N LEU A 15 877 522 886 59 71 -115 N
ATOM 97 CA LEU A 15 15.318 2.909 33.932 1.00 6.16 C
ANISOU 97 CA LEU A 15 847 627 868 138 -146 -161 C
ATOM 98 C LEU A 15 14.312 1.769 33.778 1.00 6.66 C
ANISOU 98 C LEU A 15 938 506 1086 111 58 -99 C
ATOM 99 O LEU A 15 13.373 1.721 34.567 1.00 9.37 O
ANISOU 99 O LEU A 15 1249 1005 1308 -120 354 -315 O
ATOM 100 CB LEU A 15 16.076 2.704 35.236 1.00 9.11 C
ANISOU 100 CB LEU A 15 907 1607 946 141 -203 175 C
ATOM 101 CG LEU A 15 17.009 1.511 35.376 1.00 11.28 C
ANISOU 101 CG LEU A 15 1233 1902 1149 382 -342 380 C
ATOM 102 CD1 LEU A 15 18.039 1.417 34.282 1.00 16.16 C
ANISOU 102 CD1 LEU A 15 1470 2790 1880 1013 93 393 C
ATOM 103 CD2 LEU A 15 17.689 1.604 36.732 1.00 17.46 C
ANISOU 103 CD2 LEU A 15 2445 2602 1588 915 -1102 45 C
ATOM 104 N GLY A 16 14.538 0.965 32.774 1.00 6.16 N
ANISOU 104 N GLY A 16 710 686 946 -56 -46 -124 N
ATOM 105 CA GLY A 16 13.716 -0.232 32.542 1.00 6.22 C
ANISOU 105 CA GLY A 16 791 655 916 -93 83 -90 C
ATOM 106 C GLY A 16 14.582 -1.467 32.360 1.00 5.50 C
ANISOU 106 C GLY A 16 568 717 806 -141 -143 -211 C
ATOM 107 O GLY A 16 15.801 -1.376 32.211 1.00 6.79 O
ANISOU 107 O GLY A 16 622 881 1078 -130 81 164 O
ATOM 108 N LEU A 17 13.884 -2.609 32.389 1.00 5.43 N
ANISOU 108 N LEU A 17 653 599 813 -67 126 -80 N
ATOM 109 CA LEU A 17 14.509 -3.920 32.179 1.00 5.67 C
ANISOU 109 CA LEU A 17 824 662 670 60 30 -45 C
ATOM 110 C LEU A 17 14.309 -4.376 30.741 1.00 4.60 C
ANISOU 110 C LEU A 17 610 542 597 108 6 77 C
ATOM 111 O LEU A 17 13.162 -4.511 30.277 1.00 6.40 O
ANISOU 111 O LEU A 17 623 954 853 56 -65 20 O
ATOM 112 CB LEU A 17 13.881 -4.968 33.095 1.00 5.92 C
ANISOU 112 CB LEU A 17 1044 659 548 88 133 -75 C
ATOM 113 CG LEU A 17 14.537 -6.349 32.947 1.00 6.26 C
ANISOU 113 CG LEU A 17 969 626 782 31 8 -115 C
ATOM 114 CD1 LEU A 17 15.912 -6.411 33.553 1.00 8.41 C
ANISOU 114 CD1 LEU A 17 1022 942 1232 16 -151 307 C
ATOM 115 CD2 LEU A 17 13.651 -7.418 33.617 1.00 7.55 C
ANISOU 115 CD2 LEU A 17 1097 731 1041 -15 -31 119 C
ATOM 116 N GLY A 18 15.389 -4.609 30.012 1.00 5.32 N
ANISOU 116 N GLY A 18 614 704 704 -32 54 -59 N
ATOM 117 CA GLY A 18 15.336 -5.202 28.686 1.00 5.69 C
ANISOU 117 CA GLY A 18 742 624 796 24 105 -129 C
ATOM 118 C GLY A 18 15.112 -6.707 28.738 1.00 4.65 C
ANISOU 118 C GLY A 18 493 606 668 144 94 -23 C
ATOM 119 O GLY A 18 15.509 -7.355 29.727 1.00 6.39 O
ANISOU 119 O GLY A 18 883 788 759 151 -102 34 O
ATOM 120 N THR A 19 14.471 -7.267 27.695 1.00 5.51 N
ANISOU 120 N THR A 19 841 496 755 86 -106 48 N
