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1818 lines (1818 loc) · 144 KB
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HEADER OXYGEN STORAGE 05-APR-73 1MBN
TITLE THE STEREOCHEMISTRY OF THE PROTEIN MYOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOGLOBIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;
SOURCE 3 ORGANISM_COMMON: SPERM WHALE;
SOURCE 4 ORGANISM_TAXID: 9755
KEYWDS OXYGEN STORAGE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.C.WATSON,J.C.KENDREW
REVDAT 23 14-FEB-24 1MBN 1 REMARK
REVDAT 22 29-NOV-17 1MBN 1 HELIX
REVDAT 21 24-FEB-09 1MBN 1 VERSN
REVDAT 20 27-OCT-83 1MBN 1 REMARK
REVDAT 19 30-SEP-83 1MBN 1 REVDAT
REVDAT 18 12-MAY-83 1MBN 3 REMARK SEQRES ATOM
REVDAT 17 07-MAR-83 1MBN 3 ATOM
REVDAT 16 15-JAN-82 1MBN 1 REMARK
REVDAT 15 15-JUL-81 1MBN 1 REMARK SITE
REVDAT 14 31-DEC-80 1MBN 1 SOURCE REMARK
REVDAT 13 07-APR-80 1MBN 3 ATOM
REVDAT 12 06-FEB-79 1MBN 1 TURN
REVDAT 11 15-JAN-79 1MBN 3 HETATM
REVDAT 10 20-JUL-78 1MBN 2 CONECT
REVDAT 9 24-JAN-78 1MBN 1 HEADER
REVDAT 8 01-NOV-77 1MBN 1 AUTHOR JRNL REMARK FORMUL
REVDAT 7 09-SEP-77 1MBN 1 REMARK
REVDAT 6 23-AUG-77 1MBN 3 HETATM CONECT
REVDAT 5 13-JUN-77 1MBN 1 FTNOTE HET
REVDAT 4 28-MAR-77 1MBN 1 REMARK
REVDAT 3 20-SEP-76 1MBN 2 CONECT
REVDAT 2 28-JUN-76 1MBN 1 HEADER
REVDAT 1 19-MAY-76 1MBN 0
JRNL AUTH H.C.WATSON
JRNL TITL THE STEREOCHEMISTRY OF THE PROTEIN MYOGLOBIN
JRNL REF PROG.STEREOCHEM. V. 4 299 1969
JRNL REFN ISSN 0079-6808
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.C.KENDREW
REMARK 1 TITL MYOGLOBIN AND THE STRUCTURE OF PROTEINS (NOBEL LECTURE,
REMARK 1 TITL 2 DECEMBER 11, 1962)
REMARK 1 REF PRIX NOBEL 103 1963
REMARK 1 REFN ISSN 0546-8175
REMARK 1 REFERENCE 2
REMARK 1 EDIT R.J.FELDMANN
REMARK 1 REF ATLAS OF MACROMOLECULAR 125 1976
REMARK 1 REF 2 STRUCTURE ON MICROFICHE
REMARK 1 PUBL TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 84 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. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 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 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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MBN 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_1000174928.
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 (%): 36.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
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 15.45000
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 78 OE1 GLU A 85 1.81
REMARK 500 NZ LYS A 145 OE1 GLU A 148 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ALA A 19 NZ LYS A 63 2646 1.01
REMARK 500 CB HIS A 48 NZ LYS A 56 2655 1.64
REMARK 500 C ALA A 19 NZ LYS A 63 2646 2.03
REMARK 500 CG HIS A 48 NZ LYS A 56 2655 2.14
REMARK 500 O ALA A 19 CE LYS A 63 2646 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 4 CG GLU A 4 CD 0.125
REMARK 500 GLU A 4 CD GLU A 4 OE2 -0.152
REMARK 500 GLU A 6 CD GLU A 6 OE1 -0.094
REMARK 500 TRP A 14 NE1 TRP A 14 CE2 -0.159
REMARK 500 TRP A 14 CE2 TRP A 14 CZ2 0.104
REMARK 500 TRP A 14 CE2 TRP A 14 CD2 -0.075
REMARK 500 GLU A 18 CG GLU A 18 CD 0.094
REMARK 500 GLU A 18 CD GLU A 18 OE2 -0.094
REMARK 500 ARG A 31 NE ARG A 31 CZ 0.081
REMARK 500 SER A 35 CB SER A 35 OG 0.085
REMARK 500 PRO A 37 CD PRO A 37 N -0.118
REMARK 500 GLU A 38 CG GLU A 38 CD 0.091
REMARK 500 GLU A 41 CG GLU A 41 CD 0.101
REMARK 500 PHE A 46 C PHE A 46 O 0.120
REMARK 500 HIS A 48 CG HIS A 48 CD2 0.060
REMARK 500 GLU A 52 CD GLU A 52 OE2 -0.116
REMARK 500 GLU A 85 CD GLU A 85 OE2 -0.077
REMARK 500 ILE A 99 C ILE A 99 O 0.120
REMARK 500 TYR A 103 CE1 TYR A 103 CZ -0.093
REMARK 500 TYR A 103 CZ TYR A 103 CE2 0.116
REMARK 500 GLU A 105 CG GLU A 105 CD 0.110
REMARK 500 GLU A 105 CD GLU A 105 OE2 -0.130
REMARK 500 GLU A 105 C GLU A 105 O 0.146
REMARK 500 PHE A 106 CG PHE A 106 CD1 -0.098
REMARK 500 HIS A 113 CG HIS A 113 CD2 0.074
REMARK 500 ASP A 122 CG ASP A 122 OD1 0.179
REMARK 500 MET A 131 C MET A 131 O 0.120
REMARK 500 ASN A 132 CG ASN A 132 OD1 0.241
REMARK 500 GLU A 136 CD GLU A 136 OE2 -0.094
REMARK 500 ARG A 139 NE ARG A 139 CZ 0.120
REMARK 500 ARG A 139 CZ ARG A 139 NH1 -0.089
REMARK 500 GLY A 150 C GLY A 150 O 0.124
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER A 3 CB - CA - C ANGL. DEV. = -21.1 DEGREES
REMARK 500 SER A 3 N - CA - CB ANGL. DEV. = 15.1 DEGREES
REMARK 500 SER A 3 N - CA - C ANGL. DEV. = 19.4 DEGREES
REMARK 500 GLU A 4 N - CA - CB ANGL. DEV. = 25.1 DEGREES
REMARK 500 GLU A 4 OE1 - CD - OE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 GLN A 8 N - CA - CB ANGL. DEV. = 21.2 DEGREES
