HEADER LYASE 24-APR-08 3CXO
TITLE CRYSTAL STRUCTURE OF L-RHAMNONATE DEHYDRATASE FROM SALMONELLA
TITLE 2 TYPHIMURIUM COMPLEXED WITH MG AND 3-DEOXY-L-RHAMNONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE GALACTONATE DEHYDRATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM LT2;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2, SGSC1412;
SOURCE 5 ATCC: 700720;
SOURCE 6 GENE: YFAW, STM2291;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS L-RHAMNONATE DEHYDRATASE, ENOLASE SUPERFAMILY, 3-DEOXY-L-RHAMNONATE,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,J.F.RAKUS,B.K.HUBBARD,J.A.GERLT,S.C.ALMO
REVDAT 4 30-AUG-23 3CXO 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 3CXO 1 VERSN
REVDAT 2 14-OCT-08 3CXO 1 JRNL
REVDAT 1 23-SEP-08 3CXO 0
JRNL AUTH J.F.RAKUS,A.A.FEDOROV,E.V.FEDOROV,M.E.GLASNER,B.K.HUBBARD,
JRNL AUTH 2 J.D.DELLI,P.C.BABBITT,S.C.ALMO,J.A.GERLT
JRNL TITL EVOLUTION OF ENZYMATIC ACTIVITIES IN THE ENOLASE
JRNL TITL 2 SUPERFAMILY: L-RHAMNONATE DEHYDRATASE.
JRNL REF BIOCHEMISTRY V. 47 9944 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18754693
JRNL DOI 10.1021/BI800914R
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) : 24.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 8589868.920
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 57744
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) : 0.221
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2855
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) (%) : 99.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5453
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 286
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 436
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.25000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : 0.50000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
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) : 1.070 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.560 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.710 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.400 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 46.54
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 : 3LR.IN5_PAR.TXT
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : 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 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57744
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 12.80
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 3BOX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TACSIMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 4 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
REMARK 290 25555 X,Y+1/2,Z+1/2
REMARK 290 26555 -X,-Y+1/2,Z+1/2
REMARK 290 27555 -X,Y+1/2,-Z+1/2
REMARK 290 28555 X,-Y+1/2,-Z+1/2
REMARK 290 29555 Z,X+1/2,Y+1/2
REMARK 290 30555 Z,-X+1/2,-Y+1/2
REMARK 290 31555 -Z,-X+1/2,Y+1/2
REMARK 290 32555 -Z,X+1/2,-Y+1/2
REMARK 290 33555 Y,Z+1/2,X+1/2
REMARK 290 34555 -Y,Z+1/2,-X+1/2
REMARK 290 35555 Y,-Z+1/2,-X+1/2
REMARK 290 36555 -Y,-Z+1/2,X+1/2
REMARK 290 37555 Y,X+1/2,-Z+1/2
REMARK 290 38555 -Y,-X+1/2,-Z+1/2
REMARK 290 39555 Y,-X+1/2,Z+1/2
REMARK 290 40555 -Y,X+1/2,Z+1/2
REMARK 290 41555 X,Z+1/2,-Y+1/2
REMARK 290 42555 -X,Z+1/2,Y+1/2
REMARK 290 43555 -X,-Z+1/2,-Y+1/2
REMARK 290 44555 X,-Z+1/2,Y+1/2
REMARK 290 45555 Z,Y+1/2,-X+1/2
REMARK 290 46555 Z,-Y+1/2,X+1/2
REMARK 290 47555 -Z,Y+1/2,X+1/2
REMARK 290 48555 -Z,-Y+1/2,-X+1/2
REMARK 290 49555 X+1/2,Y,Z+1/2
REMARK 290 50555 -X+1/2,-Y,Z+1/2
REMARK 290 51555 -X+1/2,Y,-Z+1/2
REMARK 290 52555 X+1/2,-Y,-Z+1/2
REMARK 290 53555 Z+1/2,X,Y+1/2
REMARK 290 54555 Z+1/2,-X,-Y+1/2
REMARK 290 55555 -Z+1/2,-X,Y+1/2
REMARK 290 56555 -Z+1/2,X,-Y+1/2
REMARK 290 57555 Y+1/2,Z,X+1/2
REMARK 290 58555 -Y+1/2,Z,-X+1/2
REMARK 290 59555 Y+1/2,-Z,-X+1/2
REMARK 290 60555 -Y+1/2,-Z,X+1/2
REMARK 290 61555 Y+1/2,X,-Z+1/2
REMARK 290 62555 -Y+1/2,-X,-Z+1/2
REMARK 290 63555 Y+1/2,-X,Z+1/2
REMARK 290 64555 -Y+1/2,X,Z+1/2
REMARK 290 65555 X+1/2,Z,-Y+1/2
REMARK 290 66555 -X+1/2,Z,Y+1/2
REMARK 290 67555 -X+1/2,-Z,-Y+1/2
REMARK 290 68555 X+1/2,-Z,Y+1/2
REMARK 290 69555 Z+1/2,Y,-X+1/2
REMARK 290 70555 Z+1/2,-Y,X+1/2
REMARK 290 71555 -Z+1/2,Y,X+1/2
REMARK 290 72555 -Z+1/2,-Y,-X+1/2
REMARK 290 73555 X+1/2,Y+1/2,Z
REMARK 290 74555 -X+1/2,-Y+1/2,Z
REMARK 290 75555 -X+1/2,Y+1/2,-Z
REMARK 290 76555 X+1/2,-Y+1/2,-Z
REMARK 290 77555 Z+1/2,X+1/2,Y
REMARK 290 78555 Z+1/2,-X+1/2,-Y
REMARK 290 79555 -Z+1/2,-X+1/2,Y
REMARK 290 80555 -Z+1/2,X+1/2,-Y
REMARK 290 81555 Y+1/2,Z+1/2,X
REMARK 290 82555 -Y+1/2,Z+1/2,-X
REMARK 290 83555 Y+1/2,-Z+1/2,-X
REMARK 290 84555 -Y+1/2,-Z+1/2,X
REMARK 290 85555 Y+1/2,X+1/2,-Z
REMARK 290 86555 -Y+1/2,-X+1/2,-Z
REMARK 290 87555 Y+1/2,-X+1/2,Z
REMARK 290 88555 -Y+1/2,X+1/2,Z
REMARK 290 89555 X+1/2,Z+1/2,-Y
REMARK 290 90555 -X+1/2,Z+1/2,Y
REMARK 290 91555 -X+1/2,-Z+1/2,-Y
REMARK 290 92555 X+1/2,-Z+1/2,Y
REMARK 290 93555 Z+1/2,Y+1/2,-X
REMARK 290 94555 Z+1/2,-Y+1/2,X
REMARK 290 95555 -Z+1/2,Y+1/2,X
REMARK 290 96555 -Z+1/2,-Y+1/2,-X
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 0.00000
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 0.00000
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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 49 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 49 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 49 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 50 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 50 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 50 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 51 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 51 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 51 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 52 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 52 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 52 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 53 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 53 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 53 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 54 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 54 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 54 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 55 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 55 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 55 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 56 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 56 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 56 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 57 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 57 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 57 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 58 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 