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1784 lines (1784 loc) · 141 KB
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HEADER HORMONE 10-JUL-89 4INS
TITLE THE STRUCTURE OF 2ZN PIG INSULIN CRYSTALS AT 1.5 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN (CHAIN A);
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN (CHAIN B);
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 7 ORGANISM_COMMON: PIG;
SOURCE 8 ORGANISM_TAXID: 9823
KEYWDS HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.G.DODSON,E.J.DODSON,D.C.HODGKIN,N.W.ISAACS,M.VIJAYAN
REVDAT 7 29-NOV-17 4INS 1 HELIX
REVDAT 6 29-FEB-12 4INS 1 JRNL VERSN
REVDAT 5 24-FEB-09 4INS 1 VERSN
REVDAT 4 01-APR-03 4INS 1 JRNL
REVDAT 3 31-JUL-94 4INS 3 HETATM
REVDAT 2 15-JUL-93 4INS 1 HEADER
REVDAT 1 15-APR-90 4INS 0
SPRSDE 15-APR-90 4INS 1INS
JRNL AUTH E.N.BAKER,T.L.BLUNDELL,J.F.CUTFIELD,S.M.CUTFIELD,E.J.DODSON,
JRNL AUTH 2 G.G.DODSON,D.M.HODGKIN,R.E.HUBBARD,N.W.ISAACS,C.D.REYNOLDS,
JRNL AUTH 3 K.SAKABE,N.SAKABE,N.M.VIJAYAN
JRNL TITL THE STRUCTURE OF 2ZN PIG INSULIN CRYSTALS AT 1.5 A
JRNL TITL 2 RESOLUTION.
JRNL REF PHILOS.TRANS.R.SOC.LONDON, V. 319 369 1988
JRNL REF 2 SER.B
JRNL REFN ISSN 0080-4622
JRNL PMID 2905485
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.BORDAS,G.G.DODSON,H.GREWE,M.H.J.KOCH,B.KREBS,J.RANDALL
REMARK 1 TITL A COMPARATIVE ASSESSMENT OF THE ZINC-PROTEIN COORDINATION IN
REMARK 1 TITL 2 2ZN-INSULIN AS DETERMINED BY X-RAY ABSORPTION FINE STRUCTURE
REMARK 1 TITL 3 (EXAFS) AND X-RAY CRYSTALLOGRAPHY
REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 219 21 1983
REMARK 1 REFN ISSN 0080-4649
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.J.DODSON,G.G.DODSON,D.C.HODGKIN,C.D.REYNOLDS
REMARK 1 TITL STRUCTURAL RELATIONSHIPS IN THE TWO-ZINC INSULIN HEXAMER
REMARK 1 REF CAN.J.BIOCHEM. V. 57 469 1979
REMARK 1 REFN ISSN 0008-4018
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.W.ISAACS,R.C.AGARWAL
REMARK 1 TITL EXPERIENCE WITH FAST FOURIER LEAST SQUARES IN THE REFINEMENT
REMARK 1 TITL 2 OF THE CRYSTAL STRUCTURE OF RHOMBOHEDRAL 2-ZINC INSULIN AT
REMARK 1 TITL 3 1.5 ANGSTROMS RESOLUTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 34 782 1978
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.BENTLEY,G.DODSON,A.LEWITOVA
REMARK 1 TITL RHOMBOHEDRAL INSULIN CRYSTAL TRANSFORMATION
REMARK 1 REF J.MOL.BIOL. V. 126 871 1978
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH E.J.DODSON,N.W.ISAACS,J.S.ROLLETT
REMARK 1 TITL A METHOD FOR FITTING SATISFACTORY MODELS TO SETS OF ATOMIC
REMARK 1 TITL 2 POSITIONS IN PROTEIN STRUCTURE REFINEMENTS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 32 311 1976
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 6
REMARK 1 AUTH D.C.HODGKIN
REMARK 1 TITL VARIETIES OF INSULIN
REMARK 1 REF J.ENDOCRINOL. V. 63 1 1974
REMARK 1 REFN ISSN 0022-0795
REMARK 1 REFERENCE 7
REMARK 1 AUTH D.C.HODGKIN
REMARK 1 TITL THE STRUCTURE OF INSULIN
REMARK 1 REF DAN.TIDSSKR.FARM. V. 46 1 1972
REMARK 1 REFN ISSN 0011-6513
REMARK 1 REFERENCE 8
REMARK 1 AUTH T.BLUNDELL,G.DODSON,D.HODGKIN,D.MERCOLA
REMARK 1 TITL INSULIN. THE STRUCTURE IN THE CRYSTAL AND ITS REFLECTION IN
REMARK 1 TITL 2 CHEMISTRY AND BIOLOGY
REMARK 1 REF ADV.PROTEIN CHEM. V. 26 279 1972
REMARK 1 REFN ISSN 0065-3233
REMARK 1 REFERENCE 9
REMARK 1 AUTH T.L.BLUNDELL,J.F.CUTFIELD,E.J.DODSON,G.G.DODSON,D.C.HODGKIN,
REMARK 1 AUTH 2 D.A.MERCOLA
REMARK 1 TITL THE CRYSTAL STRUCTURE OF RHOMBOHEDRAL 2 ZINC INSULIN
REMARK 1 REF COLD SPRING HARBOR V. 36 233 1972
REMARK 1 REF 2 SYMP.QUANT.BIOL.
REMARK 1 REFN ISSN 0091-7451
REMARK 1 REFERENCE 10
REMARK 1 AUTH T.L.BLUNDELL,J.F.CUTFIELD,S.M.CUTFIELD,E.J.DODSON,
REMARK 1 AUTH 2 G.G.DODSON,D.C.HODGKIN,D.A.MERCOLA,M.VIJAYAN
REMARK 1 TITL ATOMIC POSITIONS IN RHOMBOHEDRAL 2-ZINC INSULIN CRYSTALS
REMARK 1 REF NATURE V. 231 506 1971
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 11
REMARK 1 AUTH T.L.BLUNDELL,G.G.DODSON,E.DODSON,D.C.HODGKIN,M.VIJAYAN
REMARK 1 TITL X-RAY ANALYSIS AND THE STRUCTURE OF INSULIN
REMARK 1 REF RECENT PROG.HORM.RES. V. 27 1 1971
REMARK 1 REFN ISSN 0079-9963
REMARK 1 REFERENCE 12
REMARK 1 AUTH E.N.BAKER,G.DODSON
REMARK 1 TITL X-RAY DIFFRACTION DATA ON SOME CRYSTALLINE VARIETIES OF
REMARK 1 TITL 2 INSULIN
REMARK 1 REF J.MOL.BIOL. V. 54 605 1970
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 13
REMARK 1 AUTH M.J.ADAMS,T.L.BLUNDELL,E.J.DODSON,G.G.DODSON,M.VIJAYAN,
REMARK 1 AUTH 2 E.N.BAKER,M.M.HARDING,D.C.HODGKIN,B.RIMMER,S.SHEAT
REMARK 1 TITL STRUCTURE OF RHOMBOHEDRAL 2 ZINC INSULIN CRYSTALS
REMARK 1 REF NATURE V. 224 491 1969
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 14
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 187 1972
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.005 ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
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) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 SOME RESIDUES ARE APPARENTLY DISORDERED BUT DIFFICULT TO
REMARK 3 DESCRIBE IN TERMS OF ATOMIC POSITIONS. ALA B 30 IS ONE OF
REMARK 3 THESE RESIDUES.
