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HEADER HYDROLASE 21-MAR-16 5IVK
TITLE THE ALPHA-ESTERASE-7 CARBOXYLESTERASE, E3, FROM THE BLOWFLY LUCILIA
TITLE 2 CUPRINA: PHOSPHORYLATED-ENZYME ENSEMBLE REFINEMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: GREEN BOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 GENE: LCAE7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, ORGANOPHOSPHATE, PROTEIN DYNAMICS,
KEYWDS 2 ACETYLCHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
NUMMDL 43
AUTHOR G.J.CORREY,C.J.JACKSON
REVDAT 1 22-JUN-16 5IVK 0
JRNL AUTH G.J.CORREY,P.D.CARR,T.MEIRELLES,P.D.MABBITT,N.J.FRASER,
JRNL AUTH 2 M.WEIK,C.J.JACKSON
JRNL TITL MAPPING THE ACCESSIBLE CONFORMATIONAL LANDSCAPE OF AN INSECT
JRNL TITL 2 CARBOXYLESTERASE USING CONFORMATIONAL ENSEMBLE ANALYSIS AND
JRNL TITL 3 KINETIC CRYSTALLOGRAPHY.
JRNL REF STRUCTURE V. 24 977 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27210287
JRNL DOI 10.1016/J.STR.2016.04.009
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 89888
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 : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4499
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 42.0250 - 4.7519 1.00 3029 174 0.1507 0.1742
REMARK 3 2 4.7519 - 3.7725 1.00 2938 154 0.1483 0.1596
REMARK 3 3 3.7725 - 3.2958 1.00 2921 137 0.1689 0.1908
REMARK 3 4 3.2958 - 2.9946 1.00 2877 148 0.1782 0.2278
REMARK 3 5 2.9946 - 2.7800 1.00 2908 144 0.1738 0.2148
REMARK 3 6 2.7800 - 2.6161 1.00 2856 144 0.1695 0.1938
REMARK 3 7 2.6161 - 2.4851 1.00 2841 159 0.1755 0.2036
REMARK 3 8 2.4851 - 2.3769 1.00 2846 148 0.1774 0.2620
REMARK 3 9 2.3769 - 2.2854 1.00 2884 143 0.1826 0.2080
REMARK 3 10 2.2854 - 2.2066 1.00 2845 146 0.1824 0.2397
REMARK 3 11 2.2066 - 2.1376 1.00 2866 130 0.1788 0.2326
REMARK 3 12 2.1376 - 2.0765 1.00 2854 138 0.1835 0.2173
REMARK 3 13 2.0765 - 2.0218 1.00 2818 146 0.1803 0.2401
REMARK 3 14 2.0218 - 1.9725 1.00 2801 178 0.1862 0.2440
REMARK 3 15 1.9725 - 1.9277 1.00 2875 144 0.1904 0.2043
REMARK 3 16 1.9277 - 1.8866 1.00 2825 134 0.1988 0.2849
REMARK 3 17 1.8866 - 1.8489 1.00 2800 149 0.1984 0.2308
REMARK 3 18 1.8489 - 1.8140 1.00 2848 156 0.1893 0.2483
REMARK 3 19 1.8140 - 1.7816 1.00 2764 167 0.1961 0.2487
REMARK 3 20 1.7816 - 1.7514 1.00 2856 160 0.1934 0.2540
REMARK 3 21 1.7514 - 1.7232 1.00 2759 154 0.2008 0.2641
REMARK 3 22 1.7232 - 1.6966 1.00 2887 159 0.2141 0.2649
REMARK 3 23 1.6966 - 1.6717 1.00 2749 162 0.2235 0.2942
REMARK 3 24 1.6717 - 1.6481 1.00 2852 156 0.2251 0.2876
REMARK 3 25 1.6481 - 1.6259 1.00 2764 150 0.2304 0.2842
REMARK 3 26 1.6259 - 1.6048 1.00 2864 152 0.2422 0.3134
REMARK 3 27 1.6048 - 1.5847 1.00 2799 154 0.2507 0.2957
REMARK 3 28 1.5847 - 1.5656 1.00 2823 137 0.2685 0.3117
REMARK 3 29 1.5656 - 1.5474 1.00 2819 139 0.2831 0.3088
REMARK 3 30 1.5474 - 1.5300 1.00 2821 137 0.2918 0.3189
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 : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.013 NULL
REMARK 3 ANGLE : 1.332 NULL
REMARK 3 CHIRALITY : 0.061 NULL
REMARK 3 PLANARITY : 0.009 NULL
REMARK 3 DIHEDRAL : 17.880 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219498.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8266
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89882
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 42.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.00
REMARK 200 R MERGE FOR SHELL (I) : 1.79000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 4.5, PEG 2K
REMARK 280 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.90900
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 112.90900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.90800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.62700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.90800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.62700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 112.90900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.90800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.62700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.90900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.90800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.62700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 A 829 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 1 MET A -6
REMARK 465 1 HIS A -5