ATOM 121 CA THR A 19 14.124 -8.677 27.626 1.00 5.47 C
ANISOU 121 CA THR A 19 814 481 784 55 18 109 C
ATOM 122 C THR A 19 14.501 -9.360 26.337 1.00 5.22 C
ANISOU 122 C THR A 19 611 600 774 -99 -141 -15 C
ATOM 123 O THR A 19 14.214 -10.573 26.208 1.00 6.02 O
ANISOU 123 O THR A 19 715 659 915 -192 -47 -131 O
ATOM 124 CB THR A 19 12.621 -8.901 27.890 1.00 6.82 C
ANISOU 124 CB THR A 19 811 601 1179 103 124 57 C
ATOM 125 OG1 THR A 19 11.855 -8.265 26.862 1.00 6.33 O
ANISOU 125 OG1 THR A 19 705 666 1033 33 75 -132 O
ATOM 126 CG2 THR A 19 12.213 -8.337 29.250 1.00 6.63 C
ANISOU 126 CG2 THR A 19 760 717 1041 47 132 182 C
ATOM 127 N TRP A 20 15.150 -8.712 25.387 1.00 5.28 N
ANISOU 127 N TRP A 20 553 631 820 178 -10 106 N
ATOM 128 CA TRP A 20 15.636 -9.441 24.208 1.00 5.80 C
ANISOU 128 CA TRP A 20 713 552 939 80 41 28 C
ATOM 129 C TRP A 20 16.711 -10.429 24.642 1.00 5.22 C
ANISOU 129 C TRP A 20 632 547 802 78 53 -26 C
ATOM 130 O TRP A 20 17.664 -10.045 25.312 1.00 6.14 O
ANISOU 130 O TRP A 20 743 838 751 91 -3 -135 O
ATOM 131 CB TRP A 20 16.181 -8.475 23.145 1.00 5.96 C
ANISOU 131 CB TRP A 20 652 750 865 169 54 113 C
ATOM 132 CG TRP A 20 16.786 -9.156 21.955 1.00 5.94 C
ANISOU 132 CG TRP A 20 502 770 986 53 43 -84 C
ATOM 133 CD1 TRP A 20 16.399 -10.295 21.304 1.00 6.66 C
ANISOU 133 CD1 TRP A 20 985 731 816 -197 51 109 C
ATOM 134 CD2 TRP A 20 17.962 -8.680 21.266 1.00 5.08 C
ANISOU 134 CD2 TRP A 20 510 650 769 81 -69 31 C
ATOM 135 NE1 TRP A 20 17.260 -10.573 20.265 1.00 5.94 N
ANISOU 135 NE1 TRP A 20 829 577 852 98 -98 20 N
ATOM 136 CE2 TRP A 20 18.226 -9.579 20.224 1.00 6.03 C
ANISOU 136 CE2 TRP A 20 793 706 792 83 70 36 C
ATOM 137 CE3 TRP A 20 18.806 -7.583 21.453 1.00 6.57 C
ANISOU 137 CE3 TRP A 20 790 870 838 -170 -102 62 C
ATOM 138 CZ2 TRP A 20 19.303 -9.415 19.350 1.00 7.01 C
ANISOU 138 CZ2 TRP A 20 736 1200 729 114 23 2 C
ATOM 139 CZ3 TRP A 20 19.891 -7.402 20.587 1.00 7.75 C
ANISOU 139 CZ3 TRP A 20 537 1343 1066 -237 -169 15 C
ATOM 140 CH2 TRP A 20 20.118 -8.325 19.557 1.00 7.52 C
ANISOU 140 CH2 TRP A 20 744 1285 831 -5 -37 259 C
ATOM 141 N LYS A 21 16.572 -11.683 24.245 1.00 6.11 N
ANISOU 141 N LYS A 21 673 574 1075 76 10 -47 N
ATOM 142 CA LYS A 21 17.485 -12.789 24.471 1.00 6.05 C
ANISOU 142 CA LYS A 21 855 638 806 209 -89 -239 C
ATOM 143 C LYS A 21 17.312 -13.369 25.864 1.00 6.14 C
ANISOU 143 C LYS A 21 759 774 801 276 -187 -212 C
ATOM 144 O LYS A 21 18.018 -14.296 26.254 1.00 9.91 O
ANISOU 144 O LYS A 21 1049 1231 1485 610 323 462 O
ATOM 145 CB LYS A 21 18.948 -12.438 24.250 1.00 6.03 C