58 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 58 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 59 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 59 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 59 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 60 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 60 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 60 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 61 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 61 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 61 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 62 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 62 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 62 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY1 63 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 63 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 63 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 64 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 64 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 64 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY1 65 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 65 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 65 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 66 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 66 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 66 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 67 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 67 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 67 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY1 68 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 68 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 68 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY1 69 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 69 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 69 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 70 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 70 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 70 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 71 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 71 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 71 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 72 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 72 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 72 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY1 73 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 73 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 73 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 74 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 74 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 74 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 75 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 75 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 75 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 76 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 76 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 76 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 77 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 77 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 77 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 78 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 78 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 78 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 79 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 79 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 79 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 80 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 80 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 80 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 81 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 81 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 81 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 82 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 82 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 82 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 83 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 83 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 83 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 84 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 84 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 84 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 85 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 85 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 85 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 86 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 86 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 86 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 87 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY2 87 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 87 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 88 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY2 88 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY3 88 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 89 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 89 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 89 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 90 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 90 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY3 90 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 91 -1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 91 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 91 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 92 1.000000 0.000000 0.000000 136.41650
REMARK 290 SMTRY2 92 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY3 92 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 93 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 93 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 93 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 94 0.000000 0.000000 1.000000 136.41650
REMARK 290 SMTRY2 94 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 94 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 95 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 95 0.000000 1.000000 0.000000 136.41650
REMARK 290 SMTRY3 95 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 96 0.000000 0.000000 -1.000000 136.41650
REMARK 290 SMTRY2 96 0.000000 -1.000000 0.000000 136.41650
REMARK 290 SMTRY3 96 -1.000000 0.000000 0.000000 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.7 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -175.5 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 601 LIES ON A SPECIAL POSITION.