REMARK 465 1 HIS A -4
REMARK 465 1 HIS A -3
REMARK 465 1 HIS A -2
REMARK 465 1 HIS A -1
REMARK 465 1 HIS A 0
REMARK 465 1 MET A 1
REMARK 465 1 ASN A 2
REMARK 465 1 PHE A 3
REMARK 465 1 ASN A 4
REMARK 465 2 MET A -6
REMARK 465 2 HIS A -5
REMARK 465 2 HIS A -4
REMARK 465 2 HIS A -3
REMARK 465 2 HIS A -2
REMARK 465 2 HIS A -1
REMARK 465 2 HIS A 0
REMARK 465 2 MET A 1
REMARK 465 2 ASN A 2
REMARK 465 2 PHE A 3
REMARK 465 2 ASN A 4
REMARK 465 3 MET A -6
REMARK 465 3 HIS A -5
REMARK 465 3 HIS A -4
REMARK 465 3 HIS A -3
REMARK 465 3 HIS A -2
REMARK 465 3 HIS A -1
REMARK 465 3 HIS A 0
REMARK 465 3 MET A 1
REMARK 465 3 ASN A 2
REMARK 465 3 PHE A 3
REMARK 465 3 ASN A 4
REMARK 465 4 MET A -6
REMARK 465 4 HIS A -5
REMARK 465 4 HIS A -4
REMARK 465 4 HIS A -3
REMARK 465 4 HIS A -2
REMARK 465 4 HIS A -1
REMARK 465 4 HIS A 0
REMARK 465 4 MET A 1
REMARK 465 4 ASN A 2
REMARK 465 4 PHE A 3
REMARK 465 4 ASN A 4
REMARK 465 5 MET A -6
REMARK 465 5 HIS A -5
REMARK 465 5 HIS A -4
REMARK 465 5 HIS A -3
REMARK 465 5 HIS A -2
REMARK 465 5 HIS A -1
REMARK 465 5 HIS A 0
REMARK 465 5 MET A 1
REMARK 465 5 ASN A 2
REMARK 465 5 PHE A 3
REMARK 465 5 ASN A 4
REMARK 465 6 MET A -6
REMARK 465 6 HIS A -5
REMARK 465 6 HIS A -4
REMARK 465 6 HIS A -3
REMARK 465 6 HIS A -2
REMARK 465 6 HIS A -1
REMARK 465 6 HIS A 0
REMARK 465 6 MET A 1
REMARK 465 6 ASN A 2
REMARK 465 6 PHE A 3
REMARK 465 6 ASN A 4
REMARK 465 7 MET A -6
REMARK 465 7 HIS A -5
REMARK 465 7 HIS A -4
REMARK 465 7 HIS A -3
REMARK 465 7 HIS A -2
REMARK 465 7 HIS A -1
REMARK 465 7 HIS A 0
REMARK 465 7 MET A 1
REMARK 465 7 ASN A 2
REMARK 465 7 PHE A 3
REMARK 465 7 ASN A 4
REMARK 465 8 MET A -6
REMARK 465 8 HIS A -5
REMARK 465 8 HIS A -4
REMARK 465 8 HIS A -3
REMARK 465 8 HIS A -2
REMARK 465 8 HIS A -1
REMARK 465 8 HIS A 0
REMARK 465 8 MET A 1
REMARK 465 8 ASN A 2
REMARK 465 8 PHE A 3
REMARK 465 8 ASN A 4
REMARK 465 9 MET A -6
REMARK 465 9 HIS A -5
REMARK 465 9 HIS A -4
REMARK 465 9 HIS A -3
REMARK 465 9 HIS A -2
REMARK 465 9 HIS A -1
REMARK 465 9 HIS A 0
REMARK 465 9 MET A 1
REMARK 465 9 ASN A 2
REMARK 465 9 PHE A 3
REMARK 465 9 ASN A 4
REMARK 465 10 MET A -6
REMARK 465 10 HIS A -5
REMARK 465 10 HIS A -4
REMARK 465 10 HIS A -3
REMARK 465 10 HIS A -2
REMARK 465 10 HIS A -1
REMARK 465 10 HIS A 0
REMARK 465 10 MET A 1
REMARK 465 10 ASN A 2
REMARK 465 10 PHE A 3
REMARK 465 10 ASN A 4
REMARK 465 11 MET A -6
REMARK 465 11 HIS A -5
REMARK 465 11 HIS A -4
REMARK 465 11 HIS A -3
REMARK 465 11 HIS A -2
REMARK 465 11 HIS A -1
REMARK 465 11 HIS A 0
REMARK 465 11 MET A 1
REMARK 465 11 ASN A 2
REMARK 465 11 PHE A 3
REMARK 465 11 ASN A 4
REMARK 465 12 MET A -6
REMARK 465 12 HIS A -5
REMARK 465 12 HIS A -4
REMARK 465 12 HIS A -3
REMARK 465 12 HIS A -2
REMARK 465 12 HIS A -1
REMARK 465 12 HIS A 0
REMARK 465 12 MET A 1
REMARK 465 12 ASN A 2
REMARK 465 12 PHE A 3
REMARK 465 12 ASN A 4
REMARK 465 13 MET A -6
REMARK 465 13 HIS A -5
REMARK 465 13 HIS A -4
REMARK 465 13 HIS A -3
REMARK 465 13 HIS A -2
REMARK 465 13 HIS A -1
REMARK 465 13 HIS A 0
REMARK 465 13 MET A 1
REMARK 465 13 ASN A 2
REMARK 465 13 PHE A 3
REMARK 465 13 ASN A 4
REMARK 465 14 MET A -6
REMARK 465 14 HIS A -5
REMARK 465 14 HIS A -4
REMARK 465 14 HIS A -3
REMARK 465 14 HIS A -2
REMARK 465 14 HIS A -1
REMARK 465 14 HIS A 0
REMARK 465 14 MET A 1
REMARK 465 14 ASN A 2
REMARK 465 14 PHE A 3
REMARK 465 14 ASN A 4
REMARK 465 15 MET A -6
REMARK 465 15 HIS A -5
REMARK 465 15 HIS A -4
REMARK 465 15 HIS A -3
REMARK 465 15 HIS A -2
REMARK 465 15 HIS A -1
REMARK 465 15 HIS A 0
REMARK 465 15 MET A 1
REMARK 465 15 ASN A 2
REMARK 465 15 PHE A 3
REMARK 465 15 ASN A 4
REMARK 465 16 MET A -6
REMARK 465 16 HIS A -5
REMARK 465 16 HIS A -4
REMARK 465 16 HIS A -3
REMARK 465 16 HIS A -2
REMARK 465 16 HIS A -1
REMARK 465 16 HIS A 0
REMARK 465 16 MET A 1
REMARK 465 16 ASN A 2
REMARK 465 16 PHE A 3
REMARK 465 16 ASN A 4
REMARK 465 17 MET A -6
REMARK 465 17 HIS A -5
REMARK 465 17 HIS A -4
REMARK 465 17 HIS A -3
REMARK 465 17 HIS A -2
REMARK 465 17 HIS A -1
REMARK 465 17 HIS A 0
REMARK 465 17 MET A 1
REMARK 465 17 ASN A 2
REMARK 465 17 PHE A 3
REMARK 465 17 ASN A 4
REMARK 465 18 MET A -6
REMARK 465 18 HIS A -5
REMARK 465 18 HIS A -4
REMARK 465 18 HIS A -3
REMARK 465 18 HIS A -2
REMARK 465 18 HIS A -1
REMARK 465 18 HIS A 0
REMARK 465 18 MET A 1
REMARK 465 18 ASN A 2
REMARK 465 18 PHE A 3
REMARK 465 18 ASN A 4
REMARK 465 19 MET A -6
REMARK 465 19 HIS A -5
