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pdb1crn.ent
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HEADER PLANT PROTEIN 30-APR-81 1CRN
TITLE WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC RESOLUTION.
TITLE 2 PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF CRAMBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRAMBIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA SUBSP. ABYSSINICA;
SOURCE 3 ORGANISM_TAXID: 3721;
SOURCE 4 STRAIN: SUBSP. ABYSSINICA
KEYWDS PLANT SEED PROTEIN, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.A.HENDRICKSON,M.M.TEETER
REVDAT 8 29-NOV-17 1CRN 1 HELIX
REVDAT 7 11-JUL-12 1CRN 1 SCALE1 VERSN HEADER
REVDAT 6 24-FEB-09 1CRN 1 VERSN
REVDAT 5 16-APR-87 1CRN 1 HEADER
REVDAT 4 04-MAR-85 1CRN 1 REMARK
REVDAT 3 30-SEP-83 1CRN 1 REVDAT
REVDAT 2 03-DEC-81 1CRN 1 SHEET
REVDAT 1 28-JUL-81 1CRN 0
JRNL AUTH M.M.TEETER
JRNL TITL WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC
JRNL TITL 2 RESOLUTION: PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF
JRNL TITL 3 CRAMBIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 81 6014 1984
JRNL REFN ISSN 0027-8424
JRNL PMID 16593516
JRNL DOI 10.1073/PNAS.81.19.6014
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.A.HENDRICKSON,M.M.TEETER
REMARK 1 TITL STRUCTURE OF THE HYDROPHOBIC PROTEIN CRAMBIN DETERMINED
REMARK 1 TITL 2 DIRECTLY FROM THE ANOMALOUS SCATTERING OF SULPHUR
REMARK 1 REF NATURE V. 290 107 1981
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.M.TEETER,W.A.HENDRICKSON
REMARK 1 TITL HIGHLY ORDERED CRYSTALS OF THE PLANT SEED PROTEIN CRAMBIN
REMARK 1 REF J.MOL.BIOL. V. 127 219 1979
REMARK 1 REFN ISSN 0022-2836
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) : NULL
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 : 327
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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) : NULL ; 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: NULL
REMARK 4
REMARK 4 1CRN 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_1000172485.
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 (%): 32.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 9.32500
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE SECONDARY STRUCTURE SPECIFICATIONS ARE THOSE DEFINED
REMARK 400 IN REFERENCE 1 ABOVE AND DEPEND ON PARTICULAR DEFINITIONS
REMARK 400 THAT MAY AFFECT THE DETERMINATION OF END POINTS. PLEASE
REMARK 400 CONSULT THE PRIMARY REFERENCE AND EXAMINE STRUCTURAL
REMARK 400 DETAILS SUCH AS HYDROGEN BONDING AND CONFORMATION ANGLES
REMARK 400 WHEN MAKING USE OF THE SPECIFICATIONS.