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 SER A 0
REMARK 465 LEU A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 GLU A 406
REMARK 465 GLY A 407
REMARK 465 HIS A 408
REMARK 465 HIS A 409
REMARK 465 HIS A 410
REMARK 465 HIS A 411
REMARK 465 HIS A 412
REMARK 465 HIS A 413
REMARK 465 MET B -1
REMARK 465 SER B 0
REMARK 465 LEU B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
REMARK 465 GLU B 406
REMARK 465 GLY B 407
REMARK 465 HIS B 408
REMARK 465 HIS B 409
REMARK 465 HIS B 410
REMARK 465 HIS B 411
REMARK 465 HIS B 412
REMARK 465 HIS B 413
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 ND2 ASN B 376 ND2 ASN B 376 22555 1.83
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 ARG A 268 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG B 268 CD - NE - CZ ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG B 268 NE - CZ - NH1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG B 268 NE - CZ - NH2 ANGL. DEV. = 6.8 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 ALA A 23 -151.09 -146.67
REMARK 500 ARG A 79 -2.37 75.46
REMARK 500 ALA A 88 -31.16 -173.69
REMARK 500 HIS A 99 -64.32 -139.69
REMARK 500 ASP A 111 39.95 -79.40
REMARK 500 TRP A 228 62.86 30.74
REMARK 500 MET A 229 15.73 53.41
REMARK 500 GLU A 253 55.59 39.21
REMARK 500 SER A 278 -178.06 -179.03
REMARK 500 THR A 284 141.90 79.90
REMARK 500 SER A 331 -4.14 75.55
REMARK 500 SER A 332 -137.16 46.04
REMARK 500 LEU A 360 52.13 -90.06
REMARK 500 ALA B 23 -150.85 -146.06
REMARK 500 ARG B 79 -2.05 75.22
REMARK 500 ALA B 88 -30.39 -173.15
REMARK 500 HIS B 99 -64.61 -139.65
REMARK 500 ASP B 111 41.49 -78.67
REMARK 500 TRP B 228 62.45 30.93
REMARK 500 MET B 229 16.52 53.62
REMARK 500 GLU B 253 55.49 37.77
REMARK 500 SER B 278 -178.26 179.34
REMARK 500 THR B 284 142.74 79.34
REMARK 500 SER B 331 -4.33 76.09
REMARK 500 SER B 332 -136.21 46.26
REMARK 500 LEU B 360 52.06 -90.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 226 OD2
REMARK 620 2 GLU A 252 OE2 90.9
REMARK 620 3 GLU A 280 OE1 175.8 91.0
REMARK 620 4 3LR A 501 O1B 85.7 87.1 98.1
REMARK 620 5 3LR A 501 O2 87.9 161.7 91.4 74.7
REMARK 620 6 HOH A 767 O 88.7 108.7 87.1 163.3 89.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 226 OD2
REMARK 620 2 GLU B 252 OE2 88.2
REMARK 620 3 GLU B 280 OE1 176.6 89.8
REMARK 620 4 1N5 B 502 O1A 85.0 85.1 97.5
REMARK 620 5 1N5 B 502 O2 89.6 161.3 93.2 76.2
REMARK 620 6 HOH B 672 O 79.9 108.6 98.2 159.1 89.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3LR A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1N5 B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BOX RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT BOUND LIGAND
DBREF 3CXO A 2 405 UNP Q8ZNF9 Q8ZNF9_SALTY 2 405