REMARK 465 19 HIS A -4
REMARK 465 19 HIS A -3
REMARK 465 19 HIS A -2
REMARK 465 19 HIS A -1
REMARK 465 19 HIS A 0
REMARK 465 19 MET A 1
REMARK 465 19 ASN A 2
REMARK 465 19 PHE A 3
REMARK 465 19 ASN A 4
REMARK 465 20 MET A -6
REMARK 465 20 HIS A -5
REMARK 465 20 HIS A -4
REMARK 465 20 HIS A -3
REMARK 465 20 HIS A -2
REMARK 465 20 HIS A -1
REMARK 465 20 HIS A 0
REMARK 465 20 MET A 1
REMARK 465 20 ASN A 2
REMARK 465 20 PHE A 3
REMARK 465 20 ASN A 4
REMARK 465 21 MET A -6
REMARK 465 21 HIS A -5
REMARK 465 21 HIS A -4
REMARK 465 21 HIS A -3
REMARK 465 21 HIS A -2
REMARK 465 21 HIS A -1
REMARK 465 21 HIS A 0
REMARK 465 21 MET A 1
REMARK 465 21 ASN A 2
REMARK 465 21 PHE A 3
REMARK 465 21 ASN A 4
REMARK 465 22 MET A -6
REMARK 465 22 HIS A -5
REMARK 465 22 HIS A -4
REMARK 465 22 HIS A -3
REMARK 465 22 HIS A -2
REMARK 465 22 HIS A -1
REMARK 465 22 HIS A 0
REMARK 465 22 MET A 1
REMARK 465 22 ASN A 2
REMARK 465 22 PHE A 3
REMARK 465 22 ASN A 4
REMARK 465 23 MET A -6
REMARK 465 23 HIS A -5
REMARK 465 23 HIS A -4
REMARK 465 23 HIS A -3
REMARK 465 23 HIS A -2
REMARK 465 23 HIS A -1
REMARK 465 23 HIS A 0
REMARK 465 23 MET A 1
REMARK 465 23 ASN A 2
REMARK 465 23 PHE A 3
REMARK 465 23 ASN A 4
REMARK 465 24 MET A -6
REMARK 465 24 HIS A -5
REMARK 465 24 HIS A -4
REMARK 465 24 HIS A -3
REMARK 465 24 HIS A -2
REMARK 465 24 HIS A -1
REMARK 465 24 HIS A 0
REMARK 465 24 MET A 1
REMARK 465 24 ASN A 2
REMARK 465 24 PHE A 3
REMARK 465 24 ASN A 4
REMARK 465 25 MET A -6
REMARK 465 25 HIS A -5
REMARK 465 25 HIS A -4
REMARK 465 25 HIS A -3
REMARK 465 25 HIS A -2
REMARK 465 25 HIS A -1
REMARK 465 25 HIS A 0
REMARK 465 25 MET A 1
REMARK 465 25 ASN A 2
REMARK 465 25 PHE A 3
REMARK 465 25 ASN A 4
REMARK 465 26 MET A -6
REMARK 465 26 HIS A -5
REMARK 465 26 HIS A -4
REMARK 465 26 HIS A -3
REMARK 465 26 HIS A -2
REMARK 465 26 HIS A -1
REMARK 465 26 HIS A 0
REMARK 465 26 MET A 1
REMARK 465 26 ASN A 2
REMARK 465 26 PHE A 3
REMARK 465 26 ASN A 4
REMARK 465 27 MET A -6
REMARK 465 27 HIS A -5
REMARK 465 27 HIS A -4
REMARK 465 27 HIS A -3
REMARK 465 27 HIS A -2
REMARK 465 27 HIS A -1
REMARK 465 27 HIS A 0
REMARK 465 27 MET A 1
REMARK 465 27 ASN A 2
REMARK 465 27 PHE A 3
REMARK 465 27 ASN A 4
REMARK 465 28 MET A -6
REMARK 465 28 HIS A -5
REMARK 465 28 HIS A -4
REMARK 465 28 HIS A -3
REMARK 465 28 HIS A -2
REMARK 465 28 HIS A -1
REMARK 465 28 HIS A 0
REMARK 465 28 MET A 1
REMARK 465 28 ASN A 2
REMARK 465 28 PHE A 3
REMARK 465 28 ASN A 4
REMARK 465 29 MET A -6
REMARK 465 29 HIS A -5
REMARK 465 29 HIS A -4
REMARK 465 29 HIS A -3
REMARK 465 29 HIS A -2
REMARK 465 29 HIS A -1
REMARK 465 29 HIS A 0
REMARK 465 29 MET A 1
REMARK 465 29 ASN A 2
REMARK 465 29 PHE A 3
REMARK 465 29 ASN A 4
REMARK 465 30 MET A -6
REMARK 465 30 HIS A -5
REMARK 465 30 HIS A -4
REMARK 465 30 HIS A -3
REMARK 465 30 HIS A -2
REMARK 465 30 HIS A -1
REMARK 465 30 HIS A 0
REMARK 465 30 MET A 1
REMARK 465 30 ASN A 2
REMARK 465 30 PHE A 3
REMARK 465 30 ASN A 4
REMARK 465 31 MET A -6
REMARK 465 31 HIS A -5
REMARK 465 31 HIS A -4
REMARK 465 31 HIS A -3
REMARK 465 31 HIS A -2
REMARK 465 31 HIS A -1
REMARK 465 31 HIS A 0
REMARK 465 31 MET A 1
REMARK 465 31 ASN A 2
REMARK 465 31 PHE A 3
REMARK 465 31 ASN A 4
REMARK 465 32 MET A -6
REMARK 465 32 HIS A -5
REMARK 465 32 HIS A -4
REMARK 465 32 HIS A -3
REMARK 465 32 HIS A -2
REMARK 465 32 HIS A -1
REMARK 465 32 HIS A 0
REMARK 465 32 MET A 1
REMARK 465 32 ASN A 2
REMARK 465 32 PHE A 3
REMARK 465 32 ASN A 4
REMARK 465 33 MET A -6
REMARK 465 33 HIS A -5
REMARK 465 33 HIS A -4
REMARK 465 33 HIS A -3
REMARK 465 33 HIS A -2
REMARK 465 33 HIS A -1
REMARK 465 33 HIS A 0
REMARK 465 33 MET A 1
REMARK 465 33 ASN A 2
REMARK 465 33 PHE A 3
REMARK 465 33 ASN A 4
REMARK 465 34 MET A -6
REMARK 465 34 HIS A -5
REMARK 465 34 HIS A -4
REMARK 465 34 HIS A -3
REMARK 465 34 HIS A -2
REMARK 465 34 HIS A -1
REMARK 465 34 HIS A 0
REMARK 465 34 MET A 1
REMARK 465 34 ASN A 2
REMARK 465 34 PHE A 3
REMARK 465 34 ASN A 4
REMARK 465 35 MET A -6
REMARK 465 35 HIS A -5
REMARK 465 35 HIS A -4
REMARK 465 35 HIS A -3
REMARK 465 35 HIS A -2
REMARK 465 35 HIS A -1
REMARK 465 35 HIS A 0
REMARK 465 35 MET A 1
REMARK 465 35 ASN A 2
REMARK 465 35 PHE A 3
REMARK 465 35 ASN A 4
REMARK 465 36 MET A -6
REMARK 465 36 HIS A -5
REMARK 465 36 HIS A -4
REMARK 465 36 HIS A -3
REMARK 465 36 HIS A -2
REMARK 465 36 HIS A -1
REMARK 465 36 HIS A 0
REMARK 465 36 MET A 1
REMARK 465 36 ASN A 2