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 10 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 29 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CRN A 1 46 UNP P01542 CRAM_CRAAB 1 46
SEQRES 1 A 46 THR THR CYS CYS PRO SER ILE VAL ALA ARG SER ASN PHE
SEQRES 2 A 46 ASN VAL CYS ARG LEU PRO GLY THR PRO GLU ALA ILE CYS
SEQRES 3 A 46 ALA THR TYR THR GLY CYS ILE ILE ILE PRO GLY ALA THR
SEQRES 4 A 46 CYS PRO GLY ASP TYR ALA ASN
HELIX 1 H1 ILE A 7 PRO A 19 13/10 CONFORMATION RES 17,19 13
HELIX 2 H2 GLU A 23 THR A 30 1DISTORTED 3/10 AT RES 30 8
SHEET 1 S1 2 THR A 1 CYS A 4 0
SHEET 2 S1 2 CYS A 32 ILE A 35 -1
SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.00
SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.04
SSBOND 3 CYS A 16 CYS A 26 1555 1555 2.05
CRYST1 40.960 18.650 22.520 90.00 90.77 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 0.024414 0.000000 0.000328 0.00000
SCALE2 0.000000 0.053619 0.000000 0.00000
SCALE3 0.000000 0.000000 0.044409 0.00000
ATOM 1 N THR A 1 17.047 14.099 3.625 1.00 13.79 N
ATOM 2 CA THR A 1 16.967 12.784 4.338 1.00 10.80 C
ATOM 3 C THR A 1 15.685 12.755 5.133 1.00 9.19 C
ATOM 4 O THR A 1 15.268 13.825 5.594 1.00 9.85 O
ATOM 5 CB THR A 1 18.170 12.703 5.337 1.00 13.02 C
ATOM 6 OG1 THR A 1 19.334 12.829 4.463 1.00 15.06 O
ATOM 7 CG2 THR A 1 18.150 11.546 6.304 1.00 14.23 C
ATOM 8 N THR A 2 15.115 11.555 5.265 1.00 7.81 N
ATOM 9 CA THR A 2 13.856 11.469 6.066 1.00 8.31 C
ATOM 10 C THR A 2 14.164 10.785 7.379 1.00 5.80 C
ATOM 11 O THR A 2 14.993 9.862 7.443 1.00 6.94 O
ATOM 12 CB THR A 2 12.732 10.711 5.261 1.00 10.32 C
ATOM 13 OG1 THR A 2 13.308 9.439 4.926 1.00 12.81 O
ATOM 14 CG2 THR A 2 12.484 11.442 3.895 1.00 11.90 C
ATOM 15 N CYS A 3 13.488 11.241 8.417 1.00 5.24 N
ATOM 16 CA CYS A 3 13.660 10.707 9.787 1.00 5.39 C
ATOM 17 C CYS A 3 12.269 10.431 10.323 1.00 4.45 C
ATOM 18 O CYS A 3 11.393 11.308 10.185 1.00 6.54 O
ATOM 19 CB CYS A 3 14.368 11.748 10.691 1.00 5.99 C
ATOM 20 SG CYS A 3 15.885 12.426 10.016 1.00 7.01 S
ATOM 21 N CYS A 4 12.019 9.272 10.928 1.00 3.90 N
ATOM 22 CA CYS A 4 10.646 8.991 11.408 1.00 4.24 C
ATOM 23 C CYS A 4 10.654 8.793 12.919 1.00 3.72 C
ATOM 24 O CYS A 4 11.659 8.296 13.491 1.00 5.30 O
ATOM 25 CB CYS A 4 10.057 7.752 10.682 1.00 4.41 C
ATOM 26 SG CYS A 4 9.837 8.018 8.904 1.00 4.72 S
ATOM 27 N PRO A 5 9.561 9.108 13.563 1.00 3.96 N
ATOM 28 CA PRO A 5 9.448 9.034 15.012 1.00 4.25 C
ATOM 29 C PRO A 5 9.288 7.670 15.606 1.00 4.96 C
ATOM 30 O PRO A 5 9.490 7.519 16.819 1.00 7.44 O
ATOM 31 CB PRO A 5 8.230 9.957 15.345 1.00 5.11 C
