| content |
HEADER HYDROLASE 21-JUN-06 2HDW
TITLE CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN PA2218 FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PA2218;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS PA2218, ALPHA/BETA HYDROLASE FOLD, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NEW YORK STRUCTURAL GENOMIX
KEYWDS 3 RESEARCH CONSORTIUM, NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,U.RAMAGOPAL,S.C.ALMO,S.K.BURLEY,NEW
AUTHOR 2 YORK STRUCTURAL GENOMIX RESEARCH CONSORTIUM (NYSGXRC)
REVDAT 1 28-NOV-06 2HDW 0
JRNL AUTH A.A.FEDOROV,E.V.FEDOROV,U.RAMAGOPAL,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN PA2218
JRNL TITL 2 FROM PSEUDOMONAS AERUGINOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.100
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 261609.240
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 37451
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) : 0.198
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1904
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3491
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 187
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5027
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 6.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.50000
REMARK 3 B22 (A**2) : -7.37000
REMARK 3 B33 (A**2) : -2.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.08
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.86
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) : 1.090 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.530 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.530 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 41.99
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 : 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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HDW COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-18)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .
REMARK 100 THE RCSB ID CODE IS RCSB038239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979, 0.97934, 0.97911,
REMARK 200 0.97166
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : 37451
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
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: 20% PEG3350, 0.1M BIS-TRIS, 0.1M
REMARK 280 NACL, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 68.16850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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
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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 HIS A 5
REMARK 465 SER A 6
REMARK 465 ASN A 7
REMARK 465 ARG A 8
REMARK 465 ALA A 9
REMARK 465 ARG A 10
REMARK 465 SER A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
REMARK 465 GLY A 14
REMARK 465 ALA A 15
REMARK 465 LEU A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 VAL A 20
REMARK 465 LEU A 21
REMARK 465 ALA A 22
REMARK 465 GLY A 23
REMARK 465 ALA A 24
REMARK 465 LEU A 25
REMARK 465 MET A 26
REMARK 465 ALA A 27
