HEADER CHAPERONE 06-MAY-11 2YHT
TITLE CRYSTAL STRUCTURE OF HFQ RIBOREGULATOR FROM E. COLI (P1 SPACE GROUP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN HFQ;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 FRAGMENT: SM-LIKE FOLD, RESIDUES 1-72;
COMPND 5 SYNONYM: HF-1, HOST FACTOR-I PROTEIN, HF-I;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PETM11
KEYWDS CHAPERONE, RNA CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BASQUIN,C.SAUTER
REVDAT 4 20-DEC-23 2YHT 1 REMARK
REVDAT 3 08-MAY-19 2YHT 1 REMARK
REVDAT 2 04-MAR-15 2YHT 1 REMARK
REVDAT 1 16-NOV-11 2YHT 0
JRNL AUTH L.BONNEFOND,P.SCHELLENBERGER,J.BASQUIN,G.DEMANGEAT,
JRNL AUTH 2 C.RITZENTHALER,R.CHENEVERT,C.BALG,M.FRUGIER,
JRNL AUTH 3 J.RUDINGER-THIRION,R.GIEGE,B.LORBER,C.SAUTER
JRNL TITL EXPLOITING PROTEIN ENGINEERING AND CRYSTAL POLYMORPHISM FOR
JRNL TITL 2 SUCCESSFUL X-RAY STRUCTURE DETERMINATION
JRNL REF CRYST.GROWTH DES. V. 11 4334 2011
JRNL REFN ISSN 1528-7483
JRNL DOI 10.1021/CG101468P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.SAUTER,J.BASQUIN,D.SUCK
REMARK 1 TITL SM-LIKE PROTEINS IN EUBACTERIA: THE CRYSTAL STRUCTURE OF THE
REMARK 1 TITL 2 HFQ PROTEIN FROM ESCHERICHIA COLI.
REMARK 1 REF NUCLEIC ACIDS RES. V. 31 4091 2003
REMARK 1 REFN ISSN 0305-1048
REMARK 1 PMID 12853626
REMARK 1 DOI 10.1093/NAR/GKG480
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.050
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 14073
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 700
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 30.5672 - 4.9535 0.99 2764 143 0.1922 0.2458
REMARK 3 2 4.9535 - 3.9344 0.96 2681 133 0.1578 0.1895
REMARK 3 3 3.9344 - 3.4378 0.97 2669 158 0.1840 0.2407
REMARK 3 4 3.4378 - 3.1238 0.98 2728 150 0.1739 0.2290
REMARK 3 5 3.1238 - 2.9001 0.90 2531 116 0.2157 0.2652
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 19.06
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.91520
REMARK 3 B22 (A**2) : -9.25560
REMARK 3 B33 (A**2) : 18.93690
REMARK 3 B12 (A**2) : -0.97800
REMARK 3 B13 (A**2) : 0.32090
REMARK 3 B23 (A**2) : 0.95280
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 : 0.009 6156
REMARK 3 ANGLE : 1.154 8352
REMARK 3 CHIRALITY : 0.069 1008
REMARK 3 PLANARITY : 0.005 1056
REMARK 3 DIHEDRAL : 14.740 2340
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 : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.044
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.047
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.045
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.053
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.044
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.046
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.039
REMARK 3 NCS OPERATOR : 8
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN I AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.041
REMARK 3 NCS OPERATOR : 9
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN J AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.045
REMARK 3 NCS OPERATOR : 10
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN K AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.047
REMARK 3 NCS OPERATOR : 11
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 SELECTION : CHAIN L AND (RESSEQ 7:24 OR RESSEQ 32:38
REMARK 3 OR RESSEQ 44:68)
REMARK 3 ATOM PAIRS NUMBER : 396
REMARK 3 RMSD : 0.047
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.035
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.034
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.034
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.046
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.047
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.030
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN I AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.034
REMARK 3 NCS OPERATOR : 8
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN J AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.041
REMARK 3 NCS OPERATOR : 9
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN K AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.048
REMARK 3 NCS OPERATOR : 10
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 38:44)
REMARK 3 SELECTION : CHAIN L AND (RESSEQ 38:44)
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.042
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.036
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.043
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.046
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.060
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.050
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.041
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN I AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.053
REMARK 3 NCS OPERATOR : 8
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN J AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.048
REMARK 3 NCS OPERATOR : 9
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 24:32)
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 24:32)
REMARK 3 ATOM PAIRS NUMBER : 72
REMARK 3 RMSD : 0.048
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2YHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1290048187.
