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3HHB.pdb
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3HHB.pdb
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HEADER OXYGEN TRANSPORT 07-MAR-84 3HHB
TITLE THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN (DEOXY) (ALPHA CHAIN);
COMPND 3 CHAIN: A, C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: HEMOGLOBIN (DEOXY) (BETA CHAIN);
COMPND 6 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS OXYGEN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR G.FERMI,M.F.PERUTZ
REVDAT 4 13-JUL-11 3HHB 1 VERSN
REVDAT 3 24-FEB-09 3HHB 1 VERSN
REVDAT 2 01-APR-03 3HHB 1 JRNL
REVDAT 1 18-JUL-84 3HHB 0
SPRSDE 18-JUL-84 3HHB 1HHB
JRNL AUTH G.FERMI,M.F.PERUTZ,B.SHAANAN,R.FOURME
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 A
JRNL TITL 2 RESOLUTION
JRNL REF J.MOL.BIOL. V. 175 159 1984
JRNL REFN ISSN 0022-2836
JRNL PMID 6726807
JRNL DOI 10.1016/0022-2836(84)90472-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.F.PERUTZ,S.S.HASNAIN,P.J.DUKE,J.L.SESSLER,J.E.HAHN
REMARK 1 TITL STEREOCHEMISTRY OF IRON IN DEOXYHAEMOGLOBIN
REMARK 1 REF NATURE V. 295 535 1982
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.FERMI,M.F.PERUTZ
REMARK 1 REF HAEMOGLOBIN AND MYOGLOBIN. V. 2 1981
REMARK 1 REF 2 ATLAS OF MOLECULAR
REMARK 1 REF 3 STRUCTURES IN BIOLOGY
REMARK 1 PUBL OXFORD UNIVERSITY PRESS
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.F.PERUTZ
REMARK 1 TITL REGULATION OF OXYGEN AFFINITY OF HEMOGLOBIN. INFLUENCE OF
REMARK 1 TITL 2 STRUCTURE OF THE GLOBIN ON THE HEME IRON
REMARK 1 REF ANNU.REV.BIOCHEM. V. 48 327 1979
REMARK 1 REFN ISSN 0066-4154
REMARK 1 REFERENCE 4
REMARK 1 AUTH L.F.TENEYCK,A.ARNONE
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN DEOXYHEMOGLOBIN
REMARK 1 TITL 2 AT 2.5 ANGSTROMS RESOLUTION, I.X-RAY ANALYSIS
REMARK 1 REF J.MOL.BIOL. V. 100 3 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.FERMI
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN
REMARK 1 TITL 2 DEOXYHAEMOGLOBIN AT 2.5 ANGSTROMS RESOLUTION, REFINEMENT OF
REMARK 1 TITL 3 THE ATOMIC MODEL
REMARK 1 REF J.MOL.BIOL. V. 97 237 1975
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH H.MUIRHEAD,J.GREER
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN
REMARK 1 TITL 2 DEOXYHAEMOGLOBIN AT 3.5 ANGSTROMS RESOLUTION
REMARK 1 REF NATURE V. 228 516 1970
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 7
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 56 1972
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 8
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 64 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. 1.74 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) : 1.74
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) : 0.200
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 : 4384
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 174
REMARK 3 SOLVENT ATOMS : 54
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:
REMARK 3 THE COORDINATES GIVEN HERE ARE IN THE ORTHOGONAL ANGSTROM
REMARK 3 SYSTEM STANDARD FOR HEMOGLOBINS. THE Y AXIS IS THE
REMARK 3 (NON CRYSTALLOGRAPHIC) MOLECULAR DIAD AND THE X AXIS IS THE
REMARK 3 PSEUDO DIAD WHICH RELATES THE ALPHA-1 AND BETA-1 CHAINS.
REMARK 4
REMARK 4 3HHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 (%): 45.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 285
REMARK 285 THE ENTRY COORDINATES
REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.
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 -0.948470 -0.315864 -0.025443 -6.70967
REMARK 290 SMTRY2 2 -0.315826 0.935913 0.155939 41.12313
REMARK 290 SMTRY3 2 -0.025432 0.155891 -0.987443 3.31148
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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 400
REMARK 400 COMPOUND
REMARK 400 THREE SETS OF COORDINATES FOR HUMAN HEMOGLOBIN WERE
REMARK 400 DEPOSITED SIMULTANEOUSLY.
REMARK 400 2HHB. REFINED BY THE METHOD OF JACK AND LEVITT. THIS
REMARK 400 ENTRY PRESENTS THE BEST ESTIMATE OF THE
REMARK 400 COORDINATES.
REMARK 400 3HHB. SYMMETRY AVERAGED ABOUT THE (NON-CRYSTALLOGRAPHIC)
REMARK 400 MOLECULAR AXIS AND THEN RE-REGULARIZED BY THE
REMARK 400 ENERGY REFINEMENT METHOD OF LEVITT. THIS ENTRY
REMARK 400 PRESENTS COORDINATES THAT ARE ADEQUATE FOR MOST
REMARK 400 PURPOSES, SUCH AS COMPARISON WITH OTHER STRUCTURES.
REMARK 400 4HHB. UNRESTRAINED REFINEMENT. THIS ENTRY PRESENTS
REMARK 400 COORDINATES THAT ARE USEFUL FOR STATISTICAL STUDIES
REMARK 400 (E.G. PHI/PSI ANGLES) WHERE DATA UNBIASED BY
REMARK 400 RESTRAINTS IS REQUIRED.
