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HEADER HYDROLASE 20-NOV-14 4X00
TITLE X-RAY CRYSTAL STRUCTURE OF A PUTATIVE ARYL ESTERASE FROM BURKHOLDERIA
TITLE 2 CENOCEPACIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 28-302;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA;
SOURCE 3 ORGANISM_TAXID: 216591;
SOURCE 4 STRAIN: ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
SOURCE 5 CF5610;
SOURCE 6 GENE: BCAL2527;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE, ARYL ESTERASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL
KEYWDS 2 GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 03-DEC-14 4X00 0
JRNL AUTH J.W.FAIRMAN,T.E.EDWARDS,D.LORIMER
JRNL TITL X-RAY CRYSTAL STRUCTURE OF A PUTATIVE ARYL ESTERASE FROM
JRNL TITL 2 BURKHOLDERIA CENOCEPACIA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 211239
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 10430
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 46.0501 - 4.2867 0.99 6822 344 0.1386 0.1444
REMARK 3 2 4.2867 - 3.4028 1.00 6786 353 0.1340 0.1496
REMARK 3 3 3.4028 - 2.9727 1.00 6700 345 0.1434 0.1477
REMARK 3 4 2.9727 - 2.7010 1.00 6719 383 0.1435 0.1670
REMARK 3 5 2.7010 - 2.5074 1.00 6712 369 0.1380 0.1718
REMARK 3 6 2.5074 - 2.3596 1.00 6683 335 0.1330 0.1573
REMARK 3 7 2.3596 - 2.2414 1.00 6772 330 0.1326 0.1673
REMARK 3 8 2.2414 - 2.1438 1.00 6674 356 0.1224 0.1535
REMARK 3 9 2.1438 - 2.0613 1.00 6664 372 0.1264 0.1600
REMARK 3 10 2.0613 - 1.9902 1.00 6711 335 0.1264 0.1558
REMARK 3 11 1.9902 - 1.9279 1.00 6730 334 0.1255 0.1580
REMARK 3 12 1.9279 - 1.8728 1.00 6703 330 0.1263 0.1772
REMARK 3 13 1.8728 - 1.8235 1.00 6686 341 0.1263 0.1710
REMARK 3 14 1.8235 - 1.7790 1.00 6759 296 0.1220 0.1682
REMARK 3 15 1.7790 - 1.7386 1.00 6703 341 0.1221 0.1543
REMARK 3 16 1.7386 - 1.7016 1.00 6665 324 0.1218 0.1704
REMARK 3 17 1.7016 - 1.6675 1.00 6727 345 0.1227 0.1835
REMARK 3 18 1.6675 - 1.6361 1.00 6623 352 0.1242 0.1798
REMARK 3 19 1.6361 - 1.6069 1.00 6657 366 0.1305 0.1848
REMARK 3 20 1.6069 - 1.5796 1.00 6717 326 0.1298 0.1695
REMARK 3 21 1.5796 - 1.5541 1.00 6664 334 0.1308 0.1720
REMARK 3 22 1.5541 - 1.5302 1.00 6689 347 0.1391 0.1817
REMARK 3 23 1.5302 - 1.5077 1.00 6651 375 0.1429 0.1819
REMARK 3 24 1.5077 - 1.4865 1.00 6622 350 0.1532 0.2012
REMARK 3 25 1.4865 - 1.4664 1.00 6717 376 0.1631 0.1952
REMARK 3 26 1.4664 - 1.4473 1.00 6631 366 0.1691 0.1994
REMARK 3 27 1.4473 - 1.4293 1.00 6630 365 0.1713 0.2272
REMARK 3 28 1.4293 - 1.4120 1.00 6681 356 0.1917 0.2324
REMARK 3 29 1.4120 - 1.3956 1.00 6694 329 0.2024 0.2564
REMARK 3 30 1.3956 - 1.3800 1.00 6617 355 0.1956 0.2428