DBREF 3CXO B 2 405 UNP Q8ZNF9 Q8ZNF9_SALTY 2 405
SEQADV 3CXO MET A -1 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO SER A 0 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO LEU A 1 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO GLU A 406 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO GLY A 407 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS A 408 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS A 409 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS A 410 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS A 411 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS A 412 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS A 413 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO MET B -1 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO SER B 0 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO LEU B 1 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO GLU B 406 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO GLY B 407 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS B 408 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS B 409 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS B 410 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS B 411 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS B 412 UNP Q8ZNF9 EXPRESSION TAG
SEQADV 3CXO HIS B 413 UNP Q8ZNF9 EXPRESSION TAG
SEQRES 1 A 415 MET SER LEU GLU ASN ILE MET THR LEU PRO LYS ILE LYS
SEQRES 2 A 415 HIS VAL ARG ALA TRP PHE ILE GLY GLY ALA THR ALA GLU
SEQRES 3 A 415 LYS GLY ALA GLY GLY GLY ASP TYR HIS ASP GLN GLY GLY
SEQRES 4 A 415 ASN HIS TRP ILE ASP ASP HIS ILE ALA THR PRO MET SER
SEQRES 5 A 415 LYS TYR ARG ASP TYR GLU GLN SER ARG GLN SER PHE GLY
SEQRES 6 A 415 ILE ASN VAL LEU GLY THR LEU ILE VAL GLU VAL GLU ALA
SEQRES 7 A 415 GLU ASN ARG GLN THR GLY PHE ALA VAL SER THR ALA GLY
SEQRES 8 A 415 GLU MET GLY CYS PHE ILE VAL GLU LYS HIS LEU ASN ARG
SEQRES 9 A 415 PHE ILE GLU GLY LYS CYS VAL SER ASP ILE LYS LEU ILE
SEQRES 10 A 415 HIS ASP GLN MET LEU GLY ALA THR MET TYR TYR SER GLY
SEQRES 11 A 415 SER GLY GLY LEU VAL MET ASN THR ILE SER CYS VAL ASP
SEQRES 12 A 415 LEU ALA LEU TRP ASP LEU PHE GLY LYS VAL VAL GLY LEU
SEQRES 13 A 415 PRO VAL TYR LYS LEU LEU GLY GLY ALA VAL ARG ASP GLU
SEQRES 14 A 415 ILE GLN PHE TYR ALA THR GLY ALA ARG PRO ASP LEU ALA
SEQRES 15 A 415 LYS GLU MET GLY PHE ILE GLY GLY LYS MET PRO THR HIS
SEQRES 16 A 415 TRP GLY PRO HIS ASP GLY ASP ALA GLY ILE ARG LYS ASP
SEQRES 17 A 415 ALA ALA MET VAL ALA ASP MET ARG GLU LYS CYS GLY PRO
SEQRES 18 A 415 ASP PHE TRP LEU MET LEU ASP CYS TRP MET SER GLN ASP
SEQRES 19 A 415 VAL ASN TYR ALA THR LYS LEU ALA HIS ALA CYS ALA PRO