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 OD2 ASP B 21 OD1 ASN C 78 2647 1.80
REMARK 500 OE1 GLN C 54 OE2 GLU D 43 1556 1.85
REMARK 500 O HIS B 117 CE LYS D 17 1655 2.09
REMARK 500 OD2 ASP B 21 CG ASN C 78 2647 2.16
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 ARG A 92 CD - NE - CZ ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLU A 116 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG B 30 CD - NE - CZ ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG B 30 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 30 NE - CZ - NH2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG C 92 CD - NE - CZ ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLU C 116 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG D 30 CD - NE - CZ ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH2 ANGL. DEV. = -10.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 75 40.20 -150.52
REMARK 500 LYS A 90 -67.19 -120.63
REMARK 500 ASN B 80 64.97 -160.59
REMARK 500 ASP C 75 40.20 -150.52
REMARK 500 LYS C 90 -67.19 -120.63
REMARK 500 ASN D 80 64.97 -160.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU A 116 0.08 SIDE CHAIN
REMARK 500 ARG B 30 0.10 SIDE CHAIN
REMARK 500 GLU C 116 0.08 SIDE CHAIN
REMARK 500 ARG D 30 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PO4 B 147
REMARK 610 PO4 D 147
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 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 142 NA 97.4
REMARK 620 3 HEM A 142 NB 96.9 86.4
REMARK 620 4 HEM A 142 NC 104.6 157.8 88.6
REMARK 620 5 HEM A 142 ND 105.4 90.4 157.7 86.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 148 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 148 NA 94.0
REMARK 620 3 HEM B 148 NB 100.0 87.5
REMARK 620 4 HEM B 148 NC 105.8 160.2 88.6
REMARK 620 5 HEM B 148 ND 100.2 89.3 159.7 87.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HEM C 142 NA 97.4
REMARK 620 3 HEM C 142 NB 96.9 86.4
REMARK 620 4 HEM C 142 NC 104.6 157.8 88.6
REMARK 620 5 HEM C 142 ND 105.4 90.4 157.7 86.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 148 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HEM D 148 NA 94.0
REMARK 620 3 HEM D 148 NB 100.0 87.5
REMARK 620 4 HEM D 148 NC 105.8 160.2 88.6
REMARK 620 5 HEM D 148 ND 100.2 89.3 159.7 87.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 148
DBREF 3HHB A 1 141 UNP P01922 HBA_HUMAN 1 141
DBREF 3HHB B 1 146 UNP P02023 HBB_HUMAN 1 146
DBREF 3HHB C 1 141 UNP P01922 HBA_HUMAN 1 141
DBREF 3HHB D 1 146 UNP P02023 HBB_HUMAN 1 146
SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 D 146 LYS TYR HIS
HET PO4 B 147 1
HET PO4 D 147 1
HET HEM A 142 43
HET HEM B 148 43
HET HEM C 142 43
HET HEM D 148 43
HETNAM PO4 PHOSPHATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 PO4 2(O4 P 3-)
FORMUL 7 HEM 4(C34 H32 FE N4 O4)
FORMUL 11 HOH *54(H2 O)
HELIX 1 AA SER A 3 GLY A 18 1 16
HELIX 2 AB HIS A 20 SER A 35 1 16
HELIX 3 AC PHE A 36 TYR A 42 1 7
HELIX 4 AD HIS A 50 GLY A 51 1DEGEN 2 RES HLX RETAIN HOMOL 2
HELIX 5 AE SER A 52 ALA A 71 1 20
HELIX 6 AF LEU A 80 ALA A 88 1 9
HELIX 7 AG ASP A 94 HIS A 112 1 19
HELIX 8 AH THR A 118 SER A 138 1 21
HELIX 9 BA THR B 4 VAL B 18 1 15
HELIX 10 BB ASN B 19 VAL B 34 1 16
HELIX 11 BC TYR B 35 PHE B 41 1 7
HELIX 12 BD THR B 50 GLY B 56 1 7
HELIX 13 BE ASN B 57 ALA B 76 1 20
HELIX 14 BF PHE B 85 CYS B 93 1 9
HELIX 15 BG ASP B 99 HIS B 117 1 19
HELIX 16 BH THR B 123 HIS B 143 1 21
HELIX 17 CA SER C 3 GLY C 18 1 16
HELIX 18 CB HIS C 20 SER C 35 1 16
HELIX 19 CC PHE C 36 TYR C 42 1 7
HELIX 20 CD HIS C 50 GLY C 51 1DEGEN 2 RES HLX RETAIN HOMOL 2
HELIX 21 CE SER C 52 ALA C 71 1 20
HELIX 22 CF LEU C 80 ALA C 88 1 9
HELIX 23 CG ASP C 94 HIS C 112 1 19
HELIX 24 CH THR C 118 SER C 138 1 21
HELIX 25 DA THR D 4 VAL D 18 1 15
HELIX 26 DB ASN D 19 VAL D 34 1 16
HELIX 27 DC TYR D 35 PHE D 41 1 7
HELIX 28 DD THR D 50 GLY D 56 1 7
HELIX 29 DE ASN D 57 ALA D 76 1 20
HELIX 30 DF PHE D 85 CYS D 93 1 9
HELIX 31 DG ASP D 99 HIS D 117 1 19