REMARK 3
REMARK 3 THE FOLLOWING RESIDUES ARE DISORDERED - GLN B 4, VAL B 12,
REMARK 3 GLU B 21, ARG B 22, ARG D 22, LYS D 29.
REMARK 4
REMARK 4 4INS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.25000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.81570
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.33333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 41.25000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 23.81570
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 11.33333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 41.25000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 23.81570
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 11.33333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.63140
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 22.66667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 47.63140
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 22.66667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 47.63140
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 22.66667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT OF INSULIN CONSISTS OF
REMARK 300 TWO INSULIN MOLECULES EACH CONSISTING OF TWO CHAINS. THIS
REMARK 300 ENTRY PRESENTS COORDINATES FOR MOLECULES I (CHAIN
REMARK 300 INDICATORS *A* AND *B*) AND II (CHAIN INDICATORS *C* AND
REMARK 300 *D*). THE QUASI-TWO-FOLD AXIS THAT TRANSFORMS MOLECULE I
REMARK 300 INTO MOLECULE II IS GIVEN IN THE *MTRIX* RECORDS BELOW.
REMARK 300 APPLYING THE THREE-FOLD CRYSTALLOGRAPHIC AXIS YIELDS A
REMARK 300 HEXAMER AROUND THE AXIS. THERE ARE TWO ZINC IONS SITUATED
REMARK 300 ON THIS THREE-FOLD AXIS. COORDINATES FOR THE ZINC IONS AND
REMARK 300 SOME WATER MOLECULES ARE INCLUDED BELOW WITH A BLANK CHAIN
REMARK 300 INDICATOR.
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: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -260.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN B 101 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN D 101 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 224 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 245 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 323 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 403 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 455 LIES ON A SPECIAL POSITION.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HIS B 10 NE2 98.9
REMARK 620 3 HIS B 10 NE2 98.7 98.8
REMARK 620 4 HOH B 213 O 90.2 163.2 93.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 HIS D 10 NE2 103.4
REMARK 620 3 HIS D 10 NE2 103.4 103.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: D1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DIMER-FORMING RESIDUES IN MOLECULE I
REMARK 800
REMARK 800 SITE_IDENTIFIER: D2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DIMER-FORMING RESIDUES IN MOLECULE II
REMARK 800
REMARK 800 SITE_IDENTIFIER: H1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HEXAMER-FORMING RESIDUES IN MOLECULE I
REMARK 800
REMARK 800 SITE_IDENTIFIER: H2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HEXAMER-FORMING RESIDUES IN MOLECULE II
REMARK 800
REMARK 800 SITE_IDENTIFIER: SI1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SURFACE-INVARIANT RESIDUES IN MOLECULE I NOT
REMARK 800 INVOLVED IN DIMERIZATION
REMARK 800
REMARK 800 SITE_IDENTIFIER: SI2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SURFACE-INVARIANT RESIDUES IN MOLECULE II NOT
REMARK 800 INVOLVED IN DIMERIZATION
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
DBREF 4INS A 1 21 UNP P01315 INS_PIG 88 108
DBREF 4INS B 1 30 UNP P01315 INS_PIG 25 54
DBREF 4INS C 1 21 UNP P01315 INS_PIG 88 108
DBREF 4INS D 1 30 UNP P01315 INS_PIG 25 54
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 30 THR PRO LYS ALA
SEQRES 1 C 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 C 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 D 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 D 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 D 30 THR PRO LYS ALA
HET ZN B 101 1
HET ZN D 101 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *350(H2 O)