REMARK 500 LEU A 9 CB - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 VAL A 10 N - CA - CB ANGL. DEV. = 20.9 DEGREES
REMARK 500 VAL A 13 N - CA - CB ANGL. DEV. = 25.6 DEGREES
REMARK 500 TRP A 14 CB - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 TRP A 14 CG - CD2 - CE3 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 14 CD2 - CE3 - CZ3 ANGL. DEV. = -9.4 DEGREES
REMARK 500 TRP A 14 CE3 - CZ3 - CH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP A 14 CH2 - CZ2 - CE2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ALA A 15 CB - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA A 15 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 LYS A 16 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 VAL A 17 CB - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 GLU A 18 OE1 - CD - OE2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ALA A 22 CB - CA - C ANGL. DEV. = 21.9 DEGREES
REMARK 500 ALA A 22 N - CA - CB ANGL. DEV. = -17.4 DEGREES
REMARK 500 HIS A 24 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 GLN A 26 CB - CA - C ANGL. DEV. = 19.3 DEGREES
REMARK 500 ASP A 27 CB - CA - C ANGL. DEV. = 20.4 DEGREES
REMARK 500 ASP A 27 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 ASP A 27 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 LEU A 29 CB - CA - C ANGL. DEV. = 18.5 DEGREES
REMARK 500 ILE A 30 CB - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 PHE A 33 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 HIS A 36 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 PRO A 37 CB - CA - C ANGL. DEV. = 14.2 DEGREES
REMARK 500 GLU A 38 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 LEU A 40 CB - CA - C ANGL. DEV. = -14.9 DEGREES
REMARK 500 GLU A 41 OE1 - CD - OE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 LYS A 42 CB - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 PHE A 43 N - CA - CB ANGL. DEV. = -16.8 DEGREES
REMARK 500 ASP A 44 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 45 N - CA - CB ANGL. DEV. = 16.4 DEGREES
REMARK 500 LYS A 47 N - CA - CB ANGL. DEV. = 15.3 DEGREES
REMARK 500 LYS A 50 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 GLU A 52 CB - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 ALA A 53 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 LYS A 56 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 ALA A 57 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 ALA A 57 N - CA - CB ANGL. DEV. = 13.6 DEGREES
REMARK 500 SER A 58 CB - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 GLU A 59 OE1 - CD - OE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 60 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 113 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 3 150.06 -49.57
REMARK 500 ALA A 15 -35.44 -39.68
REMARK 500 ASP A 27 -75.10 -39.32
REMARK 500 LEU A 49 109.62 -50.79
REMARK 500 LYS A 62 -76.57 -41.69
REMARK 500 LEU A 76 -70.64 -48.91
REMARK 500 LYS A 77 -23.21 -39.01
REMARK 500 LYS A 79 47.57 38.43
REMARK 500 HIS A 81 57.68 -91.01
REMARK 500 LYS A 87 -71.82 -44.80
REMARK 500 LYS A 96 -62.54 -137.99
REMARK 500 PHE A 106 -73.07 -44.55
REMARK 500 GLU A 109 -71.45 -67.32
REMARK 500 SER A 117 -52.98 -29.18
REMARK 500 LYS A 147 -70.97 -40.90
REMARK 500 GLU A 148 -61.93 -27.00
REMARK 500 GLN A 152 77.69 87.52
REMARK 500
REMARK 500 REMARK: NULL
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 HEM A 155 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 HEM A 155 NA 92.1
REMARK 620 3 HEM A 155 NB 92.1 89.3
REMARK 620 4 HEM A 155 NC 100.8 167.1 89.1
REMARK 620 5 HEM A 155 ND 102.2 88.4 165.6 90.0
REMARK 620 6 OH A 154 O 167.9 99.8 90.4 67.5 76.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: HMB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEM BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 155
DBREF 1MBN A 1 153 UNP P02185 MYG_PHYCA 1 153
SEQRES 1 A 153 VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS VAL
SEQRES 2 A 153 TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN
SEQRES 3 A 153 ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU THR
SEQRES 4 A 153 LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR GLU
SEQRES 5 A 153 ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY
SEQRES 6 A 153 VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS LYS
SEQRES 7 A 153 LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN
SEQRES 8 A 153 SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU
SEQRES 9 A 153 GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SER
SEQRES 10 A 153 ARG HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA
SEQRES 11 A 153 MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE ALA
SEQRES 12 A 153 ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY
HET OH A 154 1
HET HEM A 155 43
HETNAM OH HYDROXIDE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 OH H O 1-
FORMUL 3 HEM C34 H32 FE N4 O4
HELIX 1 A SER A 3 GLU A 18 1N=3.63,PHI=1.73,H=1.50 16
HELIX 2 B ASP A 20 SER A 35 1N=3.72,PHI=1.69,H=1.47 16
HELIX 3 C HIS A 36 LYS A 42 1SHORT IRREGULAR HELIX 7
HELIX 4 D THR A 51 ALA A 57 1N=3.63,PHI=1.73,H=1.45 7
HELIX 5 E SER A 58 LYS A 77 1BENT ABOUT 7 DEG. AT THR (67) 20
HELIX 6 F LEU A 86 ALA A 94 1N=3.70,PHI=1.70,H=1.46 9
HELIX 7 G PRO A 100 ARG A 118 1N=3.59,PHI=1.75,H=1.53 19
HELIX 8 H ALA A 125 GLU A 148 1N=3.63,PHI=1.73,H=1.49 24
LINK NE2 HIS A 93 FE HEM A 155 1555 1555 2.19
LINK O OH A 154 FE HEM A 155 1555 1555 2.15
SITE 1 HMB 9 PHE A 43 ARG A 45 HIS A 64 VAL A 68
SITE 2 HMB 9 ALA A 71 HIS A 93 HIS A 97 LEU A 104
SITE 3 HMB 9 ILE A 107
SITE 1 AC1 3 PHE A 43 HIS A 64 HEM A 155
SITE 1 AC2 10 PHE A 43 ARG A 45 LEU A 89 SER A 92
SITE 2 AC2 10 HIS A 93 HIS A 97 ILE A 99 TYR A 103
SITE 3 AC2 10 PHE A 138 OH A 154
CRYST1 64.500 30.900 34.700 90.00 106.00 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 0.015504 0.000000 0.004446 0.00000
SCALE2 0.000000 0.032362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029980 0.00000
ATOM 1 N VAL A 1 -2.900 17.600 15.500 1.00 0.00 N
ATOM 2 CA VAL A 1 -3.600 16.400 15.300 1.00 0.00 C
ATOM 3 C VAL A 1 -3.000 15.300 16.200 1.00 0.00 C
ATOM 4 O VAL A 1 -3.700 14.700 17.000 1.00 0.00 O
ATOM 5 CB VAL A 1 -3.500 16.000 13.800 1.00 0.00 C
ATOM 6 CG1 VAL A 1 -2.100 15.700 13.300 1.00 0.00 C
ATOM 7 CG2 VAL A 1 -4.600 14.900 13.400 1.00 0.00 C
ATOM 8 N LEU A 2 -1.700 15.100 16.000 1.00 0.00 N
ATOM 9 CA LEU A 2 -0.900 14.100 16.700 1.00 0.00 C
ATOM 10 C LEU A 2 -1.000 13.900 18.300 1.00 0.00 C
ATOM 11 O LEU A 2 -0.900 14.900 19.000 1.00 0.00 O
ATOM 12 CB LEU A 2 0.600 14.200 16.500 1.00 0.00 C
ATOM 13 CG LEU A 2 1.100 14.300 15.100 1.00 0.00 C
ATOM 14 CD1 LEU A 2 0.400 15.500 14.400 1.00 0.00 C
ATOM 15 CD2 LEU A 2 2.600 14.400 15.000 1.00 0.00 C
ATOM 16 N SER A 3 -1.100 12.600 18.600 1.00 0.00 N
ATOM 17 CA SER A 3 -1.100 12.200 20.000 1.00 0.00 C
ATOM 18 C SER A 3 -0.100 12.600 21.200 1.00 0.00 C
ATOM 19 O SER A 3 1.100 12.800 20.900 1.00 0.00 O
ATOM 20 CB SER A 3 -1.100 10.800 20.500 1.00 0.00 C
ATOM 21 OG SER A 3 0.200 10.100 20.300 1.00 0.00 O
ATOM 22 N GLU A 4 -0.700 12.600 22.400 1.00 0.00 N
ATOM 23 CA GLU A 4 0.000 12.900 23.600 1.00 0.00 C
ATOM 24 C GLU A 4 1.300 12.100 23.500 1.00 0.00 C
ATOM 25 O GLU A 4 2.400 12.600 23.600 1.00 0.00 O
ATOM 26 CB GLU A 4 -0.300 12.800 25.100 1.00 0.00 C
ATOM 27 CG GLU A 4 0.000 14.000 26.000 1.00 0.00 C
ATOM 28 CD GLU A 4 0.300 15.400 25.200 1.00 0.00 C
ATOM 29 OE1 GLU A 4 -0.600 15.500 24.300 1.00 0.00 O
ATOM 30 OE2 GLU A 4 1.200 16.000 25.400 1.00 0.00 O
ATOM 31 N GLY A 5 1.100 10.800 23.400 1.00 0.00 N
ATOM 32 CA GLY A 5 2.200 9.800 23.300 1.00 0.00 C
ATOM 33 C GLY A 5 3.200 10.200 22.200 1.00 0.00 C
ATOM 34 O GLY A 5 4.400 10.300 22.500 1.00 0.00 O
ATOM 35 N GLU A 6 2.700 10.400 21.000 1.00 0.00 N
ATOM 36 CA GLU A 6 3.500 10.700 19.800 1.00 0.00 C
ATOM 37 C GLU A 6 4.400 11.900 19.900 1.00 0.00 C
ATOM 38 O GLU A 6 5.500 11.900 19.400 1.00 0.00 O
ATOM 39 CB GLU A 6 2.600 10.700 18.600 1.00 0.00 C
ATOM 40 CG GLU A 6 2.000 9.400 18.100 1.00 0.00 C
ATOM 41 CD GLU A 6 0.900 9.500 17.000 1.00 0.00 C
ATOM 42 OE1 GLU A 6 0.700 10.600 16.700 1.00 0.00 O
ATOM 43 OE2 GLU A 6 0.400 8.500 16.600 1.00 0.00 O
ATOM 44 N TRP A 7 3.800 13.000 20.600 1.00 0.00 N
ATOM 45 CA TRP A 7 4.500 14.200 20.800 1.00 0.00 C
ATOM 46 C TRP A 7 5.700 13.700 21.700 1.00 0.00 C
ATOM 47 O TRP A 7 6.900 14.000 21.400 1.00 0.00 O
ATOM 48 CB TRP A 7 3.700 15.400 21.300 1.00 0.00 C
ATOM 49 CG TRP A 7 2.800 16.100 20.200 1.00 0.00 C
ATOM 50 CD1 TRP A 7 1.500 16.200 20.100 1.00 0.00 C
ATOM 51 CD2 TRP A 7 3.300 16.800 19.100 1.00 0.00 C
ATOM 52 NE1 TRP A 7 1.100 16.900 18.900 1.00 0.00 N
ATOM 53 CE2 TRP A 7 2.200 17.300 18.300 1.00 0.00 C
ATOM 54 CE3 TRP A 7 4.600 17.100 18.600 1.00 0.00 C
ATOM 55 CZ2 TRP A 7 2.300 18.100 17.200 1.00 0.00 C
ATOM 56 CZ3 TRP A 7 4.700 17.900 17.500 1.00 0.00 C
ATOM 57 CH2 TRP A 7 3.600 18.400 16.800 1.00 0.00 C
ATOM 58 N GLN A 8 5.400 12.900 22.700 1.00 0.00 N
ATOM 59 CA GLN A 8 6.300 12.300 23.600 1.00 0.00 C
ATOM 60 C GLN A 8 7.600 11.900 22.900 1.00 0.00 C
ATOM 61 O GLN A 8 8.700 12.300 23.200 1.00 0.00 O
ATOM 62 CB GLN A 8 6.300 12.200 25.100 1.00 0.00 C
ATOM 63 CG GLN A 8 7.600 12.200 25.700 1.00 0.00 C