HELIX 32 DH THR D 123 HIS D 143 1 21
LINK FE HEM A 142 NE2 HIS A 87 1555 1555 2.11
LINK FE HEM B 148 NE2 HIS B 92 1555 1555 2.06
LINK FE HEM C 142 NE2 HIS C 87 1555 1555 2.11
LINK FE HEM D 148 NE2 HIS D 92 1555 1555 2.06
SITE 1 AC1 16 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC1 16 HIS A 58 LYS A 61 LEU A 86 HIS A 87
SITE 3 AC1 16 LEU A 91 VAL A 93 ASN A 97 PHE A 98
SITE 4 AC1 16 LEU A 101 LEU A 136 HOH A 149 HOH A 153
SITE 1 AC2 11 ALA A 53 PHE B 42 HIS B 63 LYS B 66
SITE 2 AC2 11 VAL B 67 LEU B 91 HIS B 92 LEU B 96
SITE 3 AC2 11 ASN B 102 PHE B 103 LEU B 141
SITE 1 AC3 14 TYR C 42 PHE C 43 HIS C 45 PHE C 46
SITE 2 AC3 14 HIS C 58 LYS C 61 LEU C 86 HIS C 87
SITE 3 AC3 14 LEU C 91 VAL C 93 ASN C 97 PHE C 98
SITE 4 AC3 14 LEU C 101 LEU C 136
SITE 1 AC4 10 PHE D 42 HIS D 63 LYS D 66 VAL D 67
SITE 2 AC4 10 LEU D 91 HIS D 92 LEU D 96 ASN D 102
SITE 3 AC4 10 PHE D 103 LEU D 141
CRYST1 63.150 83.590 53.800 90.00 99.34 90.00 P 1 21 1 4
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 0.015445 0.002224 0.003676 0.26345
SCALE2 -0.001920 0.011769 0.000948 0.15308
SCALE3 -0.001073 -0.001683 0.018726 0.75186
MTRIX1 1 -1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 -1.000000 0.00000 1
ATOM 1 N VAL A 1 6.452 16.459 4.843 1.00 47.38 N
ATOM 2 CA VAL A 1 7.060 17.792 4.760 1.00 48.47 C
ATOM 3 C VAL A 1 8.561 17.703 5.038 1.00 37.13 C
ATOM 4 O VAL A 1 8.992 17.182 6.072 1.00 36.25 O
ATOM 5 CB VAL A 1 6.342 18.738 5.727 1.00 55.13 C
ATOM 6 CG1 VAL A 1 7.114 20.033 5.993 1.00 54.30 C
ATOM 7 CG2 VAL A 1 4.924 19.032 5.232 1.00 64.75 C
ATOM 8 N LEU A 2 9.333 18.209 4.095 1.00 30.18 N
ATOM 9 CA LEU A 2 10.785 18.159 4.237 1.00 35.60 C
ATOM 10 C LEU A 2 11.247 19.305 5.133 1.00 35.47 C
ATOM 11 O LEU A 2 11.017 20.477 4.819 1.00 37.64 O
ATOM 12 CB LEU A 2 11.451 18.286 2.866 1.00 35.22 C
ATOM 13 CG LEU A 2 11.081 17.137 1.927 1.00 31.04 C
ATOM 14 CD1 LEU A 2 11.766 17.306 0.570 1.00 39.08 C
ATOM 15 CD2 LEU A 2 11.427 15.778 2.539 1.00 38.96 C
ATOM 16 N SER A 3 11.883 18.937 6.233 1.00 28.20 N
ATOM 17 CA SER A 3 12.492 19.934 7.127 1.00 23.85 C
ATOM 18 C SER A 3 13.750 20.470 6.438 1.00 27.11 C
ATOM 19 O SER A 3 14.239 19.832 5.501 1.00 26.71 O
ATOM 20 CB SER A 3 12.878 19.251 8.442 1.00 21.90 C
ATOM 21 OG SER A 3 13.998 18.407 8.195 1.00 26.31 O
ATOM 22 N PRO A 4 14.254 21.625 6.859 1.00 36.77 N
ATOM 23 CA PRO A 4 15.511 22.192 6.331 1.00 29.95 C
ATOM 24 C PRO A 4 16.648 21.170 6.444 1.00 21.83 C
ATOM 25 O PRO A 4 17.502 21.090 5.554 1.00 31.84 O
ATOM 26 CB PRO A 4 15.832 23.412 7.188 1.00 40.06 C
ATOM 27 CG PRO A 4 14.547 23.757 7.933 1.00 41.50 C
ATOM 28 CD PRO A 4 13.686 22.491 7.914 1.00 36.26 C
ATOM 29 N ALA A 5 16.636 20.416 7.533 1.00 21.59 N
ATOM 30 CA ALA A 5 17.676 19.403 7.724 1.00 19.46 C
ATOM 31 C ALA A 5 17.514 18.318 6.659 1.00 21.14 C
ATOM 32 O ALA A 5 18.522 17.841 6.129 1.00 20.33 O
ATOM 33 CB ALA A 5 17.595 18.800 9.128 1.00 25.18 C
ATOM 34 N ASP A 6 16.267 17.956 6.362 1.00 18.32 N
ATOM 35 CA ASP A 6 16.059 16.945 5.311 1.00 18.41 C
ATOM 36 C ASP A 6 16.612 17.468 3.988 1.00 15.74 C
ATOM 37 O ASP A 6 17.237 16.705 3.247 1.00 16.91 O
ATOM 38 CB ASP A 6 14.579 16.607 5.095 1.00 18.63 C
ATOM 39 CG ASP A 6 13.977 15.818 6.254 1.00 21.29 C
ATOM 40 OD1 ASP A 6 14.662 14.963 6.824 1.00 19.31 O
ATOM 41 OD2 ASP A 6 12.810 16.060 6.565 1.00 21.06 O
ATOM 42 N LYS A 7 16.386 18.743 3.724 1.00 18.72 N
ATOM 43 CA LYS A 7 16.809 19.277 2.425 1.00 25.61 C
ATOM 44 C LYS A 7 18.330 19.299 2.338 1.00 22.21 C
ATOM 45 O LYS A 7 18.885 19.029 1.270 1.00 20.03 O
ATOM 46 CB LYS A 7 16.261 20.683 2.227 1.00 31.72 C
ATOM 47 CG LYS A 7 14.742 20.646 2.278 1.00 37.04 C
ATOM 48 CD LYS A 7 14.147 22.024 2.037 1.00 42.43 C
ATOM 49 CE LYS A 7 12.753 22.097 2.646 1.00 40.42 C
ATOM 50 NZ LYS A 7 12.231 23.454 2.505 1.00 51.97 N
ATOM 51 N THR A 8 18.948 19.610 3.462 1.00 20.77 N
ATOM 52 CA THR A 8 20.410 19.643 3.508 1.00 17.76 C
ATOM 53 C THR A 8 20.944 18.232 3.256 1.00 16.01 C
ATOM 54 O THR A 8 21.908 18.065 2.501 1.00 19.30 O
