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HEADER TRANSFERASE 17-OCT-03 1V2X
TITLE TRMH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA (GM18) METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.1.34;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACUROVIRUS
KEYWDS DEEP TREFOIL KNOT, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, STRUCTURAL GENOMICS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.NUREKI,K.WATANABE,S.FUKAI,R.ISHII,Y.ENDO,H.HORI,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 13-JUL-11 1V2X 1 VERSN
REVDAT 2 24-FEB-09 1V2X 1 VERSN
REVDAT 1 04-MAY-04 1V2X 0
JRNL AUTH O.NUREKI,K.WATANABE,S.FUKAI,R.ISHII,Y.ENDO,H.HORI,S.YOKOYAMA
JRNL TITL DEEP KNOT STRUCTURE FOR CONSTRUCTION OF ACTIVE SITE AND
JRNL TITL 2 COFACTOR BINDING SITE OF TRNA MODIFICATION ENZYME
JRNL REF STRUCTURE V. 12 593 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15062082
JRNL DOI 10.1016/J.STR.2004.03.003
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1127109.350
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 24289
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2399
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3172
REMARK 3 BIN R VALUE (WORKING SET) : 0.5380
REMARK 3 BIN FREE R VALUE : 0.5330
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 362
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1530
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.86000
REMARK 3 B22 (A**2) : 13.51000
REMARK 3 B33 (A**2) : -6.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.38000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.57
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.00
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.14
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.720 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.540 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.700 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 85.94
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : SAM2.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : SAM2.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V2X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-03.
REMARK 100 THE RCSB ID CODE IS RCSB006139.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60955
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 26.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, TRIS-HCL, PEG 4000,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 20K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.80050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.01150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.80050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.01150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A 192
REMARK 465 ARG A 193
REMARK 465 LYS A 194
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 OE2 GLU A 91 O HOH A 538 2.04
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 HOH A 503 O HOH A 503 2656 1.59
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 GLY A 68 N - CA - C ANGL. DEV. = -21.3 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 ALA A 7 -87.44 -102.70
REMARK 500 THR A 57 57.68 38.19
REMARK 500 ASN A 64 -62.65 -171.12
REMARK 500 GLU A 65 -109.72 -61.95
REMARK 500 THR A 66 -172.71 -61.58