ATOM 32 CG PRO A 5 7.338 9.786 14.114 1.00 5.24 C
ATOM 33 CD PRO A 5 8.366 9.804 12.958 1.00 5.20 C
ATOM 34 N SER A 6 8.875 6.686 14.796 1.00 4.83 N
ATOM 35 CA SER A 6 8.673 5.314 15.279 1.00 4.45 C
ATOM 36 C SER A 6 8.753 4.376 14.083 1.00 4.99 C
ATOM 37 O SER A 6 8.726 4.858 12.923 1.00 4.61 O
ATOM 38 CB SER A 6 7.340 5.121 15.996 1.00 5.05 C
ATOM 39 OG SER A 6 6.274 5.220 15.031 1.00 6.39 O
ATOM 40 N ILE A 7 8.881 3.075 14.358 1.00 4.94 N
ATOM 41 CA ILE A 7 8.912 2.083 13.258 1.00 6.33 C
ATOM 42 C ILE A 7 7.581 2.090 12.506 1.00 5.32 C
ATOM 43 O ILE A 7 7.670 2.031 11.245 1.00 6.85 O
ATOM 44 CB ILE A 7 9.207 0.677 13.924 1.00 8.43 C
ATOM 45 CG1 ILE A 7 10.714 0.702 14.312 1.00 9.78 C
ATOM 46 CG2 ILE A 7 8.811 -0.477 12.969 1.00 11.70 C
ATOM 47 CD1 ILE A 7 11.185 -0.516 15.142 1.00 9.92 C
ATOM 48 N VAL A 8 6.458 2.162 13.159 1.00 5.02 N
ATOM 49 CA VAL A 8 5.145 2.209 12.453 1.00 6.93 C
ATOM 50 C VAL A 8 5.115 3.379 11.461 1.00 5.39 C
ATOM 51 O VAL A 8 4.664 3.268 10.343 1.00 6.30 O
ATOM 52 CB VAL A 8 3.995 2.354 13.478 1.00 9.64 C
ATOM 53 CG1 VAL A 8 2.716 2.891 12.869 1.00 13.85 C
ATOM 54 CG2 VAL A 8 3.758 1.032 14.208 1.00 11.97 C
ATOM 55 N ALA A 9 5.606 4.546 11.941 1.00 3.73 N
ATOM 56 CA ALA A 9 5.598 5.767 11.082 1.00 3.56 C
ATOM 57 C ALA A 9 6.441 5.527 9.850 1.00 4.13 C
ATOM 58 O ALA A 9 6.052 5.933 8.744 1.00 4.36 O
ATOM 59 CB ALA A 9 6.022 6.977 11.891 1.00 4.80 C
ATOM 60 N ARG A 10 7.647 4.909 10.005 1.00 3.73 N
ATOM 61 CA ARG A 10 8.496 4.609 8.837 1.00 3.38 C
ATOM 62 C ARG A 10 7.798 3.609 7.876 1.00 3.47 C
ATOM 63 O ARG A 10 7.878 3.778 6.651 1.00 4.67 O
ATOM 64 CB ARG A 10 9.847 4.020 9.305 1.00 3.95 C
ATOM 65 CG ARG A 10 10.752 3.607 8.149 1.00 4.55 C
ATOM 66 CD ARG A 10 11.226 4.699 7.244 1.00 5.89 C
ATOM 67 NE ARG A 10 12.143 5.571 8.035 1.00 6.20 N
ATOM 68 CZ ARG A 10 12.758 6.609 7.443 1.00 7.52 C
ATOM 69 NH1 ARG A 10 12.539 6.932 6.158 1.00 10.68 N
ATOM 70 NH2 ARG A 10 13.601 7.322 8.202 1.00 9.48 N
ATOM 71 N SER A 11 7.186 2.582 8.445 1.00 5.19 N
ATOM 72 CA SER A 11 6.500 1.584 7.565 1.00 4.60 C
ATOM 73 C SER A 11 5.382 2.313 6.773 1.00 4.84 C
ATOM 74 O SER A 11 5.213 2.016 5.557 1.00 5.84 O
ATOM 75 CB SER A 11 5.908 0.462 8.400 1.00 5.91 C
ATOM 76 OG SER A 11 6.990 -0.272 9.012 1.00 8.38 O
ATOM 77 N ASN A 12 4.648 3.182 7.446 1.00 3.54 N
ATOM 78 CA ASN A 12 3.545 3.935 6.751 1.00 4.57 C
ATOM 79 C ASN A 12 4.107 4.851 5.691 1.00 4.14 C
ATOM 80 O ASN A 12 3.536 5.001 4.617 1.00 5.52 O
ATOM 81 CB ASN A 12 2.663 4.677 7.748 1.00 6.42 C
ATOM 82 CG ASN A 12 1.802 3.735 8.610 1.00 8.25 C
ATOM 83 OD1 ASN A 12 1.567 2.613 8.165 1.00 12.72 O