ANISOU 145 CB LYS A 21 810 573 911 211 -225 -111 C
ATOM 146 CG LYS A 21 19.243 -11.730 22.942 1.00 7.82 C
ANISOU 146 CG LYS A 21 925 1156 888 -10 -200 -6 C
ATOM 147 CD LYS A 21 20.674 -11.168 22.891 1.00 8.22 C
ANISOU 147 CD LYS A 21 775 1409 940 124 42 -238 C
ATOM 148 CE LYS A 21 20.803 -9.707 23.288 1.00 8.14 C
ANISOU 148 CE LYS A 21 648 1311 1133 -6 -284 31 C
ATOM 149 NZ LYS A 21 20.342 -9.437 24.656 1.00 7.67 N
ANISOU 149 NZ LYS A 21 971 672 1270 118 -225 -136 N
ATOM 150 N SER A 22 16.415 -12.845 26.672 1.00 6.39 N
ANISOU 150 N SER A 22 890 580 959 151 121 -26 N
ATOM 151 CA SER A 22 16.169 -13.435 27.997 1.00 6.14 C
ANISOU 151 CA SER A 22 650 675 1009 -3 -83 103 C
ATOM 152 C SER A 22 15.472 -14.781 27.802 1.00 6.81 C
ANISOU 152 C SER A 22 860 762 964 -89 -138 41 C
ATOM 153 O SER A 22 14.350 -14.792 27.281 1.00 7.60 O
ANISOU 153 O SER A 22 944 930 1013 -311 -229 263 O
ATOM 154 CB SER A 22 15.361 -12.472 28.827 1.00 6.27 C
ANISOU 154 CB SER A 22 680 914 790 -112 -34 -30 C
ATOM 155 OG SER A 22 16.125 -11.283 28.991 1.00 7.20 O
ANISOU 155 OG SER A 22 757 778 1202 -45 109 -72 O
ATOM 156 N PRO A 23 16.116 -15.898 28.176 1.00 7.91 N
ANISOU 156 N PRO A 23 1185 763 1056 -90 -83 334 N
ATOM 157 CA PRO A 23 15.523 -17.188 27.833 1.00 8.93 C
ANISOU 157 CA PRO A 23 1404 770 1220 -164 173 198 C
ATOM 158 C PRO A 23 14.154 -17.335 28.511 1.00 7.35 C
ANISOU 158 C PRO A 23 1465 207 1121 -123 262 -338 C
ATOM 159 O PRO A 23 13.952 -16.842 29.613 1.00 8.47 O
ANISOU 159 O PRO A 23 1702 602 915 322 -54 -239 O
ATOM 160 CB PRO A 23 16.510 -18.189 28.378 1.00 9.20 C
ANISOU 160 CB PRO A 23 1543 775 1175 70 241 14 C
ATOM 161 CG PRO A 23 17.834 -17.463 28.349 1.00 8.98 C
ANISOU 161 CG PRO A 23 1495 714 1203 132 219 90 C
ATOM 162 CD PRO A 23 17.426 -16.066 28.851 1.00 8.12 C
ANISOU 162 CD PRO A 23 1335 760 991 274 -126 58 C
ATOM 163 N PRO A 24 13.224 -18.004 27.859 1.00 7.54 N
ANISOU 163 N PRO A 24 1323 621 919 -61 70 -155 N
ATOM 164 CA PRO A 24 11.869 -18.116 28.429 1.00 9.04 C
ANISOU 164 CA PRO A 24 1311 1107 1016 -35 65 -217 C
ATOM 165 C PRO A 24 11.823 -18.794 29.783 1.00 9.61 C
ANISOU 165 C PRO A 24 1518 964 1170 -103 335 -128 C
ATOM 166 O PRO A 24 10.929 -18.448 30.587 1.00 11.63 O
ANISOU 166 O PRO A 24 1421 1585 1414 -229 524 -94 O
ATOM 167 CB PRO A 24 11.102 -18.908 27.367 1.00 11.04 C
ANISOU 167 CB PRO A 24 1231 1496 1469 -20 -108 -478 C
ATOM 168 CG PRO A 24 12.133 -19.511 26.503 1.00 11.04 C
ANISOU 168 CG PRO A 24 1258 1746 1190 -209 -117 -632 C
ATOM 169 CD PRO A 24 13.357 -18.634 26.526 1.00 7.83 C