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
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 62.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2Y90
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED BY VAPOR
REMARK 280 DIFFUSION IN 2UL SITTING DROPS. THE RESERVOIR CONTAINED 30% PEG
REMARK 280 3350, 0.1 M NA-CITRATE PH 5.4. CRYSTALLIZATIONS WERE CARRIED OUT
REMARK 280 AT 20 DEGREES CELSIUS., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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, 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
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 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLY A 4
REMARK 465 GLN A 5
REMARK 465 SER A 69
REMARK 465 HIS A 70
REMARK 465 HIS A 71
REMARK 465 SER A 72
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LYS B 3
REMARK 465 GLY B 4
REMARK 465 GLN B 5
REMARK 465 SER B 69
REMARK 465 HIS B 70
REMARK 465 HIS B 71
REMARK 465 SER B 72
REMARK 465 GLY C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 LYS C 3
REMARK 465 GLY C 4
REMARK 465 GLN C 5
REMARK 465 SER C 69
REMARK 465 HIS C 70
REMARK 465 HIS C 71
REMARK 465 SER C 72
REMARK 465 GLY D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 LYS D 3
REMARK 465 GLY D 4
REMARK 465 GLN D 5
REMARK 465 SER D 69
REMARK 465 HIS D 70
REMARK 465 HIS D 71
REMARK 465 SER D 72
REMARK 465 GLY E -1
REMARK 465 ALA E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 LYS E 3
REMARK 465 GLY E 4
REMARK 465 GLN E 5
REMARK 465 SER E 69
REMARK 465 HIS E 70
REMARK 465 HIS E 71
REMARK 465 SER E 72
REMARK 465 GLY F -1
REMARK 465 ALA F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 LYS F 3
REMARK 465 GLY F 4
REMARK 465 GLN F 5
REMARK 465 SER F 69
REMARK 465 HIS F 70
REMARK 465 HIS F 71
REMARK 465 SER F 72
REMARK 465 GLY G -1
REMARK 465 ALA G 0
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 LYS G 3
REMARK 465 GLY G 4
REMARK 465 GLN G 5
REMARK 465 SER G 69
REMARK 465 HIS G 70
REMARK 465 HIS G 71
REMARK 465 SER G 72
REMARK 465 GLY H -1
REMARK 465 ALA H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 LYS H 3
REMARK 465 GLY H 4
REMARK 465 GLN H 5
REMARK 465 SER H 69
REMARK 465 HIS H 70
REMARK 465 HIS H 71
REMARK 465 SER H 72
REMARK 465 GLY I -1
REMARK 465 ALA I 0
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 LYS I 3
REMARK 465 GLY I 4
REMARK 465 GLN I 5
REMARK 465 SER I 69
REMARK 465 HIS I 70
REMARK 465 HIS I 71
REMARK 465 SER I 72
REMARK 465 GLY J -1
REMARK 465 ALA J 0
REMARK 465 MET J 1
REMARK 465 ALA J 2
REMARK 465 LYS J 3
REMARK 465 GLY J 4
REMARK 465 GLN J 5
REMARK 465 SER J 69
REMARK 465 HIS J 70
REMARK 465 HIS J 71
REMARK 465 SER J 72
REMARK 465 GLY K -1
REMARK 465 ALA K 0
REMARK 465 MET K 1
REMARK 465 ALA K 2
REMARK 465 LYS K 3
REMARK 465 GLY K 4
REMARK 465 GLN K 5
REMARK 465 SER K 69
REMARK 465 HIS K 70
REMARK 465 HIS K 71
REMARK 465 SER K 72
REMARK 465 GLY L -1
REMARK 465 ALA L 0
REMARK 465 MET L 1
REMARK 465 ALA L 2
REMARK 465 LYS L 3
REMARK 465 GLY L 4
REMARK 465 GLN L 5
REMARK 465 SER L 69
REMARK 465 HIS L 70
REMARK 465 HIS L 71
REMARK 465 SER L 72
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 OH TYR G 55 OE1 GLN L 8 1.59
REMARK 500 OD1 ASN L 13 NH1 ARG L 16 1.82
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 40 -154.70 -134.46
REMARK 500 ASN A 48 -119.87 -155.06
REMARK 500 ARG B 19 48.43 39.92
REMARK 500 ASP B 40 -153.78 -134.99
REMARK 500 ASN B 48 -121.44 -155.97
REMARK 500 ARG C 19 47.81 38.63
REMARK 500 ASP C 40 -155.13 -135.15
REMARK 500 ASN C 48 -119.00 -154.08
REMARK 500 ASP D 40 -153.92 -135.41
REMARK 500 ASN D 48 -119.49 -155.92
REMARK 500 ARG E 19 46.84 39.90
REMARK 500 ASP E 40 -155.49 -136.00
REMARK 500 ASN E 48 -119.05 -155.40
REMARK 500 ARG F 19 48.11 38.35
REMARK 500 ASP F 40 -142.98 -123.02
REMARK 500 ASN F 48 -117.83 -152.31
REMARK 500 ASP G 40 -153.95 -134.56
