| content |
HEADER HYDROLASE 20-MAR-16 5IVH
TITLE THE ALPHA-ESTERASE-7 CARBOXYLESTERASE, E3, FROM THE BLOWFLY LUCILIA
TITLE 2 CUPRINA: APO-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 44
AUTHOR G.J.CORREY,C.J.JACKSON
REVDAT 1 22-JUN-16 5IVH 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. 1.71 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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 59125
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2999
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 45.7734 - 4.7163 1.00 2875 145 0.1512 0.1687
REMARK 3 2 4.7163 - 3.7440 1.00 2726 144 0.1370 0.1550
REMARK 3 3 3.7440 - 3.2709 1.00 2718 142 0.1513 0.1597
REMARK 3 4 3.2709 - 2.9719 1.00 2723 142 0.1560 0.2014
REMARK 3 5 2.9719 - 2.7589 1.00 2674 149 0.1602 0.2084
REMARK 3 6 2.7589 - 2.5963 1.00 2688 157 0.1495 0.2091
REMARK 3 7 2.5963 - 2.4663 1.00 2653 149 0.1563 0.2362
REMARK 3 8 2.4663 - 2.3589 1.00 2667 152 0.1505 0.2153
REMARK 3 9 2.3589 - 2.2681 1.00 2646 151 0.1510 0.2195
REMARK 3 10 2.2681 - 2.1898 1.00 2662 136 0.1578 0.2422
REMARK 3 11 2.1898 - 2.1214 1.00 2621 161 0.1682 0.2255
REMARK 3 12 2.1214 - 2.0607 1.00 2675 111 0.1801 0.2716
REMARK 3 13 2.0607 - 2.0065 1.00 2648 153 0.1909 0.2325
REMARK 3 14 2.0065 - 1.9575 1.00 2694 117 0.1884 0.3023
REMARK 3 15 1.9575 - 1.9130 1.00 2666 133 0.2068 0.2585
REMARK 3 16 1.9130 - 1.8723 1.00 2623 139 0.2275 0.2681
REMARK 3 17 1.8723 - 1.8349 1.00 2678 151 0.2623 0.2792
REMARK 3 18 1.8349 - 1.8002 1.00 2555 138 0.2845 0.3295
REMARK 3 19 1.8002 - 1.7681 1.00 2694 157 0.3126 0.3459
REMARK 3 20 1.7681 - 1.7381 1.00 2580 137 0.3359 0.3893
REMARK 3 21 1.7381 - 1.7101 0.98 2660 135 0.3776 0.4610
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 : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.590
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 : 1.355 NULL
REMARK 3 CHIRALITY : 0.107 NULL
REMARK 3 PLANARITY : 0.009 NULL
REMARK 3 DIHEDRAL : 17.980 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 5IVH 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_1000219496.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-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 : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
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 : 59125
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 45.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 29.00
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 28.30
REMARK 200 R MERGE FOR SHELL (I) : 3.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4FNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 4.5, PEG 2K
REMARK 280 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 110.85750
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 110.85750
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 24.28700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.23600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.28700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.23600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 110.85750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.28700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.23600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 110.85750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.28700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.23600
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 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 465 44 MET A -6
REMARK 465 44 HIS A -5
REMARK 465 44 HIS A -4