ANISOU 169 CD PRO A 24 1357 608 1010 106 -26 -271 C
ATOM 170 N GLY A 25 12.776 -19.674 30.051 1.00 9.93 N
ANISOU 170 N GLY A 25 2084 461 1229 -34 280 -173 N
ATOM 171 CA GLY A 25 12.903 -20.325 31.356 1.00 9.86 C
ANISOU 171 CA GLY A 25 1921 539 1284 -16 549 -84 C
ATOM 172 C GLY A 25 13.607 -19.506 32.404 1.00 9.70 C
ANISOU 172 C GLY A 25 1615 869 1201 -35 339 93 C
ATOM 173 O GLY A 25 13.678 -19.975 33.547 1.00 12.68 O
ANISOU 173 O GLY A 25 2686 867 1265 -1 330 199 O
ATOM 174 N GLN A 26 14.114 -18.330 32.080 1.00 8.67 N
ANISOU 174 N GLN A 26 1777 686 829 63 241 -69 N
ATOM 175 CA GLN A 26 14.756 -17.452 33.045 1.00 9.17 C
ANISOU 175 CA GLN A 26 1631 774 1079 230 106 -178 C
ATOM 176 C GLN A 26 14.051 -16.117 33.170 1.00 8.46 C
ANISOU 176 C GLN A 26 1318 856 1041 221 -165 -328 C
ATOM 177 O GLN A 26 14.217 -15.424 34.186 1.00 9.46 O
ANISOU 177 O GLN A 26 1763 996 836 413 -124 -288 O
ATOM 178 CB GLN A 26 16.226 -17.196 32.664 1.00 10.81 C
ANISOU 178 CB GLN A 26 1456 1229 1422 374 -16 -353 C
ATOM 179 CG GLN A 26 17.086 -18.427 32.744 1.00 13.71 C
ANISOU 179 CG GLN A 26 1570 1200 2440 358 -122 44 C
ATOM 180 CD GLN A 26 18.432 -18.403 32.050 1.00 22.54 C
ANISOU 180 CD GLN A 26 1528 1863 5172 973 544 1105 C
ATOM 181 OE1 GLN A 26 19.186 -17.449 32.173 1.00 41.94 O
ANISOU 181 OE1 GLN A 26 2133 1359 12442 559 1362 2839 O
ATOM 182 NE2 GLN A 26 18.758 -19.493 31.316 1.00 32.49 N
ANISOU 182 NE2 GLN A 26 3467 4109 4770 2230 1410 291 N
ATOM 183 N VAL A 27 13.276 -15.699 32.174 1.00 7.46 N
ANISOU 183 N VAL A 27 1447 721 668 58 98 -122 N
ATOM 184 CA VAL A 27 12.786 -14.317 32.181 1.00 7.07 C
ANISOU 184 CA VAL A 27 1219 726 743 39 87 -129 C
ATOM 185 C VAL A 27 11.661 -14.105 33.154 1.00 6.49 C
ANISOU 185 C VAL A 27 1112 809 545 106 -66 0 C
ATOM 186 O VAL A 27 11.439 -12.973 33.625 1.00 6.84 O
ANISOU 186 O VAL A 27 972 890 737 3 19 -186 O
ATOM 187 CB VAL A 27 12.357 -13.907 30.752 1.00 6.34 C
ANISOU 187 CB VAL A 27 807 860 741 69 192 -72 C
ATOM 188 CG1 VAL A 27 11.052 -14.577 30.293 1.00 8.12 C
ANISOU 188 CG1 VAL A 27 1012 1181 890 -208 108 56 C
ATOM 189 CG2 VAL A 27 12.268 -12.381 30.618 1.00 7.84 C
ANISOU 189 CG2 VAL A 27 1002 883 1095 85 -153 12 C
ATOM 190 N THR A 28 10.889 -15.134 33.488 1.00 7.29 N
ANISOU 190 N THR A 28 1218 821 731 80 88 -77 N
ATOM 191 CA THR A 28 9.823 -14.896 34.478 1.00 7.72 C
ANISOU 191 CA THR A 28 1340 779 815 -23 203 -119 C
ATOM 192 C THR A 28 10.447 -14.526 35.811 1.00 7.17 C
ANISOU 192 C THR A 28 1283 668 773 -47 199 -29 C
ATOM 193 O THR A 28 10.062 -13.547 36.461 1.00 7.41 O