REMARK 465 36 PHE A 3
REMARK 465 36 ASN A 4
REMARK 465 37 MET A -6
REMARK 465 37 HIS A -5
REMARK 465 37 HIS A -4
REMARK 465 37 HIS A -3
REMARK 465 37 HIS A -2
REMARK 465 37 HIS A -1
REMARK 465 37 HIS A 0
REMARK 465 37 MET A 1
REMARK 465 37 ASN A 2
REMARK 465 37 PHE A 3
REMARK 465 37 ASN A 4
REMARK 465 38 MET A -6
REMARK 465 38 HIS A -5
REMARK 465 38 HIS A -4
REMARK 465 38 HIS A -3
REMARK 465 38 HIS A -2
REMARK 465 38 HIS A -1
REMARK 465 38 HIS A 0
REMARK 465 38 MET A 1
REMARK 465 38 ASN A 2
REMARK 465 38 PHE A 3
REMARK 465 38 ASN A 4
REMARK 465 39 MET A -6
REMARK 465 39 HIS A -5
REMARK 465 39 HIS A -4
REMARK 465 39 HIS A -3
REMARK 465 39 HIS A -2
REMARK 465 39 HIS A -1
REMARK 465 39 HIS A 0
REMARK 465 39 MET A 1
REMARK 465 39 ASN A 2
REMARK 465 39 PHE A 3
REMARK 465 39 ASN A 4
REMARK 465 40 MET A -6
REMARK 465 40 HIS A -5
REMARK 465 40 HIS A -4
REMARK 465 40 HIS A -3
REMARK 465 40 HIS A -2
REMARK 465 40 HIS A -1
REMARK 465 40 HIS A 0
REMARK 465 40 MET A 1
REMARK 465 40 ASN A 2
REMARK 465 40 PHE A 3
REMARK 465 40 ASN A 4
REMARK 465 41 MET A -6
REMARK 465 41 HIS A -5
REMARK 465 41 HIS A -4
REMARK 465 41 HIS A -3
REMARK 465 41 HIS A -2
REMARK 465 41 HIS A -1
REMARK 465 41 HIS A 0
REMARK 465 41 MET A 1
REMARK 465 41 ASN A 2
REMARK 465 41 PHE A 3
REMARK 465 41 ASN A 4
REMARK 465 42 MET A -6
REMARK 465 42 HIS A -5
REMARK 465 42 HIS A -4
REMARK 465 42 HIS A -3
REMARK 465 42 HIS A -2
REMARK 465 42 HIS A -1
REMARK 465 42 HIS A 0
REMARK 465 42 MET A 1
REMARK 465 42 ASN A 2
REMARK 465 42 PHE A 3
REMARK 465 42 ASN A 4
REMARK 465 43 MET A -6
REMARK 465 43 HIS A -5
REMARK 465 43 HIS A -4
REMARK 465 43 HIS A -3
REMARK 465 43 HIS A -2
REMARK 465 43 HIS A -1
REMARK 465 43 HIS A 0
REMARK 465 43 MET A 1
REMARK 465 43 ASN A 2
REMARK 465 43 PHE A 3
REMARK 465 43 ASN A 4
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 1 ASP A 83 CG OD1 OD2
REMARK 470 2 ASP A 83 CG OD1 OD2
REMARK 470 3 ASP A 83 CG OD1 OD2
REMARK 470 4 ASP A 83 CG OD1 OD2
REMARK 470 5 ASP A 83 CG OD1 OD2
REMARK 470 6 ASP A 83 CG OD1 OD2
REMARK 470 7 ASP A 83 CG OD1 OD2
REMARK 470 8 ASP A 83 CG OD1 OD2
REMARK 470 9 ASP A 83 CG OD1 OD2
REMARK 470 10 ASP A 83 CG OD1 OD2
REMARK 470 11 ASP A 83 CG OD1 OD2
REMARK 470 12 ASP A 83 CG OD1 OD2
REMARK 470 13 ASP A 83 CG OD1 OD2
REMARK 470 14 ASP A 83 CG OD1 OD2
REMARK 470 15 ASP A 83 CG OD1 OD2
REMARK 470 16 ASP A 83 CG OD1 OD2
REMARK 470 17 ASP A 83 CG OD1 OD2
REMARK 470 18 ASP A 83 CG OD1 OD2
REMARK 470 19 ASP A 83 CG OD1 OD2
REMARK 470 20 ASP A 83 CG OD1 OD2
REMARK 470 21 ASP A 83 CG OD1 OD2
REMARK 470 22 ASP A 83 CG OD1 OD2
REMARK 470 23 ASP A 83 CG OD1 OD2
REMARK 470 24 ASP A 83 CG OD1 OD2
REMARK 470 25 ASP A 83 CG OD1 OD2
REMARK 470 26 ASP A 83 CG OD1 OD2
REMARK 470 27 ASP A 83 CG OD1 OD2
REMARK 470 28 ASP A 83 CG OD1 OD2
REMARK 470 29 ASP A 83 CG OD1 OD2
REMARK 470 30 ASP A 83 CG OD1 OD2
REMARK 470 31 ASP A 83 CG OD1 OD2
REMARK 470 32 ASP A 83 CG OD1 OD2
REMARK 470 33 ASP A 83 CG OD1 OD2
REMARK 470 34 ASP A 83 CG OD1 OD2
REMARK 470 35 ASP A 83 CG OD1 OD2
REMARK 470 36 ASP A 83 CG OD1 OD2
REMARK 470 37 ASP A 83 CG OD1 OD2
REMARK 470 38 ASP A 83 CG OD1 OD2
REMARK 470 39 ASP A 83 CG OD1 OD2
REMARK 470 40 ASP A 83 CG OD1 OD2
REMARK 470 41 ASP A 83 CG OD1 OD2
REMARK 470 42 ASP A 83 CG OD1 OD2
REMARK 470 43 ASP A 83 CG OD1 OD2
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 1 MET A 362 CG MET A 362 SD 0.159
REMARK 500 4 GLU A 530 CB GLU A 530 CG 0.119
REMARK 500 5 GLU A 124 CB GLU A 124 CG 0.116
REMARK 500 8 LYS A 126 C ARG A 127 N 0.204
REMARK 500 9 CYS A 89 CB CYS A 89 SG 0.196
REMARK 500 9 GLU A 379 CG GLU A 379 CD 0.097
REMARK 500 10 LYS A 126 C ARG A 127 N 0.184
REMARK 500 10 LYS A 327 CB LYS A 327 CG 0.164
REMARK 500 11 CYS A 17 CB CYS A 17 SG -0.123
REMARK 500 12 CYS A 106 CB CYS A 106 SG -0.103
REMARK 500 13 CYS A 17 CB CYS A 17 SG -0.130
REMARK 500 13 LYS A 126 C ARG A 127 N 0.257
REMARK 500 15 CYS A 17 CB CYS A 17 SG 0.113
REMARK 500 15 LYS A 126 C ARG A 127 N 0.168
REMARK 500 20 CYS A 89 CB CYS A 89 SG -0.155
REMARK 500 21 GLU A 142 CB GLU A 142 CG 0.121
REMARK 500 23 CYS A 106 CB CYS A 106 SG 0.195
REMARK 500 24 LYS A 126 C ARG A 127 N 0.215
REMARK 500 24 GLU A 295 CG GLU A 295 CD -0.092
REMARK 500 25 CYS A 89 CB CYS A 89 SG -0.100
REMARK 500 26 GLU A 534 CB GLU A 534 CG 0.133
REMARK 500 27 LYS A 126 C ARG A 127 N 0.141
REMARK 500 27 GLU A 217 CB GLU A 217 CG 0.114