ATOM 55 CB THR A 8 20.867 20.189 4.866 1.00 21.79 C
ATOM 56 OG1 THR A 8 20.438 21.543 4.974 1.00 23.74 O
ATOM 57 CG2 THR A 8 22.387 20.148 5.038 1.00 29.19 C
ATOM 58 N ASN A 9 20.285 17.247 3.863 1.00 17.13 N
ATOM 59 CA ASN A 9 20.715 15.845 3.737 1.00 16.48 C
ATOM 60 C ASN A 9 20.551 15.352 2.297 1.00 15.07 C
ATOM 61 O ASN A 9 21.413 14.625 1.791 1.00 18.71 O
ATOM 62 CB ASN A 9 19.906 14.949 4.686 1.00 18.35 C
ATOM 63 CG ASN A 9 20.351 15.126 6.139 1.00 23.61 C
ATOM 64 OD1 ASN A 9 21.447 15.630 6.404 1.00 21.10 O
ATOM 65 ND2 ASN A 9 19.503 14.692 7.059 1.00 21.18 N
ATOM 66 N VAL A 10 19.461 15.753 1.664 1.00 17.76 N
ATOM 67 CA VAL A 10 19.208 15.283 0.296 1.00 17.68 C
ATOM 68 C VAL A 10 20.198 15.944 -0.666 1.00 19.33 C
ATOM 69 O VAL A 10 20.732 15.271 -1.552 1.00 19.83 O
ATOM 70 CB VAL A 10 17.754 15.566 -0.104 1.00 18.88 C
ATOM 71 CG1 VAL A 10 17.484 15.244 -1.576 1.00 22.53 C
ATOM 72 CG2 VAL A 10 16.782 14.794 0.790 1.00 17.60 C
ATOM 73 N LYS A 11 20.450 17.230 -0.472 1.00 19.14 N
ATOM 74 CA LYS A 11 21.393 17.926 -1.357 1.00 22.11 C
ATOM 75 C LYS A 11 22.804 17.375 -1.182 1.00 21.76 C
ATOM 76 O LYS A 11 23.564 17.311 -2.153 1.00 24.51 O
ATOM 77 CB LYS A 11 21.406 19.420 -1.054 1.00 26.13 C
ATOM 78 CG LYS A 11 20.121 20.060 -1.557 1.00 33.79 C
ATOM 79 CD LYS A 11 20.029 21.532 -1.180 1.00 48.06 C
ATOM 80 CE LYS A 11 18.730 22.121 -1.720 1.00 52.89 C
ATOM 81 NZ LYS A 11 18.349 23.267 -0.893 1.00 60.15 N
ATOM 82 N ALA A 12 23.118 16.991 0.035 1.00 21.03 N
ATOM 83 CA ALA A 12 24.474 16.497 0.269 1.00 21.59 C
ATOM 84 C ALA A 12 24.640 15.139 -0.414 1.00 33.13 C
ATOM 85 O ALA A 12 25.641 14.903 -1.099 1.00 29.65 O
ATOM 86 CB ALA A 12 24.735 16.375 1.770 1.00 31.30 C
ATOM 87 N ALA A 13 23.646 14.291 -0.226 1.00 23.03 N
ATOM 88 CA ALA A 13 23.747 12.921 -0.738 1.00 21.75 C
ATOM 89 C ALA A 13 23.717 12.920 -2.265 1.00 21.98 C
ATOM 90 O ALA A 13 24.485 12.203 -2.915 1.00 22.34 O
ATOM 91 CB ALA A 13 22.582 12.088 -0.198 1.00 23.36 C
ATOM 92 N TRP A 14 22.837 13.738 -2.798 1.00 21.55 N
ATOM 93 CA TRP A 14 22.645 13.719 -4.242 1.00 20.45 C
ATOM 94 C TRP A 14 23.848 14.393 -4.905 1.00 33.66 C
ATOM 95 O TRP A 14 24.219 14.067 -6.039 1.00 26.83 O
ATOM 96 CB TRP A 14 21.326 14.412 -4.589 1.00 23.12 C
ATOM 97 CG TRP A 14 20.888 14.053 -6.021 1.00 23.37 C
ATOM 98 CD1 TRP A 14 20.980 14.830 -7.166 1.00 28.01 C
ATOM 99 CD2 TRP A 14 20.297 12.839 -6.394 1.00 20.46 C
ATOM 100 NE1 TRP A 14 20.477 14.111 -8.258 1.00 33.77 N
ATOM 101 CE2 TRP A 14 20.068 12.882 -7.780 1.00 31.68 C
ATOM 102 CE3 TRP A 14 19.971 11.717 -5.646 1.00 27.10 C
ATOM 103 CZ2 TRP A 14 19.529 11.829 -8.498 1.00 27.05 C
ATOM 104 CZ3 TRP A 14 19.421 10.646 -6.364 1.00 35.48 C
ATOM 105 CH2 TRP A 14 19.199 10.704 -7.740 1.00 33.31 C
ATOM 106 N GLY A 15 24.430 15.311 -4.153 1.00 34.14 N
ATOM 107 CA GLY A 15 25.650 15.995 -4.590 1.00 31.78 C
ATOM 108 C GLY A 15 26.744 14.955 -4.849 1.00 33.78 C
ATOM 109 O GLY A 15 27.410 15.004 -5.888 1.00 42.94 O
ATOM 110 N LYS A 16 26.887 14.026 -3.909 1.00 32.25 N
ATOM 111 CA LYS A 16 27.926 12.981 -4.000 1.00 30.66 C
ATOM 112 C LYS A 16 27.555 12.019 -5.132 1.00 28.33 C
ATOM 113 O LYS A 16 28.429 11.329 -5.665 1.00 34.67 O
ATOM 114 CB LYS A 16 27.980 12.217 -2.674 1.00 27.74 C
ATOM 115 CG LYS A 16 29.308 11.555 -2.267 1.00 51.91 C
ATOM 116 CD LYS A 16 30.494 11.578 -3.237 1.00 69.89 C
ATOM 117 CE LYS A 16 31.771 10.937 -2.656 1.00 63.67 C
ATOM 118 NZ LYS A 16 31.762 9.472 -2.789 1.00 57.22 N
ATOM 119 N VAL A 17 26.272 11.964 -5.479 1.00 33.14 N
ATOM 120 CA VAL A 17 25.899 11.070 -6.587 1.00 30.43 C
ATOM 121 C VAL A 17 26.485 11.664 -7.866 1.00 41.34 C
ATOM 122 O VAL A 17 27.105 10.950 -8.664 1.00 33.66 O
ATOM 123 CB VAL A 17 24.375 10.903 -6.662 1.00 22.73 C
ATOM 124 CG1 VAL A 17 23.884 10.435 -8.032 1.00 23.17 C
ATOM 125 CG2 VAL A 17 23.864 9.976 -5.557 1.00 31.44 C
ATOM 126 N GLY A 18 26.301 12.972 -7.961 1.00 39.90 N
ATOM 127 CA GLY A 18 26.822 13.800 -9.050 1.00 44.56 C
ATOM 128 C GLY A 18 26.612 13.171 -10.428 1.00 33.48 C