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.61
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 : 0.010 8774
REMARK 3 ANGLE : 1.291 11980
REMARK 3 CHIRALITY : 0.057 1345
REMARK 3 PLANARITY : 0.008 1569
REMARK 3 DIHEDRAL : 12.634 3235
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 4X00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204846.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97740
REMARK 200 MONOCHROMATOR : DIAMOND[111]
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 211257
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.760
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.57600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.270
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MCSG1 H1: 0.2 M POTASSIUM FLUORIDE,
REMARK 280 20% PEG3350, BUCEA.00095.A.B1.PW37307 AT 26.4 MG/ML
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.18500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: BIOLOGICAL UNIT IS A MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
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: 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: 3
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: C
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: 4
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: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 ALA C 9
REMARK 465 ALA C 10
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 ALA D 9
REMARK 465 ALA D 10
REMARK 465 ALA D 11
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 ARG A 12 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 58 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 250 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 283 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 33 CG CD OE1 OE2
REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 ARG B 179 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 217 CG CD CE NZ
REMARK 470 GLU B 267 CG CD OE1 OE2
REMARK 470 ARG B 283 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 12 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 33 CG CD OE1 OE2
REMARK 470 ARG C 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 105 CG CD CE NZ
REMARK 470 LYS C 128 CG CD CE NZ
REMARK 470 ARG C 179 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 250 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 278 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 12 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 58 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 128 CG CD CE NZ
REMARK 470 LYS D 217 CG CD CE NZ