REMARK 500 ASN G 48 -119.65 -155.21
REMARK 500 ARG H 19 46.49 37.65
REMARK 500 ASP H 40 -154.32 -134.40
REMARK 500 ASN H 48 -119.41 -155.30
REMARK 500 ARG I 19 47.89 38.96
REMARK 500 ASP I 40 -153.80 -135.49
REMARK 500 ASN I 48 -119.70 -153.69
REMARK 500 ARG J 19 47.26 38.77
REMARK 500 ASP J 40 -154.67 -134.72
REMARK 500 ASN J 48 -120.56 -156.01
REMARK 500 ASP K 40 -153.75 -134.26
REMARK 500 ASN K 48 -119.10 -153.38
REMARK 500 ASP L 40 -152.69 -135.78
REMARK 500 ASN L 48 -120.08 -155.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 30-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 31-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "GA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 30-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 31-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M7C RELATED DB: PDB
REMARK 900 STUCTURAL MODEL OF E. COLI HFQ
REMARK 900 RELATED ID: 2Y90 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HFQ RIBOREGULATOR FROM E. COLI ( P6 SPACE
REMARK 900 GROUP)
REMARK 900 RELATED ID: 1OOU RELATED DB: PDB
REMARK 900 STRUCTURAL MODELLING OF E. COLI HFQ
REMARK 900 RELATED ID: 1HK9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1OOV RELATED DB: PDB
REMARK 900 COMPLEX OF E. COLI HFQ WITH A RA7 OLIGONUCLEOTIDE
DBREF 2YHT A 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT B 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT C 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT D 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT E 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT F 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT G 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT H 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT I 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT J 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT K 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
DBREF 2YHT L 1 72 UNP P0A6X3 HFQ_ECOLI 1 72
SEQADV 2YHT GLY A -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA A 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY B -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA B 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY C -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA C 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY D -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA D 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY E -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA E 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY F -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA F 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY G -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA G 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY H -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA H 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY I -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA I 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY J -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA J 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY K -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA K 0 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT GLY L -1 UNP P0A6X3 EXPRESSION TAG
SEQADV 2YHT ALA L 0 UNP P0A6X3 EXPRESSION TAG