ATOM 84 ND2 ASN A 12 1.394 4.252 9.767 1.00 9.92 N
ATOM 85 N PHE A 13 5.259 5.498 6.005 1.00 3.43 N
ATOM 86 CA PHE A 13 5.929 6.358 5.055 1.00 3.49 C
ATOM 87 C PHE A 13 6.304 5.578 3.799 1.00 3.40 C
ATOM 88 O PHE A 13 6.136 6.072 2.653 1.00 4.07 O
ATOM 89 CB PHE A 13 7.183 6.994 5.754 1.00 5.48 C
ATOM 90 CG PHE A 13 7.884 8.006 4.883 1.00 5.57 C
ATOM 91 CD1 PHE A 13 8.906 7.586 4.027 1.00 6.99 C
ATOM 92 CD2 PHE A 13 7.532 9.373 4.983 1.00 6.52 C
ATOM 93 CE1 PHE A 13 9.560 8.539 3.194 1.00 8.20 C
ATOM 94 CE2 PHE A 13 8.176 10.281 4.145 1.00 6.34 C
ATOM 95 CZ PHE A 13 9.141 9.845 3.292 1.00 6.84 C
ATOM 96 N ASN A 14 6.900 4.390 3.989 1.00 3.64 N
ATOM 97 CA ASN A 14 7.331 3.607 2.791 1.00 4.31 C
ATOM 98 C ASN A 14 6.116 3.210 1.915 1.00 3.98 C
ATOM 99 O ASN A 14 6.240 3.144 0.684 1.00 6.22 O
ATOM 100 CB ASN A 14 8.145 2.404 3.240 1.00 5.81 C
ATOM 101 CG ASN A 14 9.555 2.856 3.730 1.00 6.82 C
ATOM 102 OD1 ASN A 14 10.013 3.895 3.323 1.00 9.43 O
ATOM 103 ND2 ASN A 14 10.120 1.956 4.539 1.00 8.21 N
ATOM 104 N VAL A 15 4.993 2.927 2.571 1.00 3.76 N
ATOM 105 CA VAL A 15 3.782 2.599 1.742 1.00 3.98 C
ATOM 106 C VAL A 15 3.296 3.871 1.004 1.00 3.80 C
ATOM 107 O VAL A 15 2.947 3.817 -0.189 1.00 4.85 O
ATOM 108 CB VAL A 15 2.698 1.953 2.608 1.00 4.71 C
ATOM 109 CG1 VAL A 15 1.384 1.826 1.806 1.00 6.67 C
ATOM 110 CG2 VAL A 15 3.174 0.533 3.005 1.00 6.26 C
ATOM 111 N CYS A 16 3.321 4.987 1.720 1.00 3.79 N
ATOM 112 CA CYS A 16 2.890 6.285 1.126 1.00 3.54 C
ATOM 113 C CYS A 16 3.687 6.597 -0.111 1.00 3.48 C
ATOM 114 O CYS A 16 3.200 7.147 -1.103 1.00 4.63 O
ATOM 115 CB CYS A 16 3.039 7.369 2.240 1.00 4.58 C
ATOM 116 SG CYS A 16 2.559 9.014 1.649 1.00 5.66 S
ATOM 117 N ARG A 17 4.997 6.227 -0.100 1.00 3.99 N
ATOM 118 CA ARG A 17 5.895 6.489 -1.213 1.00 3.83 C
ATOM 119 C ARG A 17 5.738 5.560 -2.409 1.00 3.79 C
ATOM 120 O ARG A 17 6.228 5.901 -3.507 1.00 5.39 O
ATOM 121 CB ARG A 17 7.370 6.507 -0.731 1.00 4.11 C
ATOM 122 CG ARG A 17 7.717 7.687 0.206 1.00 4.69 C
ATOM 123 CD ARG A 17 7.949 8.947 -0.615 1.00 5.10 C
ATOM 124 NE ARG A 17 9.212 8.856 -1.337 1.00 4.71 N
ATOM 125 CZ ARG A 17 9.537 9.533 -2.431 1.00 5.28 C
ATOM 126 NH1 ARG A 17 8.659 10.350 -3.032 1.00 6.67 N
ATOM 127 NH2 ARG A 17 10.793 9.491 -2.899 1.00 6.41 N
ATOM 128 N LEU A 18 5.051 4.411 -2.204 1.00 4.70 N
ATOM 129 CA LEU A 18 4.933 3.431 -3.326 1.00 5.46 C
ATOM 130 C LEU A 18 4.397 4.014 -4.620 1.00 5.13 C
ATOM 131 O LEU A 18 4.988 3.755 -5.687 1.00 5.55 O
ATOM 132 CB LEU A 18 4.196 2.184 -2.863 1.00 6.47 C
ATOM 133 CG LEU A 18 4.960 1.178 -1.991 1.00 7.43 C