ATOM 64 CD GLN A 8 7.700 12.200 27.200 1.00 0.00 C
ATOM 65 OE1 GLN A 8 8.800 11.900 27.800 1.00 0.00 O
ATOM 66 NE2 GLN A 8 6.600 12.500 27.800 1.00 0.00 N
ATOM 67 N LEU A 9 7.400 11.000 21.900 1.00 0.00 N
ATOM 68 CA LEU A 9 8.400 10.400 21.100 1.00 0.00 C
ATOM 69 C LEU A 9 9.100 11.400 20.300 1.00 0.00 C
ATOM 70 O LEU A 9 10.400 11.500 20.200 1.00 0.00 O
ATOM 71 CB LEU A 9 7.900 9.600 19.900 1.00 0.00 C
ATOM 72 CG LEU A 9 7.900 8.100 19.900 1.00 0.00 C
ATOM 73 CD1 LEU A 9 8.200 7.700 21.400 1.00 0.00 C
ATOM 74 CD2 LEU A 9 6.600 7.600 19.500 1.00 0.00 C
ATOM 75 N VAL A 10 8.300 12.200 19.600 1.00 0.00 N
ATOM 76 CA VAL A 10 8.800 13.300 18.700 1.00 0.00 C
ATOM 77 C VAL A 10 9.800 14.200 19.500 1.00 0.00 C
ATOM 78 O VAL A 10 10.900 14.500 19.000 1.00 0.00 O
ATOM 79 CB VAL A 10 8.100 14.200 17.700 1.00 0.00 C
ATOM 80 CG1 VAL A 10 8.900 15.400 17.300 1.00 0.00 C
ATOM 81 CG2 VAL A 10 7.600 13.400 16.500 1.00 0.00 C
ATOM 82 N LEU A 11 9.400 14.500 20.700 1.00 0.00 N
ATOM 83 CA LEU A 11 10.200 15.400 21.600 1.00 0.00 C
ATOM 84 C LEU A 11 11.600 15.000 22.200 1.00 0.00 C
ATOM 85 O LEU A 11 12.500 15.800 22.300 1.00 0.00 O
ATOM 86 CB LEU A 11 9.500 16.300 22.500 1.00 0.00 C
ATOM 87 CG LEU A 11 8.700 17.400 21.900 1.00 0.00 C
ATOM 88 CD1 LEU A 11 7.700 18.000 22.900 1.00 0.00 C
ATOM 89 CD2 LEU A 11 9.600 18.500 21.400 1.00 0.00 C
ATOM 90 N HIS A 12 11.600 13.700 22.600 1.00 0.00 N
ATOM 91 CA HIS A 12 12.800 13.100 23.200 1.00 0.00 C
ATOM 92 C HIS A 12 13.900 13.000 22.200 1.00 0.00 C
ATOM 93 O HIS A 12 15.100 13.200 22.600 1.00 0.00 O
ATOM 94 CB HIS A 12 12.300 11.700 23.500 1.00 0.00 C
ATOM 95 CG HIS A 12 13.400 10.800 24.000 1.00 0.00 C
ATOM 96 ND1 HIS A 12 14.000 10.900 25.300 1.00 0.00 N
ATOM 97 CD2 HIS A 12 14.000 9.700 23.400 1.00 0.00 C
ATOM 98 CE1 HIS A 12 14.900 9.900 25.400 1.00 0.00 C
ATOM 99 NE2 HIS A 12 15.000 9.200 24.300 1.00 0.00 N
ATOM 100 N VAL A 13 13.600 12.700 21.000 1.00 0.00 N
ATOM 101 CA VAL A 13 14.500 12.600 19.800 1.00 0.00 C
ATOM 102 C VAL A 13 15.100 14.000 19.600 1.00 0.00 C
ATOM 103 O VAL A 13 16.300 14.200 19.400 1.00 0.00 O
ATOM 104 CB VAL A 13 14.400 12.100 18.400 1.00 0.00 C
ATOM 105 CG1 VAL A 13 15.800 11.900 17.700 1.00 0.00 C
ATOM 106 CG2 VAL A 13 13.500 10.900 18.300 1.00 0.00 C
ATOM 107 N TRP A 14 14.200 15.000 19.700 1.00 0.00 N
ATOM 108 CA TRP A 14 14.600 16.400 19.600 1.00 0.00 C
ATOM 109 C TRP A 14 15.700 16.700 20.500 1.00 0.00 C
ATOM 110 O TRP A 14 16.800 17.000 20.100 1.00 0.00 O
ATOM 111 CB TRP A 14 13.400 17.400 19.200 1.00 0.00 C
ATOM 112 CG TRP A 14 13.900 18.800 18.700 1.00 0.00 C
ATOM 113 CD1 TRP A 14 14.000 19.900 19.400 1.00 0.00 C
ATOM 114 CD2 TRP A 14 14.200 19.200 17.400 1.00 0.00 C
ATOM 115 NE1 TRP A 14 14.400 21.000 18.500 1.00 0.00 N
ATOM 116 CE2 TRP A 14 14.500 20.500 17.400 1.00 0.00 C
ATOM 117 CE3 TRP A 14 14.200 18.400 16.200 1.00 0.00 C
ATOM 118 CZ2 TRP A 14 14.900 21.300 16.200 1.00 0.00 C
ATOM 119 CZ3 TRP A 14 14.600 19.200 15.100 1.00 0.00 C
ATOM 120 CH2 TRP A 14 15.000 20.500 15.100 1.00 0.00 C
ATOM 121 N ALA A 15 15.400 16.600 21.800 1.00 0.00 N
ATOM 122 CA ALA A 15 16.300 16.800 22.900 1.00 0.00 C
ATOM 123 C ALA A 15 17.700 16.200 22.600 1.00 0.00 C
ATOM 124 O ALA A 15 18.800 16.800 23.000 1.00 0.00 O
ATOM 125 CB ALA A 15 16.100 16.000 24.200 1.00 0.00 C
ATOM 126 N LYS A 16 17.700 15.100 21.900 1.00 0.00 N
ATOM 127 CA LYS A 16 18.900 14.400 21.500 1.00 0.00 C
ATOM 128 C LYS A 16 19.600 15.100 20.400 1.00 0.00 C
ATOM 129 O LYS A 16 20.900 15.300 20.400 1.00 0.00 O
ATOM 130 CB LYS A 16 18.300 13.000 21.300 1.00 0.00 C
ATOM 131 CG LYS A 16 18.400 12.100 22.500 1.00 0.00 C
ATOM 132 CD LYS A 16 17.800 10.700 22.300 1.00 0.00 C
ATOM 133 CE LYS A 16 17.600 9.900 23.500 1.00 0.00 C
ATOM 134 NZ LYS A 16 17.000 8.600 23.300 1.00 0.00 N
ATOM 135 N VAL A 17 18.800 15.500 19.400 1.00 0.00 N
ATOM 136 CA VAL A 17 19.300 16.300 18.200 1.00 0.00 C
ATOM 137 C VAL A 17 19.900 17.600 18.700 1.00 0.00 C
ATOM 138 O VAL A 17 20.900 18.100 18.100 1.00 0.00 O
ATOM 139 CB VAL A 17 18.200 17.000 17.500 1.00 0.00 C
ATOM 140 CG1 VAL A 17 18.700 18.100 16.500 1.00 0.00 C
ATOM 141 CG2 VAL A 17 17.300 16.000 16.800 1.00 0.00 C
ATOM 142 N GLU A 18 19.400 18.100 19.800 1.00 0.00 N
ATOM 143 CA GLU A 18 19.800 19.300 20.500 1.00 0.00 C
ATOM 144 C GLU A 18 21.200 19.200 21.100 1.00 0.00 C
ATOM 145 O GLU A 18 21.800 20.200 21.500 1.00 0.00 O
ATOM 146 CB GLU A 18 18.800 19.900 21.400 1.00 0.00 C
ATOM 147 CG GLU A 18 18.500 21.400 21.200 1.00 0.00 C
ATOM 148 CD GLU A 18 17.000 21.900 21.500 1.00 0.00 C
ATOM 149 OE1 GLU A 18 16.600 22.500 20.500 1.00 0.00 O