REMARK 465 44 HIS A -3
REMARK 465 44 HIS A -2
REMARK 465 44 HIS A -1
REMARK 465 44 HIS A 0
REMARK 465 44 MET A 1
REMARK 465 44 ASN A 2
REMARK 465 44 PHE A 3
REMARK 465 44 ASN A 4
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 2 TYR A 457 CB TYR A 457 CG -0.104
REMARK 500 2 TYR A 457 CD1 TYR A 457 CE1 -0.113
REMARK 500 2 GLU A 517 CB GLU A 517 CG 0.139
REMARK 500 7 CYS A 323 CB CYS A 323 SG -0.108
REMARK 500 8 GLU A 544 CG GLU A 544 CD 0.093
REMARK 500 9 GLU A 519 CB GLU A 519 CG 0.139
REMARK 500 9 GLU A 519 CG GLU A 519 CD 0.096
REMARK 500 10 PRO A 66 C PRO A 67 N 0.115
REMARK 500 11 CYS A 89 CB CYS A 89 SG -0.101
REMARK 500 12 CYS A 323 CB CYS A 323 SG -0.106
REMARK 500 13 LYS A 155 CE LYS A 155 NZ 0.152
REMARK 500 14 CYS A 106 CB CYS A 106 SG 0.104
REMARK 500 15 GLU A 294 CG GLU A 294 CD 0.098
REMARK 500 18 GLU A 498 CG GLU A 498 CD 0.091
REMARK 500 19 CYS A 106 CB CYS A 106 SG -0.130
REMARK 500 19 LYS A 155 CE LYS A 155 NZ 0.202
REMARK 500 20 CYS A 106 CB CYS A 106 SG 0.138
REMARK 500 21 CYS A 106 CB CYS A 106 SG 0.170
REMARK 500 21 GLU A 331 CB GLU A 331 CG 0.130
REMARK 500 24 GLU A 331 CB GLU A 331 CG 0.139
REMARK 500 27 GLU A 530 CB GLU A 530 CG 0.115
REMARK 500 28 GLU A 451 CB GLU A 451 CG 0.146
REMARK 500 30 ASP A 322 CB ASP A 322 CG 0.130
REMARK 500 33 GLU A 294 CG GLU A 294 CD 0.116
REMARK 500 33 TYR A 457 CE2 TYR A 457 CD2 -0.092
REMARK 500 40 CYS A 106 CB CYS A 106 SG 0.221
REMARK 500 40 GLU A 517 CG GLU A 517 CD -0.097
REMARK 500 40 TRP A 526 C ASP A 527 N 0.202
REMARK 500 42 CYS A 17 CB CYS A 17 SG 0.151
REMARK 500 42 ASP A 527 C PRO A 528 N -0.115
REMARK 500 43 GLU A 9 CB GLU A 9 CG 0.132
REMARK 500 43 PRO A 66 C PRO A 67 N 0.135
REMARK 500 43 GLU A 530 CB GLU A 530 CG 0.159
REMARK 500 43 GLU A 530 CG GLU A 530 CD 0.108
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 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 15.2 DEGREES
REMARK 500 2 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.4 DEGREES
REMARK 500 3 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.3 DEGREES
REMARK 500 4 CYS A 106 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 4 LEU A 300 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 4 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.8 DEGREES
REMARK 500 5 MET A 193 CB - CG - SD ANGL. DEV. = 26.7 DEGREES
REMARK 500 5 ARG A 330 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 5 ARG A 464 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 6 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 7 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 7 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.9 DEGREES
REMARK 500 8 MET A 193 CA - CB - CG ANGL. DEV. = -10.2 DEGREES
REMARK 500 8 ARG A 330 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 LEU A 364 CA - CB - CG ANGL. DEV. = 18.2 DEGREES
REMARK 500 8 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 15.6 DEGREES
REMARK 500 9 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 13.7 DEGREES
REMARK 500 10 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.6 DEGREES
REMARK 500 10 ARG A 486 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 11 MET A 147 CG - SD - CE ANGL. DEV. = -10.1 DEGREES
REMARK 500 11 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 15.1 DEGREES
REMARK 500 12 MET A 147 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 12 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 13 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 13 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.1 DEGREES