ATOM 129 O GLY A 18 25.480 13.028 -10.902 1.00 38.93 O
ATOM 130 N ALA A 19 27.723 12.785 -11.018 1.00 27.83 N
ATOM 131 CA ALA A 19 27.749 12.396 -12.429 1.00 37.49 C
ATOM 132 C ALA A 19 27.311 10.947 -12.646 1.00 32.48 C
ATOM 133 O ALA A 19 27.111 10.527 -13.790 1.00 37.60 O
ATOM 134 CB ALA A 19 29.167 12.614 -12.962 1.00 49.51 C
ATOM 135 N HIS A 20 27.156 10.204 -11.569 1.00 25.28 N
ATOM 136 CA HIS A 20 26.775 8.793 -11.715 1.00 28.52 C
ATOM 137 C HIS A 20 25.263 8.634 -11.695 1.00 20.08 C
ATOM 138 O HIS A 20 24.786 7.495 -11.719 1.00 19.73 O
ATOM 139 CB HIS A 20 27.303 7.993 -10.540 1.00 36.91 C
ATOM 140 CG HIS A 20 28.839 8.000 -10.478 1.00 46.89 C
ATOM 141 ND1 HIS A 20 29.609 7.317 -11.420 1.00 48.79 N
ATOM 142 CD2 HIS A 20 29.672 8.623 -9.569 1.00 45.45 C
ATOM 143 CE1 HIS A 20 30.954 7.521 -11.090 1.00 57.52 C
ATOM 144 NE2 HIS A 20 30.992 8.330 -9.945 1.00 52.90 N
ATOM 145 N ALA A 21 24.583 9.762 -11.631 1.00 29.44 N
ATOM 146 CA ALA A 21 23.135 9.749 -11.417 1.00 31.12 C
ATOM 147 C ALA A 21 22.435 8.835 -12.425 1.00 32.96 C
ATOM 148 O ALA A 21 21.566 8.048 -12.037 1.00 27.04 O
ATOM 149 CB ALA A 21 22.593 11.179 -11.476 1.00 26.63 C
ATOM 150 N GLY A 22 22.850 8.925 -13.677 1.00 27.49 N
ATOM 151 CA GLY A 22 22.226 8.131 -14.747 1.00 20.97 C
ATOM 152 C GLY A 22 22.488 6.633 -14.565 1.00 31.36 C
ATOM 153 O GLY A 22 21.604 5.803 -14.800 1.00 29.56 O
ATOM 154 N GLU A 23 23.692 6.318 -14.152 1.00 25.05 N
ATOM 155 CA GLU A 23 24.091 4.921 -13.981 1.00 17.20 C
ATOM 156 C GLU A 23 23.314 4.327 -12.803 1.00 16.82 C
ATOM 157 O GLU A 23 22.919 3.155 -12.828 1.00 15.93 O
ATOM 158 CB GLU A 23 25.592 4.959 -13.713 1.00 27.91 C
ATOM 159 CG GLU A 23 26.308 3.619 -13.618 1.00 47.00 C
ATOM 160 CD GLU A 23 27.725 3.971 -13.173 1.00 75.01 C
ATOM 161 OE1 GLU A 23 28.156 3.483 -12.124 1.00 58.53 O
ATOM 162 OE2 GLU A 23 28.360 4.790 -13.847 1.00 53.65 O
ATOM 163 N TYR A 24 23.078 5.166 -11.803 1.00 18.93 N
ATOM 164 CA TYR A 24 22.375 4.686 -10.602 1.00 19.40 C
ATOM 165 C TYR A 24 20.891 4.535 -10.925 1.00 18.22 C
ATOM 166 O TYR A 24 20.227 3.652 -10.374 1.00 15.69 O
ATOM 167 CB TYR A 24 22.554 5.636 -9.409 1.00 18.39 C
ATOM 168 CG TYR A 24 23.992 5.730 -8.849 1.00 16.99 C
ATOM 169 CD1 TYR A 24 24.285 6.595 -7.809 1.00 27.04 C
ATOM 170 CD2 TYR A 24 24.996 4.952 -9.391 1.00 18.02 C
ATOM 171 CE1 TYR A 24 25.582 6.674 -7.304 1.00 27.21 C
ATOM 172 CE2 TYR A 24 26.286 5.025 -8.900 1.00 23.15 C
ATOM 173 CZ TYR A 24 26.589 5.890 -7.860 1.00 30.88 C
ATOM 174 OH TYR A 24 27.877 5.967 -7.375 1.00 32.52 O
ATOM 175 N GLY A 25 20.415 5.398 -11.809 1.00 16.11 N
ATOM 176 CA GLY A 25 19.009 5.348 -12.224 1.00 16.62 C
ATOM 177 C GLY A 25 18.729 4.022 -12.932 1.00 14.89 C
ATOM 178 O GLY A 25 17.694 3.392 -12.693 1.00 15.69 O
ATOM 179 N ALA A 26 19.662 3.613 -13.778 1.00 16.16 N
ATOM 180 CA ALA A 26 19.466 2.370 -14.535 1.00 12.73 C
ATOM 181 C ALA A 26 19.536 1.171 -13.591 1.00 13.25 C
ATOM 182 O ALA A 26 18.786 0.203 -13.756 1.00 13.50 O
ATOM 183 CB ALA A 26 20.541 2.239 -15.616 1.00 15.45 C
ATOM 184 N GLU A 27 20.433 1.269 -12.624 1.00 15.53 N
ATOM 185 CA GLU A 27 20.608 0.151 -11.695 1.00 17.09 C
ATOM 186 C GLU A 27 19.337 -0.022 -10.864 1.00 10.72 C
ATOM 187 O GLU A 27 18.894 -1.153 -10.644 1.00 13.03 O
ATOM 188 CB GLU A 27 21.812 0.400 -10.785 1.00 16.00 C
ATOM 189 CG GLU A 27 22.006 -0.753 -9.796 1.00 17.10 C
ATOM 190 CD GLU A 27 23.218 -0.493 -8.905 1.00 32.44 C
ATOM 191 OE1 GLU A 27 23.149 -0.780 -7.706 1.00 18.52 O
ATOM 192 OE2 GLU A 27 24.226 -0.012 -9.430 1.00 22.86 O
ATOM 193 N ALA A 28 18.774 1.099 -10.441 1.00 10.31 N
ATOM 194 CA ALA A 28 17.549 1.057 -9.635 1.00 12.12 C
ATOM 195 C ALA A 28 16.413 0.416 -10.431 1.00 14.08 C
ATOM 196 O ALA A 28 15.624 -0.347 -9.864 1.00 10.87 O
ATOM 197 CB ALA A 28 17.162 2.472 -9.207 1.00 15.79 C
ATOM 198 N LEU A 29 16.358 0.729 -11.719 1.00 13.33 N
ATOM 199 CA LEU A 29 15.308 0.145 -12.566 1.00 15.37 C
ATOM 200 C LEU A 29 15.493 -1.366 -12.644 1.00 9.48 C
ATOM 201 O LEU A 29 14.524 -2.114 -12.497 1.00 10.16 O