ATOM 150 OE2 GLU A 18 16.500 21.600 22.500 1.00 0.00 O
ATOM 151 N ALA A 19 21.700 18.000 21.200 1.00 0.00 N
ATOM 152 CA ALA A 19 23.000 17.700 21.700 1.00 0.00 C
ATOM 153 C ALA A 19 24.100 18.200 20.800 1.00 0.00 C
ATOM 154 O ALA A 19 25.200 18.700 21.300 1.00 0.00 O
ATOM 155 CB ALA A 19 23.100 16.200 22.000 1.00 0.00 C
ATOM 156 N ASP A 20 23.800 18.100 19.500 1.00 0.00 N
ATOM 157 CA ASP A 20 24.800 18.600 18.500 1.00 0.00 C
ATOM 158 C ASP A 20 24.000 19.200 17.200 1.00 0.00 C
ATOM 159 O ASP A 20 24.100 18.500 16.100 1.00 0.00 O
ATOM 160 CB ASP A 20 26.100 17.900 18.300 1.00 0.00 C
ATOM 161 CG ASP A 20 26.700 18.200 16.900 1.00 0.00 C
ATOM 162 OD1 ASP A 20 27.000 17.300 16.100 1.00 0.00 O
ATOM 163 OD2 ASP A 20 26.800 19.300 16.600 1.00 0.00 O
ATOM 164 N VAL A 21 23.400 20.300 17.400 1.00 0.00 N
ATOM 165 CA VAL A 21 22.700 21.000 16.400 1.00 0.00 C
ATOM 166 C VAL A 21 23.300 21.200 15.000 1.00 0.00 C
ATOM 167 O VAL A 21 22.800 20.900 14.000 1.00 0.00 O
ATOM 168 CB VAL A 21 22.200 22.300 17.000 1.00 0.00 C
ATOM 169 CG1 VAL A 21 21.400 23.300 16.100 1.00 0.00 C
ATOM 170 CG2 VAL A 21 21.300 22.000 18.200 1.00 0.00 C
ATOM 171 N ALA A 22 24.500 21.900 15.100 1.00 0.00 N
ATOM 172 CA ALA A 22 25.300 22.200 13.900 1.00 0.00 C
ATOM 173 C ALA A 22 25.700 20.900 13.100 1.00 0.00 C
ATOM 174 O ALA A 22 25.800 20.900 11.800 1.00 0.00 O
ATOM 175 CB ALA A 22 26.100 23.200 14.600 1.00 0.00 C
ATOM 176 N GLY A 23 26.000 19.900 13.800 1.00 0.00 N
ATOM 177 CA GLY A 23 26.400 18.600 13.300 1.00 0.00 C
ATOM 178 C GLY A 23 25.200 18.200 12.400 1.00 0.00 C
ATOM 179 O GLY A 23 25.300 18.000 11.200 1.00 0.00 O
ATOM 180 N HIS A 24 24.100 18.000 13.100 1.00 0.00 N
ATOM 181 CA HIS A 24 22.800 17.600 12.400 1.00 0.00 C
ATOM 182 C HIS A 24 22.400 18.400 11.200 1.00 0.00 C
ATOM 183 O HIS A 24 22.100 17.900 10.100 1.00 0.00 O
ATOM 184 CB HIS A 24 21.900 17.800 13.600 1.00 0.00 C
ATOM 185 CG HIS A 24 21.700 16.500 14.500 1.00 0.00 C
ATOM 186 ND1 HIS A 24 22.600 16.200 15.500 1.00 0.00 N
ATOM 187 CD2 HIS A 24 20.800 15.500 14.500 1.00 0.00 C
ATOM 188 CE1 HIS A 24 22.300 15.100 16.000 1.00 0.00 C
ATOM 189 NE2 HIS A 24 21.200 14.700 15.500 1.00 0.00 N
ATOM 190 N GLY A 25 22.400 19.800 11.400 1.00 0.00 N
ATOM 191 CA GLY A 25 22.100 20.700 10.300 1.00 0.00 C
ATOM 192 C GLY A 25 23.000 20.400 9.100 1.00 0.00 C
ATOM 193 O GLY A 25 22.500 20.200 8.000 1.00 0.00 O
ATOM 194 N GLN A 26 24.300 20.400 9.400 1.00 0.00 N
ATOM 195 CA GLN A 26 25.300 20.100 8.400 1.00 0.00 C
ATOM 196 C GLN A 26 24.800 18.900 7.800 1.00 0.00 C
ATOM 197 O GLN A 26 24.500 18.900 6.500 1.00 0.00 O
ATOM 198 CB GLN A 26 26.700 20.400 9.000 1.00 0.00 C
ATOM 199 CG GLN A 26 27.800 20.400 8.100 1.00 0.00 C
ATOM 200 CD GLN A 26 29.200 20.700 8.600 1.00 0.00 C
ATOM 201 OE1 GLN A 26 30.100 21.000 7.800 1.00 0.00 O
ATOM 202 NE2 GLN A 26 29.300 20.600 9.900 1.00 0.00 N
ATOM 203 N ASP A 27 24.600 17.900 8.600 1.00 0.00 N
ATOM 204 CA ASP A 27 24.000 16.600 8.100 1.00 0.00 C
ATOM 205 C ASP A 27 22.900 16.700 7.100 1.00 0.00 C
ATOM 206 O ASP A 27 23.100 16.500 5.900 1.00 0.00 O
ATOM 207 CB ASP A 27 24.100 15.800 9.400 1.00 0.00 C
ATOM 208 CG ASP A 27 25.500 15.100 9.500 1.00 0.00 C
ATOM 209 OD1 ASP A 27 26.300 15.100 8.700 1.00 0.00 O
ATOM 210 OD2 ASP A 27 25.800 14.700 10.600 1.00 0.00 O
ATOM 211 N ILE A 28 21.700 17.100 7.700 1.00 0.00 N
ATOM 212 CA ILE A 28 20.500 17.300 6.900 1.00 0.00 C
ATOM 213 C ILE A 28 20.800 18.000 5.600 1.00 0.00 C
ATOM 214 O ILE A 28 20.400 17.600 4.500 1.00 0.00 O
ATOM 215 CB ILE A 28 19.400 17.900 7.800 1.00 0.00 C
ATOM 216 CG1 ILE A 28 19.000 17.000 9.000 1.00 0.00 C
ATOM 217 CG2 ILE A 28 18.300 18.300 6.800 1.00 0.00 C
ATOM 218 CD1 ILE A 28 18.500 17.700 10.200 1.00 0.00 C
ATOM 219 N LEU A 29 21.500 19.200 5.700 1.00 0.00 N
ATOM 220 CA LEU A 29 21.900 20.000 4.600 1.00 0.00 C
ATOM 221 C LEU A 29 22.500 19.200 3.500 1.00 0.00 C
ATOM 222 O LEU A 29 21.900 19.200 2.400 1.00 0.00 O
ATOM 223 CB LEU A 29 22.300 21.400 5.100 1.00 0.00 C
ATOM 224 CG LEU A 29 21.500 22.200 6.100 1.00 0.00 C
ATOM 225 CD1 LEU A 29 22.300 23.300 6.700 1.00 0.00 C
ATOM 226 CD2 LEU A 29 20.200 22.700 5.500 1.00 0.00 C
ATOM 227 N ILE A 30 23.600 18.600 3.800 1.00 0.00 N
ATOM 228 CA ILE A 30 24.400 17.800 2.900 1.00 0.00 C
ATOM 229 C ILE A 30 23.500 16.700 2.200 1.00 0.00 C
ATOM 230 O ILE A 30 23.500 16.600 1.000 1.00 0.00 O
ATOM 231 CB ILE A 30 25.700 17.600 3.700 1.00 0.00 C
ATOM 232 CG1 ILE A 30 26.400 19.000 3.900 1.00 0.00 C
ATOM 233 CG2 ILE A 30 26.500 16.600 2.800 1.00 0.00 C
ATOM 234 CD1 ILE A 30 27.700 18.800 4.800 1.00 0.00 C
ATOM 235 N ARG A 31 22.800 16.000 3.100 1.00 0.00 N