REMARK 500 SER A 67 101.43 115.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 532 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH A 562 DISTANCE = 5.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000912.1 RELATED DB: TARGETDB
DBREF 1V2X A 1 194 UNP Q9FAC4 Q9FAC4_THETH 1 194
SEQRES 1 A 194 MET ARG GLU ARG THR GLU ALA ARG ARG ARG ARG ILE GLU
SEQRES 2 A 194 GLU VAL LEU ARG ARG ARG GLN PRO ASP LEU THR VAL LEU
SEQRES 3 A 194 LEU GLU ASN VAL HIS LYS PRO HIS ASN LEU SER ALA ILE
SEQRES 4 A 194 LEU ARG THR CYS ASP ALA VAL GLY VAL LEU GLU ALA HIS
SEQRES 5 A 194 ALA VAL ASN PRO THR GLY GLY VAL PRO THR PHE ASN GLU
SEQRES 6 A 194 THR SER GLY GLY SER HIS LYS TRP VAL TYR LEU ARG VAL
SEQRES 7 A 194 HIS PRO ASP LEU HIS GLU ALA PHE ARG PHE LEU LYS GLU
SEQRES 8 A 194 ARG GLY PHE THR VAL TYR ALA THR ALA LEU ARG GLU ASP
SEQRES 9 A 194 ALA ARG ASP PHE ARG GLU VAL ASP TYR THR LYS PRO THR
SEQRES 10 A 194 ALA VAL LEU PHE GLY ALA GLU LYS TRP GLY VAL SER GLU
SEQRES 11 A 194 GLU ALA LEU ALA LEU ALA ASP GLY ALA ILE LYS ILE PRO
SEQRES 12 A 194 MET LEU GLY MET VAL GLN SER LEU ASN VAL SER VAL ALA
SEQRES 13 A 194 ALA ALA VAL ILE LEU PHE GLU ALA GLN ARG GLN ARG LEU
SEQRES 14 A 194 LYS ALA GLY LEU TYR ASP ARG PRO ARG LEU ASP PRO GLU
SEQRES 15 A 194 LEU TYR GLN LYS VAL LEU ALA ASP TRP LEU ARG LYS
HET PO4 A 201 5
HET PO4 A 202 5
HET SAM A 400 27
HETNAM PO4 PHOSPHATE ION
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 SAM C15 H22 N6 O5 S
FORMUL 5 HOH *190(H2 O)
HELIX 1 1 ALA A 7 ARG A 17 1 11
HELIX 2 2 LYS A 32 VAL A 46 1 15
HELIX 3 3 PRO A 56 VAL A 60 5 5
HELIX 4 4 GLY A 69 TRP A 73 5 5
HELIX 5 5 ASP A 81 ARG A 92 1 12
HELIX 6 6 ARG A 109 VAL A 111 5 3
HELIX 7 7 SER A 129 ALA A 136 1 8
HELIX 8 8 ASN A 152 ALA A 171 1 20
HELIX 9 9 GLY A 172 ARG A 176 5 5
HELIX 10 10 ASP A 180 TRP A 191 1 12
SHEET 1 A 7 TYR A 75 HIS A 79 0
SHEET 2 A 7 GLU A 50 VAL A 54 1 N ALA A 51 O TYR A 75
SHEET 3 A 7 LEU A 23 GLU A 28 1 N LEU A 27 O HIS A 52
SHEET 4 A 7 THR A 117 PHE A 121 1 O PHE A 121 N LEU A 26
SHEET 5 A 7 THR A 95 THR A 99 1 N TYR A 97 O LEU A 120
SHEET 6 A 7 GLY A 138 LYS A 141 1 O GLY A 138 N ALA A 98
SHEET 7 A 7 ARG A 106 ASP A 107 1 N ARG A 106 O LYS A 141
SITE 1 AC1 10 LYS A 32 HIS A 34 ASN A 35 ARG A 41
SITE 2 AC1 10 GLU A 65 THR A 66 GLU A 124 ASN A 152
SITE 3 AC1 10 HOH A 419 HOH A 464
SITE 1 AC2 8 ARG A 9 GLU A 13 ASN A 29 HIS A 31
SITE 2 AC2 8 ASN A 55 GLY A 58 HOH A 408 HOH A 483
SITE 1 AC3 18 ARG A 41 THR A 99 PHE A 121 GLY A 122
SITE 2 AC3 18 ALA A 123 GLU A 124 LYS A 125 TRP A 126
SITE 3 AC3 18 GLY A 127 ILE A 142 MET A 144 LEU A 151
SITE 4 AC3 18 VAL A 153 ALA A 156 HOH A 442 HOH A 561
SITE 5 AC3 18 HOH A 568 HOH A 583
CRYST1 77.601 44.023 56.756 90.00 120.78 90.00 C 1 2 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 0.012886 0.000000 0.007675 0.00000
SCALE2 0.000000 0.022715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020507 0.00000
ATOM 1 N MET A 1 38.675 -3.951 7.508 1.00 84.76 N
ATOM 2 CA MET A 1 38.426 -3.041 8.667 1.00 85.22 C
ATOM 3 C MET A 1 37.378 -1.974 8.369 1.00 84.29 C
ATOM 4 O MET A 1 36.484 -1.733 9.182 1.00 84.63 O
ATOM 5 CB MET A 1 39.723 -2.350 9.094 1.00 86.84 C
ATOM 6 CG MET A 1 39.518 -1.300 10.178 1.00 88.84 C
ATOM 7 SD MET A 1 40.968 -0.265 10.459 1.00 94.09 S
ATOM 8 CE MET A 1 41.568 -0.924 12.032 1.00 92.99 C
ATOM 9 N ARG A 2 37.492 -1.321 7.215 1.00 81.45 N