SEQRES 20 A 415 PHE ASN LEU LYS TRP ILE GLU GLU CYS LEU PRO PRO GLN
SEQRES 21 A 415 GLN TYR GLU GLY TYR ARG GLU LEU LYS ARG ASN ALA PRO
SEQRES 22 A 415 ALA GLY MET MET VAL THR SER GLY GLU HIS HIS GLY THR
SEQRES 23 A 415 LEU GLN SER PHE ARG THR LEU ALA GLU THR GLY ILE ASP
SEQRES 24 A 415 ILE MET GLN PRO ASP VAL GLY TRP CYS GLY GLY LEU THR
SEQRES 25 A 415 THR LEU VAL GLU ILE ALA ALA LEU ALA LYS SER ARG GLY
SEQRES 26 A 415 GLN LEU VAL VAL PRO HIS GLY SER SER VAL TYR SER HIS
SEQRES 27 A 415 HIS ALA VAL ILE THR PHE THR ASN THR PRO PHE SER GLU
SEQRES 28 A 415 PHE LEU MET THR SER PRO ASP CYS SER THR LEU ARG PRO
SEQRES 29 A 415 GLN PHE ASP PRO ILE LEU LEU ASP GLU PRO VAL PRO VAL
SEQRES 30 A 415 ASN GLY ARG ILE HIS LYS SER VAL LEU ASP LYS PRO GLY
SEQRES 31 A 415 PHE GLY VAL GLU LEU ASN ARG ASP CYS HIS LEU LYS ARG
SEQRES 32 A 415 PRO TYR SER HIS GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 415 MET SER LEU GLU ASN ILE MET THR LEU PRO LYS ILE LYS
SEQRES 2 B 415 HIS VAL ARG ALA TRP PHE ILE GLY GLY ALA THR ALA GLU
SEQRES 3 B 415 LYS GLY ALA GLY GLY GLY ASP TYR HIS ASP GLN GLY GLY
SEQRES 4 B 415 ASN HIS TRP ILE ASP ASP HIS ILE ALA THR PRO MET SER
SEQRES 5 B 415 LYS TYR ARG ASP TYR GLU GLN SER ARG GLN SER PHE GLY
SEQRES 6 B 415 ILE ASN VAL LEU GLY THR LEU ILE VAL GLU VAL GLU ALA
SEQRES 7 B 415 GLU ASN ARG GLN THR GLY PHE ALA VAL SER THR ALA GLY
SEQRES 8 B 415 GLU MET GLY CYS PHE ILE VAL GLU LYS HIS LEU ASN ARG
SEQRES 9 B 415 PHE ILE GLU GLY LYS CYS VAL SER ASP ILE LYS LEU ILE
SEQRES 10 B 415 HIS ASP GLN MET LEU GLY ALA THR MET TYR TYR SER GLY
SEQRES 11 B 415 SER GLY GLY LEU VAL MET ASN THR ILE SER CYS VAL ASP
SEQRES 12 B 415 LEU ALA LEU TRP ASP LEU PHE GLY LYS VAL VAL GLY LEU
SEQRES 13 B 415 PRO VAL TYR LYS LEU LEU GLY GLY ALA VAL ARG ASP GLU
SEQRES 14 B 415 ILE GLN PHE TYR ALA THR GLY ALA ARG PRO ASP LEU ALA
SEQRES 15 B 415 LYS GLU MET GLY PHE ILE GLY GLY LYS MET PRO THR HIS
SEQRES 16 B 415 TRP GLY PRO HIS ASP GLY ASP ALA GLY ILE ARG LYS ASP
SEQRES 17 B 415 ALA ALA MET VAL ALA ASP MET ARG GLU LYS CYS GLY PRO
SEQRES 18 B 415 ASP PHE TRP LEU MET LEU ASP CYS TRP MET SER GLN ASP
SEQRES 19 B 415 VAL ASN TYR ALA THR LYS LEU ALA HIS ALA CYS ALA PRO
SEQRES 20 B 415 PHE ASN LEU LYS TRP ILE GLU GLU CYS LEU PRO PRO GLN
SEQRES 21 B 415 GLN TYR GLU GLY TYR ARG GLU LEU LYS ARG ASN ALA PRO
SEQRES 22 B 415 ALA GLY MET MET VAL THR SER GLY GLU HIS HIS GLY THR
SEQRES 23 B 415 LEU GLN SER PHE ARG THR LEU ALA GLU THR GLY ILE ASP
SEQRES 24 B 415 ILE MET GLN PRO ASP VAL GLY TRP CYS GLY GLY LEU THR
SEQRES 25 B 415 THR LEU VAL GLU ILE ALA ALA LEU ALA LYS SER ARG GLY
SEQRES 26 B 415 GLN LEU VAL VAL PRO HIS GLY SER SER VAL TYR SER HIS
SEQRES 27 B 415 HIS ALA VAL ILE THR PHE THR ASN THR PRO PHE SER GLU