REMARK 500 14 PHE A 22 CB - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 14 PHE A 22 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 14 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 13.9 DEGREES
REMARK 500 15 LEU A 121 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 15 MET A 308 CB - CG - SD ANGL. DEV. = 23.9 DEGREES
REMARK 500 15 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.4 DEGREES
REMARK 500 16 PHE A 22 CB - CG - CD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 16 CYS A 256 CA - CB - SG ANGL. DEV. = 9.2 DEGREES
REMARK 500 16 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.6 DEGREES
REMARK 500 17 CYS A 106 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 17 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 13.7 DEGREES
REMARK 500 18 MET A 147 CG - SD - CE ANGL. DEV. = -12.0 DEGREES
REMARK 500 18 LYS A 155 CD - CE - NZ ANGL. DEV. = 16.0 DEGREES
REMARK 500 18 MET A 332 CB - CG - SD ANGL. DEV. = -23.1 DEGREES
REMARK 500 18 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 19 LYS A 155 CD - CE - NZ ANGL. DEV. = 15.9 DEGREES
REMARK 500 19 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 13.8 DEGREES
REMARK 500 20 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 14.8 DEGREES
REMARK 500 20 MET A 425 CG - SD - CE ANGL. DEV. = -13.0 DEGREES
REMARK 500 20 ARG A 464 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 20 ARG A 464 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 21 VAL A 373 CG1 - CB - CG2 ANGL. DEV. = 13.3 DEGREES
REMARK 500 22 CYS A 17 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 SER A 6 -53.02 68.83
REMARK 500 1 MET A 8 -70.67 -31.32
REMARK 500 1 ILE A 15 32.06 -84.71
REMARK 500 1 ILE A 101 -62.11 -99.93
REMARK 500 1 ASP A 157 59.75 -96.10
REMARK 500 1 ASP A 179 -61.59 -14.00
REMARK 500 1 SER A 218 -122.71 65.15
REMARK 500 1 GLU A 295 -58.53 1.10
REMARK 500 1 THR A 320 -159.93 -115.12
REMARK 500 1 ALA A 321 -66.30 -25.71
REMARK 500 1 VAL A 324 -32.11 -132.72
REMARK 500 1 TYR A 350 59.27 -150.74
REMARK 500 1 PHE A 354 36.74 -73.30
REMARK 500 1 PRO A 363 -10.43 -25.94
REMARK 500 1 LEU A 365 -34.83 -39.53
REMARK 500 1 GLU A 368 -51.11 -21.82
REMARK 500 1 PHE A 421 -59.77 -132.19
REMARK 500 1 THR A 436 -148.31 -158.28
REMARK 500 1 SER A 437 159.46 133.32
REMARK 500 1 ARG A 461 74.62 -103.16
REMARK 500 1 SER A 462 65.09 -61.99
REMARK 500 1 ARG A 464 126.46 49.49
REMARK 500 1 LYS A 467 -157.53 -74.81
REMARK 500 1 HIS A 471 131.44 -39.55
REMARK 500 1 THR A 472 -6.67 83.37
REMARK 500 1 ASN A 516 7.36 -64.06
REMARK 500 1 LYS A 531 91.61 -57.94
REMARK 500 1 SER A 532 -40.93 144.71
REMARK 500 1 SER A 542 -151.13 -135.08
REMARK 500 2 PHE A 100 -114.53 -8.86
REMARK 500 2 ILE A 101 -77.21 -21.66
REMARK 500 2 LYS A 126 152.55 -45.92
REMARK 500 2 SER A 218 -128.19 63.61
REMARK 500 2 ARG A 234 92.55 -38.66
REMARK 500 2 GLN A 288 -67.82 -20.41
REMARK 500 2 ASN A 305 10.12 -65.01
REMARK 500 2 LYS A 306 89.21 46.14
REMARK 500 2 ALA A 321 -41.04 -25.58
REMARK 500 2 TYR A 350 54.49 -150.53
REMARK 500 2 PHE A 354 20.16 -79.79
REMARK 500 2 MET A 362 43.63 -171.84
REMARK 500 2 PRO A 363 -10.21 -22.23
REMARK 500 2 THR A 406 134.65 -173.51
REMARK 500 2 PHE A 421 -58.76 -130.95
REMARK 500 2 HIS A 435 -20.97 -141.71
REMARK 500 2 THR A 436 -113.53 -65.77
REMARK 500 2 SER A 437 -76.82 -164.29
REMARK 500 2 ARG A 461 102.55 -56.19
REMARK 500 2 SER A 462 -38.99 -32.03
REMARK 500 2 ARG A 464 126.94 48.22
REMARK 500
REMARK 500 THIS ENTRY HAS 1395 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 HIS A 435 THR A 436 1 -142.77