ATOM 134 CD1 LEU A 18 3.907 0.097 -1.634 1.00 8.70 C
ATOM 135 CD2 LEU A 18 6.129 0.606 -2.768 1.00 9.39 C
ATOM 136 N PRO A 19 3.329 4.795 -4.543 1.00 4.28 N
ATOM 137 CA PRO A 19 2.792 5.376 -5.797 1.00 5.38 C
ATOM 138 C PRO A 19 3.573 6.540 -6.322 1.00 6.30 C
ATOM 139 O PRO A 19 3.260 7.045 -7.422 1.00 9.62 O
ATOM 140 CB PRO A 19 1.358 5.766 -5.472 1.00 5.87 C
ATOM 141 CG PRO A 19 1.223 5.694 -3.993 1.00 6.47 C
ATOM 142 CD PRO A 19 2.421 4.941 -3.408 1.00 6.45 C
ATOM 143 N GLY A 20 4.565 7.047 -5.559 1.00 4.94 N
ATOM 144 CA GLY A 20 5.366 8.191 -6.018 1.00 5.39 C
ATOM 145 C GLY A 20 5.007 9.481 -5.280 1.00 5.03 C
ATOM 146 O GLY A 20 5.535 10.510 -5.730 1.00 7.34 O
ATOM 147 N THR A 21 4.181 9.438 -4.262 1.00 4.10 N
ATOM 148 CA THR A 21 3.767 10.609 -3.513 1.00 3.94 C
ATOM 149 C THR A 21 5.017 11.397 -3.042 1.00 3.96 C
ATOM 150 O THR A 21 5.947 10.757 -2.523 1.00 5.82 O
ATOM 151 CB THR A 21 2.992 10.188 -2.225 1.00 4.13 C
ATOM 152 OG1 THR A 21 2.051 9.144 -2.623 1.00 5.45 O
ATOM 153 CG2 THR A 21 2.260 11.349 -1.551 1.00 5.41 C
ATOM 154 N PRO A 22 4.971 12.703 -3.176 1.00 5.04 N
ATOM 155 CA PRO A 22 6.143 13.513 -2.696 1.00 4.69 C
ATOM 156 C PRO A 22 6.400 13.233 -1.225 1.00 4.19 C
ATOM 157 O PRO A 22 5.485 13.061 -0.382 1.00 4.47 O
ATOM 158 CB PRO A 22 5.703 14.969 -2.920 1.00 7.12 C
ATOM 159 CG PRO A 22 4.676 14.893 -3.996 1.00 7.03 C
ATOM 160 CD PRO A 22 3.964 13.567 -3.811 1.00 4.90 C
ATOM 161 N GLU A 23 7.728 13.297 -0.921 1.00 5.16 N
ATOM 162 CA GLU A 23 8.114 13.103 0.500 1.00 5.31 C
ATOM 163 C GLU A 23 7.427 14.073 1.410 1.00 4.11 C
ATOM 164 O GLU A 23 7.036 13.682 2.540 1.00 5.11 O
ATOM 165 CB GLU A 23 9.648 13.285 0.660 1.00 6.16 C
ATOM 166 CG GLU A 23 10.440 12.093 0.063 1.00 7.48 C
ATOM 167 CD GLU A 23 11.941 12.170 0.391 1.00 9.40 C
ATOM 168 OE1 GLU A 23 12.416 13.225 0.681 1.00 10.40 O
ATOM 169 OE2 GLU A 23 12.539 11.070 0.292 1.00 13.32 O
ATOM 170 N ALA A 24 7.212 15.334 0.966 1.00 4.56 N
ATOM 171 CA ALA A 24 6.614 16.317 1.913 1.00 4.49 C
ATOM 172 C ALA A 24 5.212 15.936 2.350 1.00 4.10 C
ATOM 173 O ALA A 24 4.782 16.166 3.495 1.00 5.64 O
ATOM 174 CB ALA A 24 6.605 17.695 1.246 1.00 5.80 C
ATOM 175 N ILE A 25 4.445 15.318 1.405 1.00 4.37 N
ATOM 176 CA ILE A 25 3.074 14.894 1.756 1.00 5.44 C
ATOM 177 C ILE A 25 3.085 13.643 2.645 1.00 4.32 C
ATOM 178 O ILE A 25 2.315 13.523 3.578 1.00 4.72 O
ATOM 179 CB ILE A 25 2.204 14.637 0.462 1.00 6.42 C
ATOM 180 CG1 ILE A 25 1.815 16.048 -0.129 1.00 7.50 C
ATOM 181 CG2 ILE A 25 0.903 13.864 0.811 1.00 7.65 C
ATOM 182 CD1 ILE A 25 0.756 16.761 0.757 1.00 7.80 C
ATOM 183 N CYS A 26 4.032 12.764 2.313 1.00 3.92 N