REMARK 470 ARG D 250 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 267 CG CD OE1 OE2
REMARK 470 ARG D 271 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 278 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 419 O HOH A 451 2.09
REMARK 500 O HOH A 524 O HOH A 697 2.13
REMARK 500 NZ LYS C 236 O HOH C 703 2.13
REMARK 500 O HOH C 465 O HOH C 658 2.15
REMARK 500 O HOH A 518 O HOH A 745 2.16
REMARK 500 O HOH A 402 O HOH A 457 2.17
REMARK 500 OG SER D 282 O HOH D 701 2.18
REMARK 500 O HOH A 642 O HOH A 718 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 440 O HOH C 450 1455 2.02
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 D 170 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG D 170 NE - CZ - NH2 ANGL. DEV. = 3.9 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 LYS A 105 69.00 32.53
REMARK 500 SER A 112 -111.88 60.83
REMARK 500 ILE A 140 -70.23 -100.21
REMARK 500 SER B 112 -113.12 58.79
REMARK 500 ILE B 140 -70.03 -100.86
REMARK 500 GLU B 210 59.31 -93.30
REMARK 500 SER C 112 -112.90 60.58
REMARK 500 ILE C 140 -68.86 -98.78
REMARK 500 GLU C 210 59.16 -95.60
REMARK 500 SER D 112 -113.79 60.33
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 648 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH C 589 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH D 521 DISTANCE = 8.35 ANGSTROMS
REMARK 525 HOH D 694 DISTANCE = 6.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F D 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-BUCEA.00095.A RELATED DB: TARGETTRACK
DBREF 4X00 A 9 283 UNP B4E794 B4E794_BURCJ 28 302
DBREF 4X00 B 9 283 UNP B4E794 B4E794_BURCJ 28 302
DBREF 4X00 C 9 283 UNP B4E794 B4E794_BURCJ 28 302
DBREF 4X00 D 9 283 UNP B4E794 B4E794_BURCJ 28 302
SEQADV 4X00 MET A 1 UNP B4E794 INITIATING METHIONINE
SEQADV 4X00 ALA A 2 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS A 3 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS A 4 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS A 5 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS A 6 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS A 7 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS A 8 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 MET B 1 UNP B4E794 INITIATING METHIONINE
SEQADV 4X00 ALA B 2 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS B 3 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS B 4 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS B 5 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS B 6 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS B 7 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS B 8 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 MET C 1 UNP B4E794 INITIATING METHIONINE