ATOM 202 CB LEU A 29 15.367 0.717 -13.981 1.00 13.97 C
ATOM 203 CG LEU A 29 14.877 2.160 -14.053 1.00 12.13 C
ATOM 204 CD1 LEU A 29 15.158 2.748 -15.433 1.00 17.48 C
ATOM 205 CD2 LEU A 29 13.392 2.268 -13.694 1.00 16.68 C
ATOM 206 N GLU A 30 16.729 -1.770 -12.868 1.00 13.29 N
ATOM 207 CA GLU A 30 17.005 -3.199 -13.017 1.00 15.75 C
ATOM 208 C GLU A 30 16.678 -3.929 -11.714 1.00 13.45 C
ATOM 209 O GLU A 30 16.147 -5.046 -11.746 1.00 14.64 O
ATOM 210 CB GLU A 30 18.468 -3.409 -13.410 1.00 19.99 C
ATOM 211 CG GLU A 30 18.806 -4.898 -13.484 1.00 27.81 C
ATOM 212 CD GLU A 30 20.188 -5.104 -14.094 1.00 39.82 C
ATOM 213 OE1 GLU A 30 20.926 -4.125 -14.238 1.00 38.30 O
ATOM 214 OE2 GLU A 30 20.509 -6.248 -14.430 1.00 42.30 O
ATOM 215 N ARG A 31 16.983 -3.278 -10.601 1.00 12.39 N
ATOM 216 CA ARG A 31 16.680 -3.889 -9.304 1.00 12.83 C
ATOM 217 C ARG A 31 15.167 -4.061 -9.174 1.00 16.49 C
ATOM 218 O ARG A 31 14.704 -5.098 -8.687 1.00 16.72 O
ATOM 219 CB ARG A 31 17.214 -3.027 -8.157 1.00 8.86 C
ATOM 220 CG ARG A 31 18.740 -3.081 -8.053 1.00 10.40 C
ATOM 221 CD ARG A 31 19.255 -2.241 -6.879 1.00 15.86 C
ATOM 222 NE ARG A 31 20.720 -2.316 -6.804 1.00 14.16 N
ATOM 223 CZ ARG A 31 21.367 -3.284 -6.161 1.00 9.91 C
ATOM 224 NH1 ARG A 31 20.728 -4.276 -5.554 1.00 11.66 N
ATOM 225 NH2 ARG A 31 22.686 -3.261 -6.141 1.00 15.56 N
ATOM 226 N MET A 32 14.443 -3.056 -9.642 1.00 11.83 N
ATOM 227 CA MET A 32 12.978 -3.070 -9.533 1.00 10.02 C
ATOM 228 C MET A 32 12.392 -4.184 -10.403 1.00 10.88 C
ATOM 229 O MET A 32 11.499 -4.902 -9.947 1.00 12.37 O
ATOM 230 CB MET A 32 12.411 -1.709 -9.952 1.00 9.58 C
ATOM 231 CG MET A 32 10.888 -1.643 -9.809 1.00 13.07 C
ATOM 232 SD MET A 32 10.214 -0.086 -10.427 1.00 16.77 S
ATOM 233 CE MET A 32 10.629 -0.261 -12.175 1.00 16.20 C
ATOM 234 N PHE A 33 12.900 -4.334 -11.619 1.00 14.27 N
ATOM 235 CA PHE A 33 12.322 -5.344 -12.527 1.00 12.02 C
ATOM 236 C PHE A 33 12.585 -6.759 -12.013 1.00 14.48 C
ATOM 237 O PHE A 33 11.777 -7.659 -12.258 1.00 16.35 O
ATOM 238 CB PHE A 33 12.900 -5.218 -13.938 1.00 8.98 C
ATOM 239 CG PHE A 33 12.556 -3.893 -14.643 1.00 12.35 C
ATOM 240 CD1 PHE A 33 11.284 -3.366 -14.547 1.00 16.53 C
ATOM 241 CD2 PHE A 33 13.523 -3.226 -15.370 1.00 17.05 C
ATOM 242 CE1 PHE A 33 10.970 -2.169 -15.180 1.00 14.75 C
ATOM 243 CE2 PHE A 33 13.222 -2.026 -16.007 1.00 17.11 C
ATOM 244 CZ PHE A 33 11.943 -1.494 -15.908 1.00 14.64 C
ATOM 245 N LEU A 34 13.694 -6.934 -11.314 1.00 14.55 N
ATOM 246 CA LEU A 34 14.025 -8.281 -10.823 1.00 13.82 C
ATOM 247 C LEU A 34 13.307 -8.579 -9.507 1.00 14.12 C
ATOM 248 O LEU A 34 12.857 -9.709 -9.294 1.00 18.60 O
ATOM 249 CB LEU A 34 15.533 -8.435 -10.599 1.00 15.66 C
ATOM 250 CG LEU A 34 16.343 -8.445 -11.897 1.00 27.18 C
ATOM 251 CD1 LEU A 34 17.835 -8.613 -11.604 1.00 27.92 C
ATOM 252 CD2 LEU A 34 15.858 -9.536 -12.853 1.00 40.26 C
ATOM 253 N SER A 35 13.212 -7.580 -8.645 1.00 13.39 N
ATOM 254 CA SER A 35 12.660 -7.820 -7.301 1.00 13.89 C
ATOM 255 C SER A 35 11.136 -7.791 -7.318 1.00 15.09 C
ATOM 256 O SER A 35 10.495 -8.493 -6.528 1.00 14.56 O
ATOM 257 CB SER A 35 13.140 -6.749 -6.320 1.00 13.65 C
ATOM 258 OG SER A 35 14.540 -6.872 -6.101 1.00 18.50 O
ATOM 259 N PHE A 36 10.597 -6.960 -8.199 1.00 14.68 N
ATOM 260 CA PHE A 36 9.137 -6.759 -8.291 1.00 14.24 C
ATOM 261 C PHE A 36 8.677 -6.864 -9.743 1.00 12.48 C
ATOM 262 O PHE A 36 8.434 -5.837 -10.384 1.00 13.97 O
ATOM 263 CB PHE A 36 8.785 -5.364 -7.762 1.00 14.16 C
ATOM 264 CG PHE A 36 9.369 -5.110 -6.361 1.00 16.87 C
ATOM 265 CD1 PHE A 36 10.418 -4.228 -6.193 1.00 15.89 C
ATOM 266 CD2 PHE A 36 8.841 -5.769 -5.267 1.00 19.99 C
ATOM 267 CE1 PHE A 36 10.949 -4.001 -4.927 1.00 19.19 C
ATOM 268 CE2 PHE A 36 9.362 -5.551 -3.997 1.00 16.46 C
ATOM 269 CZ PHE A 36 10.422 -4.668 -3.827 1.00 16.23 C
ATOM 270 N PRO A 37 8.560 -8.084 -10.231 1.00 17.38 N
ATOM 271 CA PRO A 37 8.342 -8.369 -11.658 1.00 20.47 C
ATOM 272 C PRO A 37 7.040 -7.759 -12.185 1.00 16.11 C
ATOM 273 O PRO A 37 6.891 -7.596 -13.399 1.00 16.28 O