ATOM 184 CA CYS A 26 4.180 11.549 3.187 1.00 4.37 C
ATOM 185 C CYS A 26 4.632 11.944 4.596 1.00 3.95 C
ATOM 186 O CYS A 26 4.227 11.252 5.547 1.00 4.74 O
ATOM 187 CB CYS A 26 5.038 10.518 2.539 1.00 4.63 C
ATOM 188 SG CYS A 26 4.349 9.794 1.022 1.00 5.61 S
ATOM 189 N ALA A 27 5.408 13.012 4.694 1.00 3.89 N
ATOM 190 CA ALA A 27 5.879 13.502 6.026 1.00 4.43 C
ATOM 191 C ALA A 27 4.696 13.908 6.882 1.00 4.26 C
ATOM 192 O ALA A 27 4.528 13.422 8.025 1.00 5.44 O
ATOM 193 CB ALA A 27 6.880 14.615 5.830 1.00 5.36 C
ATOM 194 N THR A 28 3.827 14.802 6.358 1.00 4.53 N
ATOM 195 CA THR A 28 2.691 15.221 7.194 1.00 5.08 C
ATOM 196 C THR A 28 1.672 14.132 7.434 1.00 4.62 C
ATOM 197 O THR A 28 0.947 14.112 8.468 1.00 7.80 O
ATOM 198 CB THR A 28 1.986 16.520 6.614 1.00 6.03 C
ATOM 199 OG1 THR A 28 1.664 16.221 5.230 1.00 7.19 O
ATOM 200 CG2 THR A 28 2.914 17.739 6.700 1.00 7.34 C
ATOM 201 N TYR A 29 1.621 13.190 6.511 1.00 5.01 N
ATOM 202 CA TYR A 29 0.715 12.045 6.657 1.00 6.60 C
ATOM 203 C TYR A 29 1.125 11.125 7.815 1.00 4.92 C
ATOM 204 O TYR A 29 0.286 10.632 8.545 1.00 7.13 O
ATOM 205 CB TYR A 29 0.755 11.229 5.322 1.00 9.66 C
ATOM 206 CG TYR A 29 -0.203 10.044 5.354 1.00 11.56 C
ATOM 207 CD1 TYR A 29 -1.547 10.337 5.645 1.00 12.85 C
ATOM 208 CD2 TYR A 29 0.193 8.750 5.100 1.00 14.44 C
ATOM 209 CE1 TYR A 29 -2.496 9.329 5.673 1.00 16.61 C
ATOM 210 CE2 TYR A 29 -0.801 7.705 5.156 1.00 17.11 C
ATOM 211 CZ TYR A 29 -2.079 8.031 5.430 1.00 19.99 C
ATOM 212 OH TYR A 29 -3.097 7.057 5.458 1.00 28.98 O
ATOM 213 N THR A 30 2.470 10.984 7.995 1.00 5.31 N
ATOM 214 CA THR A 30 2.986 9.994 8.950 1.00 5.70 C
ATOM 215 C THR A 30 3.609 10.505 10.230 1.00 6.28 C
ATOM 216 O THR A 30 3.766 9.715 11.186 1.00 8.77 O
ATOM 217 CB THR A 30 4.076 9.103 8.225 1.00 6.55 C
ATOM 218 OG1 THR A 30 5.125 10.027 7.824 1.00 6.57 O
ATOM 219 CG2 THR A 30 3.493 8.324 7.035 1.00 7.29 C
ATOM 220 N GLY A 31 3.984 11.764 10.241 1.00 4.99 N
ATOM 221 CA GLY A 31 4.769 12.336 11.360 1.00 5.50 C
ATOM 222 C GLY A 31 6.255 12.243 11.106 1.00 4.19 C
ATOM 223 O GLY A 31 7.037 12.750 11.954 1.00 6.12 O
ATOM 224 N CYS A 32 6.710 11.631 9.992 1.00 4.30 N
ATOM 225 CA CYS A 32 8.140 11.694 9.635 1.00 4.89 C
ATOM 226 C CYS A 32 8.500 13.141 9.206 1.00 5.50 C
ATOM 227 O CYS A 32 7.581 13.949 8.944 1.00 5.82 O
ATOM 228 CB CYS A 32 8.504 10.686 8.530 1.00 4.66 C
ATOM 229 SG CYS A 32 8.048 8.987 8.881 1.00 5.33 S
ATOM 230 N ILE A 33 9.793 13.410 9.173 1.00 6.02 N
ATOM 231 CA ILE A 33 10.280 14.760 8.823 1.00 5.24 C
ATOM 232 C ILE A 33 11.346 14.658 7.743 1.00 5.16 C
ATOM 233 O ILE A 33 11.971 13.583 7.552 1.00 7.19 O