REMARK 500 MET A 460 ARG A 461 1 137.72
REMARK 500 ARG A 461 SER A 462 1 -149.34
REMARK 500 LYS A 92 ASP A 93 2 -144.50
REMARK 500 ILE A 101 THR A 102 2 -142.58
REMARK 500 ASP A 273 ASN A 274 2 147.69
REMARK 500 GLN A 361 MET A 362 2 146.56
REMARK 500 VAL A 5 SER A 6 3 -137.22
REMARK 500 GLU A 9 LYS A 10 3 149.68
REMARK 500 LYS A 14 ILE A 15 3 149.64
REMARK 500 LYS A 327 HIS A 328 3 144.97
REMARK 500 HIS A 435 THR A 436 3 -111.75
REMARK 500 SER A 437 GLY A 438 3 -147.78
REMARK 500 SER A 177 GLU A 178 4 145.27
REMARK 500 THR A 439 PRO A 440 4 -148.60
REMARK 500 SER A 6 LEU A 7 6 -145.39
REMARK 500 LEU A 121 ASN A 122 6 144.06
REMARK 500 ALA A 321 ASP A 322 6 145.72
REMARK 500 GLY A 463 ARG A 464 6 141.48
REMARK 500 ASP A 99 PHE A 100 7 -148.90
REMARK 500 VAL A 105 CYS A 106 8 146.99
REMARK 500 ASP A 322 CYS A 323 8 141.84
REMARK 500 SER A 6 LEU A 7 9 145.09
REMARK 500 CYS A 106 GLY A 107 9 -147.63
REMARK 500 ASP A 273 ASN A 274 9 139.21
REMARK 500 GLN A 319 THR A 320 9 148.37
REMARK 500 ARG A 461 SER A 462 9 -140.09
REMARK 500 LEU A 121 ASN A 122 10 136.36
REMARK 500 GLY A 465 VAL A 466 10 146.22
REMARK 500 ILE A 518 GLU A 519 10 147.34
REMARK 500 ASP A 99 PHE A 100 11 -142.77
REMARK 500 THR A 436 SER A 437 11 136.06
REMARK 500 ILE A 518 GLU A 519 11 131.34
REMARK 500 PHE A 100 ILE A 101 12 -144.31
REMARK 500 ASP A 273 ASN A 274 12 140.01
REMARK 500 ASP A 322 CYS A 323 12 144.67
REMARK 500 THR A 125 LYS A 126 13 148.44
REMARK 500 ALA A 252 ASN A 253 13 -148.24
REMARK 500 ASP A 273 ASN A 274 13 148.88
REMARK 500 PRO A 363 LEU A 364 13 146.67
REMARK 500 THR A 436 SER A 437 13 136.81
REMARK 500 SER A 462 GLY A 463 13 145.23
REMARK 500 VAL A 5 SER A 6 14 -142.88
REMARK 500 LEU A 7 MET A 8 14 -125.12
REMARK 500 LEU A 364 LEU A 365 14 137.41
REMARK 500 SER A 437 GLY A 438 14 141.14
REMARK 500 GLY A 463 ARG A 464 14 -142.77
REMARK 500 LEU A 7 MET A 8 15 -149.81
REMARK 500 LEU A 7 MET A 8 16 -142.38
REMARK 500 LYS A 104 VAL A 105 16 -142.42
REMARK 500
REMARK 500 THIS ENTRY HAS 219 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 834 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 821 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A 822 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A 817 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A 819 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 830 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 824 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 825 DISTANCE = 7.94 ANGSTROMS
REMARK 525 HOH A 806 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A 814 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A 824 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 836 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 831 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A 842 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A 832 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 833 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A 823 DISTANCE = 5.96 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IVK RELATED DB: PDB
REMARK 900 RELATED ID: 5IVD RELATED DB: PDB
REMARK 900 RELATED ID: 5IVI RELATED DB: PDB
DBREF 5IVH A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5IVH MET A -6 UNP Q25252 INITIATING METHIONINE
SEQADV 5IVH HIS A -5 UNP Q25252 EXPRESSION TAG
SEQADV 5IVH HIS A -4 UNP Q25252 EXPRESSION TAG
SEQADV 5IVH HIS A -3 UNP Q25252 EXPRESSION TAG
SEQADV 5IVH HIS A -2 UNP Q25252 EXPRESSION TAG
SEQADV 5IVH HIS A -1 UNP Q25252 EXPRESSION TAG
SEQADV 5IVH HIS A 0 UNP Q25252 EXPRESSION TAG