HELIX 1 A11 GLY A 1 ILE A 10 1VAL 203 O H-BONDED TO HOH 10
HELIX 2 A12 SER A 12 GLU A 17 5CNTCTS MOSTLY GT 3A,NOT IDEAL 6
HELIX 3 B11 SER B 9 GLY B 20 1CYS 67 GLY 68, 3(10) CONTACTS 12
HELIX 4 A21 GLY C 1 ILE C 10 1NOT IDEAL ALPH,SOME PI CNTCTS 10
HELIX 5 A22 SER C 12 GLU C 17 5CNTCTS MOSTLY GT 3A,NOT IDEAL 6
HELIX 6 B21 SER D 9 GLY D 20 1CYS 67,GLY 68, 3(10) CONTACTS 12
SHEET 1 B 2 PHE B 24 TYR B 26 0
SHEET 2 B 2 PHE D 24 TYR D 26 -1 N PHE B 24 O TYR D 26
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.05
SSBOND 2 CYS A 7 CYS B 7 1555 1555 1.97
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.00
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.06
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.01
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.02
LINK ZN ZN B 101 NE2 HIS B 10 1555 1555 2.11
LINK ZN ZN D 101 NE2 HIS D 10 1555 1555 2.08
LINK ZN ZN B 101 NE2 HIS B 10 1555 2555 2.10
LINK ZN ZN B 101 NE2 HIS B 10 1555 3555 2.11
LINK ZN ZN D 101 NE2 HIS D 10 1555 3555 2.08
LINK ZN ZN D 101 NE2 HIS D 10 1555 2555 2.08
LINK ZN ZN B 101 O HOH B 213 1555 1555 2.19
SITE 1 D1 5 VAL B 12 TYR B 16 PHE B 24 PHE B 25
SITE 2 D1 5 TYR B 26
SITE 1 D2 5 VAL D 12 TYR D 16 PHE D 24 PHE D 25
SITE 2 D2 5 TYR D 26
SITE 1 H1 7 LEU A 13 TYR A 14 PHE B 1 GLU B 13
SITE 2 H1 7 ALA B 14 LEU B 17 VAL B 18
SITE 1 H2 7 LEU C 13 TYR C 14 PHE D 1 GLU D 13
SITE 2 H2 7 ALA D 14 LEU D 17 VAL D 18
SITE 1 SI1 7 GLY A 1 GLU A 4 GLN A 5 CYS A 7
SITE 2 SI1 7 TYR A 19 ASN A 21 CYS B 7
SITE 1 SI2 7 GLY C 1 GLU C 4 GLN C 5 CYS C 7
SITE 2 SI2 7 TYR C 19 ASN C 21 CYS D 7
SITE 1 AC1 1 HIS B 10
SITE 1 AC2 1 HIS D 10
CRYST1 82.500 82.500 34.000 90.00 90.00 120.00 H 3 18
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 0.012121 0.006998 0.000000 0.00000
SCALE2 0.000000 0.013996 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029412 0.00000
MTRIX1 1 -0.878620 -0.476960 0.023050 0.00000 1
MTRIX2 1 -0.477430 0.878370 -0.022860 0.00000 1
MTRIX3 1 -0.009350 -0.031090 -0.999470 0.00000 1
ATOM 1 N GLY A 1 -8.863 16.944 14.289 1.00 21.88 N
ATOM 2 CA GLY A 1 -9.929 17.026 13.244 1.00 22.85 C
ATOM 3 C GLY A 1 -10.051 15.625 12.618 1.00 43.92 C
ATOM 4 O GLY A 1 -9.782 14.728 13.407 1.00 25.22 O
ATOM 5 N ILE A 2 -10.333 15.531 11.332 1.00 26.28 N
ATOM 6 CA ILE A 2 -10.488 14.266 10.600 1.00 20.84 C
ATOM 7 C ILE A 2 -9.367 13.302 10.658 1.00 11.81 C
ATOM 8 O ILE A 2 -9.580 12.092 10.969 1.00 20.31 O
ATOM 9 CB ILE A 2 -10.883 14.493 9.095 1.00 40.00 C
ATOM 10 CG1 ILE A 2 -11.579 13.146 8.697 1.00 36.74 C
ATOM 11 CG2 ILE A 2 -9.741 14.794 8.140 1.00 23.02 C
ATOM 12 CD1 ILE A 2 -12.813 13.031 9.640 1.00 26.69 C
ATOM 13 N VAL A 3 -8.133 13.759 10.483 1.00 16.57 N
ATOM 14 CA VAL A 3 -6.966 12.901 10.576 1.00 15.75 C
ATOM 15 C VAL A 3 -6.892 12.161 11.922 1.00 22.09 C
ATOM 16 O VAL A 3 -6.547 10.990 12.037 1.00 24.52 O
ATOM 17 CB VAL A 3 -5.697 13.708 10.225 1.00 21.34 C
ATOM 18 CG1 VAL A 3 -4.382 12.960 10.448 1.00 32.48 C
ATOM 19 CG2 VAL A 3 -5.842 14.209 8.777 1.00 26.35 C
ATOM 20 N GLU A 4 -7.043 13.019 12.935 1.00 16.58 N
ATOM 21 CA GLU A 4 -6.889 12.474 14.295 1.00 15.32 C
ATOM 22 C GLU A 4 -8.004 11.558 14.610 1.00 16.88 C
ATOM 23 O GLU A 4 -7.888 10.474 15.128 1.00 23.30 O
ATOM 24 CB GLU A 4 -6.809 13.691 15.266 1.00 17.11 C
ATOM 25 CG GLU A 4 -5.615 14.565 14.951 1.00 21.45 C
ATOM 26 CD GLU A 4 -5.704 15.457 13.735 1.00 21.59 C
ATOM 27 OE1 GLU A 4 -6.757 15.959 13.377 1.00 23.43 O
ATOM 28 OE2 GLU A 4 -4.568 15.569 13.179 1.00 25.36 O
ATOM 29 N GLN A 5 -9.199 12.048 14.356 1.00 15.69 N
ATOM 30 CA GLN A 5 -10.407 11.299 14.630 1.00 12.38 C
ATOM 31 C GLN A 5 -10.431 9.940 13.980 1.00 19.86 C
ATOM 32 O GLN A 5 -10.815 8.931 14.542 1.00 16.83 O
ATOM 33 CB GLN A 5 -11.594 12.130 14.152 1.00 21.13 C
ATOM 34 CG GLN A 5 -12.860 11.374 14.561 1.00 22.06 C
ATOM 35 CD GLN A 5 -13.946 11.901 13.634 1.00 42.02 C
ATOM 36 OE1 GLN A 5 -13.908 13.027 13.169 1.00 55.10 O
ATOM 37 NE2 GLN A 5 -14.943 11.030 13.351 1.00 27.27 N
ATOM 38 N CYS A 6 -10.033 9.815 12.695 1.00 13.19 N
ATOM 39 CA CYS A 6 -10.050 8.518 12.065 1.00 12.63 C