SEQADV 4X00 ALA C 2 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS C 3 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS C 4 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS C 5 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS C 6 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS C 7 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS C 8 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 MET D 1 UNP B4E794 INITIATING METHIONINE
SEQADV 4X00 ALA D 2 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS D 3 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS D 4 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS D 5 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS D 6 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS D 7 UNP B4E794 EXPRESSION TAG
SEQADV 4X00 HIS D 8 UNP B4E794 EXPRESSION TAG
SEQRES 1 A 283 MET ALA HIS HIS HIS HIS HIS HIS ALA ALA ALA ARG ASP
SEQRES 2 A 283 TYR THR VAL THR ALA PRO ASP GLY VAL VAL LEU ALA VAL
SEQRES 3 A 283 GLN GLU ALA GLY ASP PRO GLU GLY SER PRO ILE ILE PHE
SEQRES 4 A 283 ILE HIS GLY LEU LEU GLY SER ARG LEU ASN TRP SER LYS
SEQRES 5 A 283 GLN LEU GLN ASP PRO ARG LEU GLN HIS TYR ARG LEU ILE
SEQRES 6 A 283 THR TYR ASP LEU ARG GLY HIS GLY LEU SER GLY LYS PRO
SEQRES 7 A 283 ALA GLU ALA SER SER TYR THR ASP GLY ARG ARG TRP ALA
SEQRES 8 A 283 ASP ASP LEU ALA ALA ILE ILE GLU SER THR HIS ALA ARG
SEQRES 9 A 283 LYS PRO VAL LEU VAL GLY TRP SER LEU GLY GLY ALA VAL
SEQRES 10 A 283 ILE SER ASN TYR LEU ALA ALA TYR GLY ASP LYS GLY ILE
SEQRES 11 A 283 ALA GLY ALA VAL TYR VAL ASP GLY VAL ILE GLU LEU LYS
SEQRES 12 A 283 PRO ASP GLN ILE VAL ALA HIS PRO GLU VAL TYR ARG ASP
SEQRES 13 A 283 MET ILE ALA SER ASP LEU GLN THR HIS LEU ASP GLY GLU
SEQRES 14 A 283 ARG ALA PHE LEU ARG LEU CYS PHE HIS ARG GLN PRO ASP
SEQRES 15 A 283 ALA THR THR PHE SER LEU LEU LEU ALA ASN ALA ALA LEU
SEQRES 16 A 283 ALA SER TRP ASP MET GLN ARG ALA VAL ARG SER MET THR
SEQRES 17 A 283 VAL GLU ALA ALA LYS GLY LEU SER LYS ALA GLU VAL PRO
SEQRES 18 A 283 LEU LEU LEU LEU TYR GLY ALA GLN ASP ALA LEU VAL LYS
SEQRES 19 A 283 ALA LYS PRO SER ILE ALA ARG ALA LYS SER LEU ASN PRO
SEQRES 20 A 283 ARG ILE ARG SER GLU LEU TYR ALA ASP SER GLY HIS ALA
SEQRES 21 A 283 PRO PHE LEU GLU GLU PRO GLU ARG PHE ASN ARG ASP LEU
SEQRES 22 A 283 SER ASP PHE VAL ARG MET ALA LEU SER ARG
SEQRES 1 B 283 MET ALA HIS HIS HIS HIS HIS HIS ALA ALA ALA ARG ASP
SEQRES 2 B 283 TYR THR VAL THR ALA PRO ASP GLY VAL VAL LEU ALA VAL
SEQRES 3 B 283 GLN GLU ALA GLY ASP PRO GLU GLY SER PRO ILE ILE PHE