REMARK 500 28 LYS A 126 C ARG A 127 N 0.234
REMARK 500 29 PRO A 66 C PRO A 67 N -0.116
REMARK 500 29 GLU A 331 CB GLU A 331 CG 0.141
REMARK 500 30 CYS A 89 CB CYS A 89 SG 0.166
REMARK 500 30 GLU A 498 CB GLU A 498 CG 0.115
REMARK 500 31 GLU A 70 CB GLU A 70 CG 0.125
REMARK 500 31 GLU A 331 CG GLU A 331 CD 0.092
REMARK 500 31 GLU A 498 CB GLU A 498 CG 0.146
REMARK 500 33 LYS A 126 C ARG A 127 N 0.155
REMARK 500 33 VAL A 524 CB VAL A 524 CG1 -0.133
REMARK 500 34 LYS A 126 C ARG A 127 N 0.241
REMARK 500 34 GLU A 370 CB GLU A 370 CG 0.149
REMARK 500 34 GLU A 384 CB GLU A 384 CG 0.136
REMARK 500 35 LYS A 126 C ARG A 127 N 0.175
REMARK 500 38 PRO A 66 C PRO A 67 N -0.136
REMARK 500 38 CYS A 106 CB CYS A 106 SG 0.117
REMARK 500 39 PRO A 66 C PRO A 67 N -0.114
REMARK 500 40 LYS A 126 C ARG A 127 N 0.164
REMARK 500 40 GLU A 295 CB GLU A 295 CG 0.141
REMARK 500 40 GLU A 295 CG GLU A 295 CD 0.092
REMARK 500 42 PRO A 66 C PRO A 67 N -0.122
REMARK 500 42 MET A 147 CB MET A 147 CG 0.223
REMARK 500 43 LYS A 126 C ARG A 127 N 0.151
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 1 ASP A 179 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 1 ASP A 179 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 1 PRO A 513 C - N - CD ANGL. DEV. = -18.7 DEGREES
REMARK 500 2 CYS A 106 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 2 MET A 362 CB - CG - SD ANGL. DEV. = -19.3 DEGREES
REMARK 500 3 ARG A 78 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 ARG A 461 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 ARG A 486 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 LYS A 92 CD - CE - NZ ANGL. DEV. = 15.0 DEGREES
REMARK 500 4 MET A 147 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 4 LEU A 236 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 4 GLU A 544 OE1 - CD - OE2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 6 ASP A 289 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 7 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 7 ARG A 464 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 CYS A 89 CA - CB - SG ANGL. DEV. = 13.2 DEGREES
REMARK 500 9 ASP A 146 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 9 ASP A 289 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 10 MET A 362 CB - CG - SD ANGL. DEV. = -23.1 DEGREES
REMARK 500 10 ARG A 486 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 11 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 12 MET A 308 CG - SD - CE ANGL. DEV. = -12.3 DEGREES
REMARK 500 12 LEU A 475 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 12 ARG A 499 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 ARG A 567 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 MET A 308 CG - SD - CE ANGL. DEV. = -13.2 DEGREES
REMARK 500 13 MET A 521 CG - SD - CE ANGL. DEV. = 12.1 DEGREES
REMARK 500 14 ASP A 53 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 14 PHE A 570 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 15 CYS A 17 CA - CB - SG ANGL. DEV. = 21.9 DEGREES
REMARK 500 15 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 15 ASP A 99 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 15 ASP A 99 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 16 ARG A 458 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 16 MET A 460 CG - SD - CE ANGL. DEV. = -11.0 DEGREES
REMARK 500 17 ASP A 93 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 17 ASP A 93 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 17 MET A 147 CG - SD - CE ANGL. DEV. = -15.2 DEGREES
REMARK 500 17 ARG A 458 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 17 MET A 460 CB - CG - SD ANGL. DEV. = 19.3 DEGREES
REMARK 500 17 LYS A 537 CD - CE - NZ ANGL. DEV. = 14.3 DEGREES
REMARK 500 18 ARG A 78 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 18 LEU A 300 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 18 MET A 521 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 19 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 19 LEU A 300 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 20 ARG A 78 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 20 PHE A 100 CB - CG - CD2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 20 MET A 147 CG - SD - CE ANGL. DEV. = 10.0 DEGREES
REMARK 500 20 LEU A 300 CB - CG - CD2 ANGL. DEV. = 13.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 91 ANGLE DEVIATIONS.