REMARK 465 LEU A 28
REMARK 465 VAL A 29
REMARK 465 GLY A 30
REMARK 465 CYS A 31
REMARK 465 GLN A 32
REMARK 465 THR A 33
REMARK 465 SER A 34
REMARK 465 PRO A 35
REMARK 465 ALA A 36
REMARK 465 ALA A 37
REMARK 465 THR A 38
REMARK 465 THR A 39
REMARK 465 SER A 40
REMARK 465 SER A 41
REMARK 465 ASN A 42
REMARK 465 THR A 43
REMARK 465 GLY A 44
REMARK 465 GLY A 45
REMARK 465 THR A 46
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 LYS B 4
REMARK 465 HIS B 5
REMARK 465 SER B 6
REMARK 465 ASN B 7
REMARK 465 ARG B 8
REMARK 465 ALA B 9
REMARK 465 ARG B 10
REMARK 465 SER B 11
REMARK 465 ARG B 12
REMARK 465 LYS B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LEU B 16
REMARK 465 ARG B 17
REMARK 465 GLY B 18
REMARK 465 ALA B 19
REMARK 465 VAL B 20
REMARK 465 LEU B 21
REMARK 465 ALA B 22
REMARK 465 GLY B 23
REMARK 465 ALA B 24
REMARK 465 LEU B 25
REMARK 465 MET B 26
REMARK 465 ALA B 27
REMARK 465 LEU B 28
REMARK 465 VAL B 29
REMARK 465 GLY B 30
REMARK 465 CYS B 31
REMARK 465 GLN B 32
REMARK 465 THR B 33
REMARK 465 SER B 34
REMARK 465 PRO B 35
REMARK 465 ALA B 36
REMARK 465 ALA B 37
REMARK 465 THR B 38
REMARK 465 THR B 39
REMARK 465 SER B 40
REMARK 465 SER B 41
REMARK 465 ASN B 42
REMARK 465 THR B 43
REMARK 465 GLY B 44
REMARK 465 GLY B 45
REMARK 465 THR B 46
REMARK 465 ASN B 47
REMARK 465 MET B 48
REMARK 465 GLN B 49
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 A 120 SD MET A 120 CE -0.093
REMARK 500 MET A 203 CG MET A 203 SD 0.043
REMARK 500 MET A 206 CG MET A 206 SD 0.042
REMARK 500 MET A 210 SD MET A 210 CE -0.046
REMARK 500 MET A 268 SD MET A 268 CE 0.040
REMARK 500 MET A 293 SD MET A 293 CE -0.051
REMARK 500 MET B 120 SD MET B 120 CE -0.152
REMARK 500 MET B 203 CG MET B 203 SD 0.047
REMARK 500 MET B 286 SD MET B 286 CE -0.048
REMARK 500 MET B 293 SD MET B 293 CE -0.049
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 PRO A 97 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 VAL A 126 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 VAL A 145 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 TYR A 204 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP A 205 N - CA - C ANGL. DEV. =-15.6 DEGREES
REMARK 500 ILE A 304 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 PRO A 306 C - N - CA ANGL. DEV. = 8.4 DEGREES
REMARK 500 PRO B 97 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 SER B 112 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL B 126 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 VAL B 145 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 MET B 203 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 TYR B 204 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ASP B 205 N - CA - C ANGL. DEV. =-15.0 DEGREES
REMARK 500 ILE B 304 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ASP B 349 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-2896C RELATED DB: TARGETDB
DBREF 2HDW A 1 367 UNP Q01609 Y2218_PSEAE 5 371
DBREF 2HDW B 1 367 UNP Q01609 Y2218_PSEAE 5 371
SEQRES 1 A 367 MET GLU THR LYS HIS SER ASN ARG ALA ARG SER ARG LYS