ATOM 10 CA ARG A 2 36.528 -0.288 6.869 1.00 79.57 C
ATOM 11 C ARG A 2 35.290 -0.943 6.258 1.00 79.10 C
ATOM 12 O ARG A 2 34.217 -0.348 6.202 1.00 81.03 O
ATOM 13 CB ARG A 2 37.138 0.733 5.895 1.00 77.44 C
ATOM 14 CG ARG A 2 38.558 1.192 6.221 1.00 72.71 C
ATOM 15 CD ARG A 2 38.840 1.289 7.723 1.00 71.34 C
ATOM 16 NE ARG A 2 37.884 2.121 8.450 1.00 68.82 N
ATOM 17 CZ ARG A 2 38.030 2.485 9.725 1.00 65.65 C
ATOM 18 NH1 ARG A 2 39.092 2.096 10.420 1.00 62.32 N
ATOM 19 NH2 ARG A 2 37.112 3.239 10.309 1.00 61.59 N
ATOM 20 N GLU A 3 35.435 -2.179 5.804 1.00 77.28 N
ATOM 21 CA GLU A 3 34.302 -2.891 5.233 1.00 76.88 C
ATOM 22 C GLU A 3 33.391 -3.231 6.420 1.00 75.41 C
ATOM 23 O GLU A 3 32.159 -3.210 6.333 1.00 73.32 O
ATOM 24 CB GLU A 3 34.789 -4.170 4.542 1.00 79.80 C
ATOM 25 CG GLU A 3 35.945 -3.973 3.532 1.00 81.63 C
ATOM 26 CD GLU A 3 37.297 -3.665 4.187 1.00 82.08 C
ATOM 27 OE1 GLU A 3 37.719 -4.421 5.092 1.00 80.21 O
ATOM 28 OE2 GLU A 3 37.943 -2.672 3.783 1.00 80.66 O
ATOM 29 N ARG A 4 34.040 -3.521 7.540 1.00 74.79 N
ATOM 30 CA ARG A 4 33.389 -3.870 8.792 1.00 73.42 C
ATOM 31 C ARG A 4 32.779 -2.641 9.468 1.00 73.71 C
ATOM 32 O ARG A 4 31.713 -2.709 10.083 1.00 72.31 O
ATOM 33 CB ARG A 4 34.432 -4.527 9.715 1.00 71.82 C
ATOM 34 CG ARG A 4 34.146 -4.467 11.209 1.00 73.57 C
ATOM 35 CD ARG A 4 32.851 -5.176 11.535 1.00 76.96 C
ATOM 36 NE ARG A 4 32.782 -5.665 12.909 1.00 80.38 N
ATOM 37 CZ ARG A 4 31.858 -6.519 13.343 1.00 81.40 C
ATOM 38 NH1 ARG A 4 30.933 -6.975 12.506 1.00 80.52 N
ATOM 39 NH2 ARG A 4 31.856 -6.918 14.609 1.00 82.09 N
ATOM 40 N THR A 5 33.451 -1.507 9.331 1.00 73.92 N
ATOM 41 CA THR A 5 32.989 -0.295 9.977 1.00 74.33 C
ATOM 42 C THR A 5 32.423 0.728 8.978 1.00 75.05 C
ATOM 43 O THR A 5 31.271 1.145 9.091 1.00 73.60 O
ATOM 44 CB THR A 5 34.161 0.286 10.841 1.00 74.08 C
ATOM 45 OG1 THR A 5 33.645 1.121 11.888 1.00 73.16 O
ATOM 46 CG2 THR A 5 35.143 1.048 9.976 1.00 73.26 C
ATOM 47 N GLU A 6 33.215 1.098 7.981 1.00 76.28 N
ATOM 48 CA GLU A 6 32.783 2.079 6.991 1.00 76.89 C
ATOM 49 C GLU A 6 31.492 1.671 6.302 1.00 74.43 C
ATOM 50 O GLU A 6 30.738 2.523 5.850 1.00 75.87 O
ATOM 51 CB GLU A 6 33.889 2.286 5.950 1.00 80.23 C
ATOM 52 CG GLU A 6 33.729 3.507 5.065 1.00 84.19 C
ATOM 53 CD GLU A 6 34.994 3.799 4.271 1.00 88.16 C
ATOM 54 OE1 GLU A 6 36.091 3.763 4.881 1.00 88.44 O
ATOM 55 OE2 GLU A 6 34.896 4.070 3.048 1.00 89.13 O
ATOM 56 N ALA A 7 31.220 0.376 6.235 1.00 71.16 N
ATOM 57 CA ALA A 7 30.011 -0.070 5.560 1.00 68.96 C
ATOM 58 C ALA A 7 28.875 -0.471 6.492 1.00 66.16 C
ATOM 59 O ALA A 7 28.010 0.339 6.818 1.00 66.67 O
ATOM 60 CB ALA A 7 30.342 -1.222 4.615 1.00 70.14 C
ATOM 61 N ARG A 8 28.883 -1.735 6.900 1.00 62.64 N
ATOM 62 CA ARG A 8 27.861 -2.280 7.770 1.00 57.57 C
ATOM 63 C ARG A 8 27.549 -1.313 8.906 1.00 54.41 C
ATOM 64 O ARG A 8 26.414 -0.871 9.063 1.00 51.34 O
ATOM 65 CB ARG A 8 28.333 -3.620 8.335 1.00 59.14 C
ATOM 66 CG ARG A 8 27.227 -4.446 8.950 1.00 64.14 C
ATOM 67 CD ARG A 8 27.776 -5.602 9.780 1.00 69.31 C
ATOM 68 NE ARG A 8 26.713 -6.257 10.544 1.00 75.84 N
ATOM 69 CZ ARG A 8 26.863 -6.744 11.775 1.00 78.24 C
ATOM 70 NH1 ARG A 8 28.038 -6.654 12.390 1.00 77.74 N
ATOM 71 NH2 ARG A 8 25.834 -7.307 12.399 1.00 78.35 N
ATOM 72 N ARG A 9 28.579 -0.983 9.679 1.00 49.26 N
ATOM 73 CA ARG A 9 28.468 -0.088 10.819 1.00 45.92 C