SEQRES 1 A 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 A 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 A 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 A 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 A 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 A 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 B 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 B 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 B 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 B 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 B 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 B 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 C 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 C 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 C 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 C 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 C 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 C 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 D 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 D 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 D 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 D 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 D 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 D 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 E 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 E 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 E 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 E 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 E 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 E 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 F 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 F 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 F 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 F 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 F 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 F 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 G 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 G 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 G 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 G 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 G 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 G 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 H 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 H 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 H 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 H 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 H 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 H 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 I 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 I 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 I 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 I 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 I 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 I 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 J 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 J 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 J 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 J 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 J 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 J 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 K 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 K 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 K 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 K 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 K 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 K 74 PRO SER ARG PRO VAL SER HIS HIS SER
SEQRES 1 L 74 GLY ALA MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE
SEQRES 2 L 74 LEU ASN ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE
SEQRES 3 L 74 TYR LEU VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU
SEQRES 4 L 74 SER PHE ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL
SEQRES 5 L 74 SER GLN MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL
SEQRES 6 L 74 PRO SER ARG PRO VAL SER HIS HIS SER
HELIX 1 1 LEU A 7 GLU A 18 1 12
HELIX 2 2 LEU B 7 GLU B 18 1 12
HELIX 3 3 LEU C 7 GLU C 18 1 12
HELIX 4 4 LEU D 7 GLU D 18 1 12
HELIX 5 5 LEU E 7 GLU E 18 1 12
HELIX 6 6 LEU F 7 GLU F 18 1 12
HELIX 7 7 LEU G 7 GLU G 18 1 12
HELIX 8 8 LEU H 7 GLU H 18 1 12
HELIX 9 9 LEU I 7 GLU I 18 1 12