SEQRES 4 B 283 ILE HIS GLY LEU LEU GLY SER ARG LEU ASN TRP SER LYS
SEQRES 5 B 283 GLN LEU GLN ASP PRO ARG LEU GLN HIS TYR ARG LEU ILE
SEQRES 6 B 283 THR TYR ASP LEU ARG GLY HIS GLY LEU SER GLY LYS PRO
SEQRES 7 B 283 ALA GLU ALA SER SER TYR THR ASP GLY ARG ARG TRP ALA
SEQRES 8 B 283 ASP ASP LEU ALA ALA ILE ILE GLU SER THR HIS ALA ARG
SEQRES 9 B 283 LYS PRO VAL LEU VAL GLY TRP SER LEU GLY GLY ALA VAL
SEQRES 10 B 283 ILE SER ASN TYR LEU ALA ALA TYR GLY ASP LYS GLY ILE
SEQRES 11 B 283 ALA GLY ALA VAL TYR VAL ASP GLY VAL ILE GLU LEU LYS
SEQRES 12 B 283 PRO ASP GLN ILE VAL ALA HIS PRO GLU VAL TYR ARG ASP
SEQRES 13 B 283 MET ILE ALA SER ASP LEU GLN THR HIS LEU ASP GLY GLU
SEQRES 14 B 283 ARG ALA PHE LEU ARG LEU CYS PHE HIS ARG GLN PRO ASP
SEQRES 15 B 283 ALA THR THR PHE SER LEU LEU LEU ALA ASN ALA ALA LEU
SEQRES 16 B 283 ALA SER TRP ASP MET GLN ARG ALA VAL ARG SER MET THR
SEQRES 17 B 283 VAL GLU ALA ALA LYS GLY LEU SER LYS ALA GLU VAL PRO
SEQRES 18 B 283 LEU LEU LEU LEU TYR GLY ALA GLN ASP ALA LEU VAL LYS
SEQRES 19 B 283 ALA LYS PRO SER ILE ALA ARG ALA LYS SER LEU ASN PRO
SEQRES 20 B 283 ARG ILE ARG SER GLU LEU TYR ALA ASP SER GLY HIS ALA
SEQRES 21 B 283 PRO PHE LEU GLU GLU PRO GLU ARG PHE ASN ARG ASP LEU
SEQRES 22 B 283 SER ASP PHE VAL ARG MET ALA LEU SER ARG
SEQRES 1 C 283 MET ALA HIS HIS HIS HIS HIS HIS ALA ALA ALA ARG ASP
SEQRES 2 C 283 TYR THR VAL THR ALA PRO ASP GLY VAL VAL LEU ALA VAL
SEQRES 3 C 283 GLN GLU ALA GLY ASP PRO GLU GLY SER PRO ILE ILE PHE
SEQRES 4 C 283 ILE HIS GLY LEU LEU GLY SER ARG LEU ASN TRP SER LYS
SEQRES 5 C 283 GLN LEU GLN ASP PRO ARG LEU GLN HIS TYR ARG LEU ILE
SEQRES 6 C 283 THR TYR ASP LEU ARG GLY HIS GLY LEU SER GLY LYS PRO
SEQRES 7 C 283 ALA GLU ALA SER SER TYR THR ASP GLY ARG ARG TRP ALA
SEQRES 8 C 283 ASP ASP LEU ALA ALA ILE ILE GLU SER THR HIS ALA ARG
SEQRES 9 C 283 LYS PRO VAL LEU VAL GLY TRP SER LEU GLY GLY ALA VAL
SEQRES 10 C 283 ILE SER ASN TYR LEU ALA ALA TYR GLY ASP LYS GLY ILE
SEQRES 11 C 283 ALA GLY ALA VAL TYR VAL ASP GLY VAL ILE GLU LEU LYS
SEQRES 12 C 283 PRO ASP GLN ILE VAL ALA HIS PRO GLU VAL TYR ARG ASP
SEQRES 13 C 283 MET ILE ALA SER ASP LEU GLN THR HIS LEU ASP GLY GLU
SEQRES 14 C 283 ARG ALA PHE LEU ARG LEU CYS PHE HIS ARG GLN PRO ASP
SEQRES 15 C 283 ALA THR THR PHE SER LEU LEU LEU ALA ASN ALA ALA LEU
SEQRES 16 C 283 ALA SER TRP ASP MET GLN ARG ALA VAL ARG SER MET THR
SEQRES 17 C 283 VAL GLU ALA ALA LYS GLY LEU SER LYS ALA GLU VAL PRO
SEQRES 18 C 283 LEU LEU LEU LEU TYR GLY ALA GLN ASP ALA LEU VAL LYS
SEQRES 19 C 283 ALA LYS PRO SER ILE ALA ARG ALA LYS SER LEU ASN PRO
SEQRES 20 C 283 ARG ILE ARG SER GLU LEU TYR ALA ASP SER GLY HIS ALA