ANISOU 193 O THR A 28 1239 700 878 87 -77 -98 O
ATOM 194 CB THR A 28 8.900 -16.117 34.647 1.00 7.55 C
ANISOU 194 CB THR A 28 1082 801 985 45 -118 107 C
ATOM 195 OG1 THR A 28 8.275 -16.389 33.388 1.00 8.85 O
ANISOU 195 OG1 THR A 28 1510 982 870 -156 -106 151 O
ATOM 196 CG2 THR A 28 7.857 -15.907 35.734 1.00 8.20 C
ANISOU 196 CG2 THR A 28 987 1224 905 -229 -164 55 C
ATOM 197 N GLU A 29 11.464 -15.271 36.259 1.00 8.02 N
ANISOU 197 N GLU A 29 1280 742 1026 90 145 -166 N
ATOM 198 CA GLU A 29 12.162 -14.912 37.499 1.00 8.07 C
ANISOU 198 CA GLU A 29 1111 1048 908 337 270 -255 C
ATOM 199 C GLU A 29 12.865 -13.574 37.351 1.00 8.42 C
ANISOU 199 C GLU A 29 1145 1118 938 170 -49 -248 C
ATOM 200 O GLU A 29 12.875 -12.786 38.292 1.00 8.46 O
ANISOU 200 O GLU A 29 1214 1145 854 382 -290 -207 O
ATOM 201 CB GLU A 29 13.127 -15.975 37.997 1.00 10.99 C
ANISOU 201 CB GLU A 29 1404 1339 1433 395 94 176 C
ATOM 202 CG GLU A 29 13.834 -15.551 39.281 1.00 14.49 C
ANISOU 202 CG GLU A 29 2322 1742 1441 33 -382 650 C
ATOM 203 CD GLU A 29 12.962 -15.553 40.540 1.00 17.22 C
ANISOU 203 CD GLU A 29 2604 2836 1103 88 -504 876 C
ATOM 204 OE1 GLU A 29 13.529 -15.203 41.630 1.00 19.27 O
ANISOU 204 OE1 GLU A 29 3692 2200 1428 399 -749 354 O
ATOM 205 OE2 GLU A 29 11.758 -15.897 40.477 1.00 20.60 O
ANISOU 205 OE2 GLU A 29 2025 3757 2047 900 -136 360 O
ATOM 206 N ALA A 30 13.458 -13.250 36.195 1.00 7.67 N
ANISOU 206 N ALA A 30 1142 840 930 268 -109 -163 N
ATOM 207 CA ALA A 30 14.146 -11.982 36.015 1.00 7.65 C
ANISOU 207 CA ALA A 30 793 1032 1080 169 10 -373 C
ATOM 208 C ALA A 30 13.209 -10.814 36.241 1.00 5.91 C
ANISOU 208 C ALA A 30 815 788 642 105 -143 -188 C
ATOM 209 O ALA A 30 13.571 -9.834 36.889 1.00 7.25 O
ANISOU 209 O ALA A 30 904 905 945 -112 -24 -325 O
ATOM 210 CB ALA A 30 14.745 -11.900 34.606 1.00 8.27 C
ANISOU 210 CB ALA A 30 768 1266 1108 -113 78 -519 C
ATOM 211 N VAL A 31 12.011 -10.905 35.679 1.00 6.46 N
ANISOU 211 N VAL A 31 819 831 804 22 -158 -147 N
ATOM 212 CA VAL A 31 11.045 -9.815 35.812 1.00 5.64 C
ANISOU 212 CA VAL A 31 591 737 814 -130 4 91 C
ATOM 213 C VAL A 31 10.450 -9.733 37.222 1.00 6.50 C
ANISOU 213 C VAL A 31 767 859 845 -213 114 8 C
ATOM 214 O VAL A 31 10.276 -8.642 37.741 1.00 6.93 O
ANISOU 214 O VAL A 31 930 883 820 32 -118 13 O
ATOM 215 CB VAL A 31 9.954 -9.926 34.731 1.00 5.63 C
ANISOU 215 CB VAL A 31 621 589 927 -201 -73 12 C
ATOM 216 CG1 VAL A 31 8.856 -8.900 34.956 1.00 6.98 C
ANISOU 216 CG1 VAL A 31 868 810 974 82 -165 59 C
ATOM 217 CG2 VAL A 31 10.548 -9.796 33.357 1.00 6.44 C