SEQRES 2 A 367 GLY ALA LEU ARG GLY ALA VAL LEU ALA GLY ALA LEU MET
SEQRES 3 A 367 ALA LEU VAL GLY CYS GLN THR SER PRO ALA ALA THR THR
SEQRES 4 A 367 SER SER ASN THR GLY GLY THR ASN MET GLN LEU GLN LEU
SEQRES 5 A 367 THR GLN GLU TRP ASP LYS THR PHE PRO LEU SER ALA LYS
SEQRES 6 A 367 VAL GLU HIS ARG LYS VAL THR PHE ALA ASN ARG TYR GLY
SEQRES 7 A 367 ILE THR LEU ALA ALA ASP LEU TYR LEU PRO LYS ASN ARG
SEQRES 8 A 367 GLY GLY ASP ARG LEU PRO ALA ILE VAL ILE GLY GLY PRO
SEQRES 9 A 367 PHE GLY ALA VAL LYS GLU GLN SER SER GLY LEU TYR ALA
SEQRES 10 A 367 GLN THR MET ALA GLU ARG GLY PHE VAL THR LEU ALA PHE
SEQRES 11 A 367 ASP PRO SER TYR THR GLY GLU SER GLY GLY GLN PRO ARG
SEQRES 12 A 367 ASN VAL ALA SER PRO ASP ILE ASN THR GLU ASP PHE SER
SEQRES 13 A 367 ALA ALA VAL ASP PHE ILE SER LEU LEU PRO GLU VAL ASN
SEQRES 14 A 367 ARG GLU ARG ILE GLY VAL ILE GLY ILE CYS GLY TRP GLY
SEQRES 15 A 367 GLY MET ALA LEU ASN ALA VAL ALA VAL ASP LYS ARG VAL
SEQRES 16 A 367 LYS ALA VAL VAL THR SER THR MET TYR ASP MET THR ARG
SEQRES 17 A 367 VAL MET SER LYS GLY TYR ASN ASP SER VAL THR LEU GLU
SEQRES 18 A 367 GLN ARG THR ARG THR LEU GLU GLN LEU GLY GLN GLN ARG
SEQRES 19 A 367 TRP LYS ASP ALA GLU SER GLY THR PRO ALA TYR GLN PRO
SEQRES 20 A 367 PRO TYR ASN GLU LEU LYS GLY GLY GLU ALA GLN PHE LEU
SEQRES 21 A 367 VAL ASP TYR HIS ASP TYR TYR MET THR PRO ARG GLY TYR
SEQRES 22 A 367 HIS PRO ARG ALA VAL ASN SER GLY ASN ALA TRP THR MET
SEQRES 23 A 367 THR THR PRO LEU SER PHE MET ASN MET PRO ILE LEU THR
SEQRES 24 A 367 TYR ILE LYS GLU ILE SER PRO ARG PRO ILE LEU LEU ILE
SEQRES 25 A 367 HIS GLY GLU ARG ALA HIS SER ARG TYR PHE SER GLU THR
SEQRES 26 A 367 ALA TYR ALA ALA ALA ALA GLU PRO LYS GLU LEU LEU ILE
SEQRES 27 A 367 VAL PRO GLY ALA SER HIS VAL ASP LEU TYR ASP ARG LEU
SEQRES 28 A 367 ASP ARG ILE PRO PHE ASP ARG ILE ALA GLY PHE PHE ASP
SEQRES 29 A 367 GLU HIS LEU
SEQRES 1 B 367 MET GLU THR LYS HIS SER ASN ARG ALA ARG SER ARG LYS
SEQRES 2 B 367 GLY ALA LEU ARG GLY ALA VAL LEU ALA GLY ALA LEU MET
SEQRES 3 B 367 ALA LEU VAL GLY CYS GLN THR SER PRO ALA ALA THR THR
SEQRES 4 B 367 SER SER ASN THR GLY GLY THR ASN MET GLN LEU GLN LEU
SEQRES 5 B 367 THR GLN GLU TRP ASP LYS THR PHE PRO LEU SER ALA LYS
SEQRES 6 B 367 VAL GLU HIS ARG LYS VAL THR PHE ALA ASN ARG TYR GLY
SEQRES 7 B 367 ILE THR LEU ALA ALA ASP LEU TYR LEU PRO LYS ASN ARG
SEQRES 8 B 367 GLY GLY ASP ARG LEU PRO ALA ILE VAL ILE GLY GLY PRO
SEQRES 9 B 367 PHE GLY ALA VAL LYS GLU GLN SER SER GLY LEU TYR ALA
SEQRES 10 B 367 GLN THR MET ALA GLU ARG GLY PHE VAL THR LEU ALA PHE
SEQRES 11 B 367 ASP PRO SER TYR THR GLY GLU SER GLY GLY GLN PRO ARG
SEQRES 12 B 367 ASN VAL ALA SER PRO ASP ILE ASN THR GLU ASP PHE SER
SEQRES 13 B 367 ALA ALA VAL ASP PHE ILE SER LEU LEU PRO GLU VAL ASN
SEQRES 14 B 367 ARG GLU ARG ILE GLY VAL ILE GLY ILE CYS GLY TRP GLY
SEQRES 15 B 367 GLY MET ALA LEU ASN ALA VAL ALA VAL ASP LYS ARG VAL
SEQRES 16 B 367 LYS ALA VAL VAL THR SER THR MET TYR ASP MET THR ARG
SEQRES 17 B 367 VAL MET SER LYS GLY TYR ASN ASP SER VAL THR LEU GLU
SEQRES 18 B 367 GLN ARG THR ARG THR LEU GLU GLN LEU GLY GLN GLN ARG