ATOM 234 CB ILE A 33 10.790 15.535 10.085 1.00 5.49 C
ATOM 235 CG1 ILE A 33 12.059 14.803 10.671 1.00 6.85 C
ATOM 236 CG2 ILE A 33 9.684 15.686 11.138 1.00 6.45 C
ATOM 237 CD1 ILE A 33 12.733 15.676 11.781 1.00 8.94 C
ATOM 238 N ILE A 34 11.490 15.773 7.038 1.00 5.52 N
ATOM 239 CA ILE A 34 12.552 15.877 6.036 1.00 6.82 C
ATOM 240 C ILE A 34 13.590 16.917 6.560 1.00 6.92 C
ATOM 241 O ILE A 34 13.168 18.006 6.945 1.00 9.22 O
ATOM 242 CB ILE A 34 11.987 16.360 4.681 1.00 8.11 C
ATOM 243 CG1 ILE A 34 10.914 15.338 4.163 1.00 9.59 C
ATOM 244 CG2 ILE A 34 13.131 16.517 3.629 1.00 9.73 C
ATOM 245 CD1 ILE A 34 10.151 16.024 2.938 1.00 13.41 C
ATOM 246 N ILE A 35 14.856 16.493 6.536 1.00 7.06 N
ATOM 247 CA ILE A 35 15.930 17.454 6.941 1.00 7.52 C
ATOM 248 C ILE A 35 16.913 17.550 5.819 1.00 6.63 C
ATOM 249 O ILE A 35 17.097 16.660 4.970 1.00 7.90 O
ATOM 250 CB ILE A 35 16.622 16.995 8.285 1.00 8.07 C
ATOM 251 CG1 ILE A 35 17.360 15.651 8.067 1.00 9.41 C
ATOM 252 CG2 ILE A 35 15.592 16.974 9.434 1.00 9.46 C
ATOM 253 CD1 ILE A 35 18.298 15.206 9.219 1.00 9.85 C
ATOM 254 N PRO A 36 17.664 18.669 5.806 1.00 8.07 N
ATOM 255 CA PRO A 36 18.635 18.861 4.738 1.00 8.78 C
ATOM 256 C PRO A 36 19.925 18.042 4.949 1.00 8.31 C
ATOM 257 O PRO A 36 20.593 17.742 3.945 1.00 9.09 O
ATOM 258 CB PRO A 36 18.945 20.364 4.783 1.00 9.67 C
ATOM 259 CG PRO A 36 18.238 20.937 5.908 1.00 10.15 C
ATOM 260 CD PRO A 36 17.371 19.900 6.596 1.00 9.53 C
ATOM 261 N GLY A 37 20.172 17.730 6.217 1.00 8.48 N
ATOM 262 CA GLY A 37 21.452 16.969 6.513 1.00 9.20 C
ATOM 263 C GLY A 37 21.143 15.478 6.427 1.00 10.41 C
ATOM 264 O GLY A 37 20.138 15.023 5.878 1.00 12.06 O
ATOM 265 N ALA A 38 22.055 14.701 7.032 1.00 9.24 N
ATOM 266 CA ALA A 38 22.019 13.242 7.020 1.00 9.24 C
ATOM 267 C ALA A 38 21.944 12.628 8.396 1.00 9.60 C
ATOM 268 O ALA A 38 21.869 11.387 8.435 1.00 13.65 O
ATOM 269 CB ALA A 38 23.246 12.697 6.275 1.00 10.43 C
ATOM 270 N THR A 39 21.894 13.435 9.436 1.00 8.70 N
ATOM 271 CA THR A 39 21.936 12.911 10.809 1.00 9.46 C
ATOM 272 C THR A 39 20.615 13.191 11.521 1.00 8.32 C
ATOM 273 O THR A 39 20.357 14.317 11.948 1.00 9.89 O
ATOM 274 CB THR A 39 23.131 13.601 11.593 1.00 10.72 C
ATOM 275 OG1 THR A 39 24.284 13.401 10.709 1.00 11.66 O
ATOM 276 CG2 THR A 39 23.340 12.935 12.962 1.00 11.81 C
ATOM 277 N CYS A 40 19.827 12.110 11.642 1.00 7.64 N
ATOM 278 CA CYS A 40 18.504 12.312 12.298 1.00 8.05 C
ATOM 279 C CYS A 40 18.684 12.451 13.784 1.00 7.63 C
ATOM 280 O CYS A 40 19.533 11.718 14.362 1.00 9.64 O
ATOM 281 CB CYS A 40 17.582 11.117 11.996 1.00 7.80 C