ATOM 274 CB PRO A 37 8.346 -9.891 -11.808 1.00 21.78 C
ATOM 275 CG PRO A 37 8.469 -10.483 -10.407 1.00 27.10 C
ATOM 276 CD PRO A 37 8.780 -9.325 -9.465 1.00 21.92 C
ATOM 277 N THR A 38 6.129 -7.421 -11.287 1.00 15.75 N
ATOM 278 CA THR A 38 4.849 -6.856 -11.722 1.00 16.17 C
ATOM 279 C THR A 38 5.080 -5.493 -12.385 1.00 15.75 C
ATOM 280 O THR A 38 4.280 -5.059 -13.218 1.00 13.69 O
ATOM 281 CB THR A 38 3.912 -6.758 -10.515 1.00 12.96 C
ATOM 282 OG1 THR A 38 4.341 -5.713 -9.652 1.00 19.48 O
ATOM 283 CG2 THR A 38 3.887 -8.079 -9.739 1.00 40.10 C
ATOM 284 N THR A 39 6.188 -4.849 -12.038 1.00 14.32 N
ATOM 285 CA THR A 39 6.476 -3.521 -12.607 1.00 10.80 C
ATOM 286 C THR A 39 6.833 -3.620 -14.092 1.00 9.13 C
ATOM 287 O THR A 39 6.765 -2.618 -14.811 1.00 14.55 O
ATOM 288 CB THR A 39 7.604 -2.828 -11.832 1.00 13.34 C
ATOM 289 OG1 THR A 39 8.813 -3.571 -11.945 1.00 11.05 O
ATOM 290 CG2 THR A 39 7.248 -2.659 -10.355 1.00 14.53 C
ATOM 291 N LYS A 40 7.191 -4.808 -14.546 1.00 11.25 N
ATOM 292 CA LYS A 40 7.553 -4.934 -15.967 1.00 15.31 C
ATOM 293 C LYS A 40 6.335 -4.786 -16.880 1.00 15.15 C
ATOM 294 O LYS A 40 6.504 -4.650 -18.096 1.00 14.13 O
ATOM 295 CB LYS A 40 8.101 -6.315 -16.271 1.00 13.81 C
ATOM 296 CG LYS A 40 9.387 -6.733 -15.579 1.00 15.86 C
ATOM 297 CD LYS A 40 9.516 -8.182 -16.019 1.00 24.17 C
ATOM 298 CE LYS A 40 10.498 -9.049 -15.255 1.00 37.24 C
ATOM 299 NZ LYS A 40 10.315 -10.402 -15.792 1.00 23.57 N
ATOM 300 N THR A 41 5.141 -4.839 -16.299 1.00 15.14 N
ATOM 301 CA THR A 41 3.927 -4.747 -17.127 1.00 16.60 C
ATOM 302 C THR A 41 3.812 -3.357 -17.757 1.00 21.59 C
ATOM 303 O THR A 41 3.009 -3.159 -18.673 1.00 20.09 O
ATOM 304 CB THR A 41 2.663 -5.035 -16.307 1.00 13.85 C
ATOM 305 OG1 THR A 41 2.548 -4.073 -15.269 1.00 13.72 O
ATOM 306 CG2 THR A 41 2.642 -6.442 -15.704 1.00 14.43 C
ATOM 307 N TYR A 42 4.605 -2.413 -17.279 1.00 12.01 N
ATOM 308 CA TYR A 42 4.518 -1.055 -17.836 1.00 10.16 C
ATOM 309 C TYR A 42 5.562 -0.852 -18.925 1.00 9.08 C
ATOM 310 O TYR A 42 5.556 0.181 -19.605 1.00 13.30 O
ATOM 311 CB TYR A 42 4.728 -0.013 -16.743 1.00 13.24 C
ATOM 312 CG TYR A 42 3.563 -0.024 -15.742 1.00 14.81 C
ATOM 313 CD1 TYR A 42 2.396 0.652 -16.039 1.00 15.89 C
ATOM 314 CD2 TYR A 42 3.677 -0.710 -14.550 1.00 12.80 C
ATOM 315 CE1 TYR A 42 1.335 0.647 -15.142 1.00 16.51 C
ATOM 316 CE2 TYR A 42 2.625 -0.724 -13.645 1.00 12.40 C
ATOM 317 CZ TYR A 42 1.450 -0.045 -13.940 1.00 16.06 C
ATOM 318 OH TYR A 42 0.403 -0.058 -13.048 1.00 15.27 O
ATOM 319 N PHE A 43 6.432 -1.836 -19.071 1.00 12.81 N
ATOM 320 CA PHE A 43 7.479 -1.702 -20.098 1.00 14.00 C
ATOM 321 C PHE A 43 7.496 -2.865 -21.098 1.00 19.95 C
ATOM 322 O PHE A 43 8.570 -3.434 -21.320 1.00 18.41 O
ATOM 323 CB PHE A 43 8.835 -1.620 -19.382 1.00 19.60 C
ATOM 324 CG PHE A 43 9.002 -0.400 -18.448 1.00 15.31 C
ATOM 325 CD1 PHE A 43 8.564 -0.454 -17.137 1.00 17.25 C
ATOM 326 CD2 PHE A 43 9.586 0.758 -18.921 1.00 14.22 C
ATOM 327 CE1 PHE A 43 8.714 0.641 -16.292 1.00 18.88 C
ATOM 328 CE2 PHE A 43 9.744 1.861 -18.088 1.00 18.09 C
ATOM 329 CZ PHE A 43 9.301 1.804 -16.771 1.00 14.99 C
ATOM 330 N PRO A 44 6.370 -3.232 -21.729 1.00 18.18 N
ATOM 331 CA PRO A 44 6.334 -4.397 -22.635 1.00 22.79 C
ATOM 332 C PRO A 44 7.096 -4.100 -23.930 1.00 21.86 C
ATOM 333 O PRO A 44 7.467 -5.016 -24.668 1.00 24.57 O
ATOM 334 CB PRO A 44 4.848 -4.655 -22.902 1.00 28.58 C
ATOM 335 CG PRO A 44 4.191 -3.293 -22.739 1.00 29.41 C
ATOM 336 CD PRO A 44 5.017 -2.623 -21.649 1.00 20.66 C
ATOM 337 N HIS A 45 7.345 -2.826 -24.169 1.00 21.80 N
ATOM 338 CA HIS A 45 7.962 -2.357 -25.415 1.00 27.70 C
ATOM 339 C HIS A 45 9.472 -2.188 -25.252 1.00 32.41 C
ATOM 340 O HIS A 45 10.151 -1.728 -26.177 1.00 27.78 O
ATOM 341 CB HIS A 45 7.333 -1.019 -25.816 1.00 31.60 C
ATOM 342 CG HIS A 45 7.413 0.099 -24.748 1.00 27.93 C
ATOM 343 ND1 HIS A 45 6.887 -0.041 -23.455 1.00 26.95 N
ATOM 344 CD2 HIS A 45 7.974 1.365 -24.847 1.00 28.94 C
ATOM 345 CE1 HIS A 45 7.126 1.144 -22.745 1.00 33.80 C
ATOM 346 NE2 HIS A 45 7.800 2.018 -23.607 1.00 32.08 N