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 1 LYS A 92 -142.93 -101.85
REMARK 500 1 ASN A 120 104.92 -171.63
REMARK 500 1 LYS A 126 158.12 -47.57
REMARK 500 1 SER A 218 -119.76 59.19
REMARK 500 1 ASN A 305 0.99 -69.45
REMARK 500 1 CYS A 323 129.09 -36.02
REMARK 500 1 TYR A 350 66.35 -151.67
REMARK 500 1 THR A 356 -71.78 -57.50
REMARK 500 1 ARG A 385 32.42 73.55
REMARK 500 1 PHE A 421 -62.26 -138.83
REMARK 500 1 ASP A 447 34.55 -140.71
REMARK 500 1 HIS A 471 128.36 -39.70
REMARK 500 1 THR A 472 -6.26 87.55
REMARK 500 1 TYR A 514 4.78 -155.14
REMARK 500 1 SER A 515 71.71 -32.60
REMARK 500 1 ASN A 516 -17.59 -46.74
REMARK 500 1 GLU A 517 95.24 -57.77
REMARK 500 1 MET A 521 -75.03 -39.23
REMARK 500 1 GLU A 522 61.16 154.48
REMARK 500 1 SER A 532 41.99 -80.86
REMARK 500 1 SER A 542 -143.21 -125.78
REMARK 500 1 HIS A 566 53.88 -140.91
REMARK 500 2 LYS A 21 -80.50 -38.48
REMARK 500 2 PHE A 73 -7.80 73.20
REMARK 500 2 LYS A 92 -167.47 -108.34
REMARK 500 2 ILE A 101 -72.68 -71.54
REMARK 500 2 ASN A 120 115.20 -160.12
REMARK 500 2 ASN A 122 59.32 -112.89
REMARK 500 2 SER A 218 -121.24 59.36
REMARK 500 2 LYS A 276 -70.51 -46.43
REMARK 500 2 LYS A 306 16.49 81.82
REMARK 500 2 TYR A 350 66.57 -152.59
REMARK 500 2 GLN A 361 -78.82 -84.66
REMARK 500 2 PHE A 421 -61.48 -138.00
REMARK 500 2 HIS A 435 45.56 -149.01
REMARK 500 2 SER A 437 71.97 -113.92
REMARK 500 2 SER A 462 35.95 92.15
REMARK 500 2 HIS A 471 129.23 -35.75
REMARK 500 2 THR A 472 -8.46 85.24
REMARK 500 2 GLU A 490 34.96 -84.26
REMARK 500 2 GLU A 517 47.12 -63.22
REMARK 500 2 ILE A 518 -153.57 -128.02
REMARK 500 2 MET A 521 -159.22 -64.29
REMARK 500 2 GLU A 522 48.38 -96.10
REMARK 500 2 TRP A 526 75.06 -117.92
REMARK 500 2 SER A 542 -142.87 -122.93
REMARK 500 2 GLU A 564 -77.12 -3.42
REMARK 500 3 PHE A 100 16.79 -64.09
REMARK 500 3 ILE A 101 -43.44 -151.28
REMARK 500 3 ASN A 122 58.16 -160.39
REMARK 500
REMARK 500 THIS ENTRY HAS 1093 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 518 GLU A 519 1 142.64
REMARK 500 GLY A 520 MET A 521 1 -142.98
REMARK 500 GLU A 522 ASN A 523 1 148.33
REMARK 500 GLU A 517 ILE A 518 2 -147.11
REMARK 500 ILE A 518 GLU A 519 2 141.91
REMARK 500 GLY A 520 MET A 521 2 -141.75
REMARK 500 GLU A 517 ILE A 518 3 -136.93
REMARK 500 ILE A 518 GLU A 519 3 137.91
REMARK 500 MET A 521 GLU A 522 3 -144.91
REMARK 500 THR A 386 ALA A 387 4 -148.95
REMARK 500 GLU A 522 ASN A 523 4 126.17
REMARK 500 GLY A 438 THR A 439 5 149.04
REMARK 500 ASN A 516 GLU A 517 7 147.67
REMARK 500 LYS A 126 ARG A 127 8 -149.81
REMARK 500 PHE A 100 ILE A 101 9 148.62
REMARK 500 ALA A 381 ASP A 382 9 140.41
REMARK 500 MET A 521 GLU A 522 9 -149.94
REMARK 500 ASP A 99 PHE A 100 10 -148.70
REMARK 500 LYS A 327 HIS A 328 10 -149.99
REMARK 500 GLU A 384 ARG A 385 10 -137.89
REMARK 500 GLY A 438 THR A 439 10 -147.55
REMARK 500 MET A 521 GLU A 522 10 143.25
REMARK 500 ILE A 101 THR A 102 11 124.10
REMARK 500 ALA A 383 GLU A 384 11 147.74
REMARK 500 MET A 521 GLU A 522 11 148.26
REMARK 500 ASP A 99 PHE A 100 12 -144.01
REMARK 500 ILE A 101 THR A 102 12 141.07
REMARK 500 THR A 102 GLY A 103 12 -130.19
REMARK 500 GLY A 103 LYS A 104 12 146.29
REMARK 500 PHE A 100 ILE A 101 13 141.93
REMARK 500 GLY A 463 ARG A 464 13 146.40
REMARK 500 GLU A 517 ILE A 518 13 141.40
REMARK 500 PHE A 100 ILE A 101 14 147.57
REMARK 500 CYS A 89 ASN A 90 15 137.28
REMARK 500 ASN A 90 HIS A 91 15 -139.35
REMARK 500 GLU A 384 ARG A 385 15 -124.23
REMARK 500 GLY A 520 MET A 521 15 -126.55
REMARK 500 MET A 521 GLU A 522 15 -147.55
REMARK 500 SER A 437 GLY A 438 16 -122.79
REMARK 500 TYR A 514 SER A 515 16 149.94
REMARK 500 SER A 532 ASP A 533 16 -127.22
REMARK 500 ASP A 533 GLU A 534 16 -145.07
REMARK 500 THR A 125 LYS A 126 17 143.71
REMARK 500 ASP A 146 MET A 147 17 142.21
REMARK 500 GLU A 384 ARG A 385 17 -137.54
REMARK 500 SER A 437 GLY A 438 17 -145.00
REMARK 500 ASN A 523 VAL A 524 17 -147.14
REMARK 500 ALA A 383 GLU A 384 18 141.41
REMARK 500 GLU A 384 ARG A 385 18 -116.35
REMARK 500 THR A 436 SER A 437 18 -128.08
REMARK 500
REMARK 500 THIS ENTRY HAS 142 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 21 THR A 125 11.73
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 A1099 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1077 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A1078 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A1079 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A1080 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A1053 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1054 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A1055 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A1056 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A1086 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A1077 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A1078 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1079 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A1065 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A1072 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A1073 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1063 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A1064 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A1065 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH A1058 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1059 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A1060 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A1096 