SEQRES 21 C 283 PRO PHE LEU GLU GLU PRO GLU ARG PHE ASN ARG ASP LEU
SEQRES 22 C 283 SER ASP PHE VAL ARG MET ALA LEU SER ARG
SEQRES 1 D 283 MET ALA HIS HIS HIS HIS HIS HIS ALA ALA ALA ARG ASP
SEQRES 2 D 283 TYR THR VAL THR ALA PRO ASP GLY VAL VAL LEU ALA VAL
SEQRES 3 D 283 GLN GLU ALA GLY ASP PRO GLU GLY SER PRO ILE ILE PHE
SEQRES 4 D 283 ILE HIS GLY LEU LEU GLY SER ARG LEU ASN TRP SER LYS
SEQRES 5 D 283 GLN LEU GLN ASP PRO ARG LEU GLN HIS TYR ARG LEU ILE
SEQRES 6 D 283 THR TYR ASP LEU ARG GLY HIS GLY LEU SER GLY LYS PRO
SEQRES 7 D 283 ALA GLU ALA SER SER TYR THR ASP GLY ARG ARG TRP ALA
SEQRES 8 D 283 ASP ASP LEU ALA ALA ILE ILE GLU SER THR HIS ALA ARG
SEQRES 9 D 283 LYS PRO VAL LEU VAL GLY TRP SER LEU GLY GLY ALA VAL
SEQRES 10 D 283 ILE SER ASN TYR LEU ALA ALA TYR GLY ASP LYS GLY ILE
SEQRES 11 D 283 ALA GLY ALA VAL TYR VAL ASP GLY VAL ILE GLU LEU LYS
SEQRES 12 D 283 PRO ASP GLN ILE VAL ALA HIS PRO GLU VAL TYR ARG ASP
SEQRES 13 D 283 MET ILE ALA SER ASP LEU GLN THR HIS LEU ASP GLY GLU
SEQRES 14 D 283 ARG ALA PHE LEU ARG LEU CYS PHE HIS ARG GLN PRO ASP
SEQRES 15 D 283 ALA THR THR PHE SER LEU LEU LEU ALA ASN ALA ALA LEU
SEQRES 16 D 283 ALA SER TRP ASP MET GLN ARG ALA VAL ARG SER MET THR
SEQRES 17 D 283 VAL GLU ALA ALA LYS GLY LEU SER LYS ALA GLU VAL PRO
SEQRES 18 D 283 LEU LEU LEU LEU TYR GLY ALA GLN ASP ALA LEU VAL LYS
SEQRES 19 D 283 ALA LYS PRO SER ILE ALA ARG ALA LYS SER LEU ASN PRO
SEQRES 20 D 283 ARG ILE ARG SER GLU LEU TYR ALA ASP SER GLY HIS ALA
SEQRES 21 D 283 PRO PHE LEU GLU GLU PRO GLU ARG PHE ASN ARG ASP LEU
SEQRES 22 D 283 SER ASP PHE VAL ARG MET ALA LEU SER ARG
HET EDO A 301 4
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HET EDO A 307 4
HET GOL A 308 6
HET EDO B 301 4
HET EDO B 302 4
HET EDO B 303 4
HET F B 304 1
HET EDO C 301 4
HET EDO C 302 4
HET GOL C 303 6
HET F C 304 1
HET EDO D 301 4
HET EDO D 302 4
HET GOL D 303 6
HET F D 304 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM F FLUORIDE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 EDO 14(C2 H6 O2)
FORMUL 12 GOL 3(C3 H8 O3)
FORMUL 16 F 3(F 1-)
FORMUL 25 HOH *1289(H2 O)
HELIX 1 AA1 SER A 46 ASN A 49 5 4
HELIX 2 AA2 TRP A 50 GLN A 55 1 6
HELIX 3 AA3 ASP A 56 GLN A 60 5 5
HELIX 4 AA4 ALA A 81 ASP A 86 1 6
HELIX 5 AA5 ASP A 86 THR A 101 1 16
HELIX 6 AA6 LEU A 113 GLY A 126 1 14
HELIX 7 AA7 HIS A 150 MET A 157 1 8
HELIX 8 AA8 ASP A 161 LEU A 175 1 15
HELIX 9 AA9 ASP A 182 LEU A 195 1 14
HELIX 10 AB1 SER A 197 ARG A 205 1 9
HELIX 11 AB2 GLU A 210 LYS A 217 1 8
HELIX 12 AB3 LYS A 234 ASN A 246 1 13
HELIX 13 AB4 ALA A 260 GLU A 265 1 6
HELIX 14 AB5 GLU A 265 LEU A 281 1 17
HELIX 15 AB6 SER B 46 ASN B 49 5 4