ATOM 74 C ARG A 9 27.772 1.243 10.503 1.00 44.95 C
ATOM 75 O ARG A 9 26.800 1.604 11.161 1.00 43.13 O
ATOM 76 CB ARG A 9 29.867 0.164 11.396 1.00 50.29 C
ATOM 77 CG ARG A 9 29.917 1.146 12.561 1.00 52.28 C
ATOM 78 CD ARG A 9 28.731 0.932 13.476 1.00 53.65 C
ATOM 79 NE ARG A 9 28.633 1.953 14.515 1.00 55.52 N
ATOM 80 CZ ARG A 9 29.197 1.856 15.715 1.00 49.64 C
ATOM 81 NH1 ARG A 9 29.909 0.781 16.039 1.00 51.27 N
ATOM 82 NH2 ARG A 9 29.019 2.825 16.599 1.00 44.10 N
ATOM 83 N ARG A 10 28.271 1.952 9.496 1.00 43.09 N
ATOM 84 CA ARG A 10 27.734 3.254 9.081 1.00 45.92 C
ATOM 85 C ARG A 10 26.319 3.198 8.498 1.00 44.70 C
ATOM 86 O ARG A 10 25.482 4.033 8.849 1.00 43.48 O
ATOM 87 CB ARG A 10 28.705 3.917 8.077 1.00 50.32 C
ATOM 88 CG ARG A 10 28.084 4.590 6.824 1.00 59.45 C
ATOM 89 CD ARG A 10 29.200 4.832 5.773 1.00 64.04 C
ATOM 90 NE ARG A 10 28.777 5.385 4.479 1.00 66.70 N
ATOM 91 CZ ARG A 10 29.476 5.239 3.345 1.00 68.68 C
ATOM 92 NH1 ARG A 10 30.616 4.554 3.349 1.00 66.26 N
ATOM 93 NH2 ARG A 10 29.056 5.789 2.208 1.00 64.08 N
ATOM 94 N ARG A 11 26.035 2.238 7.618 1.00 38.64 N
ATOM 95 CA ARG A 11 24.691 2.165 7.049 1.00 41.27 C
ATOM 96 C ARG A 11 23.637 1.798 8.102 1.00 38.54 C
ATOM 97 O ARG A 11 22.528 2.320 8.081 1.00 38.07 O
ATOM 98 CB ARG A 11 24.613 1.156 5.891 1.00 44.36 C
ATOM 99 CG ARG A 11 24.113 -0.215 6.299 1.00 46.81 C
ATOM 100 CD ARG A 11 23.512 -0.969 5.130 1.00 51.67 C
ATOM 101 NE ARG A 11 22.149 -0.534 4.854 1.00 54.89 N
ATOM 102 CZ ARG A 11 21.371 -1.077 3.923 1.00 54.23 C
ATOM 103 NH1 ARG A 11 21.831 -2.074 3.177 1.00 54.26 N
ATOM 104 NH2 ARG A 11 20.128 -0.638 3.751 1.00 50.76 N
ATOM 105 N ILE A 12 23.976 0.903 9.024 1.00 35.78 N
ATOM 106 CA ILE A 12 23.032 0.510 10.058 1.00 33.08 C
ATOM 107 C ILE A 12 22.679 1.682 10.993 1.00 32.47 C
ATOM 108 O ILE A 12 21.529 1.838 11.430 1.00 28.01 O
ATOM 109 CB ILE A 12 23.605 -0.649 10.917 1.00 34.55 C
ATOM 110 CG1 ILE A 12 23.574 -1.965 10.133 1.00 40.53 C
ATOM 111 CG2 ILE A 12 22.842 -0.737 12.222 1.00 37.99 C
ATOM 112 CD1 ILE A 12 24.319 -3.122 10.815 1.00 38.68 C
ATOM 113 N GLU A 13 23.670 2.500 11.320 1.00 23.17 N
ATOM 114 CA GLU A 13 23.403 3.600 12.227 1.00 24.61 C
ATOM 115 C GLU A 13 22.610 4.623 11.467 1.00 19.11 C
ATOM 116 O GLU A 13 21.725 5.254 12.030 1.00 22.14 O
ATOM 117 CB GLU A 13 24.695 4.249 12.709 1.00 25.31 C
ATOM 118 CG GLU A 13 25.423 3.509 13.766 1.00 31.74 C
ATOM 119 CD GLU A 13 26.328 4.443 14.556 1.00 32.12 C
ATOM 120 OE1 GLU A 13 25.807 5.301 15.316 1.00 39.28 O
ATOM 121 OE2 GLU A 13 27.548 4.315 14.395 1.00 36.46 O
ATOM 122 N GLU A 14 22.932 4.798 10.196 1.00 22.01 N
ATOM 123 CA GLU A 14 22.204 5.770 9.386 1.00 28.73 C
ATOM 124 C GLU A 14 20.714 5.476 9.458 1.00 30.75 C
ATOM 125 O GLU A 14 19.897 6.380 9.635 1.00 28.44 O
ATOM 126 CB GLU A 14 22.665 5.756 7.931 1.00 32.02 C
ATOM 127 CG GLU A 14 22.762 7.158 7.357 1.00 45.05 C
ATOM 128 CD GLU A 14 22.215 7.276 5.948 1.00 52.72 C
ATOM 129 OE1 GLU A 14 22.571 8.255 5.249 1.00 56.73 O
ATOM 130 OE2 GLU A 14 21.425 6.400 5.539 1.00 55.24 O
ATOM 131 N VAL A 15 20.363 4.207 9.321 1.00 25.66 N
ATOM 132 CA VAL A 15 18.980 3.784 9.394 1.00 29.14 C
ATOM 133 C VAL A 15 18.404 3.867 10.809 1.00 24.53 C
ATOM 134 O VAL A 15 17.239 4.239 11.008 1.00 22.52 O
ATOM 135 CB VAL A 15 18.859 2.339 8.881 1.00 34.08 C
ATOM 136 CG1 VAL A 15 17.462 1.806 9.101 1.00 34.56 C