ATOM 40 C CYS A 6 -9.105 7.520 12.667 1.00 9.95 C
ATOM 41 O CYS A 6 -9.395 6.288 12.666 1.00 14.22 O
ATOM 42 CB CYS A 6 -9.660 8.673 10.559 1.00 12.54 C
ATOM 43 SG CYS A 6 -10.925 9.459 9.579 1.00 13.00 S
ATOM 44 N CYS A 7 -8.018 7.992 13.171 1.00 10.84 N
ATOM 45 CA CYS A 7 -6.964 7.186 13.808 1.00 17.02 C
ATOM 46 C CYS A 7 -7.236 6.948 15.358 1.00 13.71 C
ATOM 47 O CYS A 7 -7.061 5.782 15.768 1.00 19.28 O
ATOM 48 CB CYS A 7 -5.578 7.826 13.656 1.00 20.24 C
ATOM 49 SG CYS A 7 -4.181 6.819 14.134 1.00 13.80 S
ATOM 50 N THR A 8 -7.655 7.937 16.058 1.00 12.57 N
ATOM 51 CA THR A 8 -7.862 7.732 17.520 1.00 19.99 C
ATOM 52 C THR A 8 -9.143 6.997 17.870 1.00 26.34 C
ATOM 53 O THR A 8 -9.189 6.157 18.795 1.00 25.43 O
ATOM 54 CB THR A 8 -7.728 9.055 18.386 1.00 20.77 C
ATOM 55 OG1 THR A 8 -8.889 9.918 18.117 1.00 26.76 O
ATOM 56 CG2 THR A 8 -6.334 9.700 18.196 1.00 26.50 C
ATOM 57 N SER A 9 -10.170 7.350 17.058 1.00 20.01 N
ATOM 58 CA SER A 9 -11.509 6.803 17.121 1.00 16.88 C
ATOM 59 C SER A 9 -11.796 5.981 15.856 1.00 12.70 C
ATOM 60 O SER A 9 -11.139 5.010 15.473 1.00 17.60 O
ATOM 61 CB SER A 9 -12.331 8.067 17.439 1.00 19.52 C
ATOM 62 OG SER A 9 -13.674 7.774 17.650 1.00 32.34 O
ATOM 63 N ILE A 10 -12.883 6.382 15.159 1.00 15.34 N
ATOM 64 CA ILE A 10 -13.350 5.723 13.932 1.00 20.23 C
ATOM 65 C ILE A 10 -13.969 6.902 13.106 1.00 17.50 C
ATOM 66 O ILE A 10 -14.355 7.922 13.623 1.00 16.60 O
ATOM 67 CB ILE A 10 -14.366 4.524 14.047 1.00 19.39 C
ATOM 68 CG1 ILE A 10 -15.702 4.874 14.742 1.00 22.05 C
ATOM 69 CG2 ILE A 10 -13.711 3.300 14.723 1.00 23.30 C
ATOM 70 CD1 ILE A 10 -16.702 3.722 15.005 1.00 42.11 C
ATOM 71 N CYS A 11 -14.080 6.685 11.767 1.00 12.14 N
ATOM 72 CA CYS A 11 -14.665 7.679 10.880 1.00 11.24 C
ATOM 73 C CYS A 11 -15.301 6.881 9.766 1.00 12.17 C
ATOM 74 O CYS A 11 -14.962 5.692 9.528 1.00 21.14 O
ATOM 75 CB CYS A 11 -13.695 8.702 10.417 1.00 13.03 C
ATOM 76 SG CYS A 11 -12.375 8.019 9.385 1.00 13.60 S
ATOM 77 N SER A 12 -16.233 7.557 9.095 1.00 11.37 N
ATOM 78 CA SER A 12 -16.999 6.978 8.005 1.00 9.91 C
ATOM 79 C SER A 12 -16.563 7.644 6.726 1.00 7.40 C
ATOM 80 O SER A 12 -15.967 8.753 6.711 1.00 9.67 O
ATOM 81 CB SER A 12 -18.516 7.183 8.084 1.00 16.64 C
ATOM 82 OG SER A 12 -18.869 8.543 7.881 1.00 17.14 O
ATOM 83 N LEU A 13 -16.852 6.914 5.612 1.00 11.35 N
ATOM 84 CA LEU A 13 -16.530 7.444 4.259 1.00 11.35 C
ATOM 85 C LEU A 13 -17.317 8.715 4.030 1.00 12.55 C
ATOM 86 O LEU A 13 -16.835 9.521 3.226 1.00 11.78 O
ATOM 87 CB LEU A 13 -16.774 6.348 3.232 1.00 11.66 C
ATOM 88 CG LEU A 13 -15.940 5.046 3.316 1.00 18.12 C
ATOM 89 CD1 LEU A 13 -16.050 4.197 2.018 1.00 18.76 C
ATOM 90 CD2 LEU A 13 -14.471 5.320 3.537 1.00 17.26 C
ATOM 91 N TYR A 14 -18.491 8.790 4.629 1.00 10.84 N
ATOM 92 CA TYR A 14 -19.282 10.035 4.368 1.00 10.75 C
ATOM 93 C TYR A 14 -18.639 11.228 4.963 1.00 12.81 C
ATOM 94 O TYR A 14 -18.706 12.298 4.341 1.00 15.11 O
ATOM 95 CB TYR A 14 -20.746 9.900 4.799 1.00 12.90 C
ATOM 96 CG TYR A 14 -21.463 8.764 4.079 1.00 18.23 C
ATOM 97 CD1 TYR A 14 -22.110 9.123 2.891 1.00 18.95 C
ATOM 98 CD2 TYR A 14 -21.461 7.440 4.475 1.00 15.42 C
ATOM 99 CE1 TYR A 14 -22.767 8.167 2.086 1.00 18.15 C
ATOM 100 CE2 TYR A 14 -22.118 6.436 3.676 1.00 14.31 C
ATOM 101 CZ TYR A 14 -22.738 6.856 2.556 1.00 15.47 C
ATOM 102 OH TYR A 14 -23.436 5.926 1.716 1.00 24.86 O
ATOM 103 N GLN A 15 -17.945 11.100 6.091 1.00 9.63 N
ATOM 104 CA GLN A 15 -17.178 12.138 6.774 1.00 9.40 C
ATOM 105 C GLN A 15 -16.012 12.543 5.900 1.00 10.52 C
ATOM 106 O GLN A 15 -15.611 13.717 5.722 1.00 14.25 O
ATOM 107 CB GLN A 15 -16.774 11.841 8.205 1.00 13.89 C
ATOM 108 CG GLN A 15 -17.894 11.668 9.206 1.00 17.53 C
ATOM 109 CD GLN A 15 -17.524 11.056 10.515 1.00 28.21 C
ATOM 110 OE1 GLN A 15 -16.865 10.027 10.598 1.00 20.14 O
ATOM 111 NE2 GLN A 15 -17.994 11.650 11.624 1.00 30.25 N
ATOM 112 N LEU A 16 -15.352 11.525 5.325 1.00 12.99 N
ATOM 113 CA LEU A 16 -14.185 11.826 4.470 1.00 11.19 C
ATOM 114 C LEU A 16 -14.605 12.634 3.249 1.00 15.54 C
ATOM 115 O LEU A 16 -13.767 13.398 2.745 1.00 16.01 O
ATOM 116 CB LEU A 16 -13.588 10.521 4.060 1.00 12.67 C