SEQADV 5IVH ALA A 83 UNP Q25252 ASP 83 CONFLICT
SEQADV 5IVH LEU A 364 UNP Q25252 MET 364 CONFLICT
SEQADV 5IVH PHE A 419 UNP Q25252 ILE 419 CONFLICT
SEQADV 5IVH THR A 472 UNP Q25252 ALA 472 CONFLICT
SEQADV 5IVH THR A 505 UNP Q25252 ILE 505 CONFLICT
SEQADV 5IVH GLU A 530 UNP Q25252 LYS 530 CONFLICT
SEQADV 5IVH 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 ALA 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
FORMUL 2 HOH *234(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 MET A 283 1 10
HELIX 13 AB4 LYS A 286 GLU A 295 1 10
HELIX 14 AB5 THR A 299 ASN A 305 1 7
HELIX 15 AB6 HIS A 328 VAL A 333 1 6
HELIX 16 AB7 LYS A 334 THR A 335 5 2
HELIX 17 AB8 ALA A 336 ILE A 341 5 6
HELIX 18 AB9 TYR A 350 PHE A 354 5 5
HELIX 19 AC1 PHE A 355 GLN A 361 1 7
HELIX 20 AC2 MET A 362 THR A 371 5 10
HELIX 21 AC3 CYS A 372 VAL A 376 5 5
HELIX 22 AC4 ALA A 387 VAL A 402 1 16
HELIX 23 AC5 THR A 408 PHE A 421 1 14
HELIX 24 AC6 PHE A 421 ASN A 434 1 14
HELIX 25 AC7 PRO A 456 ARG A 461 1 6
HELIX 26 AC8 THR A 472 PHE A 478 5 7
HELIX 27 AC9 SER A 491 GLY A 511 1 21
HELIX 28 AD1 GLU A 552 SER A 561 1 10
HELIX 29 AD2 MET A 562 GLU A 564 5 3
HELIX 30 AD3 HIS A 566 PHE A 570 5 5
SHEET 1 AA1 3 THR A 28 ALA A 35 0
SHEET 2 AA1 3 LYS A 41 LEU A 48 -1 O LYS A 46 N GLU A 31
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 43
SHEET 1 AA212 THR A 28 ALA A 35 0
SHEET 2 AA212 LYS A 41 LEU A 48 -1 O LYS A 46 N GLU A 31
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 VAL A 116 N PHE A 58
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 TYR A 132 O ILE A 161
SHEET 7 AA212 GLY A 207 GLU A 217 1 O THR A 213 N VAL A 131
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 TYR A 442 N MET A 345
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 LYS A 546 N ASN A 540
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
CRYST1 48.574 100.472 221.715 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 0.020587 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004510 0.00000
MODEL 1
TER 9038 PHE A 570
ENDMDL
MODEL 2
TER 9038 PHE A 570
ENDMDL
MODEL 3
TER 9038 PHE A 570
ENDMDL
MODEL 4
TER 9038 PHE A 570
ENDMDL
MODEL 5
TER 9038 PHE A 570
ENDMDL
MODEL 6
TER 9038 PHE A 570
ENDMDL
MODEL 7
TER 9038 PHE A 570
ENDMDL
MODEL 8
TER 9038 PHE A 570
ENDMDL
MODEL 9
TER 9038 PHE A 570
ENDMDL
MODEL 10
TER 9038 PHE A 570
ENDMDL
MODEL 11
TER 9038 PHE A 570
ENDMDL
MODEL 12
TER 9038 PHE A 570
ENDMDL
MODEL 13
TER 9038 PHE A 570
ENDMDL
MODEL 14
TER 9038 PHE A 570
ENDMDL
MODEL 15
TER 9038 PHE A 570
ENDMDL
MODEL 16
TER 9038 PHE A 570
ENDMDL
MODEL 17
TER 9038 PHE A 570
ENDMDL
MODEL 18
TER 9038 PHE A 570
ENDMDL
MODEL 19
TER 9038 PHE A 570
ENDMDL
MODEL 20
TER 9038 PHE A 570
ENDMDL
MODEL 21
TER 9038 PHE A 570
ENDMDL
MODEL 22
TER 9038 PHE A 570
ENDMDL
MODEL 23
TER 9038 PHE A 570
ENDMDL
MODEL 24
TER 9038 PHE A 570
ENDMDL
MODEL 25
TER 9038 PHE A 570
ENDMDL
MODEL 26
TER 9038 PHE A 570
ENDMDL
MODEL 27
TER 9038 PHE A 570
ENDMDL
MODEL 28
TER 9038 PHE A 570
ENDMDL
MODEL 29
TER 9038 PHE A 570
ENDMDL
MODEL 30
TER 9038 PHE A 570
ENDMDL
MODEL 31
TER 9038 PHE A 570
ENDMDL
MODEL 32
TER 9038 PHE A 570
ENDMDL
MODEL 33
TER 9038 PHE A 570
ENDMDL
MODEL 34
TER 9038 PHE A 570
ENDMDL
MODEL 35
TER 9038 PHE A 570
ENDMDL
MODEL 36
TER 9038 PHE A 570
ENDMDL
MODEL 37
TER 9038 PHE A 570
ENDMDL
MODEL 38
TER 9038 PHE A 570
ENDMDL
MODEL 39
TER 9038 PHE A 570
ENDMDL
MODEL 40
TER 9038 PHE A 570
ENDMDL
MODEL 41
TER 9038 PHE A 570
ENDMDL
MODEL 42
TER 9038 PHE A 570
ENDMDL
MODEL 43
TER 9038 PHE A 570
ENDMDL
MODEL 44
TER 9038 PHE A 570
ENDMDL
MASTER 1008 0 0 30 17 0 0 6 4791 1 0 45
END |