HELIX 16 AB7 TRP B 50 GLN B 55 1 6
HELIX 17 AB8 ARG B 58 HIS B 61 5 4
HELIX 18 AB9 ALA B 81 ASP B 86 1 6
HELIX 19 AC1 ASP B 86 HIS B 102 1 17
HELIX 20 AC2 LEU B 113 GLY B 126 1 14
HELIX 21 AC3 HIS B 150 MET B 157 1 8
HELIX 22 AC4 ASP B 161 CYS B 176 1 16
HELIX 23 AC5 ASP B 182 LEU B 195 1 14
HELIX 24 AC6 SER B 197 VAL B 204 1 8
HELIX 25 AC7 ARG B 205 MET B 207 5 3
HELIX 26 AC8 GLU B 210 ALA B 218 1 9
HELIX 27 AC9 LYS B 234 ASN B 246 1 13
HELIX 28 AD1 ALA B 260 GLU B 265 1 6
HELIX 29 AD2 GLU B 265 ARG B 283 1 19
HELIX 30 AD3 SER C 46 ASN C 49 5 4
HELIX 31 AD4 TRP C 50 GLN C 55 1 6
HELIX 32 AD5 ARG C 58 HIS C 61 5 4
HELIX 33 AD6 ALA C 81 ASP C 86 1 6
HELIX 34 AD7 ASP C 86 HIS C 102 1 17
HELIX 35 AD8 LEU C 113 GLY C 126 1 14
HELIX 36 AD9 HIS C 150 MET C 157 1 8
HELIX 37 AE1 ASP C 161 LEU C 175 1 15
HELIX 38 AE2 ASP C 182 LEU C 195 1 14
HELIX 39 AE3 SER C 197 VAL C 204 1 8
HELIX 40 AE4 ARG C 205 MET C 207 5 3
HELIX 41 AE5 GLU C 210 ALA C 218 1 9
HELIX 42 AE6 LYS C 234 ASN C 246 1 13
HELIX 43 AE7 ALA C 260 GLU C 265 1 6
HELIX 44 AE8 GLU C 265 SER C 282 1 18
HELIX 45 AE9 SER D 46 ASN D 49 5 4
HELIX 46 AF1 TRP D 50 GLN D 55 1 6
HELIX 47 AF2 ARG D 58 HIS D 61 5 4
HELIX 48 AF3 ALA D 81 ASP D 86 1 6
HELIX 49 AF4 ASP D 86 HIS D 102 1 17
HELIX 50 AF5 LEU D 113 GLY D 126 1 14
HELIX 51 AF6 HIS D 150 MET D 157 1 8
HELIX 52 AF7 ASP D 161 LEU D 175 1 15
HELIX 53 AF8 ASP D 182 LEU D 195 1 14
HELIX 54 AF9 SER D 197 ARG D 205 1 9
HELIX 55 AG1 GLU D 210 ALA D 218 1 9
HELIX 56 AG2 LYS D 234 ASN D 246 1 13
HELIX 57 AG3 ALA D 260 GLU D 265 1 6
HELIX 58 AG4 GLU D 265 ARG D 283 1 19
SHEET 1 AA1 8 ARG A 12 THR A 17 0
SHEET 2 AA1 8 VAL A 23 GLY A 30 -1 O LEU A 24 N VAL A 16
SHEET 3 AA1 8 ARG A 63 TYR A 67 -1 O THR A 66 N GLN A 27
SHEET 4 AA1 8 PRO A 36 ILE A 40 1 N ILE A 37 O ILE A 65
SHEET 5 AA1 8 VAL A 107 TRP A 111 1 O VAL A 109 N ILE A 40
SHEET 6 AA1 8 GLY A 132 VAL A 136 1 O VAL A 136 N GLY A 110
SHEET 7 AA1 8 LEU A 222 GLY A 227 1 O LEU A 225 N TYR A 135
SHEET 8 AA1 8 ARG A 250 TYR A 254 1 O TYR A 254 N TYR A 226
SHEET 1 AA2 8 ASP B 13 THR B 17 0
SHEET 2 AA2 8 VAL B 23 GLY B 30 -1 O LEU B 24 N VAL B 16
SHEET 3 AA2 8 ARG B 63 TYR B 67 -1 O THR B 66 N GLN B 27
SHEET 4 AA2 8 PRO B 36 ILE B 40 1 N ILE B 37 O ILE B 65
SHEET 5 AA2 8 VAL B 107 TRP B 111 1 O VAL B 109 N ILE B 40
SHEET 6 AA2 8 GLY B 132 VAL B 136 1 O VAL B 136 N GLY B 110
SHEET 7 AA2 8 LEU B 222 GLY B 227 1 O LEU B 225 N TYR B 135
SHEET 8 AA2 8 ARG B 250 TYR B 254 1 O TYR B 254 N TYR B 226
SHEET 1 AA3 8 ARG C 12 THR C 17 0
SHEET 2 AA3 8 VAL C 23 GLY C 30 -1 O LEU C 24 N VAL C 16
SHEET 3 AA3 8 ARG C 63 TYR C 67 -1 O THR C 66 N GLN C 27