ATOM 137 CG2 VAL A 15 19.253 2.303 7.438 1.00 35.69 C
ATOM 138 N LEU A 16 19.227 3.540 11.811 1.00 17.74 N
ATOM 139 CA LEU A 16 18.770 3.594 13.181 1.00 18.79 C
ATOM 140 C LEU A 16 18.405 5.034 13.531 1.00 18.81 C
ATOM 141 O LEU A 16 17.514 5.291 14.348 1.00 22.04 O
ATOM 142 CB LEU A 16 19.890 3.139 14.110 1.00 23.63 C
ATOM 143 CG LEU A 16 19.564 2.229 15.269 1.00 31.06 C
ATOM 144 CD1 LEU A 16 20.711 2.281 16.290 1.00 29.86 C
ATOM 145 CD2 LEU A 16 18.255 2.621 15.871 1.00 33.39 C
ATOM 146 N ARG A 17 19.107 5.960 12.898 1.00 20.63 N
ATOM 147 CA ARG A 17 18.888 7.390 13.140 1.00 21.39 C
ATOM 148 C ARG A 17 17.569 7.908 12.581 1.00 26.11 C
ATOM 149 O ARG A 17 17.144 9.023 12.900 1.00 19.17 O
ATOM 150 CB ARG A 17 20.071 8.201 12.586 1.00 20.97 C
ATOM 151 CG ARG A 17 21.355 8.101 13.417 1.00 22.48 C
ATOM 152 CD ARG A 17 22.488 8.785 12.694 1.00 24.33 C
ATOM 153 NE ARG A 17 22.454 10.242 12.877 1.00 33.19 N
ATOM 154 CZ ARG A 17 22.870 10.864 13.983 1.00 33.42 C
ATOM 155 NH1 ARG A 17 23.352 10.169 15.002 1.00 33.56 N
ATOM 156 NH2 ARG A 17 22.781 12.186 14.080 1.00 39.29 N
ATOM 157 N ARG A 18 16.911 7.111 11.743 1.00 22.34 N
ATOM 158 CA ARG A 18 15.621 7.501 11.200 1.00 19.84 C
ATOM 159 C ARG A 18 14.490 6.717 11.901 1.00 17.86 C
ATOM 160 O ARG A 18 13.340 6.888 11.562 1.00 20.45 O
ATOM 161 CB ARG A 18 15.542 7.245 9.669 1.00 20.57 C
ATOM 162 CG ARG A 18 16.309 8.236 8.838 1.00 25.28 C
ATOM 163 CD ARG A 18 16.476 7.775 7.409 1.00 33.31 C
ATOM 164 NE ARG A 18 17.691 8.380 6.865 1.00 38.10 N
ATOM 165 CZ ARG A 18 18.489 7.777 5.997 1.00 36.79 C
ATOM 166 NH1 ARG A 18 18.199 6.550 5.573 1.00 40.73 N
ATOM 167 NH2 ARG A 18 19.574 8.395 5.558 1.00 48.32 N
ATOM 168 N ARG A 19 14.802 5.864 12.869 1.00 21.21 N
ATOM 169 CA ARG A 19 13.740 5.108 13.532 1.00 17.90 C
ATOM 170 C ARG A 19 12.824 5.997 14.368 1.00 20.34 C
ATOM 171 O ARG A 19 13.307 6.876 15.082 1.00 23.48 O
ATOM 172 CB ARG A 19 14.326 4.002 14.399 1.00 17.30 C
ATOM 173 CG ARG A 19 14.784 2.778 13.575 1.00 20.84 C
ATOM 174 CD ARG A 19 13.594 2.190 12.867 1.00 21.17 C
ATOM 175 NE ARG A 19 13.661 0.746 12.524 1.00 16.48 N
ATOM 176 CZ ARG A 19 13.661 0.295 11.267 1.00 24.05 C
ATOM 177 NH1 ARG A 19 13.668 1.126 10.227 1.00 14.90 N
ATOM 178 NH2 ARG A 19 13.478 -0.991 11.020 1.00 13.79 N
ATOM 179 N GLN A 20 11.511 5.768 14.272 1.00 17.75 N
ATOM 180 CA GLN A 20 10.502 6.576 14.965 1.00 16.99 C
ATOM 181 C GLN A 20 9.953 5.750 16.133 1.00 19.66 C
ATOM 182 O GLN A 20 9.263 4.743 15.913 1.00 22.08 O
ATOM 183 CB GLN A 20 9.349 6.917 14.000 1.00 19.26 C
ATOM 184 CG GLN A 20 9.804 7.542 12.679 1.00 21.25 C
ATOM 185 CD GLN A 20 10.314 8.920 12.891 1.00 22.26 C
ATOM 186 OE1 GLN A 20 9.585 9.796 13.349 1.00 24.72 O
ATOM 187 NE2 GLN A 20 11.578 9.120 12.602 1.00 20.63 N
ATOM 188 N PRO A 21 10.260 6.133 17.377 1.00 18.57 N
ATOM 189 CA PRO A 21 9.747 5.348 18.501 1.00 21.55 C
ATOM 190 C PRO A 21 8.263 5.630 18.767 1.00 23.71 C
ATOM 191 O PRO A 21 7.604 4.871 19.479 1.00 21.74 O
ATOM 192 CB PRO A 21 10.638 5.793 19.653 1.00 23.71 C
ATOM 193 CG PRO A 21 10.708 7.328 19.353 1.00 19.94 C
ATOM 194 CD PRO A 21 11.004 7.323 17.866 1.00 21.94 C
ATOM 195 N ASP A 22 7.726 6.687 18.146 1.00 17.61 N
ATOM 196 CA ASP A 22 6.361 7.056 18.381 1.00 21.15 C
ATOM 197 C ASP A 22 5.442 6.930 17.166 1.00 18.86 C
ATOM 198 O ASP A 22 4.536 7.740 16.999 1.00 18.45 O