ANISOU 217 CG2 VAL A 31 841 733 874 -88 -95 131 C
ATOM 218 N LYS A 32 10.193 -10.870 37.861 1.00 6.59 N
ANISOU 218 N LYS A 32 797 860 846 4 175 83 N
ATOM 219 CA LYS A 32 9.784 -10.872 39.284 1.00 6.34 C
ANISOU 219 CA LYS A 32 708 774 927 -200 272 21 C
ATOM 220 C LYS A 32 10.838 -10.178 40.146 1.00 6.75 C
ANISOU 220 C LYS A 32 902 667 997 -137 89 -12 C
ATOM 221 O LYS A 32 10.494 -9.368 40.978 1.00 6.71 O
ANISOU 221 O LYS A 32 1051 588 910 44 7 105 O
ATOM 222 CB LYS A 32 9.570 -12.314 39.761 1.00 6.78 C
ANISOU 222 CB LYS A 32 1370 627 579 -225 242 -249 C
ATOM 223 CG LYS A 32 8.290 -12.964 39.200 1.00 7.51 C
ANISOU 223 CG LYS A 32 1328 794 731 -403 318 -131 C
ATOM 224 CD LYS A 32 8.193 -14.417 39.696 1.00 11.75 C
ANISOU 224 CD LYS A 32 1964 1005 1494 -749 -38 225 C
ATOM 225 CE LYS A 32 6.903 -15.040 39.286 1.00 13.38 C
ANISOU 225 CE LYS A 32 2255 1354 1476 -1106 -174 419 C
ATOM 226 NZ LYS A 32 6.911 -16.470 39.730 1.00 18.07 N
ANISOU 226 NZ LYS A 32 2302 1495 3069 -1238 -1016 890 N
ATOM 227 N VAL A 33 12.121 -10.558 39.988 1.00 7.16 N
ANISOU 227 N VAL A 33 868 1003 848 -164 57 -200 N
ATOM 228 CA VAL A 33 13.186 -9.947 40.747 1.00 6.48 C
ANISOU 228 CA VAL A 33 942 822 700 52 -93 -150 C
ATOM 229 C VAL A 33 13.245 -8.464 40.442 1.00 6.28 C
ANISOU 229 C VAL A 33 846 827 713 36 -69 -141 C
ATOM 230 O VAL A 33 13.353 -7.646 41.361 1.00 6.79 O
ANISOU 230 O VAL A 33 1099 803 676 82 48 -140 O
ATOM 231 CB VAL A 33 14.538 -10.626 40.441 1.00 7.37 C
ANISOU 231 CB VAL A 33 977 957 869 168 -83 -43 C
ATOM 232 CG1 VAL A 33 15.724 -9.798 40.955 1.00 8.87 C
ANISOU 232 CG1 VAL A 33 872 1051 1447 157 1 -119 C
ATOM 233 CG2 VAL A 33 14.602 -12.036 41.015 1.00 8.53 C
ANISOU 233 CG2 VAL A 33 1423 841 975 220 -277 -179 C
ATOM 234 N ALA A 34 13.176 -8.098 39.169 1.00 5.84 N
ANISOU 234 N ALA A 34 813 711 693 107 -71 -211 N
ATOM 235 CA ALA A 34 13.228 -6.678 38.814 1.00 6.67 C
ANISOU 235 CA ALA A 34 832 796 905 259 -116 -58 C
ATOM 236 C ALA A 34 12.158 -5.885 39.546 1.00 5.66 C
ANISOU 236 C ALA A 34 809 566 777 14 68 20 C
ATOM 237 O ALA A 34 12.455 -4.855 40.144 1.00 6.70 O
ANISOU 237 O ALA A 34 1066 652 827 -60 25 -49 O
ATOM 238 CB ALA A 34 13.141 -6.522 37.328 1.00 6.76 C
ANISOU 238 CB ALA A 34 911 795 862 -17 144 -56 C
ATOM 239 N ILE A 35 10.934 -6.342 39.523 1.00 6.86 N
ANISOU 239 N ILE A 35 791 1086 729 -38 -34 -232 N
ATOM 240 CA ILE A 35 9.860 -5.600 40.195 1.00 6.05 C
ANISOU 240 CA ILE A 35 848 749 702 -21 175 227 C
ATOM 241 C ILE A 35 10.104 -5.600 41.698 1.00 6.32 C
ANISOU 241 C ILE A 35 978 755 668 -30 292 218 C
