HEADER TRANSCRIPTION 16-AUG-07 2QZ8
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LEUCINE RESPONSE
TITLE 2 REGULATORY PROTEIN (LRPA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE TRANSCRIPTIONAL REGULATORY PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: LEUCINE-RESPONSIVE REGULATORY PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 ATCC: 25618;
SOURCE 6 GENE: LRP, MT3390, RV3291C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS LEUCINE RESPONSIVE REGULATORY PROTEIN, HTH MOTIF, GLOBAL
KEYWDS 2 TRANSCRIPTIONAL REGULATOR, STRUCTURAL GENOMICS, TB STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, TBSGC, PSI, PROTEIN STRUCTURE INITIATIVE, DNA-
KEYWDS 4 BINDING, TRANSCRIPTION REGULATION, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.R.MANCHI,K.GOKULAN,T.IOERGER,W.R.JACOBS JR.,J.C.SACCHETTINI,TB
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 6 21-FEB-24 2QZ8 1 REMARK
REVDAT 5 20-OCT-21 2QZ8 1 SEQADV
REVDAT 4 13-JUL-11 2QZ8 1 VERSN
REVDAT 3 24-FEB-09 2QZ8 1 VERSN
REVDAT 2 01-JUL-08 2QZ8 1 JRNL
REVDAT 1 06-NOV-07 2QZ8 0
JRNL AUTH M.C.REDDY,K.GOKULAN,W.R.JACOBS,T.R.IOERGER,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LRPA, A
JRNL TITL 2 LEUCINE-RESPONSIVE GLOBAL REGULATOR ASSOCIATED WITH
JRNL TITL 3 STARVATION RESPONSE.
JRNL REF PROTEIN SCI. V. 17 159 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18042675
JRNL DOI 10.1110/PS.073192208
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 67785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.580
REMARK 3 FREE R VALUE TEST SET COUNT : 3781
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 2.1700 - 2.1600 0.07 39 0 0.2368 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.146
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 0.60000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 11.056 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED IN PHASING
REMARK 3 AND REFINEMENT. HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. PROGRAM REFMAC 5.2.0005 HAS ALSO BEEN USED IN
REMARK 3 REFINEMENT.
REMARK 4
REMARK 4 2QZ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044230.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96400, 1.00000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67785
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 105.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 1.880
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02610
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.73
REMARK 200 R MERGE FOR SHELL (I) : 0.05210
REMARK 200 R SYM FOR SHELL (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 16.70
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 (%): 52.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 70MM SODIUM ACETATE, 20% GLYCEROL,
REMARK 280 5.6% PEG 4000, PH 6.0, VAPOR DIFFUSION, TEMPERATURE 291.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 31.25300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.25300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 73.14200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.95000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 73.14200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.95000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.25300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 73.14200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.95000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.25300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 73.14200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.95000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31660 ANGSTROM**2
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 149.90000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.50600