ATOM 199 CB ASP A 22 6.314 8.487 18.930 1.00 21.42 C
ATOM 200 CG ASP A 22 7.064 9.450 18.063 1.00 29.96 C
ATOM 201 OD1 ASP A 22 7.758 9.000 17.113 1.00 23.69 O
ATOM 202 OD2 ASP A 22 6.966 10.678 18.327 1.00 28.45 O
ATOM 203 N LEU A 23 5.696 5.940 16.301 1.00 18.21 N
ATOM 204 CA LEU A 23 4.830 5.670 15.148 1.00 16.35 C
ATOM 205 C LEU A 23 4.787 4.143 15.128 1.00 15.55 C
ATOM 206 O LEU A 23 5.823 3.510 15.097 1.00 17.64 O
ATOM 207 CB LEU A 23 5.453 6.138 13.861 1.00 14.56 C
ATOM 208 CG LEU A 23 4.612 5.790 12.622 1.00 15.53 C
ATOM 209 CD1 LEU A 23 3.253 6.413 12.692 1.00 17.26 C
ATOM 210 CD2 LEU A 23 5.374 6.224 11.380 1.00 16.66 C
ATOM 211 N THR A 24 3.604 3.585 15.184 1.00 15.79 N
ATOM 212 CA THR A 24 3.519 2.116 15.193 1.00 17.26 C
ATOM 213 C THR A 24 2.165 1.631 14.681 1.00 16.58 C
ATOM 214 O THR A 24 1.280 2.405 14.347 1.00 16.64 O
ATOM 215 CB THR A 24 3.759 1.582 16.654 1.00 17.19 C
ATOM 216 OG1 THR A 24 3.890 0.142 16.628 1.00 18.69 O
ATOM 217 CG2 THR A 24 2.630 1.931 17.561 1.00 15.18 C
ATOM 218 N VAL A 25 2.002 0.305 14.623 1.00 15.18 N
ATOM 219 CA VAL A 25 0.768 -0.299 14.220 1.00 13.88 C
ATOM 220 C VAL A 25 0.394 -1.364 15.258 1.00 16.91 C
ATOM 221 O VAL A 25 1.278 -1.917 15.963 1.00 17.96 O
ATOM 222 CB VAL A 25 0.854 -1.009 12.825 1.00 18.34 C
ATOM 223 CG1 VAL A 25 1.203 0.022 11.749 1.00 19.74 C
ATOM 224 CG2 VAL A 25 1.845 -2.182 12.852 1.00 20.69 C
ATOM 225 N LEU A 26 -0.907 -1.576 15.400 1.00 15.18 N
ATOM 226 CA LEU A 26 -1.416 -2.657 16.261 1.00 17.20 C
ATOM 227 C LEU A 26 -2.195 -3.593 15.325 1.00 15.85 C
ATOM 228 O LEU A 26 -3.209 -3.216 14.727 1.00 16.07 O
ATOM 229 CB LEU A 26 -2.312 -2.126 17.383 1.00 17.29 C
ATOM 230 CG LEU A 26 -2.971 -3.230 18.266 1.00 17.59 C
ATOM 231 CD1 LEU A 26 -1.936 -4.262 18.749 1.00 20.56 C
ATOM 232 CD2 LEU A 26 -3.630 -2.566 19.447 1.00 22.53 C
ATOM 233 N LEU A 27 -1.725 -4.837 15.204 1.00 17.95 N
ATOM 234 CA LEU A 27 -2.374 -5.802 14.318 1.00 18.92 C
ATOM 235 C LEU A 27 -3.268 -6.737 15.143 1.00 19.52 C
ATOM 236 O LEU A 27 -2.769 -7.435 15.985 1.00 18.69 O
ATOM 237 CB LEU A 27 -1.301 -6.617 13.582 1.00 17.80 C
ATOM 238 CG LEU A 27 -0.233 -5.754 12.903 1.00 16.09 C
ATOM 239 CD1 LEU A 27 0.737 -6.691 12.110 1.00 18.59 C
ATOM 240 CD2 LEU A 27 -0.904 -4.759 11.930 1.00 18.98 C
ATOM 241 N GLU A 28 -4.575 -6.709 14.900 1.00 23.31 N
ATOM 242 CA GLU A 28 -5.508 -7.540 15.656 1.00 21.90 C
ATOM 243 C GLU A 28 -5.914 -8.746 14.830 1.00 20.88 C
ATOM 244 O GLU A 28 -6.601 -8.618 13.835 1.00 20.40 O
ATOM 245 CB GLU A 28 -6.769 -6.749 16.014 1.00 22.57 C
ATOM 246 CG GLU A 28 -7.782 -7.600 16.824 1.00 19.92 C
ATOM 247 CD GLU A 28 -9.123 -6.947 17.047 1.00 21.97 C
ATOM 248 OE1 GLU A 28 -9.669 -6.364 16.086 1.00 22.46 O
ATOM 249 OE2 GLU A 28 -9.660 -7.046 18.183 1.00 25.61 O
ATOM 250 N ASN A 29 -5.500 -9.925 15.256 1.00 17.58 N
ATOM 251 CA ASN A 29 -5.883 -11.104 14.524 1.00 21.78 C
ATOM 252 C ASN A 29 -5.541 -11.139 13.044 1.00 20.12 C
ATOM 253 O ASN A 29 -6.392 -11.571 12.228 1.00 24.04 O
ATOM 254 CB ASN A 29 -7.383 -11.284 14.624 1.00 27.20 C
ATOM 255 CG ASN A 29 -7.743 -12.348 15.559 1.00 41.52 C
ATOM 256 OD1 ASN A 29 -7.834 -12.123 16.772 1.00 43.19 O
ATOM 257 ND2 ASN A 29 -7.928 -13.554 15.023 1.00 39.52 N
ATOM 258 N VAL A 30 -4.353 -10.684 12.666 1.00 18.92 N
ATOM 259 CA VAL A 30 -4.002 -10.754 11.270 1.00 20.20 C
ATOM 260 C VAL A 30 -3.473 -12.151 11.144 1.00 18.71 C