ATOM 282 SG CYS A 40 17.199 10.929 10.237 1.00 7.30 S
ATOM 283 N PRO A 41 17.880 13.266 14.426 1.00 8.00 N
ATOM 284 CA PRO A 41 17.924 13.421 15.877 1.00 8.96 C
ATOM 285 C PRO A 41 17.392 12.206 16.594 1.00 9.06 C
ATOM 286 O PRO A 41 16.652 11.368 16.033 1.00 8.82 O
ATOM 287 CB PRO A 41 17.076 14.658 16.145 1.00 10.39 C
ATOM 288 CG PRO A 41 16.098 14.689 14.997 1.00 10.99 C
ATOM 289 CD PRO A 41 16.859 14.150 13.779 1.00 10.49 C
ATOM 290 N GLY A 42 17.728 12.124 17.884 1.00 7.55 N
ATOM 291 CA GLY A 42 17.334 10.956 18.691 1.00 8.00 C
ATOM 292 C GLY A 42 15.875 10.688 18.871 1.00 7.22 C
ATOM 293 O GLY A 42 15.434 9.550 19.166 1.00 8.41 O
ATOM 294 N ASP A 43 15.036 11.747 18.715 1.00 5.54 N
ATOM 295 CA ASP A 43 13.564 11.573 18.836 1.00 5.85 C
ATOM 296 C ASP A 43 12.936 11.227 17.470 1.00 5.87 C
ATOM 297 O ASP A 43 11.720 11.040 17.428 1.00 7.29 O
ATOM 298 CB ASP A 43 12.933 12.737 19.580 1.00 6.72 C
ATOM 299 CG ASP A 43 13.140 14.094 18.958 1.00 8.59 C
ATOM 300 OD1 ASP A 43 14.109 14.303 18.212 1.00 9.59 O
ATOM 301 OD2 ASP A 43 12.267 14.963 19.265 1.00 11.45 O
ATOM 302 N TYR A 44 13.725 11.174 16.425 1.00 5.22 N
ATOM 303 CA TYR A 44 13.257 10.745 15.081 1.00 5.56 C
ATOM 304 C TYR A 44 14.275 9.687 14.612 1.00 4.61 C
ATOM 305 O TYR A 44 14.930 9.862 13.568 1.00 6.04 O
ATOM 306 CB TYR A 44 13.200 11.914 14.071 1.00 5.41 C
ATOM 307 CG TYR A 44 12.000 12.819 14.399 1.00 5.34 C
ATOM 308 CD1 TYR A 44 12.119 13.853 15.332 1.00 6.59 C
ATOM 309 CD2 TYR A 44 10.775 12.617 13.762 1.00 5.94 C
ATOM 310 CE1 TYR A 44 11.045 14.675 15.610 1.00 5.97 C
ATOM 311 CE2 TYR A 44 9.676 13.433 14.048 1.00 5.17 C
ATOM 312 CZ TYR A 44 9.802 14.456 14.996 1.00 5.96 C
ATOM 313 OH TYR A 44 8.740 15.265 15.269 1.00 8.60 O
ATOM 314 N ALA A 45 14.342 8.640 15.422 1.00 4.76 N
ATOM 315 CA ALA A 45 15.445 7.667 15.246 1.00 5.89 C
ATOM 316 C ALA A 45 15.171 6.533 14.280 1.00 6.67 C
ATOM 317 O ALA A 45 16.093 5.705 14.039 1.00 7.56 O
ATOM 318 CB ALA A 45 15.680 7.099 16.682 1.00 6.82 C
ATOM 319 N ASN A 46 13.966 6.502 13.739 1.00 5.80 N
ATOM 320 CA ASN A 46 13.512 5.395 12.878 1.00 6.15 C
ATOM 321 C ASN A 46 13.311 5.853 11.455 1.00 6.61 C
ATOM 322 O ASN A 46 13.733 6.929 11.026 1.00 7.18 O
ATOM 323 CB ASN A 46 12.266 4.769 13.501 1.00 7.27 C
ATOM 324 CG ASN A 46 12.538 4.304 14.922 1.00 7.98 C
ATOM 325 OD1 ASN A 46 11.982 4.849 15.886 1.00 11.00 O
ATOM 326 ND2 ASN A 46 13.407 3.298 15.015 1.00 10.32 N
ATOM 327 OXT ASN A 46 12.703 4.973 10.746 1.00 7.86 O
TER 328 ASN A 46
CONECT 20 282
CONECT 26 229
CONECT 116 188
CONECT 188 116
CONECT 229 26
CONECT 282 20
MASTER 225 0 0 2 2 0 0 6 327 1 6 4
END