ATOM 117 CG LEU A 16 -12.954 9.717 5.182 1.00 13.07 C
ATOM 118 CD1 LEU A 16 -12.115 8.571 4.602 1.00 16.61 C
ATOM 119 CD2 LEU A 16 -12.041 10.559 6.028 1.00 16.50 C
ATOM 120 N GLU A 17 -15.779 12.420 2.759 1.00 17.50 N
ATOM 121 CA GLU A 17 -16.223 13.179 1.589 1.00 17.72 C
ATOM 122 C GLU A 17 -16.171 14.693 1.811 1.00 19.21 C
ATOM 123 O GLU A 17 -16.118 15.466 0.803 1.00 18.48 O
ATOM 124 CB GLU A 17 -17.645 12.862 1.215 1.00 17.38 C
ATOM 125 CG GLU A 17 -17.885 11.629 0.360 1.00 27.97 C
ATOM 126 CD GLU A 17 -19.225 11.667 -0.391 1.00 26.70 C
ATOM 127 OE1 GLU A 17 -20.201 11.466 0.276 1.00 29.93 O
ATOM 128 OE2 GLU A 17 -19.127 11.873 -1.643 1.00 34.66 O
ATOM 129 N ASN A 18 -16.094 15.074 3.104 1.00 15.10 N
ATOM 130 CA ASN A 18 -16.029 16.534 3.332 1.00 18.85 C
ATOM 131 C ASN A 18 -14.703 17.131 2.954 1.00 18.46 C
ATOM 132 O ASN A 18 -14.545 18.377 2.834 1.00 19.68 O
ATOM 133 CB ASN A 18 -16.489 16.934 4.738 1.00 20.66 C
ATOM 134 CG ASN A 18 -17.868 16.338 5.142 1.00 29.79 C
ATOM 135 OD1 ASN A 18 -18.813 16.053 4.382 1.00 34.48 O
ATOM 136 ND2 ASN A 18 -17.991 16.168 6.452 1.00 36.00 N
ATOM 137 N TYR A 19 -13.697 16.327 2.738 1.00 15.68 N
ATOM 138 CA TYR A 19 -12.358 16.724 2.380 1.00 14.19 C
ATOM 139 C TYR A 19 -12.154 16.695 0.899 1.00 13.20 C
ATOM 140 O TYR A 19 -11.010 17.038 0.480 1.00 16.12 O
ATOM 141 CB TYR A 19 -11.364 15.840 3.178 1.00 14.35 C
ATOM 142 CG TYR A 19 -11.586 16.223 4.634 1.00 21.24 C
ATOM 143 CD1 TYR A 19 -10.853 17.300 5.129 1.00 26.61 C
ATOM 144 CD2 TYR A 19 -12.562 15.703 5.445 1.00 19.21 C
ATOM 145 CE1 TYR A 19 -11.084 17.801 6.393 1.00 27.80 C
ATOM 146 CE2 TYR A 19 -12.833 16.207 6.714 1.00 23.98 C
ATOM 147 CZ TYR A 19 -12.081 17.267 7.187 1.00 34.08 C
ATOM 148 OH TYR A 19 -12.227 17.849 8.400 1.00 37.96 O
ATOM 149 N CYS A 20 -13.057 16.313 0.077 1.00 13.05 N
ATOM 150 CA CYS A 20 -12.838 16.309 -1.389 1.00 18.69 C
ATOM 151 C CYS A 20 -12.984 17.799 -1.802 1.00 19.09 C
ATOM 152 O CYS A 20 -13.588 18.579 -1.084 1.00 19.31 O
ATOM 153 CB CYS A 20 -13.850 15.490 -2.157 1.00 15.99 C
ATOM 154 SG CYS A 20 -13.923 13.761 -1.584 1.00 12.90 S
ATOM 155 N ASN A 21 -12.380 18.063 -2.909 1.00 17.63 N
ATOM 156 CA ASN A 21 -12.404 19.399 -3.608 1.00 25.23 C
ATOM 157 C ASN A 21 -13.642 19.696 -4.447 1.00 34.82 C
ATOM 158 O ASN A 21 -14.146 18.703 -4.956 1.00 31.24 O
ATOM 159 CB ASN A 21 -11.228 19.392 -4.521 1.00 19.06 C
ATOM 160 CG ASN A 21 -10.020 20.283 -4.456 1.00 40.71 C
ATOM 161 OD1 ASN A 21 -10.067 21.380 -5.083 1.00 68.22 O
ATOM 162 ND2 ASN A 21 -9.004 19.667 -3.808 1.00 39.69 N
ATOM 163 OXT ASN A 21 -13.881 20.890 -4.604 1.00 41.83 O
TER 164 ASN A 21
ATOM 165 N PHE B 1 -21.768 1.132 3.577 1.00 25.87 N
ATOM 166 CA PHE B 1 -20.374 1.368 4.053 1.00 24.30 C
ATOM 167 C PHE B 1 -20.341 1.145 5.585 1.00 39.74 C
ATOM 168 O PHE B 1 -21.423 1.141 6.173 1.00 38.10 O
ATOM 169 CB PHE B 1 -19.806 2.718 3.624 1.00 22.51 C
ATOM 170 CG PHE B 1 -19.924 2.916 2.131 1.00 16.52 C
ATOM 171 CD1 PHE B 1 -20.067 4.204 1.618 1.00 35.58 C
ATOM 172 CD2 PHE B 1 -19.709 1.873 1.262 1.00 20.86 C
ATOM 173 CE1 PHE B 1 -20.093 4.444 0.243 1.00 52.66 C
ATOM 174 CE2 PHE B 1 -19.824 2.067 -0.123 1.00 51.46 C
ATOM 175 CZ PHE B 1 -20.011 3.332 -0.631 1.00 42.63 C
ATOM 176 N VAL B 2 -19.104 0.899 6.027 1.00 21.12 N
ATOM 177 CA VAL B 2 -18.754 0.598 7.406 1.00 36.74 C
ATOM 178 C VAL B 2 -17.780 1.656 7.965 1.00 23.52 C
ATOM 179 O VAL B 2 -17.104 2.328 7.197 1.00 19.56 O
ATOM 180 CB VAL B 2 -18.048 -0.765 7.638 1.00 30.58 C
ATOM 181 CG1 VAL B 2 -18.993 -1.953 7.609 1.00 25.73 C
ATOM 182 CG2 VAL B 2 -16.776 -0.916 6.799 1.00 22.31 C
ATOM 183 N ASN B 3 -17.741 1.753 9.278 1.00 13.38 N
ATOM 184 CA ASN B 3 -16.872 2.691 9.950 1.00 13.94 C
ATOM 185 C ASN B 3 -15.457 2.100 9.881 1.00 15.03 C
ATOM 186 O ASN B 3 -15.312 0.857 9.926 1.00 24.85 O
ATOM 187 CB ASN B 3 -17.272 3.010 11.382 1.00 25.01 C
ATOM 188 CG ASN B 3 -18.513 3.844 11.511 1.00 49.04 C
ATOM 189 OD1 ASN B 3 -18.658 4.774 10.724 1.00 34.50 O
ATOM 190 ND2 ASN B 3 -19.333 3.415 12.473 1.00 35.00 N
ATOM 191 N GLN B 4 -14.509 3.031 9.767 1.00 12.52 N
ATOM 192 CA GLN B 4 -13.137 2.542 9.571 1.00 22.69 C