SEQRES 28 B 415 PHE LEU MET THR SER PRO ASP CYS SER THR LEU ARG PRO
SEQRES 29 B 415 GLN PHE ASP PRO ILE LEU LEU ASP GLU PRO VAL PRO VAL
SEQRES 30 B 415 ASN GLY ARG ILE HIS LYS SER VAL LEU ASP LYS PRO GLY
SEQRES 31 B 415 PHE GLY VAL GLU LEU ASN ARG ASP CYS HIS LEU LYS ARG
SEQRES 32 B 415 PRO TYR SER HIS GLU GLY HIS HIS HIS HIS HIS HIS
HET 3LR A 501 11
HET MG A 500 1
HET MG B 500 1
HET 1N5 B 502 12
HETNAM 3LR 3,6-DIDEOXY-L-ARABINO-HEXONIC ACID
HETNAM MG MAGNESIUM ION
HETNAM 1N5 (2R,4S)-2,4,7-TRIHYDROXYHEPTANOIC ACID
HETSYN 3LR 3-DEOXY-L-RHAMNONIC ACID
FORMUL 3 3LR C6 H12 O5
FORMUL 4 MG 2(MG 2+)
FORMUL 6 1N5 C7 H14 O5
FORMUL 7 HOH *436(H2 O)
HELIX 1 1 HIS A 39 ASP A 43 5 5
HELIX 2 2 TYR A 52 GLU A 56 5 5
HELIX 3 3 ARG A 59 GLY A 63 5 5
HELIX 4 4 ALA A 88 HIS A 99 1 12
HELIX 5 5 LEU A 100 GLU A 105 1 6
HELIX 6 6 ASP A 111 MET A 124 1 14
HELIX 7 7 GLY A 131 GLY A 153 1 23
HELIX 8 8 PRO A 155 LEU A 160 1 6
HELIX 9 9 ARG A 176 GLY A 184 1 9
HELIX 10 10 GLY A 195 HIS A 197 5 3
HELIX 11 11 ASP A 198 GLY A 218 1 21
HELIX 12 12 ASP A 232 ALA A 244 1 13
HELIX 13 13 PRO A 245 ASN A 247 5 3
HELIX 14 14 GLN A 259 ALA A 270 1 12
HELIX 15 15 THR A 284 GLU A 293 1 10
HELIX 16 16 GLY A 308 ARG A 322 1 15
HELIX 17 17 SER A 331 ILE A 340 1 10
HELIX 18 18 SER A 382 ASP A 385 5 4
HELIX 19 19 HIS B 39 ASP B 43 5 5
HELIX 20 20 TYR B 52 GLU B 56 5 5
HELIX 21 21 ARG B 59 GLY B 63 5 5
HELIX 22 22 ALA B 88 HIS B 99 1 12
HELIX 23 23 LEU B 100 GLU B 105 1 6
HELIX 24 24 ASP B 111 MET B 124 1 14
HELIX 25 25 GLY B 131 GLY B 153 1 23
HELIX 26 26 PRO B 155 LEU B 160 1 6
HELIX 27 27 ARG B 176 GLY B 184 1 9
HELIX 28 28 GLY B 195 HIS B 197 5 3
HELIX 29 29 ASP B 198 GLY B 218 1 21
HELIX 30 30 ASP B 232 ALA B 244 1 13
HELIX 31 31 PRO B 245 ASN B 247 5 3
HELIX 32 32 GLN B 259 ALA B 270 1 12
HELIX 33 33 THR B 284 GLU B 293 1 10
HELIX 34 34 GLY B 308 ARG B 322 1 15
HELIX 35 35 SER B 331 ILE B 340 1 10
HELIX 36 36 SER B 382 ASP B 385 5 4
SHEET 1 A 3 ILE A 10 ILE A 18 0
SHEET 2 A 3 THR A 69 ALA A 76 -1 O GLU A 75 N HIS A 12
SHEET 3 A 3 THR A 81 THR A 87 -1 O SER A 86 N LEU A 70
SHEET 1 B 8 LEU A 325 VAL A 326 0
SHEET 2 B 8 ILE A 298 MET A 299 1 N MET A 299 O LEU A 325
SHEET 3 B 8 MET A 275 SER A 278 1 N SER A 278 O ILE A 298
SHEET 4 B 8 TRP A 250 GLU A 252 1 N ILE A 251 O MET A 275
SHEET 5 B 8 TRP A 222 ASP A 226 1 N LEU A 225 O GLU A 252
SHEET 6 B 8 GLY A 187 PRO A 191 1 N MET A 190 O ASP A 226
SHEET 7 B 8 GLU A 167 THR A 173 1 N ALA A 172 O GLY A 187
SHEET 8 B 8 SER A 348 LEU A 351 1 O PHE A 350 N THR A 173
SHEET 1 C 8 LEU A 325 VAL A 326 0
SHEET 2 C 8 ILE A 298 MET A 299 1 N MET A 299 O LEU A 325
SHEET 3 C 8 MET A 275 SER A 278 1 N SER A 278 O ILE A 298
SHEET 4 C 8 TRP A 250 GLU A 252 1 N ILE A 251 O MET A 275
