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HEADER IMMUNE SYSTEM 05-JAN-00 1DQZ
TITLE CRYSTAL STRUCTURE OF ANTIGEN 85C FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIGEN 85-C;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 85C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA
KEYWDS ANTIGEN, 85C, MYCOBACTERIUM TUBERCULOSIS, FIBRONECTIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.RONNING,T.KLABUNDE,J.C.SACCHETTINI
REVDAT 1 12-JUL-00 1DQZ 0
JRNL AUTH D.R.RONNING,T.KLABUNDE,G.S.BESRA,V.D.VISSA,
JRNL AUTH 2 J.T.BELISLE,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURE OF THE SECRETED FORM OF ANTIGEN
JRNL TITL 2 85C REVEALS POTENTIAL TARGETS FOR MYCOBACTERIAL
JRNL TITL 3 DRUGS AND VACCINES
JRNL REF NAT.STRUCT.BIOL. V. 7 141 2000
JRNL REFN ASTM NSBIEW US ISSN 1072-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 104747
REMARK 3
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) : 0.166
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.200
REMARK 3 FREE R VALUE TEST SET COUNT : 10476
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 : 4362
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 581
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) : -2.60400
REMARK 3 B22 (A**2) : 1.94700
REMARK 3 B33 (A**2) : 0.65600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.70
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
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DQZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-2000.
REMARK 100 THE RCSB ID CODE IS RCSB010311.
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) : M
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 : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
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 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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 33.85900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.69400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.97350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.69400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.85900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.97350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET B 692 CE MET B 692 SD 0.091
REMARK 500 PRO B 755 CG PRO B 755 CB 0.101
REMARK 500 PRO B 763 CG PRO B 763 CB 0.091
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN B 552 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 LYS B 611 CD - CE - NZ ANGL. DEV. =-10.8 DEGREES
REMARK 500 LEU B 651 N - CA - C ANGL. DEV. = 10.2 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 86 137.50 -44.73
REMARK 500 SER B 586 135.44 -41.59
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 1475 DISTANCE = 5.07 ANGSTROMS
REMARK 525 0 HOH 1568 DISTANCE = 6.40 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DQY RELATED DB: PDB
DBREF 1DQZ A 3 282 SWS P31953 A85C_MYCTU 49 328
DBREF 1DQZ B 503 782 SWS P31953 A85C_MYCTU 49 328
SEQADV 1DQZ SER A 156 SWS P31953 GLY 202 CONFLICT
SEQADV 1DQZ SER B 656 SWS P31953 GLY 202 CONFLICT
SEQRES 1 A 280 ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN VAL PRO SER
SEQRES 2 A 280 ALA SER MET GLY ARG ASP ILE LYS VAL GLN PHE GLN GLY
SEQRES 3 A 280 GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP GLY LEU ARG
SEQRES 4 A 280 ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE ASN THR PRO
SEQRES 5 A 280 ALA PHE GLU GLU TYR TYR GLN SER GLY LEU SER VAL ILE
SEQRES 6 A 280 MET PRO VAL GLY GLY GLN SER SER PHE TYR THR ASP TRP
SEQRES 7 A 280 TYR GLN PRO SER GLN SER ASN GLY GLN ASN TYR THR TYR
SEQRES 8 A 280 LYS TRP GLU THR PHE LEU THR ARG GLU MET PRO ALA TRP
SEQRES 9 A 280 LEU GLN ALA ASN LYS GLY VAL SER PRO THR GLY ASN ALA
SEQRES 10 A 280 ALA VAL GLY LEU SER MET SER GLY GLY SER ALA LEU ILE
SEQRES 11 A 280 LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO TYR ALA ALA
SEQRES 12 A 280 SER LEU SER GLY PHE LEU ASN PRO SER GLU SER TRP TRP
SEQRES 13 A 280 PRO THR LEU ILE GLY LEU ALA MET ASN ASP SER GLY GLY
SEQRES 14 A 280 TYR ASN ALA ASN SER MET TRP GLY PRO SER SER ASP PRO