ATOM 193 C GLN B 4 -12.213 3.224 10.580 1.00 13.29 C
ATOM 194 O GLN B 4 -12.347 4.333 11.118 1.00 20.53 O
ATOM 195 CB GLN B 4 -12.666 2.760 8.116 1.00 39.18 C
ATOM 196 CG AGLN B 4 -13.007 1.731 7.035 0.60 11.45 C
ATOM 197 CG BGLN B 4 -12.978 1.763 6.996 0.40 37.30 C
ATOM 198 CD AGLN B 4 -12.270 0.520 6.830 0.60 12.42 C
ATOM 199 CD BGLN B 4 -14.070 2.781 6.746 0.40 32.97 C
ATOM 200 OE1AGLN B 4 -12.812 -0.612 6.494 0.60 17.67 O
ATOM 201 OE1BGLN B 4 -14.059 3.957 7.112 0.40 40.00 O
ATOM 202 NE2AGLN B 4 -10.898 0.624 6.949 0.60 28.94 N
ATOM 203 NE2BGLN B 4 -15.108 2.179 6.165 0.40 35.67 N
ATOM 204 N HIS B 5 -11.158 2.442 10.837 1.00 13.02 N
ATOM 205 CA HIS B 5 -10.083 3.000 11.779 1.00 17.05 C
ATOM 206 C HIS B 5 -8.855 3.149 10.899 1.00 10.95 C
ATOM 207 O HIS B 5 -8.284 2.166 10.380 1.00 17.14 O
ATOM 208 CB HIS B 5 -9.982 1.956 12.877 1.00 22.24 C
ATOM 209 CG HIS B 5 -8.934 2.400 13.860 1.00 25.74 C
ATOM 210 ND1 HIS B 5 -8.072 1.535 14.436 1.00 35.32 N
ATOM 211 CD2 HIS B 5 -8.637 3.596 14.329 1.00 28.02 C
ATOM 212 CE1 HIS B 5 -7.275 2.240 15.211 1.00 28.73 C
ATOM 213 NE2 HIS B 5 -7.571 3.509 15.150 1.00 30.21 N
ATOM 214 N LEU B 6 -8.529 4.400 10.604 1.00 11.30 N
ATOM 215 CA LEU B 6 -7.468 4.709 9.611 1.00 11.13 C
ATOM 216 C LEU B 6 -6.399 5.604 10.158 1.00 11.03 C
ATOM 217 O LEU B 6 -6.695 6.779 10.484 1.00 13.66 O
ATOM 218 CB LEU B 6 -8.231 5.398 8.411 1.00 14.13 C
ATOM 219 CG LEU B 6 -9.251 4.634 7.563 1.00 13.39 C
ATOM 220 CD1 LEU B 6 -10.017 5.598 6.671 1.00 14.70 C
ATOM 221 CD2 LEU B 6 -8.620 3.517 6.767 1.00 18.25 C
ATOM 222 N CYS B 7 -5.180 5.069 10.115 1.00 10.06 N
ATOM 223 CA CYS B 7 -4.058 5.835 10.569 1.00 10.70 C
ATOM 224 C CYS B 7 -3.033 5.982 9.484 1.00 13.26 C
ATOM 225 O CYS B 7 -2.955 5.198 8.573 1.00 19.10 O
ATOM 226 CB CYS B 7 -3.434 5.105 11.762 1.00 15.88 C
ATOM 227 SG CYS B 7 -4.523 5.099 13.246 1.00 16.40 S
ATOM 228 N GLY B 8 -2.181 6.993 9.540 1.00 12.37 N
ATOM 229 CA GLY B 8 -1.070 7.261 8.632 1.00 12.72 C
ATOM 230 C GLY B 8 -1.465 7.317 7.204 1.00 13.24 C
ATOM 231 O GLY B 8 -2.470 7.884 6.744 1.00 11.92 O
ATOM 232 N SER B 9 -0.609 6.582 6.429 1.00 11.74 N
ATOM 233 CA SER B 9 -0.863 6.544 4.980 1.00 15.89 C
ATOM 234 C SER B 9 -2.183 5.870 4.578 1.00 9.73 C
ATOM 235 O SER B 9 -2.649 6.111 3.528 1.00 10.43 O
ATOM 236 CB SER B 9 0.309 5.921 4.206 1.00 17.74 C
ATOM 237 OG SER B 9 0.534 4.626 4.735 1.00 17.37 O
ATOM 238 N HIS B 10 -2.721 5.100 5.451 1.00 10.19 N
ATOM 239 CA HIS B 10 -3.940 4.379 5.188 1.00 7.66 C
ATOM 240 C HIS B 10 -5.081 5.431 5.075 1.00 10.17 C
ATOM 241 O HIS B 10 -6.021 5.163 4.291 1.00 10.92 O
ATOM 242 CB HIS B 10 -4.234 3.316 6.228 1.00 9.55 C
ATOM 243 CG HIS B 10 -3.192 2.269 6.364 1.00 9.55 C
ATOM 244 ND1 HIS B 10 -3.043 1.310 5.423 1.00 15.86 N
ATOM 245 CD2 HIS B 10 -2.289 1.991 7.311 1.00 8.47 C
ATOM 246 CE1 HIS B 10 -2.078 0.573 5.774 1.00 10.65 C
ATOM 247 NE2 HIS B 10 -1.589 0.939 6.878 1.00 9.41 N
ATOM 248 N LEU B 11 -5.016 6.497 5.810 1.00 8.93 N
ATOM 249 CA LEU B 11 -6.071 7.518 5.617 1.00 9.64 C
ATOM 250 C LEU B 11 -5.967 8.182 4.279 1.00 7.89 C
ATOM 251 O LEU B 11 -6.969 8.462 3.666 1.00 9.74 O
ATOM 252 CB LEU B 11 -5.860 8.541 6.740 1.00 6.93 C
ATOM 253 CG LEU B 11 -6.949 9.607 6.783 1.00 14.50 C
ATOM 254 CD1 LEU B 11 -8.376 9.229 6.627 1.00 18.34 C
ATOM 255 CD2 LEU B 11 -6.742 10.309 8.115 1.00 20.70 C
ATOM 256 N VAL B 12 -4.751 8.449 3.799 1.00 10.12 N
ATOM 257 CA VAL B 12 -4.579 9.057 2.495 1.00 8.05 C
ATOM 258 C VAL B 12 -5.050 8.131 1.372 1.00 8.14 C
ATOM 259 O VAL B 12 -5.595 8.653 0.398 1.00 11.63 O
ATOM 260 CB VAL B 12 -3.153 9.538 2.230 1.00 11.54 C
ATOM 261 CG1AVAL B 12 -2.822 9.786 0.799 0.50 4.68 C
ATOM 262 CG1BVAL B 12 -2.809 10.670 3.148 0.50 17.75 C
ATOM 263 CG2AVAL B 12 -2.809 10.670 3.148 0.50 17.75 C
ATOM 264 CG2BVAL B 12 -1.963 8.655 2.123 0.50 10.87 C
ATOM 265 N GLU B 13 -4.906 6.880 1.502 1.00 6.12 N
ATOM 266 CA GLU B 13 -5.432 5.946 0.542 1.00 8.88 C
ATOM 267 C GLU B 13 -6.966 6.014 0.472 1.00 12.22 C
ATOM 268 O GLU B 13 -7.578 6.035 -0.614 1.00 11.15 O
ATOM 269 CB GLU B 13 -4.996 4.506 0.854 1.00 12.65 C
ATOM 270 CG GLU B 13 -3.497 4.444 0.582 1.00 15.60 C