ATOM 242 O ILE A 35 9.925 -4.556 42.348 1.00 7.04 O
ANISOU 242 O ILE A 35 990 849 834 -23 122 53 O
ATOM 243 CB ILE A 35 8.504 -6.190 39.794 1.00 7.01 C
ANISOU 243 CB ILE A 35 819 813 1031 70 128 161 C
ATOM 244 CG1 ILE A 35 8.233 -5.925 38.314 1.00 7.53 C
ANISOU 244 CG1 ILE A 35 1140 698 1022 -14 -101 -20 C
ATOM 245 CG2 ILE A 35 7.392 -5.642 40.677 1.00 7.72 C
ANISOU 245 CG2 ILE A 35 710 1078 1143 89 -38 -171 C
ATOM 246 CD1 ILE A 35 7.055 -6.639 37.697 1.00 9.67 C
ANISOU 246 CD1 ILE A 35 1075 1095 1504 -19 -61 -467 C
ATOM 247 N ASP A 36 10.557 -6.703 42.279 1.00 6.87 N
ANISOU 247 N ASP A 36 1052 752 806 -180 -111 230 N
ATOM 248 CA ASP A 36 10.842 -6.723 43.718 1.00 6.79 C
ANISOU 248 CA ASP A 36 943 815 824 43 -149 54 C
ATOM 249 C ASP A 36 11.925 -5.731 44.121 1.00 7.14 C
ANISOU 249 C ASP A 36 995 867 850 18 -42 -43 C
ATOM 250 O ASP A 36 11.888 -5.192 45.224 1.00 8.79 O
ANISOU 250 O ASP A 36 1343 1118 878 -239 49 -153 O
ATOM 251 CB ASP A 36 11.266 -8.138 44.165 1.00 6.67 C
ANISOU 251 CB ASP A 36 841 906 788 34 -125 179 C
ATOM 252 CG ASP A 36 10.167 -9.183 44.176 1.00 7.16 C
ANISOU 252 CG ASP A 36 1021 897 802 -51 19 190 C
ATOM 253 OD1 ASP A 36 8.970 -8.777 44.196 1.00 7.30 O
ANISOU 253 OD1 ASP A 36 975 916 881 -140 200 106 O
ATOM 254 OD2 ASP A 36 10.463 -10.388 44.165 1.00 9.05 O
ANISOU 254 OD2 ASP A 36 1365 896 1177 19 -59 331 O
ATOM 255 N VAL A 37 12.909 -5.459 43.284 1.00 7.23 N
ANISOU 255 N VAL A 37 1032 1049 668 -153 -167 -18 N
ATOM 256 CA VAL A 37 13.989 -4.581 43.655 1.00 6.87 C
ANISOU 256 CA VAL A 37 902 960 749 -29 -270 22 C
ATOM 257 C VAL A 37 13.794 -3.167 43.141 1.00 7.48 C
ANISOU 257 C VAL A 37 1330 932 582 -89 -393 -58 C
ATOM 258 O VAL A 37 14.697 -2.310 43.303 1.00 10.33 O
ANISOU 258 O VAL A 37 1675 979 1269 -303 -612 68 O
ATOM 259 CB VAL A 37 15.375 -5.133 43.219 1.00 7.37 C
ANISOU 259 CB VAL A 37 1078 1032 689 -141 174 -75 C
ATOM 260 CG1 VAL A 37 15.601 -6.522 43.793 1.00 9.64 C
ATOM 261 CG2 VAL A 37 15.557 -5.122 41.726 1.00 10.63 C
ATOM 262 N GLY A 38 12.646 -2.859 42.513 1.00 7.30 N
ANISOU 262 N GLY A 38 1228 870 677 110 -215 -52 N
ATOM 263 CA GLY A 38 12.324 -1.473 42.231 1.00 8.16 C
ANISOU 263 CA GLY A 38 1419 794 889 -70 -552 -145 C
ATOM 264 C GLY A 38 12.002 -1.098 40.786 1.00 7.67 C
ANISOU 264 C GLY A 38 1193 820 899 -14 -369 31 C
ATOM 265 O GLY A 38 11.499 -0.021 40.503 1.00 8.03 O
ANISOU 265 O GLY A 38 1361 758 931 -39 -21 143 O
ATOM 266 N TYR A 39 12.261 -1.983 39.820 1.00 6.63 N
ANISOU 266 N TYR A 39 976 784 759 -7 -228 191 N