SEQRES 19 B 367 TRP LYS ASP ALA GLU SER GLY THR PRO ALA TYR GLN PRO
SEQRES 20 B 367 PRO TYR ASN GLU LEU LYS GLY GLY GLU ALA GLN PHE LEU
SEQRES 21 B 367 VAL ASP TYR HIS ASP TYR TYR MET THR PRO ARG GLY TYR
SEQRES 22 B 367 HIS PRO ARG ALA VAL ASN SER GLY ASN ALA TRP THR MET
SEQRES 23 B 367 THR THR PRO LEU SER PHE MET ASN MET PRO ILE LEU THR
SEQRES 24 B 367 TYR ILE LYS GLU ILE SER PRO ARG PRO ILE LEU LEU ILE
SEQRES 25 B 367 HIS GLY GLU ARG ALA HIS SER ARG TYR PHE SER GLU THR
SEQRES 26 B 367 ALA TYR ALA ALA ALA ALA GLU PRO LYS GLU LEU LEU ILE
SEQRES 27 B 367 VAL PRO GLY ALA SER HIS VAL ASP LEU TYR ASP ARG LEU
SEQRES 28 B 367 ASP ARG ILE PRO PHE ASP ARG ILE ALA GLY PHE PHE ASP
SEQRES 29 B 367 GLU HIS LEU
FORMUL 3 HOH *194(H2 O)
HELIX 1 1 GLN A 111 ARG A 123 1 13
HELIX 2 2 SER A 147 LEU A 165 1 19
HELIX 3 3 GLY A 180 ASP A 192 1 13
HELIX 4 4 ASP A 205 GLY A 213 1 9
HELIX 5 5 THR A 219 GLY A 241 1 23
HELIX 6 6 ALA A 257 MET A 268 1 12
HELIX 7 7 THR A 288 MET A 293 1 6
HELIX 8 8 TYR A 300 SER A 305 5 6
HELIX 9 9 SER A 319 ALA A 330 1 12
HELIX 10 10 VAL A 345 ARG A 350 1 6
HELIX 11 11 PRO A 355 LEU A 367 1 13
HELIX 12 12 GLN B 111 ARG B 123 1 13
HELIX 13 13 SER B 147 SER B 163 1 17
HELIX 14 14 GLY B 180 ASP B 192 1 13
HELIX 15 15 ASP B 205 GLY B 213 1 9
HELIX 16 16 TYR B 214 SER B 217 5 4
HELIX 17 17 THR B 219 GLY B 241 1 23
HELIX 18 18 ALA B 257 MET B 268 1 12
HELIX 19 19 THR B 288 MET B 293 1 6
HELIX 20 20 TYR B 300 ILE B 304 5 5
HELIX 21 21 SER B 319 ALA B 330 1 12
HELIX 22 22 VAL B 345 ARG B 350 1 6
HELIX 23 23 PRO B 355 LEU B 367 1 13
SHEET 1 A 8 VAL A 66 ALA A 74 0
SHEET 2 A 8 THR A 80 PRO A 88 -1 O LEU A 81 N PHE A 73
SHEET 3 A 8 VAL A 126 PHE A 130 -1 O THR A 127 N TYR A 86
SHEET 4 A 8 LEU A 96 GLY A 102 1 N ILE A 101 O LEU A 128
SHEET 5 A 8 VAL A 168 ILE A 178 1 O ARG A 172 N ALA A 98
SHEET 6 A 8 ALA A 197 SER A 201 1 O SER A 201 N GLY A 177
SHEET 7 A 8 ILE A 309 GLY A 314 1 O ILE A 312 N THR A 200
SHEET 8 A 8 LYS A 334 VAL A 339 1 O LEU A 337 N LEU A 311
SHEET 1 B 8 VAL B 66 ALA B 74 0
SHEET 2 B 8 THR B 80 PRO B 88 -1 O LEU B 81 N PHE B 73
SHEET 3 B 8 VAL B 126 PHE B 130 -1 O ALA B 129 N ASP B 84
SHEET 4 B 8 LEU B 96 GLY B 102 1 N ILE B 101 O LEU B 128
SHEET 5 B 8 VAL B 168 ILE B 178 1 O ILE B 178 N GLY B 102
SHEET 6 B 8 VAL B 195 SER B 201 1 O LYS B 196 N ILE B 173
SHEET 7 B 8 ILE B 309 GLY B 314 1 O ILE B 312 N THR B 200
SHEET 8 B 8 LYS B 334 VAL B 339 1 O LEU B 337 N LEU B 311
CISPEP 1 GLY A 103 PRO A 104 0 -0.36
CISPEP 2 GLN A 141 PRO A 142 0 -0.03
CISPEP 3 SER A 305 PRO A 306 0 0.20
CISPEP 4 GLU A 332 PRO A 333 0 0.00
CISPEP 5 GLY B 103 PRO B 104 0 -0.23
CISPEP 6 GLN B 141 PRO B 142 0 0.27
CISPEP 7 SER B 305 PRO B 306 0 0.21
CISPEP 8 GLU B 332 PRO B 333 0 0.02
CRYST1 46.264 136.337 48.134 90.00 108.74 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 0.021615 0.000000 0.007333 0.00000
SCALE2 0.000000 0.007335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021938 0.00000
TER 2527 LEU A 367
TER 5029 LEU B 367
MASTER 375 0 0 23 16 0 0 6 5221 2 0 58
END |