ATOM 347 N PHE A 46 9.985 -2.564 -24.088 1.00 20.23 N
ATOM 348 CA PHE A 46 11.432 -2.435 -23.847 1.00 16.01 C
ATOM 349 C PHE A 46 12.129 -3.790 -23.869 1.00 20.59 C
ATOM 350 O PHE A 46 11.544 -4.820 -23.525 1.00 21.01 O
ATOM 351 CB PHE A 46 11.715 -1.860 -22.457 1.00 22.14 C
ATOM 352 CG PHE A 46 11.773 -0.329 -22.306 1.00 19.36 C
ATOM 353 CD1 PHE A 46 12.516 0.227 -21.282 1.00 25.66 C
ATOM 354 CD2 PHE A 46 11.093 0.494 -23.181 1.00 26.05 C
ATOM 355 CE1 PHE A 46 12.578 1.607 -21.123 1.00 22.11 C
ATOM 356 CE2 PHE A 46 11.147 1.875 -23.033 1.00 31.47 C
ATOM 357 CZ PHE A 46 11.895 2.434 -22.005 1.00 27.18 C
ATOM 358 N ASP A 47 13.376 -3.735 -24.268 1.00 21.55 N
ATOM 359 CA ASP A 47 14.290 -4.839 -24.019 1.00 18.87 C
ATOM 360 C ASP A 47 14.743 -4.651 -22.571 1.00 19.07 C
ATOM 361 O ASP A 47 15.442 -3.686 -22.262 1.00 19.65 O
ATOM 362 CB ASP A 47 15.475 -4.720 -24.980 1.00 26.30 C
ATOM 363 CG ASP A 47 16.459 -5.875 -24.805 1.00 35.07 C
ATOM 364 OD1 ASP A 47 16.185 -6.784 -24.016 1.00 35.11 O
ATOM 365 OD2 ASP A 47 17.497 -5.859 -25.475 1.00 42.93 O
ATOM 366 N LEU A 48 14.326 -5.541 -21.698 1.00 23.64 N
ATOM 367 CA LEU A 48 14.678 -5.353 -20.284 1.00 20.62 C
ATOM 368 C LEU A 48 15.871 -6.226 -19.906 1.00 29.20 C
ATOM 369 O LEU A 48 16.082 -6.484 -18.716 1.00 35.13 O
ATOM 370 CB LEU A 48 13.504 -5.731 -19.379 1.00 19.03 C
ATOM 371 CG LEU A 48 12.274 -4.841 -19.568 1.00 23.12 C
ATOM 372 CD1 LEU A 48 11.099 -5.353 -18.733 1.00 31.43 C
ATOM 373 CD2 LEU A 48 12.577 -3.377 -19.241 1.00 21.67 C
ATOM 374 N SER A 49 16.634 -6.671 -20.897 1.00 34.97 N
ATOM 375 CA SER A 49 17.773 -7.517 -20.525 1.00 33.47 C
ATOM 376 C SER A 49 18.866 -6.631 -19.932 1.00 29.45 C
ATOM 377 O SER A 49 18.865 -5.409 -20.127 1.00 24.29 O
ATOM 378 CB SER A 49 18.291 -8.358 -21.699 1.00 30.63 C
ATOM 379 OG SER A 49 18.598 -7.535 -22.818 1.00 37.11 O
ATOM 380 N HIS A 50 19.751 -7.270 -19.192 1.00 31.85 N
ATOM 381 CA HIS A 50 20.777 -6.497 -18.516 1.00 31.35 C
ATOM 382 C HIS A 50 21.609 -5.728 -19.546 1.00 25.68 C
ATOM 383 O HIS A 50 22.179 -6.304 -20.480 1.00 29.85 O
ATOM 384 CB HIS A 50 21.657 -7.415 -17.653 1.00 41.89 C
ATOM 385 CG HIS A 50 22.822 -6.669 -16.940 1.00 34.16 C
ATOM 386 ND1 HIS A 50 23.564 -7.201 -15.880 1.00 46.57 N
ATOM 387 CD2 HIS A 50 23.350 -5.417 -17.203 1.00 49.98 C
ATOM 388 CE1 HIS A 50 24.516 -6.225 -15.503 1.00 43.13 C
ATOM 389 NE2 HIS A 50 24.366 -5.127 -16.346 1.00 49.17 N
ATOM 390 N GLY A 51 21.630 -4.423 -19.336 1.00 24.31 N
ATOM 391 CA GLY A 51 22.630 -3.570 -19.979 1.00 34.51 C
ATOM 392 C GLY A 51 22.000 -2.921 -21.196 1.00 29.12 C
ATOM 393 O GLY A 51 22.683 -2.246 -21.972 1.00 29.64 O
ATOM 394 N SER A 52 20.713 -3.157 -21.315 1.00 29.81 N
ATOM 395 CA SER A 52 19.977 -2.649 -22.471 1.00 27.68 C
ATOM 396 C SER A 52 20.002 -1.118 -22.513 1.00 25.49 C
ATOM 397 O SER A 52 19.845 -0.445 -21.488 1.00 26.33 O
ATOM 398 CB SER A 52 18.547 -3.163 -22.407 1.00 32.19 C
ATOM 399 OG SER A 52 17.665 -2.050 -22.491 1.00 24.51 O
ATOM 400 N ALA A 53 20.229 -0.617 -23.716 1.00 23.66 N
ATOM 401 CA ALA A 53 20.311 0.826 -23.967 1.00 29.92 C
ATOM 402 C ALA A 53 19.009 1.518 -23.564 1.00 21.14 C
ATOM 403 O ALA A 53 19.040 2.668 -23.118 1.00 18.73 O
ATOM 404 CB ALA A 53 20.590 1.079 -25.451 1.00 38.93 C
ATOM 405 N GLN A 54 17.900 0.813 -23.730 1.00 22.73 N
ATOM 406 CA GLN A 54 16.593 1.400 -23.402 1.00 21.48 C
ATOM 407 C GLN A 54 16.499 1.669 -21.903 1.00 22.47 C
ATOM 408 O GLN A 54 16.000 2.723 -21.494 1.00 20.16 O
ATOM 409 CB GLN A 54 15.461 0.470 -23.845 1.00 18.50 C
ATOM 410 CG GLN A 54 15.176 0.622 -25.341 1.00 24.89 C
ATOM 411 CD GLN A 54 14.228 -0.475 -25.825 1.00 19.21 C
ATOM 412 OE1 GLN A 54 14.488 -1.656 -25.592 1.00 25.94 O
ATOM 413 NE2 GLN A 54 13.173 -0.078 -26.519 1.00 30.39 N
ATOM 414 N VAL A 55 16.991 0.721 -21.128 1.00 18.42 N
ATOM 415 CA VAL A 55 16.910 0.869 -19.673 1.00 20.22 C
ATOM 416 C VAL A 55 17.910 1.930 -19.217 1.00 15.83 C
ATOM 417 O VAL A 55 17.584 2.739 -18.343 1.00 17.42 O
ATOM 418 CB VAL A 55 17.164 -0.481 -18.994 1.00 15.63 C