SHEET 4 AA3 8 PRO C 36 ILE C 40 1 N ILE C 37 O ILE C 65
SHEET 5 AA3 8 VAL C 107 TRP C 111 1 O VAL C 109 N ILE C 40
SHEET 6 AA3 8 GLY C 132 VAL C 136 1 O VAL C 136 N GLY C 110
SHEET 7 AA3 8 LEU C 222 GLY C 227 1 O LEU C 223 N TYR C 135
SHEET 8 AA3 8 ARG C 250 TYR C 254 1 O TYR C 254 N TYR C 226
SHEET 1 AA4 8 ASP D 13 THR D 17 0
SHEET 2 AA4 8 VAL D 23 GLY D 30 -1 O LEU D 24 N VAL D 16
SHEET 3 AA4 8 ARG D 63 TYR D 67 -1 O THR D 66 N GLN D 27
SHEET 4 AA4 8 PRO D 36 ILE D 40 1 N ILE D 37 O ILE D 65
SHEET 5 AA4 8 VAL D 107 TRP D 111 1 O VAL D 109 N ILE D 40
SHEET 6 AA4 8 GLY D 132 VAL D 136 1 O VAL D 136 N GLY D 110
SHEET 7 AA4 8 LEU D 222 GLY D 227 1 O LEU D 225 N TYR D 135
SHEET 8 AA4 8 ARG D 250 TYR D 254 1 O TYR D 254 N TYR D 226
SITE 1 AC1 6 SER A 187 HOH A 415 HOH A 438 HOH A 744
SITE 2 AC1 6 ARG D 170 ARG D 174
SITE 1 AC2 5 LEU A 48 SER A 51 LEU A 263 HOH A 662
SITE 2 AC2 5 HOH A 756
SITE 1 AC3 7 ALA A 228 ASP A 230 VAL A 233 LYS A 234
SITE 2 AC3 7 ALA A 235 HOH A 525 HOH A 617
SITE 1 AC4 6 GLU A 252 ARG A 268 ARG A 271 ASP A 272
SITE 2 AC4 6 HOH A 421 GLU D 99
SITE 1 AC5 6 HOH A 406 HOH A 411 ILE D 98 GLU D 99
SITE 2 AC5 6 TYR D 121 TYR D 125
SITE 1 AC6 6 ASP A 275 ARG A 278 HOH A 417 HOH A 428
SITE 2 AC6 6 PRO D 19 ASP D 20
SITE 1 AC7 5 LYS A 52 ARG A 179 PRO A 181 LEU A 263
SITE 2 AC7 5 HOH A 566
SITE 1 AC8 2 SER A 112 LEU A 232
SITE 1 AC9 8 ALA B 228 ASP B 230 VAL B 233 LYS B 234
SITE 2 AC9 8 ALA B 235 HOH B 508 HOH B 585 HOH B 591
SITE 1 AD1 5 LYS B 77 ALA B 194 LEU B 195 ALA B 196
SITE 2 AD1 5 LEU C 195
SITE 1 AD2 7 ILE B 98 GLU B 99 TYR B 121 TYR B 125
SITE 2 AD2 7 HOH B 404 ARG C 268 HOH C 415
SITE 1 AD3 1 SER C 187
SITE 1 AD4 7 ALA C 228 ASP C 230 VAL C 233 LYS C 234
SITE 2 AD4 7 ALA C 235 HOH C 517 HOH C 581
SITE 1 AD5 7 GLU B 99 GLU C 252 TYR C 254 ARG C 268
SITE 2 AD5 7 ARG C 271 ASP C 272 HOH C 404
SITE 1 AD6 5 HIS C 150 PRO C 151 GLU C 152 VAL C 153
SITE 2 AD6 5 HOH C 695
SITE 1 AD7 2 SER B 187 ARG C 174
SITE 1 AD8 6 LEU D 48 ASN D 49 SER D 51 LEU D 188
SITE 2 AD8 6 LEU D 263 HOH D 564
SITE 1 AD9 9 TYR A 254 ALA A 255 ASP A 256 GLU A 265
SITE 2 AD9 9 ARG A 268 ILE D 98 GLU D 99 HOH D 402
SITE 3 AD9 9 HOH D 441
SITE 1 AE1 3 SER D 112 TYR D 154 HOH D 600
SITE 1 AE2 1 SER D 187
CRYST1 65.720 80.370 99.400 90.00 93.07 90.00 P 1 21 1 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 0.015216 0.000000 0.000815 0.00000
SCALE2 0.000000 0.012442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010075 0.00000
TER 2134 ARG A 283
TER 4257 ARG B 283
TER 6377 ARG C 283
TER 8489 ARG D 283
MASTER 508 0 20 58 32 0 36 6 9644 4 74 88
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