SEQRES 15 A 280 ALA TRP LYS ARG ASN ASP PRO MET VAL GLN ILE PRO ARG
SEQRES 16 A 280 LEU VAL ALA ASN ASN THR ARG ILE TRP VAL TYR CYS GLY
SEQRES 17 A 280 ASN GLY THR PRO SER ASP LEU GLY GLY ASP ASN ILE PRO
SEQRES 18 A 280 ALA LYS PHE LEU GLU GLY LEU THR LEU ARG THR ASN GLN
SEQRES 19 A 280 THR PHE ARG ASP THR TYR ALA ALA ASP GLY GLY ARG ASN
SEQRES 20 A 280 GLY VAL PHE ASN PHE PRO PRO ASN GLY THR HIS SER TRP
SEQRES 21 A 280 PRO TYR TRP ASN GLU GLN LEU VAL ALA MET LYS ALA ASP
SEQRES 22 A 280 ILE GLN HIS VAL LEU ASN GLY
SEQRES 1 B 280 ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN VAL PRO SER
SEQRES 2 B 280 ALA SER MET GLY ARG ASP ILE LYS VAL GLN PHE GLN GLY
SEQRES 3 B 280 GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP GLY LEU ARG
SEQRES 4 B 280 ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE ASN THR PRO
SEQRES 5 B 280 ALA PHE GLU GLU TYR TYR GLN SER GLY LEU SER VAL ILE
SEQRES 6 B 280 MET PRO VAL GLY GLY GLN SER SER PHE TYR THR ASP TRP
SEQRES 7 B 280 TYR GLN PRO SER GLN SER ASN GLY GLN ASN TYR THR TYR
SEQRES 8 B 280 LYS TRP GLU THR PHE LEU THR ARG GLU MET PRO ALA TRP
SEQRES 9 B 280 LEU GLN ALA ASN LYS GLY VAL SER PRO THR GLY ASN ALA
SEQRES 10 B 280 ALA VAL GLY LEU SER MET SER GLY GLY SER ALA LEU ILE
SEQRES 11 B 280 LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO TYR ALA ALA
SEQRES 12 B 280 SER LEU SER GLY PHE LEU ASN PRO SER GLU SER TRP TRP
SEQRES 13 B 280 PRO THR LEU ILE GLY LEU ALA MET ASN ASP SER GLY GLY
SEQRES 14 B 280 TYR ASN ALA ASN SER MET TRP GLY PRO SER SER ASP PRO
SEQRES 15 B 280 ALA TRP LYS ARG ASN ASP PRO MET VAL GLN ILE PRO ARG
SEQRES 16 B 280 LEU VAL ALA ASN ASN THR ARG ILE TRP VAL TYR CYS GLY
SEQRES 17 B 280 ASN GLY THR PRO SER ASP LEU GLY GLY ASP ASN ILE PRO
SEQRES 18 B 280 ALA LYS PHE LEU GLU GLY LEU THR LEU ARG THR ASN GLN
SEQRES 19 B 280 THR PHE ARG ASP THR TYR ALA ALA ASP GLY GLY ARG ASN
SEQRES 20 B 280 GLY VAL PHE ASN PHE PRO PRO ASN GLY THR HIS SER TRP
SEQRES 21 B 280 PRO TYR TRP ASN GLU GLN LEU VAL ALA MET LYS ALA ASP
SEQRES 22 B 280 ILE GLN HIS VAL LEU ASN GLY
FORMUL 3 HOH *581(H2 O1)
HELIX 1 1 ASN A 47 THR A 53 1 7
HELIX 2 2 PRO A 54 TYR A 60 1 7
HELIX 3 3 LYS A 94 ARG A 101 1 8
HELIX 4 4 ARG A 101 GLY A 112 1 12
HELIX 5 5 SER A 124 TYR A 137 1 14
HELIX 6 6 TRP A 157 SER A 169 1 13
HELIX 7 7 ASN A 173 GLY A 179 1 7
HELIX 8 8 ASP A 183 ASN A 189 1 7
HELIX 9 9 GLN A 194 ASN A 202 1 9
HELIX 10 10 ASN A 221 ASP A 245 1 25
HELIX 11 11 SER A 261 MET A 272 1 12
HELIX 12 12 MET A 272 GLY A 282 1 11
HELIX 13 13 ASN B 547 THR B 553 1 7
HELIX 14 14 PRO B 554 TYR B 560 1 7
HELIX 15 15 LYS B 594 ARG B 601 1 8
HELIX 16 16 ARG B 601 GLY B 612 1 12
HELIX 17 17 SER B 624 TYR B 637 1 14
HELIX 18 18 TRP B 657 SER B 669 1 13
HELIX 19 19 ASN B 673 GLY B 679 1 7
HELIX 20 20 PRO B 684 ASN B 689 1 6
HELIX 21 21 GLN B 694 ASN B 701 1 8
HELIX 22 22 ASN B 721 ASP B 745 1 25
HELIX 23 23 SER B 761 GLY B 782 1 22
SHEET 1 A 8 VAL A 8 SER A 15 0
SHEET 2 A 8 ARG A 20 GLN A 27 -1 O ARG A 20 N SER A 15
SHEET 3 A 8 SER A 65 PRO A 69 -1 N VAL A 66 O GLN A 27
SHEET 4 A 8 ALA A 33 LEU A 36 1 O VAL A 34 N ILE A 67
SHEET 5 A 8 ALA A 119 LEU A 123 1 O ALA A 119 N TYR A 35
SHEET 6 A 8 TYR A 143 LEU A 147 1 O TYR A 143 N ALA A 120
SHEET 7 A 8 ARG A 204 TYR A 208 1 O ARG A 204 N ALA A 144
SHEET 8 A 8 GLY A 250 ASN A 253 1 O VAL A 251 N VAL A 207
SHEET 1 B 8 GLU B 509 SER B 515 0
SHEET 2 B 8 ARG B 520 GLN B 527 -1 O ARG B 520 N SER B 515
SHEET 3 B 8 SER B 565 PRO B 569 -1 N VAL B 566 O GLN B 527
SHEET 4 B 8 ALA B 533 LEU B 536 1 O VAL B 534 N ILE B 567
SHEET 5 B 8 ALA B 619 LEU B 623 1 O ALA B 619 N TYR B 535
SHEET 6 B 8 TYR B 643 LEU B 647 1 O TYR B 643 N ALA B 620
SHEET 7 B 8 ARG B 704 TYR B 708 1 O ARG B 704 N ALA B 644
SHEET 8 B 8 GLY B 750 ASN B 753 1 O VAL B 751 N VAL B 707
CISPEP 1 LEU B 506 PRO B 507 0 0.05
CRYST1 67.718 75.947 137.388 90.00 90.00 90.00 P 21 21 21 8
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 0.014767 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013167 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007279 0.00000
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