HELIX 10 10 LEU J 7 GLU J 18 1 12
HELIX 11 11 LEU K 7 GLU K 18 1 12
HELIX 12 12 LEU L 7 GLU L 18 1 12
SHEET 1 AA31 PRO A 21 LEU A 26 0
SHEET 2 AA31 LYS A 31 PHE A 39 -1 O LEU A 32 N ILE A 24
SHEET 3 AA31 VAL A 43 LYS A 47 -1 O LEU A 45 N GLU A 37
SHEET 4 AA31 GLN A 52 TYR A 55 -1 O GLN A 52 N LEU A 46
SHEET 5 AA31 ILE F 59 PRO F 64 -1 O SER F 60 N TYR A 55
SHEET 6 AA31 PRO F 21 LEU F 26 -1 O SER F 23 N VAL F 63
SHEET 7 AA31 LYS F 31 PHE F 39 -1 O LEU F 32 N ILE F 24
SHEET 8 AA31 VAL F 43 LYS F 47 -1 O LEU F 45 N GLU F 37
SHEET 9 AA31 GLN F 52 TYR F 55 -1 O GLN F 52 N LEU F 46
SHEET 10 AA31 ILE E 59 PRO E 64 -1 O SER E 60 N TYR F 55
SHEET 11 AA31 PRO E 21 LEU E 26 -1 O SER E 23 N VAL E 63
SHEET 12 AA31 LYS E 31 PHE E 39 -1 O LEU E 32 N ILE E 24
SHEET 13 AA31 VAL E 43 LYS E 47 -1 O LEU E 45 N GLU E 37
SHEET 14 AA31 GLN E 52 TYR E 55 -1 O GLN E 52 N LEU E 46
SHEET 15 AA31 ILE D 59 PRO D 64 -1 O SER D 60 N TYR E 55
SHEET 16 AA31 PRO D 21 LEU D 26 -1 O SER D 23 N VAL D 63
SHEET 17 AA31 LYS D 31 PHE D 39 -1 O LEU D 32 N ILE D 24
SHEET 18 AA31 VAL D 43 LYS D 47 -1 O LEU D 45 N GLU D 37
SHEET 19 AA31 GLN D 52 TYR D 55 -1 O GLN D 52 N LEU D 46
SHEET 20 AA31 ILE C 59 PRO C 64 -1 O SER C 60 N TYR D 55
SHEET 21 AA31 PRO C 21 LEU C 26 -1 O SER C 23 N VAL C 63
SHEET 22 AA31 LYS C 31 PHE C 39 -1 O LEU C 32 N ILE C 24
SHEET 23 AA31 VAL C 43 LYS C 47 -1 O LEU C 45 N GLU C 37
SHEET 24 AA31 GLN C 52 TYR C 55 -1 O GLN C 52 N LEU C 46
SHEET 25 AA31 ILE B 59 PRO B 64 -1 O SER B 60 N TYR C 55
SHEET 26 AA31 PRO B 21 LEU B 26 -1 O SER B 23 N VAL B 63
SHEET 27 AA31 LYS B 31 PHE B 39 -1 O LEU B 32 N ILE B 24
SHEET 28 AA31 VAL B 43 LYS B 47 -1 O LEU B 45 N GLU B 37
SHEET 29 AA31 GLN B 52 TYR B 55 -1 O GLN B 52 N LEU B 46
SHEET 30 AA31 ILE A 59 PRO A 64 -1 O SER A 60 N TYR B 55
SHEET 31 AA31 PRO A 21 LEU A 26 -1 O SER A 23 N VAL A 63
SHEET 1 GA31 PRO G 21 LEU G 26 0
SHEET 2 GA31 LYS G 31 PHE G 39 -1 O LEU G 32 N ILE G 24
SHEET 3 GA31 VAL G 43 LYS G 47 -1 O LEU G 45 N GLU G 37
SHEET 4 GA31 GLN G 52 TYR G 55 -1 O GLN G 52 N LEU G 46
SHEET 5 GA31 ILE L 59 PRO L 64 -1 O SER L 60 N TYR G 55
SHEET 6 GA31 PRO L 21 LEU L 26 -1 O SER L 23 N VAL L 63
SHEET 7 GA31 LYS L 31 PHE L 39 -1 O LEU L 32 N ILE L 24
SHEET 8 GA31 VAL L 43 LYS L 47 -1 O LEU L 45 N GLU L 37
SHEET 9 GA31 GLN L 52 TYR L 55 -1 O GLN L 52 N LEU L 46
SHEET 10 GA31 ILE K 59 PRO K 64 -1 O SER K 60 N TYR L 55
SHEET 11 GA31 PRO K 21 LEU K 26 -1 O SER K 23 N VAL K 63
SHEET 12 GA31 LYS K 31 PHE K 39 -1 O LEU K 32 N ILE K 24
SHEET 13 GA31 VAL K 43 LYS K 47 -1 O LEU K 45 N GLU K 37
SHEET 14 GA31 GLN K 52 TYR K 55 -1 O GLN K 52 N LEU K 46
SHEET 15 GA31 ILE J 59 PRO J 64 -1 O SER J 60 N TYR K 55
SHEET 16 GA31 PRO J 21 LEU J 26 -1 O SER J 23 N VAL J 63
SHEET 17 GA31 LYS J 31 PHE J 39 -1 O LEU J 32 N ILE J 24
SHEET 18 GA31 VAL J 43 LYS J 47 -1 O LEU J 45 N GLU J 37
SHEET 19 GA31 GLN J 52 TYR J 55 -1 O GLN J 52 N LEU J 46
SHEET 20 GA31 ILE I 59 PRO I 64 -1 O SER I 60 N TYR J 55
SHEET 21 GA31 PRO I 21 LEU I 26 -1 O SER I 23 N VAL I 63
SHEET 22 GA31 LYS I 31 PHE I 39 -1 O LEU I 32 N ILE I 24
SHEET 23 GA31 VAL I 43 LYS I 47 -1 O LEU I 45 N GLU I 37
SHEET 24 GA31 GLN I 52 TYR I 55 -1 O GLN I 52 N LEU I 46
SHEET 25 GA31 ILE H 59 PRO H 64 -1 O SER H 60 N TYR I 55
SHEET 26 GA31 PRO H 21 LEU H 26 -1 O SER H 23 N VAL H 63
SHEET 27 GA31 LYS H 31 PHE H 39 -1 O LEU H 32 N ILE H 24
SHEET 28 GA31 VAL H 43 LYS H 47 -1 O LEU H 45 N GLU H 37
SHEET 29 GA31 GLN H 52 TYR H 55 -1 O GLN H 52 N LEU H 46
SHEET 30 GA31 ILE G 59 PRO G 64 -1 O SER G 60 N TYR H 55
SHEET 31 GA31 PRO G 21 LEU G 26 -1 O SER G 23 N VAL G 63
CRYST1 61.200 61.200 53.100 82.60 87.30 60.00 P 1 12
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 0.016340 -0.009434 0.000380 0.00000
SCALE2 0.000000 0.018868 -0.002313 0.00000
SCALE3 0.000000 0.000000 0.018994 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