ATOM 236 CA ARG A 31 21.800 15.000 2.600 1.00 0.00 C
ATOM 237 C ARG A 31 20.900 15.600 1.500 1.00 0.00 C
ATOM 238 O ARG A 31 20.800 15.000 0.400 1.00 0.00 O
ATOM 239 CB ARG A 31 21.100 14.100 3.600 1.00 0.00 C
ATOM 240 CG ARG A 31 20.200 13.000 3.000 1.00 0.00 C
ATOM 241 CD ARG A 31 21.000 12.400 1.800 1.00 0.00 C
ATOM 242 NE ARG A 31 20.300 11.200 1.300 1.00 0.00 N
ATOM 243 CZ ARG A 31 20.800 9.900 1.500 1.00 0.00 C
ATOM 244 NH1 ARG A 31 20.100 8.900 1.100 1.00 0.00 N
ATOM 245 NH2 ARG A 31 22.000 9.700 2.100 1.00 0.00 N
ATOM 246 N LEU A 32 20.300 16.700 1.900 1.00 0.00 N
ATOM 247 CA LEU A 32 19.400 17.400 1.000 1.00 0.00 C
ATOM 248 C LEU A 32 20.100 17.800 -0.300 1.00 0.00 C
ATOM 249 O LEU A 32 19.600 17.500 -1.400 1.00 0.00 O
ATOM 250 CB LEU A 32 18.600 18.600 1.600 1.00 0.00 C
ATOM 251 CG LEU A 32 17.500 19.200 0.800 1.00 0.00 C
ATOM 252 CD1 LEU A 32 16.400 18.200 0.600 1.00 0.00 C
ATOM 253 CD2 LEU A 32 16.900 20.400 1.500 1.00 0.00 C
ATOM 254 N PHE A 33 21.200 18.500 -0.200 1.00 0.00 N
ATOM 255 CA PHE A 33 22.000 19.000 -1.300 1.00 0.00 C
ATOM 256 C PHE A 33 22.500 17.900 -2.300 1.00 0.00 C
ATOM 257 O PHE A 33 22.400 18.100 -3.500 1.00 0.00 O
ATOM 258 CB PHE A 33 23.200 19.800 -0.900 1.00 0.00 C
ATOM 259 CG PHE A 33 22.800 21.200 -0.300 1.00 0.00 C
ATOM 260 CD1 PHE A 33 21.500 21.600 -0.500 1.00 0.00 C
ATOM 261 CD2 PHE A 33 23.700 22.000 0.400 1.00 0.00 C
ATOM 262 CE1 PHE A 33 21.100 22.900 0.000 1.00 0.00 C
ATOM 263 CE2 PHE A 33 23.200 23.200 0.900 1.00 0.00 C
ATOM 264 CZ PHE A 33 22.000 23.600 0.700 1.00 0.00 C
ATOM 265 N LYS A 34 22.900 16.800 -1.800 1.00 0.00 N
ATOM 266 CA LYS A 34 23.300 15.600 -2.500 1.00 0.00 C
ATOM 267 C LYS A 34 22.200 14.900 -3.200 1.00 0.00 C
ATOM 268 O LYS A 34 22.300 14.600 -4.500 1.00 0.00 O
ATOM 269 CB LYS A 34 24.100 14.900 -1.400 1.00 0.00 C
ATOM 270 CG LYS A 34 25.400 15.600 -1.000 1.00 0.00 C
ATOM 271 CD LYS A 34 26.600 14.900 -1.400 1.00 0.00 C
ATOM 272 CE LYS A 34 27.000 15.300 -2.800 1.00 0.00 C
ATOM 273 NZ LYS A 34 28.300 14.600 -3.200 1.00 0.00 N
ATOM 274 N SER A 35 21.100 14.700 -2.500 1.00 0.00 N
ATOM 275 CA SER A 35 19.900 14.100 -3.000 1.00 0.00 C
ATOM 276 C SER A 35 19.000 14.900 -4.000 1.00 0.00 C
ATOM 277 O SER A 35 18.500 14.300 -4.900 1.00 0.00 O
ATOM 278 CB SER A 35 19.100 13.700 -1.800 1.00 0.00 C
ATOM 279 OG SER A 35 19.900 12.800 -0.900 1.00 0.00 O
ATOM 280 N HIS A 36 18.900 16.200 -3.700 1.00 0.00 N
ATOM 281 CA HIS A 36 18.100 17.100 -4.600 1.00 0.00 C
ATOM 282 C HIS A 36 18.900 18.300 -4.900 1.00 0.00 C
ATOM 283 O HIS A 36 18.800 19.400 -4.300 1.00 0.00 O
ATOM 284 CB HIS A 36 16.800 17.200 -3.700 1.00 0.00 C
ATOM 285 CG HIS A 36 16.100 16.000 -3.400 1.00 0.00 C
ATOM 286 ND1 HIS A 36 15.500 15.200 -4.300 1.00 0.00 N
ATOM 287 CD2 HIS A 36 16.000 15.300 -2.200 1.00 0.00 C
ATOM 288 CE1 HIS A 36 14.900 14.100 -3.700 1.00 0.00 C
ATOM 289 NE2 HIS A 36 15.200 14.200 -2.400 1.00 0.00 N
ATOM 290 N PRO A 37 19.700 18.100 -6.000 1.00 0.00 N
ATOM 291 CA PRO A 37 20.500 19.200 -6.500 1.00 0.00 C
ATOM 292 C PRO A 37 19.800 20.500 -6.800 1.00 0.00 C
ATOM 293 O PRO A 37 20.400 21.600 -6.600 1.00 0.00 O
ATOM 294 CB PRO A 37 21.500 18.500 -7.400 1.00 0.00 C
ATOM 295 CG PRO A 37 21.200 17.000 -7.500 1.00 0.00 C
ATOM 296 CD PRO A 37 19.900 16.900 -6.600 1.00 0.00 C
ATOM 297 N GLU A 38 18.600 20.400 -7.100 1.00 0.00 N
ATOM 298 CA GLU A 38 17.700 21.600 -7.300 1.00 0.00 C
ATOM 299 C GLU A 38 17.600 22.500 -6.200 1.00 0.00 C
ATOM 300 O GLU A 38 17.800 23.800 -6.300 1.00 0.00 O
ATOM 301 CB GLU A 38 16.400 20.800 -7.900 1.00 0.00 C
ATOM 302 CG GLU A 38 15.600 20.100 -6.900 1.00 0.00 C
ATOM 303 CD GLU A 38 15.700 18.500 -7.000 1.00 0.00 C
ATOM 304 OE1 GLU A 38 14.600 18.000 -7.000 1.00 0.00 O
ATOM 305 OE2 GLU A 38 16.800 18.000 -7.000 1.00 0.00 O
ATOM 306 N THR A 39 17.400 22.000 -5.000 1.00 0.00 N
ATOM 307 CA THR A 39 17.300 22.700 -3.700 1.00 0.00 C
ATOM 308 C THR A 39 18.400 23.700 -3.300 1.00 0.00 C
ATOM 309 O THR A 39 18.200 24.700 -2.700 1.00 0.00 O
ATOM 310 CB THR A 39 17.200 21.900 -2.400 1.00 0.00 C
ATOM 311 OG1 THR A 39 18.400 21.300 -2.300 1.00 0.00 O
ATOM 312 CG2 THR A 39 16.100 20.800 -2.600 1.00 0.00 C
ATOM 313 N LEU A 40 19.600 23.300 -3.600 1.00 0.00 N
ATOM 314 CA LEU A 40 20.900 24.100 -3.300 1.00 0.00 C
ATOM 315 C LEU A 40 21.000 25.200 -4.400 1.00 0.00 C
ATOM 316 O LEU A 40 21.300 26.400 -4.000 1.00 0.00 O
ATOM 317 CB LEU A 40 22.000 23.200 -3.900 1.00 0.00 C
ATOM 318 CG LEU A 40 23.400 23.800 -4.000 1.00 0.00 C
ATOM 319 CD1 LEU A 40 23.800 24.300 -2.600 1.00 0.00 C
ATOM 320 CD2 LEU A 40 24.400 22.800 -4.500 1.00 0.00 C