ATOM 261 O VAL A 30 -2.447 -12.479 11.726 1.00 25.06 O
ATOM 262 CB VAL A 30 -2.962 -9.701 10.914 1.00 22.69 C
ATOM 263 CG1 VAL A 30 -2.427 -9.947 9.524 1.00 22.80 C
ATOM 264 CG2 VAL A 30 -3.629 -8.343 11.000 1.00 19.31 C
ATOM 265 N HIS A 31 -4.205 -12.941 10.352 1.00 22.21 N
ATOM 266 CA HIS A 31 -3.960 -14.377 10.162 1.00 26.30 C
ATOM 267 C HIS A 31 -2.927 -14.879 9.162 1.00 28.33 C
ATOM 268 O HIS A 31 -2.286 -15.892 9.412 1.00 23.96 O
ATOM 269 CB HIS A 31 -5.299 -15.040 9.787 1.00 31.35 C
ATOM 270 CG HIS A 31 -5.537 -16.344 10.470 1.00 48.31 C
ATOM 271 ND1 HIS A 31 -4.670 -17.410 10.364 1.00 52.48 N
ATOM 272 CD2 HIS A 31 -6.526 -16.744 11.307 1.00 55.45 C
ATOM 273 CE1 HIS A 31 -5.110 -18.407 11.111 1.00 55.65 C
ATOM 274 NE2 HIS A 31 -6.234 -18.031 11.694 1.00 53.48 N
ATOM 275 N LYS A 32 -2.778 -14.195 8.023 1.00 24.89 N
ATOM 276 CA LYS A 32 -1.879 -14.673 6.985 1.00 21.25 C
ATOM 277 C LYS A 32 -0.436 -14.264 7.110 1.00 23.89 C
ATOM 278 O LYS A 32 -0.132 -13.069 7.200 1.00 23.79 O
ATOM 279 CB LYS A 32 -2.400 -14.258 5.603 1.00 17.05 C
ATOM 280 CG LYS A 32 -3.886 -14.579 5.406 1.00 26.75 C
ATOM 281 CD LYS A 32 -4.314 -14.498 3.954 1.00 28.33 C
ATOM 282 CE LYS A 32 -5.821 -14.818 3.780 1.00 28.13 C
ATOM 283 NZ LYS A 32 -6.232 -14.800 2.353 1.00 30.41 N
ATOM 284 N PRO A 33 0.482 -15.233 7.132 1.00 22.08 N
ATOM 285 CA PRO A 33 1.906 -14.886 7.238 1.00 22.63 C
ATOM 286 C PRO A 33 2.320 -13.877 6.155 1.00 22.63 C
ATOM 287 O PRO A 33 3.143 -12.981 6.420 1.00 20.56 O
ATOM 288 CB PRO A 33 2.606 -16.243 7.071 1.00 25.24 C
ATOM 289 CG PRO A 33 1.627 -17.181 7.688 1.00 28.57 C
ATOM 290 CD PRO A 33 0.298 -16.702 7.162 1.00 25.85 C
ATOM 291 N HIS A 34 1.765 -13.989 4.940 1.00 19.37 N
ATOM 292 CA HIS A 34 2.185 -13.018 3.928 1.00 17.18 C
ATOM 293 C HIS A 34 1.769 -11.586 4.285 1.00 17.92 C
ATOM 294 O HIS A 34 2.448 -10.671 3.894 1.00 21.72 O
ATOM 295 CB HIS A 34 1.756 -13.393 2.486 1.00 24.79 C
ATOM 296 CG HIS A 34 0.315 -13.191 2.166 1.00 32.43 C
ATOM 297 ND1 HIS A 34 -0.528 -14.244 1.879 1.00 36.88 N
ATOM 298 CD2 HIS A 34 -0.407 -12.065 1.961 1.00 27.63 C
ATOM 299 CE1 HIS A 34 -1.708 -13.775 1.509 1.00 28.16 C
ATOM 300 NE2 HIS A 34 -1.661 -12.455 1.553 1.00 33.98 N
ATOM 301 N ASN A 35 0.670 -11.410 5.004 1.00 20.69 N
ATOM 302 CA ASN A 35 0.251 -10.050 5.397 1.00 22.20 C
ATOM 303 C ASN A 35 1.122 -9.564 6.541 1.00 21.00 C
ATOM 304 O ASN A 35 1.555 -8.400 6.564 1.00 23.54 O
ATOM 305 CB ASN A 35 -1.211 -10.063 5.807 1.00 21.24 C
ATOM 306 CG ASN A 35 -2.146 -10.181 4.615 1.00 19.10 C
ATOM 307 OD1 ASN A 35 -3.216 -10.810 4.708 1.00 23.67 O
ATOM 308 ND2 ASN A 35 -1.768 -9.560 3.503 1.00 18.46 N
ATOM 309 N LEU A 36 1.382 -10.437 7.495 1.00 22.13 N
ATOM 310 CA LEU A 36 2.233 -10.034 8.624 1.00 21.67 C
ATOM 311 C LEU A 36 3.620 -9.649 8.118 1.00 21.15 C
ATOM 312 O LEU A 36 4.177 -8.629 8.513 1.00 21.54 O
ATOM 313 CB LEU A 36 2.362 -11.170 9.645 1.00 19.68 C
ATOM 314 CG LEU A 36 3.345 -10.897 10.802 1.00 24.96 C
ATOM 315 CD1 LEU A 36 2.853 -9.631 11.612 1.00 20.95 C
ATOM 316 CD2 LEU A 36 3.438 -12.089 11.754 1.00 21.18 C
ATOM 317 N SER A 37 4.193 -10.478 7.243 1.00 19.33 N
ATOM 318 CA SER A 37 5.510 -10.207 6.722 1.00 22.29 C
ATOM 319 C SER A 37 5.513 -8.928 5.914 1.00 20.52 C
ATOM 320 O SER A 37 6.411 -8.105 6.113 1.00 20.77 O
ATOM 321 CB SER A 37 6.046 -11.357 5.855 1.00 25.49 C