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A1105 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1106 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A1078 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A1074 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A1084 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1085 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A1086 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A1057 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1062 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A1063 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1099 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A1057 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1058 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH A1059 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH A1062 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1089 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A1077 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1060 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A1061 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A1062 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A1063 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A1064 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1065 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1078 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH A1088 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A1089 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH A1090 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A1075 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A1076 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A1077 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A1092 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A1093 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A1085 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A1086 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A1087 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A1088 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH A1088 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1089 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A1090 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1088 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A1089 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A1090 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH A1075 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A1076 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1077 DISTANCE = 6.25 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DPF A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IVH RELATED DB: PDB
REMARK 900 RELATED ID: 5IVI RELATED DB: PDB
REMARK 900 RELATED ID: 5IVD RELATED DB: PDB
DBREF 5IVK A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5IVK MET A -6 UNP Q25252 INITIATING METHIONINE
SEQADV 5IVK HIS A -5 UNP Q25252 EXPRESSION TAG
SEQADV 5IVK HIS A -4 UNP Q25252 EXPRESSION TAG
SEQADV 5IVK HIS A -3 UNP Q25252 EXPRESSION TAG
SEQADV 5IVK HIS A -2 UNP Q25252 EXPRESSION TAG
SEQADV 5IVK HIS A -1 UNP Q25252 EXPRESSION TAG
SEQADV 5IVK HIS A 0 UNP Q25252 EXPRESSION TAG
SEQADV 5IVK LEU A 364 UNP Q25252 MET 364 CONFLICT
SEQADV 5IVK PHE A 419 UNP Q25252 ILE 419 CONFLICT
SEQADV 5IVK THR A 472 UNP Q25252 ALA 472 CONFLICT
SEQADV 5IVK THR A 505 UNP Q25252 ILE 505 CONFLICT
SEQADV 5IVK GLU A 530 UNP Q25252 LYS 530 CONFLICT
SEQADV 5IVK GLY A 554 UNP Q25252 ASP 554 CONFLICT
SEQRES 1 A 577 MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER
SEQRES 2 A 577 LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU
SEQRES 3 A 577 ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR
SEQRES 4 A 577 VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL
SEQRES 5 A 577 LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE
SEQRES 6 A 577 GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU
SEQRES 7 A 577 ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ASP GLY
SEQRES 8 A 577 VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN
SEQRES 9 A 577 VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP
SEQRES 10 A 577 CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO
SEQRES 11 A 577 GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY
SEQRES 12 A 577 GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY
SEQRES 13 A 577 PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN
SEQRES 14 A 577 ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU
SEQRES 15 A 577 ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU
SEQRES 16 A 577 LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN
SEQRES 17 A 577 CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL
SEQRES 18 A 577 PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET
SEQRES 19 A 577 MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY
SEQRES 20 A 577 ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN
SEQRES 21 A 577 THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU
SEQRES 22 A 577 ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU
SEQRES 23 A 577 GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS
SEQRES 24 A 577 LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN
SEQRES 25 A 577 LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR
SEQRES 26 A 577 GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU
SEQRES 27 A 577 MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET
SEQRES 28 A 577 MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER
SEQRES 29 A 577 ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU
SEQRES 30 A 577 THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA
SEQRES 31 A 577 GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS
SEQRES 32 A 577 ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA
SEQRES 33 A 577 ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP
SEQRES 34 A 577 PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS
SEQRES 35 A 577 THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE
SEQRES 36 A 577 ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG
SEQRES 37 A 577 SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU
SEQRES 38 A 577 LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET
SEQRES 39 A 577 PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET
SEQRES 40 A 577 THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO
SEQRES 41 A 577 TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP
SEQRES 42 A 577 ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU
SEQRES 43 A 577 ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU
SEQRES 44 A 577 MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS
SEQRES 45 A 577 HIS ARG ASP LEU PHE
HET DPF A 601 18
HETNAM DPF DIETHYL HYDROGEN PHOSPHATE
FORMUL 2 DPF C4 H11 O4 P
FORMUL 3 HOH *399(H2 O)
HELIX 1 AA1 SER A 6 LEU A 27 1 22
HELIX 2 AA2 VAL A 68 ARG A 72 5 5
HELIX 3 AA3 TYR A 152 LYS A 156 5 5
HELIX 4 AA4 LEU A 167 LEU A 173 1 7
HELIX 5 AA5 SER A 177 ASN A 181 5 5
HELIX 6 AA6 ASN A 185 CYS A 202 1 18
HELIX 7 AA7 ALA A 203 PHE A 205 5 3
HELIX 8 AA8 SER A 218 THR A 230 1 13
HELIX 9 AA9 GLU A 231 ARG A 234 5 4
HELIX 10 AB1 CYS A 249 ASN A 253 5 5
HELIX 11 AB2 HIS A 258 ALA A 267 1 10
HELIX 12 AB3 ASN A 274 ALA A 285 1 12
HELIX 13 AB4 LYS A 286 LEU A 293 1 8
HELIX 14 AB5 GLU A 294 VAL A 297 5 4
HELIX 15 AB6 THR A 299 ASN A 305 1 7
HELIX 16 AB7 HIS A 328 ALA A 336 1 9
HELIX 17 AB8 TRP A 337 ILE A 341 5 5
HELIX 18 AB9 TYR A 350 THR A 356 5 7
HELIX 19 AC1 SER A 357 MET A 362 1 6
HELIX 20 AC2 PRO A 363 THR A 371 5 9
HELIX 21 AC3 CYS A 372 VAL A 376 5 5
HELIX 22 AC4 PRO A 377 ALA A 381 5 5
HELIX 23 AC5 ALA A 387 VAL A 402 1 16
HELIX 24 AC6 THR A 408 PHE A 421 1 14
HELIX 25 AC7 PHE A 421 PHE A 433 1 13
HELIX 26 AC8 PRO A 456 ARG A 461 1 6
HELIX 27 AC9 THR A 472 PHE A 478 5 7
HELIX 28 AD1 SER A 491 GLY A 511 1 21
HELIX 29 AD2 GLU A 552 SER A 561 1 10
HELIX 30 AD3 MET A 562 GLU A 564 5 3
HELIX 31 AD4 HIS A 566 PHE A 570 5 5
SHEET 1 AA1 3 THR A 28 THR A 37 0
SHEET 2 AA1 3 GLY A 40 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 41
SHEET 1 AA212 THR A 28 THR A 37 0
SHEET 2 AA212 GLY A 40 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 AA212 SER A 54 PRO A 62 -1 O TYR A 55 N ARG A 47
SHEET 4 AA212 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
SHEET 5 AA212 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 AA212 ARG A 127 ILE A 133 1 N LEU A 130 O VAL A 159
SHEET 7 AA212 GLY A 207 GLU A 217 1 O THR A 213 N VAL A 129
SHEET 8 AA212 ARG A 239 MET A 243 1 O MET A 243 N GLY A 216
SHEET 9 AA212 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 AA212 VAL A 441 PHE A 446 1 O PHE A 446 N ASN A 347
SHEET 11 AA212 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 AA212 LEU A 545 ASP A 549 -1 O ILE A 548 N CYS A 538
SHEET 1 AA3 2 GLN A 97 VAL A 98 0
SHEET 2 AA3 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
LINK OG SER A 218 P1 DPF A 601 1555 1555 1.63
SITE 1 AC1 6 GLY A 136 GLY A 137 SER A 218 ALA A 219
SITE 2 AC1 6 TYR A 457 HIS A 471
CRYST1 51.816 101.254 225.818 90.00 90.00 90.00 C 2 2 21 8
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 0.019299 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009876 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004428 0.00000
MODEL 1
TER 9036 PHE A 570
ENDMDL
MODEL 2
TER 9036 PHE A 570
ENDMDL
MODEL 3
TER 9036 PHE A 570
ENDMDL
MODEL 4
TER 9036 PHE A 570
ENDMDL
MODEL 5
TER 9036 PHE A 570
ENDMDL
MODEL 6
TER 9036 PHE A 570
ENDMDL
MODEL 7
TER 9036 PHE A 570
ENDMDL
MODEL 8
TER 9036 PHE A 570
ENDMDL
MODEL 9
TER 9036 PHE A 570
ENDMDL
MODEL 10
TER 9036 PHE A 570
ENDMDL
MODEL 11
TER 9036 PHE A 570
ENDMDL
MODEL 12
TER 9036 PHE A 570
ENDMDL
MODEL 13
TER 9036 PHE A 570
ENDMDL
MODEL 14
TER 9036 PHE A 570
ENDMDL
MODEL 15
TER 9036 PHE A 570
ENDMDL
MODEL 16
TER 9036 PHE A 570
ENDMDL
MODEL 17
TER 9036 PHE A 570
ENDMDL
MODEL 18
TER 9036 PHE A 570
ENDMDL
MODEL 19
TER 9036 PHE A 570
ENDMDL
MODEL 20
TER 9036 PHE A 570
ENDMDL
MODEL 21
TER 9036 PHE A 570
ENDMDL
MODEL 22
TER 9036 PHE A 570
ENDMDL
MODEL 23
TER 9036 PHE A 570
ENDMDL
MODEL 24
TER 9036 PHE A 570
ENDMDL
MODEL 25
TER 9036 PHE A 570
ENDMDL
MODEL 26
TER 9036 PHE A 570
ENDMDL
MODEL 27
TER 9036 PHE A 570
ENDMDL
MODEL 28
TER 9036 PHE A 570
ENDMDL
MODEL 29
TER 9036 PHE A 570
ENDMDL
MODEL 30
TER 9036 PHE A 570
ENDMDL
MODEL 31
TER 9036 PHE A 570
ENDMDL
MODEL 32
TER 9036 PHE A 570
ENDMDL
MODEL 33
TER 9036 PHE A 570
ENDMDL
MODEL 34
TER 9036 PHE A 570
ENDMDL
MODEL 35
TER 9036 PHE A 570
ENDMDL
MODEL 36
TER 9036 PHE A 570
ENDMDL
MODEL 37
TER 9036 PHE A 570
ENDMDL
MODEL 38
TER 9036 PHE A 570
ENDMDL
MODEL 39
TER 9036 PHE A 570
ENDMDL
MODEL 40
TER 9036 PHE A 570
ENDMDL
MODEL 41
TER 9036 PHE A 570
ENDMDL
MODEL 42
TER 9036 PHE A 570
ENDMDL
MODEL 43
TER 9036 PHE A 570
ENDMDL
MASTER 1141 0 1 31 17 0 2 6 4964 1 19 45
END |