HEADER TSE2-BINDING PROTEIN 27-APR-11 3RQ9
TITLE STRUCTURE OF TSI2, A TSE2-IMMUNITY PROTEIN FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE VI SECRETION IMMUNITY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TSI2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: PA2703;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21A
KEYWDS IMMUNITY PROTEIN, TYPE VI SECRETION, T6S, ANTITOXIN, TSE2-BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LI,I.LE TRONG,R.E.STENKAMP,J.D.MOUGOUS
REVDAT 2 02-MAY-12 3RQ9 1 JRNL
REVDAT 1 21-MAR-12 3RQ9 0
JRNL AUTH M.LI,I.LE TRONG,M.A.CARL,E.T.LARSON,S.CHOU,J.A.DE LEON,
JRNL AUTH 2 S.L.DOVE,R.E.STENKAMP,J.D.MOUGOUS
JRNL TITL STRUCTURAL BASIS FOR TYPE VI SECRETION EFFECTOR RECOGNITION
JRNL TITL 2 BY A COGNATE IMMUNITY PROTEIN.
JRNL REF PLOS PATHOG. V. 8 02613 2012
JRNL REFN ISSN 1553-7366
JRNL PMID 22511866
JRNL DOI 10.1371/JOURNAL.PPAT.1002613
REMARK 2
REMARK 2 RESOLUTION. 1.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0095
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 60525
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 + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3246
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 0.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3556
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 176
REMARK 3 BIN FREE R VALUE : 0.2200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : -0.81000
REMARK 3 B12 (A**2) : 0.31000
REMARK 3 B13 (A**2) : -0.08000
REMARK 3 B23 (A**2) : -0.02000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.028
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.017
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.701
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1388 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 907 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1882 ; 1.700 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2255 ; 1.022 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 165 ; 5.029 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;36.879 ;26.279
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;29.886 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 210 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1521 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 235 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 842 ; 3.070 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 324 ; 1.168 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1364 ; 4.411 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 556 ; 5.896 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 541 ; 7.958 ;10.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 7119 ; 3.456 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 188 ;11.585 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2270 ; 7.616 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3RQ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB065244.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792, 0.9075
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60521
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.990
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 45.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.19700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 28.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, 0.1M SODIUM ACETATE, PH
REMARK 280 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 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 HIS A 80
REMARK 465 HIS A 81
REMARK 465 HIS A 82
REMARK 465 HIS A 83
REMARK 465 HIS A 84
REMARK 465 HIS A 85
REMARK 465 MET B 1
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 O HOH A 432 O HOH B 433 1.98
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 OD1 ASP A 29 OE1 GLN B 32 1455 1.95
REMARK 500 OD1 ASP B 30 O HOH B 407 1656 2.07
REMARK 500 OE1 GLU B 56 O HOH B 471 1554 2.12
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 14 CB CYS A 14 SG -0.117
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 ASP A 29 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 29 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
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 335 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH A 336 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH B 365 DISTANCE = 6.00 ANGSTROMS
DBREF 3RQ9 A 1 77 UNP Q9I0D9 Q9I0D9_PSEAE 1 77
DBREF 3RQ9 B 1 77 UNP Q9I0D9 Q9I0D9_PSEAE 1 77
SEQADV 3RQ9 LEU A 78 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 GLU A 79 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS A 80 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS A 81 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS A 82 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS A 83 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS A 84 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS A 85 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 LEU B 78 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 GLU B 79 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS B 80 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS B 81 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS B 82 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS B 83 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS B 84 UNP Q9I0D9 EXPRESSION TAG
SEQADV 3RQ9 HIS B 85 UNP Q9I0D9 EXPRESSION TAG
SEQRES 1 A 85 MET ASN LEU LYS PRO GLN THR LEU MET VAL ALA ILE GLN
SEQRES 2 A 85 CYS VAL ALA ALA ARG THR ARG GLU LEU ASP ALA GLN LEU
SEQRES 3 A 85 GLN ASN ASP ASP PRO GLN ASN ALA ALA GLU LEU GLU GLN
SEQRES 4 A 85 LEU LEU VAL GLY TYR ASP LEU ALA ALA ASP ASP LEU LYS
SEQRES 5 A 85 ASN ALA TYR GLU GLN ALA LEU GLY GLN TYR SER GLY LEU
SEQRES 6 A 85 PRO PRO TYR ASP ARG LEU ILE GLU GLU PRO ALA SER LEU
SEQRES 7 A 85 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 85 MET ASN LEU LYS PRO GLN THR LEU MET VAL ALA ILE GLN
SEQRES 2 B 85 CYS VAL ALA ALA ARG THR ARG GLU LEU ASP ALA GLN LEU
SEQRES 3 B 85 GLN ASN ASP ASP PRO GLN ASN ALA ALA GLU LEU GLU GLN
SEQRES 4 B 85 LEU LEU VAL GLY TYR ASP LEU ALA ALA ASP ASP LEU LYS
SEQRES 5 B 85 ASN ALA TYR GLU GLN ALA LEU GLY GLN TYR SER GLY LEU
SEQRES 6 B 85 PRO PRO TYR ASP ARG LEU ILE GLU GLU PRO ALA SER LEU
SEQRES 7 B 85 GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *175(H2 O)
HELIX 1 1 LYS A 4 LEU A 26 1 23
HELIX 2 2 ASP A 30 TYR A 62 1 33
HELIX 3 3 PRO A 67 ILE A 72 1 6
HELIX 4 4 PRO A 75 GLU A 79 5 5
HELIX 5 5 LYS B 4 ASN B 28 1 25
HELIX 6 6 ASN B 33 LEU B 59 1 27
HELIX 7 7 PRO B 67 GLU B 73 1 7
HELIX 8 8 GLU B 74 GLU B 79 5 6
CRYST1 27.807 34.063 37.650 110.48 95.94 95.82 P 1 2
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 0.035962 0.003666 0.005451 0.00000
SCALE2 0.000000 0.029509 0.011540 0.00000
SCALE3 0.000000 0.000000 0.028673 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