ATOM 322 OG SER A 37 6.233 -12.544 6.627 1.00 27.87 O
ATOM 323 N ALA A 38 4.528 -8.747 5.019 1.00 17.82 N
ATOM 324 CA ALA A 38 4.511 -7.508 4.206 1.00 18.39 C
ATOM 325 C ALA A 38 4.313 -6.253 5.051 1.00 15.30 C
ATOM 326 O ALA A 38 4.877 -5.198 4.717 1.00 18.91 O
ATOM 327 CB ALA A 38 3.402 -7.567 3.105 1.00 19.68 C
ATOM 328 N ILE A 39 3.521 -6.355 6.111 1.00 15.83 N
ATOM 329 CA ILE A 39 3.273 -5.175 6.967 1.00 16.33 C
ATOM 330 C ILE A 39 4.555 -4.807 7.748 1.00 17.25 C
ATOM 331 O ILE A 39 4.926 -3.624 7.894 1.00 15.29 O
ATOM 332 CB ILE A 39 2.109 -5.422 7.915 1.00 15.40 C
ATOM 333 CG1 ILE A 39 0.820 -5.533 7.117 1.00 13.19 C
ATOM 334 CG2 ILE A 39 2.056 -4.302 8.993 1.00 14.67 C
ATOM 335 CD1 ILE A 39 -0.311 -6.107 7.958 1.00 16.87 C
ATOM 336 N LEU A 40 5.262 -5.798 8.255 1.00 17.18 N
ATOM 337 CA LEU A 40 6.522 -5.473 8.936 1.00 18.75 C
ATOM 338 C LEU A 40 7.547 -4.855 7.952 1.00 17.45 C
ATOM 339 O LEU A 40 8.310 -3.977 8.339 1.00 18.16 O
ATOM 340 CB LEU A 40 7.122 -6.724 9.580 1.00 23.34 C
ATOM 341 CG LEU A 40 6.406 -7.215 10.819 1.00 28.78 C
ATOM 342 CD1 LEU A 40 7.197 -8.389 11.382 1.00 25.61 C
ATOM 343 CD2 LEU A 40 6.322 -6.079 11.872 1.00 18.74 C
ATOM 344 N ARG A 41 7.578 -5.315 6.685 1.00 16.32 N
ATOM 345 CA ARG A 41 8.488 -4.778 5.679 1.00 14.10 C
ATOM 346 C ARG A 41 8.114 -3.271 5.452 1.00 11.50 C
ATOM 347 O ARG A 41 8.980 -2.406 5.373 1.00 16.80 O
ATOM 348 CB ARG A 41 8.344 -5.598 4.405 1.00 18.88 C
ATOM 349 CG ARG A 41 9.301 -5.350 3.298 1.00 20.28 C
ATOM 350 CD ARG A 41 9.163 -6.577 2.331 1.00 26.33 C
ATOM 351 NE ARG A 41 9.756 -6.380 1.009 1.00 35.06 N
ATOM 352 CZ ARG A 41 9.575 -7.220 -0.021 1.00 40.17 C
ATOM 353 NH1 ARG A 41 8.822 -8.312 0.124 1.00 33.97 N
ATOM 354 NH2 ARG A 41 10.109 -6.957 -1.213 1.00 27.47 N
ATOM 355 N THR A 42 6.813 -3.013 5.392 1.00 13.77 N
ATOM 356 CA THR A 42 6.315 -1.633 5.250 1.00 14.57 C
ATOM 357 C THR A 42 6.720 -0.836 6.503 1.00 18.52 C
ATOM 358 O THR A 42 7.156 0.346 6.416 1.00 14.63 O
ATOM 359 CB THR A 42 4.777 -1.639 5.083 1.00 18.33 C
ATOM 360 OG1 THR A 42 4.443 -2.258 3.824 1.00 18.25 O
ATOM 361 CG2 THR A 42 4.218 -0.193 5.092 1.00 16.59 C
ATOM 362 N CYS A 43 6.566 -1.431 7.682 1.00 15.78 N
ATOM 363 CA CYS A 43 6.978 -0.731 8.928 1.00 15.09 C
ATOM 364 C CYS A 43 8.454 -0.342 8.823 1.00 16.04 C
ATOM 365 O CYS A 43 8.855 0.790 9.127 1.00 16.63 O
ATOM 366 CB CYS A 43 6.759 -1.646 10.149 1.00 18.83 C
ATOM 367 SG CYS A 43 5.068 -1.809 10.656 1.00 18.30 S
ATOM 368 N ASP A 44 9.301 -1.274 8.403 1.00 16.65 N
ATOM 369 CA ASP A 44 10.733 -0.953 8.266 1.00 16.39 C
ATOM 370 C ASP A 44 10.963 0.245 7.316 1.00 19.40 C
ATOM 371 O ASP A 44 11.728 1.181 7.610 1.00 18.69 O
ATOM 372 CB ASP A 44 11.506 -2.124 7.682 1.00 17.75 C
ATOM 373 CG ASP A 44 12.961 -1.760 7.390 1.00 18.02 C
ATOM 374 OD1 ASP A 44 13.762 -1.616 8.353 1.00 17.17 O
ATOM 375 OD2 ASP A 44 13.308 -1.606 6.197 1.00 21.93 O
ATOM 376 N ALA A 45 10.286 0.212 6.185 1.00 16.64 N
ATOM 377 CA ALA A 45 10.431 1.267 5.172 1.00 14.64 C
ATOM 378 C ALA A 45 10.068 2.672 5.657 1.00 18.62 C
ATOM 379 O ALA A 45 10.594 3.651 5.124 1.00 17.91 O
ATOM 380 CB ALA A 45 9.592 0.902 3.910 1.00 18.33 C
ATOM 381 N VAL A 46 9.151 2.776 6.618 1.00 17.24 N
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--> maximum size reached
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