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 ASN A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 4
REMARK 465 ASN B 2
REMARK 465 GLU B 3
REMARK 465 ALA B 4
REMARK 465 ASN C 2
REMARK 465 GLU C 3
REMARK 465 ALA C 4
REMARK 465 ASN D 2
REMARK 465 GLU D 3
REMARK 465 ALA D 4
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 ASP D 145 CB - CG - OD2 ANGL. DEV. = 6.3 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 ASP A 19 109.07 -164.42
REMARK 500 LEU C 33 -150.06 -94.70
REMARK 500 ASP D 19 112.82 -165.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV3291C RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2QYD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LEUCINE RESPONSE
REMARK 900 REGULATORY PROTEIN (LRPA), LEUCINE-BOUND FORM
DBREF 2QZ8 A 5 150 UNP P96896 P96896_MYCTU 5 150
DBREF 2QZ8 B 5 150 UNP P96896 P96896_MYCTU 5 150
DBREF 2QZ8 C 5 150 UNP P96896 P96896_MYCTU 5 150
DBREF 2QZ8 D 5 150 UNP P96896 P96896_MYCTU 5 150
SEQADV 2QZ8 ASN A 2 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 GLU A 3 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 ALA A 4 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 VAL A 22 UNP P96896 ALA 22 ENGINEERED MUTATION
SEQADV 2QZ8 MET A 108 UNP P96896 LEU 108 ENGINEERED MUTATION
SEQADV 2QZ8 ASN B 2 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 GLU B 3 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 ALA B 4 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 VAL B 22 UNP P96896 ALA 22 ENGINEERED MUTATION
SEQADV 2QZ8 MET B 108 UNP P96896 LEU 108 ENGINEERED MUTATION
SEQADV 2QZ8 ASN C 2 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 GLU C 3 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 ALA C 4 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 VAL C 22 UNP P96896 ALA 22 ENGINEERED MUTATION
SEQADV 2QZ8 MET C 108 UNP P96896 LEU 108 ENGINEERED MUTATION
SEQADV 2QZ8 ASN D 2 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 GLU D 3 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 ALA D 4 UNP P96896 EXPRESSION TAG
SEQADV 2QZ8 VAL D 22 UNP P96896 ALA 22 ENGINEERED MUTATION
SEQADV 2QZ8 MET D 108 UNP P96896 LEU 108 ENGINEERED MUTATION
SEQRES 1 A 149 ASN GLU ALA LEU ASP ASP ILE ASP ARG ILE LEU VAL ARG
SEQRES 2 A 149 GLU LEU ALA ALA ASP GLY ARG VAL THR LEU SER GLU LEU
SEQRES 3 A 149 ALA THR ARG ALA GLY LEU SER VAL SER ALA VAL GLN SER
SEQRES 4 A 149 ARG VAL ARG ARG LEU GLU SER ARG GLY VAL VAL GLN GLY
SEQRES 5 A 149 TYR SER ALA ARG ILE ASN PRO GLU ALA VAL GLY HIS LEU
SEQRES 6 A 149 LEU SER ALA PHE VAL ALA ILE THR PRO LEU ASP PRO SER
SEQRES 7 A 149 GLN PRO ASP ASP ALA PRO ALA ARG LEU GLU HIS ILE GLU
SEQRES 8 A 149 GLU VAL GLU SER CYS TYR SER VAL ALA GLY GLU GLU SER
SEQRES 9 A 149 TYR VAL MET LEU VAL ARG VAL ALA SER ALA ARG ALA LEU
SEQRES 10 A 149 GLU ASP LEU LEU GLN ARG ILE ARG THR THR ALA ASN VAL
SEQRES 11 A 149 ARG THR ARG SER THR ILE ILE LEU ASN THR PHE TYR SER
SEQRES 12 A 149 ASP ARG GLN HIS ILE PRO
SEQRES 1 B 149 ASN GLU ALA LEU ASP ASP ILE ASP ARG ILE LEU VAL ARG
SEQRES 2 B 149 GLU LEU ALA ALA ASP GLY ARG VAL THR LEU SER GLU LEU
SEQRES 3 B 149 ALA THR ARG ALA GLY LEU SER VAL SER ALA VAL GLN SER
SEQRES 4 B 149 ARG VAL ARG ARG LEU GLU SER ARG GLY VAL VAL GLN GLY
SEQRES 5 B 149 TYR SER ALA ARG ILE ASN PRO GLU ALA VAL GLY HIS LEU
SEQRES 6 B 149 LEU SER ALA PHE VAL ALA ILE THR PRO LEU ASP PRO SER
SEQRES 7 B 149 GLN PRO ASP ASP ALA PRO ALA ARG LEU GLU HIS ILE GLU
SEQRES 8 B 149 GLU VAL GLU SER CYS TYR SER VAL ALA GLY GLU GLU SER
SEQRES 9 B 149 TYR VAL MET LEU VAL ARG VAL ALA SER ALA ARG ALA LEU
SEQRES 10 B 149 GLU ASP LEU LEU GLN ARG ILE ARG THR THR ALA ASN VAL
SEQRES 11 B 149 ARG THR ARG SER THR ILE ILE LEU ASN THR PHE TYR SER
SEQRES 12 B 149 ASP ARG GLN HIS ILE PRO