ATOM 271 CD GLU B 13 -3.246 3.857 -0.794 1.00 53.85 C
ATOM 272 OE1 GLU B 13 -4.238 3.643 -1.500 1.00 33.68 O
ATOM 273 OE2 GLU B 13 -2.114 3.611 -1.126 1.00 47.24 O
ATOM 274 N ALA B 14 -7.659 6.004 1.637 1.00 7.15 N
ATOM 275 CA ALA B 14 -9.061 6.164 1.719 1.00 7.29 C
ATOM 276 C ALA B 14 -9.563 7.482 1.051 1.00 6.80 C
ATOM 277 O ALA B 14 -10.595 7.468 0.346 1.00 11.10 O
ATOM 278 CB ALA B 14 -9.604 6.039 3.106 1.00 12.06 C
ATOM 279 N LEU B 15 -8.876 8.580 1.321 1.00 6.72 N
ATOM 280 CA LEU B 15 -9.224 9.854 0.717 1.00 13.51 C
ATOM 281 C LEU B 15 -9.111 9.815 -0.829 1.00 14.62 C
ATOM 282 O LEU B 15 -9.956 10.390 -1.496 1.00 12.32 O
ATOM 283 CB LEU B 15 -8.317 10.981 1.327 1.00 9.71 C
ATOM 284 CG LEU B 15 -8.755 11.581 2.649 1.00 8.92 C
ATOM 285 CD1 LEU B 15 -7.682 12.475 3.236 1.00 14.49 C
ATOM 286 CD2 LEU B 15 -10.096 12.235 2.460 1.00 12.03 C
ATOM 287 N TYR B 16 -8.050 9.147 -1.297 1.00 8.65 N
ATOM 288 CA TYR B 16 -7.838 8.961 -2.686 1.00 8.75 C
ATOM 289 C TYR B 16 -8.999 8.175 -3.284 1.00 11.14 C
ATOM 290 O TYR B 16 -9.508 8.504 -4.371 1.00 14.34 O
ATOM 291 CB TYR B 16 -6.494 8.247 -3.047 1.00 7.72 C
ATOM 292 CG TYR B 16 -6.271 8.027 -4.522 1.00 10.81 C
ATOM 293 CD1 TYR B 16 -6.450 6.784 -5.047 1.00 17.09 C
ATOM 294 CD2 TYR B 16 -6.009 9.104 -5.338 1.00 12.64 C
ATOM 295 CE1 TYR B 16 -6.354 6.581 -6.467 1.00 17.76 C
ATOM 296 CE2 TYR B 16 -5.898 8.958 -6.741 1.00 13.94 C
ATOM 297 CZ TYR B 16 -6.110 7.692 -7.259 1.00 17.34 C
ATOM 298 OH TYR B 16 -5.925 7.520 -8.594 1.00 25.34 O
ATOM 299 N LEU B 17 -9.428 7.109 -2.664 1.00 8.68 N
ATOM 300 CA LEU B 17 -10.566 6.290 -3.167 1.00 8.83 C
ATOM 301 C LEU B 17 -11.861 7.087 -3.142 1.00 10.95 C
ATOM 302 O LEU B 17 -12.650 7.046 -4.073 1.00 15.67 O
ATOM 303 CB LEU B 17 -10.665 5.052 -2.327 1.00 10.82 C
ATOM 304 CG LEU B 17 -9.594 4.104 -2.924 1.00 28.76 C
ATOM 305 CD1 LEU B 17 -9.136 3.067 -1.933 1.00 30.52 C
ATOM 306 CD2 LEU B 17 -10.280 3.540 -4.157 1.00 34.91 C
ATOM 307 N VAL B 18 -12.123 7.786 -2.036 1.00 8.85 N
ATOM 308 CA VAL B 18 -13.351 8.545 -1.933 1.00 8.77 C
ATOM 309 C VAL B 18 -13.433 9.713 -2.873 1.00 9.77 C
ATOM 310 O VAL B 18 -14.472 9.937 -3.457 1.00 16.86 O
ATOM 311 CB VAL B 18 -13.604 8.974 -0.463 1.00 14.39 C
ATOM 312 CG1 VAL B 18 -14.784 9.899 -0.282 1.00 11.72 C
ATOM 313 CG2 VAL B 18 -13.862 7.763 0.393 1.00 12.58 C
ATOM 314 N CYS B 19 -12.422 10.518 -2.958 1.00 9.03 N
ATOM 315 CA CYS B 19 -12.433 11.758 -3.756 1.00 8.88 C
ATOM 316 C CYS B 19 -11.994 11.555 -5.212 1.00 14.69 C
ATOM 317 O CYS B 19 -12.410 12.303 -6.126 1.00 16.46 O
ATOM 318 CB CYS B 19 -11.558 12.719 -3.005 1.00 11.19 C
ATOM 319 SG CYS B 19 -12.040 13.127 -1.344 1.00 10.10 S
ATOM 320 N GLY B 20 -11.149 10.609 -5.463 1.00 17.12 N
ATOM 321 CA GLY B 20 -10.685 10.359 -6.851 1.00 21.59 C
ATOM 322 C GLY B 20 -10.275 11.650 -7.524 1.00 21.38 C
ATOM 323 O GLY B 20 -9.494 12.483 -7.053 1.00 20.41 O
ATOM 324 N GLU B 21 -10.784 11.844 -8.710 1.00 29.76 N
ATOM 325 CA GLU B 21 -10.398 13.043 -9.501 1.00 24.44 C
ATOM 326 C GLU B 21 -10.898 14.356 -9.065 1.00 19.21 C
ATOM 327 O GLU B 21 -10.430 15.331 -9.665 1.00 19.00 O
ATOM 328 CB GLU B 21 -10.776 12.724 -10.968 1.00 28.66 C
ATOM 329 CG AGLU B 21 -12.310 12.519 -11.045 0.50 56.11 C
ATOM 330 CG BGLU B 21 -9.804 13.415 -11.966 0.50 75.35 C
ATOM 331 CD AGLU B 21 -12.707 11.349 -11.901 0.50 62.47 C
ATOM 332 CD BGLU B 21 -9.689 13.292 -13.466 0.50 52.68 C
ATOM 333 OE1AGLU B 21 -12.515 10.193 -11.564 0.50 48.34 O
ATOM 334 OE1BGLU B 21 -10.540 12.768 -14.159 0.50 50.28 O
ATOM 335 OE2AGLU B 21 -13.225 11.772 -12.958 0.50 49.92 O
ATOM 336 OE2BGLU B 21 -8.505 13.537 -13.781 0.50 27.33 O
ATOM 337 N ARG B 22 -11.703 14.491 -8.034 1.00 15.49 N
ATOM 338 CA ARG B 22 -12.089 15.732 -7.456 1.00 16.44 C
ATOM 339 C ARG B 22 -10.797 16.222 -6.745 1.00 17.70 C
ATOM 340 O ARG B 22 -10.636 17.458 -6.608 1.00 21.36 O
ATOM 341 CB ARG B 22 -13.234 15.678 -6.464 1.00 21.99 C
ATOM 342 CG ARG B 22 -14.645 15.427 -7.037 1.00 57.89 C
ATOM 343 CD ARG B 22 -15.675 15.167 -5.960 1.00 31.23 C
ATOM 344 NE AARG B 22 -15.739 16.404 -5.124 0.50 16.46 N
ATOM 345 NE BARG B 22 -15.629 13.808 -5.271 0.50 17.69 N