SHEET 5 C 8 TRP A 222 ASP A 226 1 N LEU A 225 O GLU A 252
SHEET 6 C 8 GLY A 187 PRO A 191 1 N MET A 190 O ASP A 226
SHEET 7 C 8 GLU A 167 THR A 173 1 N ALA A 172 O GLY A 187
SHEET 8 C 8 ARG A 378 HIS A 380 -1 O ILE A 379 N ILE A 168
SHEET 1 D 2 LEU A 368 LEU A 369 0
SHEET 2 D 2 GLU A 392 LEU A 393 -1 O GLU A 392 N LEU A 369
SHEET 1 E 3 ILE B 10 ILE B 18 0
SHEET 2 E 3 THR B 69 ALA B 76 -1 O GLU B 75 N HIS B 12
SHEET 3 E 3 THR B 81 THR B 87 -1 O SER B 86 N LEU B 70
SHEET 1 F 8 LEU B 325 VAL B 326 0
SHEET 2 F 8 ILE B 298 MET B 299 1 N MET B 299 O LEU B 325
SHEET 3 F 8 MET B 275 SER B 278 1 N SER B 278 O ILE B 298
SHEET 4 F 8 TRP B 250 GLU B 252 1 N ILE B 251 O MET B 275
SHEET 5 F 8 TRP B 222 ASP B 226 1 N LEU B 225 O GLU B 252
SHEET 6 F 8 GLY B 187 PRO B 191 1 N MET B 190 O ASP B 226
SHEET 7 F 8 GLU B 167 THR B 173 1 N ALA B 172 O GLY B 187
SHEET 8 F 8 SER B 348 LEU B 351 1 O PHE B 350 N THR B 173
SHEET 1 G 8 LEU B 325 VAL B 326 0
SHEET 2 G 8 ILE B 298 MET B 299 1 N MET B 299 O LEU B 325
SHEET 3 G 8 MET B 275 SER B 278 1 N SER B 278 O ILE B 298
SHEET 4 G 8 TRP B 250 GLU B 252 1 N ILE B 251 O MET B 275
SHEET 5 G 8 TRP B 222 ASP B 226 1 N LEU B 225 O GLU B 252
SHEET 6 G 8 GLY B 187 PRO B 191 1 N MET B 190 O ASP B 226
SHEET 7 G 8 GLU B 167 THR B 173 1 N ALA B 172 O GLY B 187
SHEET 8 G 8 ARG B 378 HIS B 380 -1 O ILE B 379 N ILE B 168
SHEET 1 H 2 LEU B 368 LEU B 369 0
SHEET 2 H 2 GLU B 392 LEU B 393 -1 O GLU B 392 N LEU B 369
LINK OD2 ASP A 226 MG MG A 500 1555 1555 2.07
LINK OE2 GLU A 252 MG MG A 500 1555 1555 1.99
LINK OE1 GLU A 280 MG MG A 500 1555 1555 2.01
LINK MG MG A 500 O1B 3LR A 501 1555 1555 2.20
LINK MG MG A 500 O2 3LR A 501 1555 1555 2.21
LINK MG MG A 500 O HOH A 767 1555 1555 2.10
LINK OD2 ASP B 226 MG MG B 500 1555 1555 2.05
LINK OE2 GLU B 252 MG MG B 500 1555 1555 2.03
LINK OE1 GLU B 280 MG MG B 500 1555 1555 2.04
LINK MG MG B 500 O1A 1N5 B 502 1555 1555 2.16
LINK MG MG B 500 O2 1N5 B 502 1555 1555 2.13
LINK MG MG B 500 O HOH B 672 1555 1555 2.11
CISPEP 1 ASP A 365 PRO A 366 0 0.13
CISPEP 2 ASP B 365 PRO B 366 0 0.12
SITE 1 AC1 12 HIS A 33 TRP A 40 ILE A 45 ARG A 59
SITE 2 AC1 12 LYS A 189 ASP A 226 TRP A 228 GLU A 252
SITE 3 AC1 12 GLU A 280 HIS A 329 GLU A 349 LEU A 351
SITE 1 AC2 3 ASP A 226 GLU A 252 GLU A 280
SITE 1 AC3 3 ASP B 226 GLU B 252 GLU B 280
SITE 1 AC4 12 HIS B 33 ILE B 45 ARG B 59 LYS B 189
SITE 2 AC4 12 PRO B 191 ASP B 226 TRP B 228 GLU B 252
SITE 3 AC4 12 GLU B 280 HIS B 329 GLU B 349 LEU B 351
CRYST1 272.833 272.833 272.833 90.00 90.00 90.00 F 4 3 2 192
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 0.003665 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003665 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