ATOM 321 N GLU A 41 20.700 24.900 -5.600 1.00 0.00 N
ATOM 322 CA GLU A 41 20.700 25.800 -6.700 1.00 0.00 C
ATOM 323 C GLU A 41 20.000 27.100 -6.200 1.00 0.00 C
ATOM 324 O GLU A 41 20.400 28.200 -6.600 1.00 0.00 O
ATOM 325 CB GLU A 41 20.100 25.300 -8.100 1.00 0.00 C
ATOM 326 CG GLU A 41 20.000 26.300 -9.200 1.00 0.00 C
ATOM 327 CD GLU A 41 21.400 26.400 -10.000 1.00 0.00 C
ATOM 328 OE1 GLU A 41 22.300 26.000 -9.300 1.00 0.00 O
ATOM 329 OE2 GLU A 41 21.400 26.900 -11.100 1.00 0.00 O
ATOM 330 N LYS A 42 19.000 26.900 -5.400 1.00 0.00 N
ATOM 331 CA LYS A 42 18.300 28.000 -4.800 1.00 0.00 C
ATOM 332 C LYS A 42 18.900 28.900 -3.700 1.00 0.00 C
ATOM 333 O LYS A 42 18.400 30.100 -3.500 1.00 0.00 O
ATOM 334 CB LYS A 42 17.200 27.500 -3.800 1.00 0.00 C
ATOM 335 CG LYS A 42 15.900 27.100 -4.400 1.00 0.00 C
ATOM 336 CD LYS A 42 15.000 28.300 -4.700 1.00 0.00 C
ATOM 337 CE LYS A 42 14.300 28.200 -6.000 1.00 0.00 C
ATOM 338 NZ LYS A 42 12.900 28.600 -5.800 1.00 0.00 N
ATOM 339 N PHE A 43 19.900 28.400 -3.100 1.00 0.00 N
ATOM 340 CA PHE A 43 20.700 29.200 -2.100 1.00 0.00 C
ATOM 341 C PHE A 43 21.900 29.700 -2.800 1.00 0.00 C
ATOM 342 O PHE A 43 22.900 29.000 -3.200 1.00 0.00 O
ATOM 343 CB PHE A 43 21.200 27.900 -1.300 1.00 0.00 C
ATOM 344 CG PHE A 43 20.400 27.700 -0.100 1.00 0.00 C
ATOM 345 CD1 PHE A 43 20.700 28.400 1.000 1.00 0.00 C
ATOM 346 CD2 PHE A 43 19.300 26.800 0.000 1.00 0.00 C
ATOM 347 CE1 PHE A 43 20.000 28.200 2.300 1.00 0.00 C
ATOM 348 CE2 PHE A 43 18.600 26.700 1.200 1.00 0.00 C
ATOM 349 CZ PHE A 43 19.000 27.300 2.300 1.00 0.00 C
ATOM 350 N ASP A 44 21.900 31.000 -3.000 1.00 0.00 N
ATOM 351 CA ASP A 44 22.900 31.800 -3.700 1.00 0.00 C
ATOM 352 C ASP A 44 24.300 31.700 -3.000 1.00 0.00 C
ATOM 353 O ASP A 44 25.300 31.500 -3.600 1.00 0.00 O
ATOM 354 CB ASP A 44 22.700 33.300 -3.800 1.00 0.00 C
ATOM 355 CG ASP A 44 22.000 33.700 -5.100 1.00 0.00 C
ATOM 356 OD1 ASP A 44 22.300 33.300 -6.200 1.00 0.00 O
ATOM 357 OD2 ASP A 44 20.900 34.300 -5.000 1.00 0.00 O
ATOM 358 N ARG A 45 24.200 31.800 -1.600 1.00 0.00 N
ATOM 359 CA ARG A 45 25.300 31.700 -0.700 1.00 0.00 C
ATOM 360 C ARG A 45 26.000 30.300 -0.700 1.00 0.00 C
ATOM 361 O ARG A 45 27.100 30.200 -0.100 1.00 0.00 O
ATOM 362 CB ARG A 45 25.400 32.300 0.700 1.00 0.00 C
ATOM 363 CG ARG A 45 24.400 31.700 1.700 1.00 0.00 C
ATOM 364 CD ARG A 45 24.100 32.800 2.700 1.00 0.00 C
ATOM 365 NE ARG A 45 24.500 32.300 4.100 1.00 0.00 N
ATOM 366 CZ ARG A 45 23.700 32.200 5.100 1.00 0.00 C
ATOM 367 NH1 ARG A 45 24.100 31.800 6.300 1.00 0.00 N
ATOM 368 NH2 ARG A 45 22.400 32.500 5.000 1.00 0.00 N
ATOM 369 N PHE A 46 25.400 29.300 -1.300 1.00 0.00 N
ATOM 370 CA PHE A 46 25.900 28.000 -1.400 1.00 0.00 C
ATOM 371 C PHE A 46 26.200 27.300 -2.700 1.00 0.00 C
ATOM 372 O PHE A 46 27.100 26.300 -2.800 1.00 0.00 O
ATOM 373 CB PHE A 46 25.300 26.900 -0.400 1.00 0.00 C
ATOM 374 CG PHE A 46 25.000 27.500 0.900 1.00 0.00 C
ATOM 375 CD1 PHE A 46 26.000 28.100 1.600 1.00 0.00 C
ATOM 376 CD2 PHE A 46 23.700 27.400 1.500 1.00 0.00 C
ATOM 377 CE1 PHE A 46 25.700 28.600 2.900 1.00 0.00 C
ATOM 378 CE2 PHE A 46 23.500 28.000 2.700 1.00 0.00 C
ATOM 379 CZ PHE A 46 24.500 28.500 3.500 1.00 0.00 C
ATOM 380 N LYS A 47 25.600 27.700 -3.700 1.00 0.00 N
ATOM 381 CA LYS A 47 25.700 27.200 -5.100 1.00 0.00 C
ATOM 382 C LYS A 47 27.200 26.900 -5.400 1.00 0.00 C
ATOM 383 O LYS A 47 27.500 25.700 -5.800 1.00 0.00 O
ATOM 384 CB LYS A 47 25.300 28.000 -6.400 1.00 0.00 C
ATOM 385 CG LYS A 47 24.600 29.300 -6.100 1.00 0.00 C
ATOM 386 CD LYS A 47 24.100 30.000 -7.400 1.00 0.00 C
ATOM 387 CE LYS A 47 23.600 31.400 -7.100 1.00 0.00 C
ATOM 388 NZ LYS A 47 23.200 32.000 -8.400 1.00 0.00 N
ATOM 389 N HIS A 48 28.000 27.900 -5.100 1.00 0.00 N
ATOM 390 CA HIS A 48 29.500 27.700 -5.300 1.00 0.00 C
ATOM 391 C HIS A 48 30.000 26.400 -4.900 1.00 0.00 C
ATOM 392 O HIS A 48 31.000 25.800 -5.500 1.00 0.00 O
ATOM 393 CB HIS A 48 30.200 28.900 -4.800 1.00 0.00 C
ATOM 394 CG HIS A 48 30.400 29.000 -3.300 1.00 0.00 C
ATOM 395 ND1 HIS A 48 29.500 29.600 -2.400 1.00 0.00 N
ATOM 396 CD2 HIS A 48 31.400 28.400 -2.500 1.00 0.00 C
ATOM 397 CE1 HIS A 48 30.000 29.400 -1.200 1.00 0.00 C
ATOM 398 NE2 HIS A 48 31.100 28.700 -1.200 1.00 0.00 N
ATOM 399 N LEU A 49 29.400 25.900 -3.800 1.00 0.00 N
ATOM 400 CA LEU A 49 29.700 24.600 -3.200 1.00 0.00 C
ATOM 401 C LEU A 49 29.700 23.400 -4.100 1.00 0.00 C
ATOM 402 O LEU A 49 28.600 22.900 -4.500 1.00 0.00 O
ATOM 403 CB LEU A 49 28.900 24.200 -2.000 1.00 0.00 C
ATOM 404 CG LEU A 49 29.400 24.600 -0.600 1.00 0.00 C
ATOM 405 CD1 LEU A 49 29.600 26.100 -0.600 1.00 0.00 C