SEQRES 1 C 149 ASN GLU ALA LEU ASP ASP ILE ASP ARG ILE LEU VAL ARG
SEQRES 2 C 149 GLU LEU ALA ALA ASP GLY ARG VAL THR LEU SER GLU LEU
SEQRES 3 C 149 ALA THR ARG ALA GLY LEU SER VAL SER ALA VAL GLN SER
SEQRES 4 C 149 ARG VAL ARG ARG LEU GLU SER ARG GLY VAL VAL GLN GLY
SEQRES 5 C 149 TYR SER ALA ARG ILE ASN PRO GLU ALA VAL GLY HIS LEU
SEQRES 6 C 149 LEU SER ALA PHE VAL ALA ILE THR PRO LEU ASP PRO SER
SEQRES 7 C 149 GLN PRO ASP ASP ALA PRO ALA ARG LEU GLU HIS ILE GLU
SEQRES 8 C 149 GLU VAL GLU SER CYS TYR SER VAL ALA GLY GLU GLU SER
SEQRES 9 C 149 TYR VAL MET LEU VAL ARG VAL ALA SER ALA ARG ALA LEU
SEQRES 10 C 149 GLU ASP LEU LEU GLN ARG ILE ARG THR THR ALA ASN VAL
SEQRES 11 C 149 ARG THR ARG SER THR ILE ILE LEU ASN THR PHE TYR SER
SEQRES 12 C 149 ASP ARG GLN HIS ILE PRO
SEQRES 1 D 149 ASN GLU ALA LEU ASP ASP ILE ASP ARG ILE LEU VAL ARG
SEQRES 2 D 149 GLU LEU ALA ALA ASP GLY ARG VAL THR LEU SER GLU LEU
SEQRES 3 D 149 ALA THR ARG ALA GLY LEU SER VAL SER ALA VAL GLN SER
SEQRES 4 D 149 ARG VAL ARG ARG LEU GLU SER ARG GLY VAL VAL GLN GLY
SEQRES 5 D 149 TYR SER ALA ARG ILE ASN PRO GLU ALA VAL GLY HIS LEU
SEQRES 6 D 149 LEU SER ALA PHE VAL ALA ILE THR PRO LEU ASP PRO SER
SEQRES 7 D 149 GLN PRO ASP ASP ALA PRO ALA ARG LEU GLU HIS ILE GLU
SEQRES 8 D 149 GLU VAL GLU SER CYS TYR SER VAL ALA GLY GLU GLU SER
SEQRES 9 D 149 TYR VAL MET LEU VAL ARG VAL ALA SER ALA ARG ALA LEU
SEQRES 10 D 149 GLU ASP LEU LEU GLN ARG ILE ARG THR THR ALA ASN VAL
SEQRES 11 D 149 ARG THR ARG SER THR ILE ILE LEU ASN THR PHE TYR SER
SEQRES 12 D 149 ASP ARG GLN HIS ILE PRO
FORMUL 5 HOH *265(H2 O)
HELIX 1 1 ASP A 6 ASP A 19 1 14
HELIX 2 2 THR A 23 GLY A 32 1 10
HELIX 3 3 SER A 34 ARG A 48 1 15
HELIX 4 4 PRO A 60 GLY A 64 5 5
HELIX 5 5 ASP A 83 GLU A 89 1 7
HELIX 6 6 SER A 114 ASN A 130 1 17
HELIX 7 7 ASP B 6 ASP B 19 1 14
HELIX 8 8 THR B 23 GLY B 32 1 10
HELIX 9 9 SER B 34 ARG B 48 1 15
HELIX 10 10 PRO B 60 GLY B 64 5 5
HELIX 11 11 ASP B 83 GLU B 89 1 7
HELIX 12 12 SER B 114 ASN B 130 1 17
HELIX 13 13 ILE C 8 ASP C 19 1 12
HELIX 14 14 THR C 23 GLY C 32 1 10
HELIX 15 15 SER C 36 ARG C 48 1 13
HELIX 16 16 PRO C 60 GLY C 64 5 5
HELIX 17 17 ASP C 83 GLU C 89 1 7
HELIX 18 18 SER C 114 ASN C 130 1 17
HELIX 19 19 ASP D 6 ASP D 19 1 14
HELIX 20 20 THR D 23 GLY D 32 1 10
HELIX 21 21 SER D 34 ARG D 48 1 15
HELIX 22 22 PRO D 60 GLY D 64 5 5
HELIX 23 23 ASP D 83 GLU D 89 1 7
HELIX 24 24 SER D 114 ASN D 130 1 17
SHEET 1 A 2 VAL A 51 GLY A 53 0
SHEET 2 A 2 ARG D 57 ILE D 58 -1 O ARG D 57 N GLN A 52
SHEET 1 B 2 ARG A 57 ILE A 58 0
SHEET 2 B 2 VAL D 51 GLY D 53 -1 O GLN D 52 N ARG A 57
SHEET 1 C 9 LEU A 67 PRO A 75 0
SHEET 2 C 9 TYR A 106 VAL A 112 -1 O VAL A 112 N LEU A 67
SHEET 3 C 9 VAL A 94 VAL A 100 -1 N GLU A 95 O LEU A 109
SHEET 4 C 9 VAL D 131 TYR D 143 -1 O TYR D 143 N CYS A 97
SHEET 5 C 9 LEU D 67 PRO D 75 -1 N PHE D 70 O THR D 136
SHEET 6 C 9 TYR D 106 VAL D 112 -1 O MET D 108 N VAL D 71
SHEET 7 C 9 VAL D 94 VAL D 100 -1 N GLU D 95 O LEU D 109
SHEET 8 C 9 VAL A 131 TYR A 143 -1 N TYR A 143 O CYS D 97
SHEET 9 C 9 LEU A 67 PRO A 75 -1 N PHE A 70 O THR A 136
SHEET 1 D 4 VAL B 94 SER B 99 0
SHEET 2 D 4 TYR B 106 VAL B 112 -1 O VAL B 107 N TYR B 98
SHEET 3 D 4 LEU B 67 PRO B 75 -1 N VAL B 71 O MET B 108
SHEET 4 D 4 VAL B 131 ILE B 137 -1 O ARG B 134 N ALA B 72
SHEET 1 E 4 VAL C 94 SER C 99 0
SHEET 2 E 4 TYR C 106 VAL C 112 -1 O VAL C 107 N TYR C 98
SHEET 3 E 4 LEU C 67 PRO C 75 -1 N VAL C 71 O MET C 108
SHEET 4 E 4 VAL C 131 ILE C 138 -1 O THR C 136 N PHE C 70
CRYST1 146.284 149.900 62.506 90.00 90.00 90.00 C 2 2 21 32
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 0.006836 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006671 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015998 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