ATOM 267 CA TYR A 39 11.989 -1.628 38.446 1.00 6.38 C
ANISOU 267 CA TYR A 39 871 742 812 123 -160 241 C
ATOM 268 C TYR A 39 10.474 -1.515 38.251 1.00 6.81 C
ANISOU 268 C TYR A 39 876 975 738 -3 -237 94 C
ATOM 269 O TYR A 39 9.691 -2.295 38.762 1.00 8.24 O
ANISOU 269 O TYR A 39 960 1120 1050 -77 -158 154 O
ATOM 270 CB TYR A 39 12.502 -2.641 37.484 1.00 7.41 C
ANISOU 270 CB TYR A 39 852 1068 896 -44 -125 -18 C
ATOM 271 CG TYR A 39 13.973 -2.869 37.287 1.00 6.48 C
ANISOU 271 CG TYR A 39 822 934 708 -75 -124 -46 C
ATOM 272 CD1 TYR A 39 14.767 -3.470 38.242 1.00 6.42 C
ANISOU 272 CD1 TYR A 39 784 926 730 -207 -110 101 C
ATOM 273 CD2 TYR A 39 14.592 -2.476 36.101 1.00 7.10 C
ANISOU 273 CD2 TYR A 39 1035 950 714 187 -43 94 C
ATOM 274 CE1 TYR A 39 16.120 -3.663 38.026 1.00 6.87 C
ANISOU 274 CE1 TYR A 39 871 1005 734 27 -71 228 C
ATOM 275 CE2 TYR A 39 15.936 -2.709 35.888 1.00 6.57 C
ANISOU 275 CE2 TYR A 39 1103 641 751 208 100 171 C
ATOM 276 CZ TYR A 39 16.702 -3.307 36.845 1.00 6.54 C
ANISOU 276 CZ TYR A 39 950 685 848 122 72 208 C
ATOM 277 OH TYR A 39 18.045 -3.522 36.591 1.00 7.80 O
ANISOU 277 OH TYR A 39 856 1036 1074 -51 40 10 O
ATOM 278 N ARG A 40 10.135 -0.525 37.458 1.00 6.47 N
ANISOU 278 N ARG A 40 802 868 790 337 -42 -10 N
ATOM 279 CA ARG A 40 8.735 -0.277 37.145 1.00 7.08 C
ANISOU 279 CA ARG A 40 744 1222 726 341 12 -150 C
ATOM 280 C ARG A 40 8.482 -0.156 35.655 1.00 7.30 C
ANISOU 280 C ARG A 40 609 1404 761 13 -16 56 C
ATOM 281 O ARG A 40 7.399 0.212 35.237 1.00 13.48 O
ANISOU 281 O ARG A 40 782 3382 956 594 -77 135 O
ATOM 282 CB ARG A 40 8.248 1.021 37.790 1.00 7.32 C
ANISOU 282 CB ARG A 40 635 1059 1088 265 126 -75 C
ATOM 283 CG ARG A 40 8.327 0.972 39.334 1.00 9.27 C
ANISOU 283 CG ARG A 40 1813 665 1043 19 210 -320 C
ATOM 284 CD ARG A 40 7.262 0.027 39.886 1.00 8.81 C
ANISOU 284 CD ARG A 40 1201 1266 882 143 90 -140 C
ATOM 285 NE ARG A 40 7.318 -0.157 41.330 1.00 11.10 N
ANISOU 285 NE ARG A 40 1605 1680 932 129 197 -126 N
ATOM 286 CZ ARG A 40 7.966 -1.094 42.008 1.00 9.58 C
ANISOU 286 CZ ARG A 40 1452 1497 692 -415 -72 -96 C
ATOM 287 NH1 ARG A 40 8.699 -2.019 41.346 1.00 9.14 N
ANISOU 287 NH1 ARG A 40 1315 1346 810 -196 -91 242 N
ATOM 288 NH2 ARG A 40 7.853 -1.080 43.332 1.00 15.77 N
ANISOU 288 NH2 ARG A 40 2109 3204 679 15 -77 -150 N
ATOM 289 N HIS A 41 9.481 -0.399 34.836 1.00 6.35 N
ANISOU 289 N HIS A 41 808 932 672 254 -28 24 N
ATOM 290 CA HIS A 41 9.451 -0.302 33.383 1.00 5.95 C
ANISOU 290 CA HIS A 41 765 828 666 36 -64 28 C
ATOM 291 C HIS A 41 10.077 -1.612 32.840 1.00 5.60 C