ATOM 406 CD2 LEU A 49 28.400 24.200 0.500 1.00 0.00 C
ATOM 407 N LYS A 50 30.800 22.800 -4.400 1.00 0.00 N
ATOM 408 CA LYS A 50 31.000 21.700 -5.300 1.00 0.00 C
ATOM 409 C LYS A 50 31.000 20.200 -4.800 1.00 0.00 C
ATOM 410 O LYS A 50 30.400 19.300 -5.500 1.00 0.00 O
ATOM 411 CB LYS A 50 31.900 21.800 -6.500 1.00 0.00 C
ATOM 412 CG LYS A 50 31.800 23.200 -7.200 1.00 0.00 C
ATOM 413 CD LYS A 50 30.400 23.400 -7.800 1.00 0.00 C
ATOM 414 CE LYS A 50 29.500 24.200 -6.900 1.00 0.00 C
ATOM 415 NZ LYS A 50 28.200 24.400 -7.500 1.00 0.00 N
ATOM 416 N THR A 51 31.700 20.000 -3.700 1.00 0.00 N
ATOM 417 CA THR A 51 31.800 18.600 -3.100 1.00 0.00 C
ATOM 418 C THR A 51 31.200 18.500 -1.700 1.00 0.00 C
ATOM 419 O THR A 51 30.900 19.500 -1.000 1.00 0.00 O
ATOM 420 CB THR A 51 33.300 18.300 -3.100 1.00 0.00 C
ATOM 421 OG1 THR A 51 33.900 19.400 -2.300 1.00 0.00 O
ATOM 422 CG2 THR A 51 33.900 18.300 -4.400 1.00 0.00 C
ATOM 423 N GLU A 52 31.200 17.200 -1.300 1.00 0.00 N
ATOM 424 CA GLU A 52 30.700 16.900 0.100 1.00 0.00 C
ATOM 425 C GLU A 52 31.700 17.400 1.000 1.00 0.00 C
ATOM 426 O GLU A 52 31.400 18.000 2.100 1.00 0.00 O
ATOM 427 CB GLU A 52 31.000 15.400 0.400 1.00 0.00 C
ATOM 428 CG GLU A 52 30.200 14.700 1.500 1.00 0.00 C
ATOM 429 CD GLU A 52 29.100 13.700 1.000 1.00 0.00 C
ATOM 430 OE1 GLU A 52 28.500 13.300 2.000 1.00 0.00 O
ATOM 431 OE2 GLU A 52 28.900 13.500 -0.100 1.00 0.00 O
ATOM 432 N ALA A 53 33.000 17.300 0.600 1.00 0.00 N
ATOM 433 CA ALA A 53 34.100 17.800 1.300 1.00 0.00 C
ATOM 434 C ALA A 53 33.900 19.300 1.600 1.00 0.00 C
ATOM 435 O ALA A 53 33.800 19.700 2.800 1.00 0.00 O
ATOM 436 CB ALA A 53 35.500 17.700 0.700 1.00 0.00 C
ATOM 437 N GLU A 54 33.800 20.000 0.500 1.00 0.00 N
ATOM 438 CA GLU A 54 33.500 21.500 0.500 1.00 0.00 C
ATOM 439 C GLU A 54 32.400 21.900 1.500 1.00 0.00 C
ATOM 440 O GLU A 54 32.700 22.800 2.300 1.00 0.00 O
ATOM 441 CB GLU A 54 33.400 22.100 -0.900 1.00 0.00 C
ATOM 442 CG GLU A 54 34.600 21.900 -1.900 1.00 0.00 C
ATOM 443 CD GLU A 54 34.400 22.500 -3.300 1.00 0.00 C
ATOM 444 OE1 GLU A 54 35.500 22.700 -3.800 1.00 0.00 O
ATOM 445 OE2 GLU A 54 33.300 22.800 -3.700 1.00 0.00 O
ATOM 446 N MET A 55 31.300 21.300 1.300 1.00 0.00 N
ATOM 447 CA MET A 55 30.100 21.500 2.200 1.00 0.00 C
ATOM 448 C MET A 55 30.500 21.400 3.700 1.00 0.00 C
ATOM 449 O MET A 55 30.400 22.500 4.400 1.00 0.00 O
ATOM 450 CB MET A 55 29.100 20.500 1.600 1.00 0.00 C
ATOM 451 CG MET A 55 28.700 20.800 0.200 1.00 0.00 C
ATOM 452 SD MET A 55 27.200 20.100 -0.300 1.00 0.00 S
ATOM 453 CE MET A 55 27.400 20.000 -2.000 1.00 0.00 C
ATOM 454 N LYS A 56 30.900 20.200 4.100 1.00 0.00 N
ATOM 455 CA LYS A 56 31.200 20.000 5.500 1.00 0.00 C
ATOM 456 C LYS A 56 32.300 21.000 5.900 1.00 0.00 C
ATOM 457 O LYS A 56 32.300 21.400 7.100 1.00 0.00 O
ATOM 458 CB LYS A 56 32.100 18.700 5.600 1.00 0.00 C
ATOM 459 CG LYS A 56 31.500 17.400 5.100 1.00 0.00 C
ATOM 460 CD LYS A 56 32.300 16.200 5.400 1.00 0.00 C
ATOM 461 CE LYS A 56 31.900 15.000 4.600 1.00 0.00 C
ATOM 462 NZ LYS A 56 32.700 13.800 4.900 1.00 0.00 N
ATOM 463 N ALA A 57 33.100 21.300 5.000 1.00 0.00 N
ATOM 464 CA ALA A 57 34.200 22.300 5.200 1.00 0.00 C
ATOM 465 C ALA A 57 33.700 23.700 5.500 1.00 0.00 C
ATOM 466 O ALA A 57 34.100 24.300 6.600 1.00 0.00 O
ATOM 467 CB ALA A 57 35.200 22.700 4.100 1.00 0.00 C
ATOM 468 N SER A 58 32.800 24.200 4.700 1.00 0.00 N
ATOM 469 CA SER A 58 32.200 25.500 4.900 1.00 0.00 C
ATOM 470 C SER A 58 31.400 25.800 6.200 1.00 0.00 C
ATOM 471 O SER A 58 30.400 25.100 6.500 1.00 0.00 O
ATOM 472 CB SER A 58 31.000 25.600 4.000 1.00 0.00 C
ATOM 473 OG SER A 58 30.300 26.800 4.200 1.00 0.00 O
ATOM 474 N GLU A 59 31.800 26.900 6.900 1.00 0.00 N
ATOM 475 CA GLU A 59 31.200 27.300 8.100 1.00 0.00 C
ATOM 476 C GLU A 59 29.800 28.000 8.100 1.00 0.00 C
ATOM 477 O GLU A 59 29.000 28.000 9.000 1.00 0.00 O
ATOM 478 CB GLU A 59 32.100 28.300 8.800 1.00 0.00 C
ATOM 479 CG GLU A 59 33.100 27.700 9.900 1.00 0.00 C
ATOM 480 CD GLU A 59 32.400 26.900 11.000 1.00 0.00 C
ATOM 481 OE1 GLU A 59 32.000 27.700 11.900 1.00 0.00 O
ATOM 482 OE2 GLU A 59 32.300 25.700 10.900 1.00 0.00 O
ATOM 483 N ASP A 60 29.600 28.700 6.900 1.00 0.00 N
ATOM 484 CA ASP A 60 28.400 29.500 6.700 1.00 0.00 C
ATOM 485 C ASP A 60 27.300 28.400 6.600 1.00 0.00 C
ATOM 486 O ASP A 60 26.200 28.600 7.200 1.00 0.00 O
ATOM 487 CB ASP A 60 28.600 30.300 5.400 1.00 0.00 C
ATOM 488 CG ASP A 60 27.500 31.300 5.200 1.00 0.00 C
ATOM 489 OD1 ASP A 60 27.100 31.700 4.200 1.00 0.00 O
ATOM 490 OD2 ASP A 60 27.100 31.800 6.300 1.00 0.00 O
ATOM 491 N LEU A 61 27.600 27.300 6.000 1.00 0.00 N