ATOM 346 CZ AARG B 22 -16.608 16.581 -4.143 0.50 39.57 C
ATOM 347 CZ BARG B 22 -16.379 13.225 -4.283 0.50 33.09 C
ATOM 348 NH1AARG B 22 -16.743 17.672 -3.416 0.50 20.14 N
ATOM 349 NH1BARG B 22 -16.987 14.046 -3.392 0.50 51.50 N
ATOM 350 NH2AARG B 22 -17.405 15.551 -3.871 0.50 35.40 N
ATOM 351 NH2BARG B 22 -16.705 11.943 -4.184 0.50 19.59 N
ATOM 352 N GLY B 23 -10.007 15.246 -6.287 1.00 19.18 N
ATOM 353 CA GLY B 23 -8.844 15.673 -5.491 1.00 11.89 C
ATOM 354 C GLY B 23 -9.339 15.932 -4.075 1.00 12.83 C
ATOM 355 O GLY B 23 -10.524 15.922 -3.626 1.00 14.47 O
ATOM 356 N PHE B 24 -8.343 16.165 -3.187 1.00 12.54 N
ATOM 357 CA PHE B 24 -8.584 16.432 -1.765 1.00 10.08 C
ATOM 358 C PHE B 24 -7.488 17.220 -1.123 1.00 10.77 C
ATOM 359 O PHE B 24 -6.411 17.409 -1.657 1.00 10.93 O
ATOM 360 CB PHE B 24 -8.754 15.111 -1.032 1.00 3.80 C
ATOM 361 CG PHE B 24 -7.638 14.114 -1.034 1.00 5.98 C
ATOM 362 CD1 PHE B 24 -7.488 13.202 -2.069 1.00 5.61 C
ATOM 363 CD2 PHE B 24 -6.667 14.205 -0.036 1.00 8.93 C
ATOM 364 CE1 PHE B 24 -6.375 12.338 -2.106 1.00 14.64 C
ATOM 365 CE2 PHE B 24 -5.573 13.387 0.027 1.00 11.74 C
ATOM 366 CZ PHE B 24 -5.457 12.470 -1.008 1.00 9.78 C
ATOM 367 N PHE B 25 -7.717 17.612 0.116 1.00 14.20 N
ATOM 368 CA PHE B 25 -6.813 18.302 1.052 1.00 12.03 C
ATOM 369 C PHE B 25 -6.569 17.356 2.221 1.00 12.69 C
ATOM 370 O PHE B 25 -7.485 16.788 2.757 1.00 15.22 O
ATOM 371 CB PHE B 25 -7.387 19.633 1.684 1.00 17.25 C
ATOM 372 CG PHE B 25 -7.105 20.689 0.637 1.00 30.38 C
ATOM 373 CD1 PHE B 25 -7.842 20.802 -0.543 1.00 61.20 C
ATOM 374 CD2 PHE B 25 -6.003 21.541 0.896 1.00 56.90 C
ATOM 375 CE1 PHE B 25 -7.445 21.790 -1.461 1.00 29.52 C
ATOM 376 CE2 PHE B 25 -5.648 22.564 -0.027 1.00 40.31 C
ATOM 377 CZ PHE B 25 -6.382 22.681 -1.235 1.00 30.38 C
ATOM 378 N TYR B 26 -5.345 17.202 2.583 1.00 11.25 N
ATOM 379 CA TYR B 26 -4.996 16.333 3.717 1.00 10.42 C
ATOM 380 C TYR B 26 -4.445 17.350 4.714 1.00 15.08 C
ATOM 381 O TYR B 26 -3.350 17.906 4.518 1.00 14.52 O
ATOM 382 CB TYR B 26 -3.949 15.288 3.319 1.00 9.51 C
ATOM 383 CG TYR B 26 -3.404 14.530 4.474 1.00 12.61 C
ATOM 384 CD1 TYR B 26 -4.243 13.688 5.178 1.00 20.50 C
ATOM 385 CD2 TYR B 26 -2.105 14.676 4.857 1.00 13.88 C
ATOM 386 CE1 TYR B 26 -3.652 12.967 6.246 1.00 16.38 C
ATOM 387 CE2 TYR B 26 -1.577 14.010 5.941 1.00 10.97 C
ATOM 388 CZ TYR B 26 -2.347 13.149 6.642 1.00 11.71 C
ATOM 389 OH TYR B 26 -1.853 12.447 7.734 1.00 16.39 O
ATOM 390 N THR B 27 -5.287 17.537 5.752 1.00 15.47 N
ATOM 391 CA THR B 27 -4.902 18.555 6.772 1.00 20.05 C
ATOM 392 C THR B 27 -4.834 18.053 8.250 1.00 15.09 C
ATOM 393 O THR B 27 -5.825 18.282 8.943 1.00 22.56 O
ATOM 394 CB THR B 27 -5.856 19.825 6.753 1.00 26.34 C
ATOM 395 OG1ATHR B 27 -7.228 19.328 6.558 0.50 39.91 O
ATOM 396 OG1BTHR B 27 -5.691 20.478 5.511 0.50 29.43 O
ATOM 397 CG2ATHR B 27 -5.505 20.781 5.606 0.50 34.53 C
ATOM 398 CG2BTHR B 27 -5.413 20.850 7.858 0.50 34.13 C
ATOM 399 N PRO B 28 -3.702 17.548 8.603 1.00 18.26 N
ATOM 400 CA PRO B 28 -3.494 17.055 9.954 1.00 21.56 C
ATOM 401 C PRO B 28 -3.306 18.220 10.892 1.00 22.68 C
ATOM 402 O PRO B 28 -3.072 19.330 10.484 1.00 21.93 O
ATOM 403 CB PRO B 28 -2.249 16.209 9.808 1.00 21.60 C
ATOM 404 CG PRO B 28 -1.544 16.617 8.595 1.00 21.39 C
ATOM 405 CD PRO B 28 -2.526 17.320 7.778 1.00 14.32 C
ATOM 406 N LYS B 29 -3.452 17.975 12.175 1.00 26.27 N
ATOM 407 CA LYS B 29 -3.227 18.941 13.307 1.00 23.17 C
ATOM 408 C LYS B 29 -1.707 18.995 13.459 1.00 52.81 C
ATOM 409 O LYS B 29 -1.026 17.919 13.406 1.00 39.37 O
ATOM 410 CB LYS B 29 -3.764 18.417 14.615 1.00 22.26 C
ATOM 411 CG LYS B 29 -3.990 19.385 15.801 1.00 48.01 C
ATOM 412 CD LYS B 29 -5.153 18.811 16.622 1.00 37.36 C
ATOM 413 CE LYS B 29 -5.067 18.493 18.087 1.00 53.09 C
ATOM 414 NZ LYS B 29 -4.208 19.418 18.841 1.00 61.16 N
ATOM 415 N ALA B 30 -1.166 20.052 13.779 1.00 53.30 N
ATOM 416 CA ALA B 30 0.148 20.539 13.902 1.00 45.30 C
ATOM 417 C ALA B 30 0.991 20.467 15.167 1.00 50.30 C
ATOM 418 O ALA B 30 0.427 20.710 16.268 1.00 62.63 O
ATOM 419 CB ALA B 30 0.033 22.113 13.690 1.00 53.30 C
ATOM 420 OXT ALA B 30 2.226 20.205 15.000 1.00 76.30 O
TER 421 ALA B 30