HEADER TRANSPORT PROTEIN 05-DEC-99 1C5K
TITLE THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT
TITLE 2 TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION
TITLE 3 DOMAIN OF COLICIN E9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TOLB PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENTIRE PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: IN E.COLI TOLB FORMS A HETERODIMER WITH PAL
COMPND 7 (PEPTIDOGLYCAN ASSOCIATED LIPOPROTEIN)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PRJ379
KEYWDS BETA PROPELLOR, PROTEIN-PROTEIN INTERACTIONS, COLICIN IMPORT,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CARR,C.N.PENFOLD,V.BAMFORD,R.JAMES,A.M.HEMMINGS
REVDAT 4 27-DEC-23 1C5K 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1C5K 1 VERSN
REVDAT 2 01-APR-03 1C5K 1 JRNL
REVDAT 1 06-DEC-00 1C5K 0
JRNL AUTH S.CARR,C.N.PENFOLD,V.BAMFORD,R.JAMES,A.M.HEMMINGS
JRNL TITL THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE
JRNL TITL 2 TOL-DEPENDENT TRANSLOCATION SYSTEM, AND ITS PROTEIN-PROTEIN
JRNL TITL 3 INTERACTION WITH THE TRANSLOCATION DOMAIN OF COLICIN E9.
JRNL REF STRUCTURE FOLD.DES. V. 8 57 2000
JRNL REFN ISSN 0969-2126
JRNL PMID 10673426
JRNL DOI 10.1016/S0969-2126(00)00079-4
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 44970
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2383
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.90
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.720
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 17.10
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000001364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91, 1.07, 1.386, 1.387
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59093
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 5.20000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 17.6000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
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 20.09500
REMARK 290 SMTRY3 2 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 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 MET A 1
REMARK 465 MET A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 ARG A 7
REMARK 465 VAL A 8
REMARK 465 ALA A 9
REMARK 465 PHE A 10
REMARK 465 GLY A 11
REMARK 465 PHE A 12
REMARK 465 LEU A 13
REMARK 465 ILE A 14
REMARK 465 LEU A 15
REMARK 465 TRP A 16
REMARK 465 ALA A 17
REMARK 465 SER A 18
REMARK 465 VAL A 19
REMARK 465 LEU A 20
REMARK 465 HIS A 21
REMARK 465 ALA A 22
REMARK 465 GLU A 23
REMARK 465 VAL A 24
REMARK 465 ARG A 25
REMARK 465 ILE A 26
REMARK 465 VAL A 27
REMARK 465 ILE A 28
REMARK 465 ASP A 29
REMARK 465 SER A 30
REMARK 465 GLY A 31
REMARK 465 VAL A 32
REMARK 465 ASP A 33
REMARK 465 SER A 34
REMARK 465 LEU A 432
REMARK 465 GLU A 433
REMARK 465 HIS A 434
REMARK 465 HIS A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
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 PRO A 48 83.18 -58.79
REMARK 500 ALA A 50 93.55 88.03
REMARK 500 SER A 83 -172.77 -170.49
REMARK 500 ALA A 84 38.60 -81.62
REMARK 500 GLN A 85 -41.25 -145.92
REMARK 500 SER A 93 -25.11 -29.61
REMARK 500 LEU A 95 33.90 -52.68
REMARK 500 ALA A 99 135.45 -175.53
REMARK 500 THR A 122 -125.31 -69.55
REMARK 500 ALA A 125 73.83 -106.06
REMARK 500 SER A 242 44.57 -148.23
REMARK 500 ARG A 245 -157.19 90.91
REMARK 500 GLN A 301 -30.60 -130.90
REMARK 500 SER A 374 25.66 -141.86
REMARK 500 THR A 380 69.95 33.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 YB A 501 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 337 OD1
REMARK 620 2 HOH A 611 O 71.2
REMARK 620 3 HOH A 616 O 132.8 70.1
REMARK 620 4 HOH A 622 O 83.4 152.0 137.9
REMARK 620 5 HOH A 651 O 76.3 90.3 129.2 72.0
REMARK 620 6 HOH A 721 O 140.6 135.5 86.5 62.0 75.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 501
DBREF 1C5K A 2 431 UNP P0A855 TOLB_ECOLI 1 430
SEQADV 1C5K LEU A 432 UNP P0A855 LINKER
SEQADV 1C5K GLU A 433 UNP P0A855 LINKER
SEQADV 1C5K HIS A 434 UNP P0A855 EXPRESSION TAG
SEQADV 1C5K HIS A 435 UNP P0A855 EXPRESSION TAG
SEQADV 1C5K HIS A 436 UNP P0A855 EXPRESSION TAG
SEQADV 1C5K HIS A 437 UNP P0A855 EXPRESSION TAG
SEQADV 1C5K HIS A 438 UNP P0A855 EXPRESSION TAG
SEQADV 1C5K HIS A 439 UNP P0A855 EXPRESSION TAG
SEQRES 1 A 439 MET MET LYS GLN ALA LEU ARG VAL ALA PHE GLY PHE LEU
SEQRES 2 A 439 ILE LEU TRP ALA SER VAL LEU HIS ALA GLU VAL ARG ILE
SEQRES 3 A 439 VAL ILE ASP SER GLY VAL ASP SER GLY ARG PRO ILE GLY
SEQRES 4 A 439 VAL VAL PRO PHE GLN TRP ALA GLY PRO GLY ALA ALA PRO
SEQRES 5 A 439 GLU ASP ILE GLY GLY ILE VAL ALA ALA ASP LEU ARG ASN
SEQRES 6 A 439 SER GLY LYS PHE ASN PRO LEU ASP ARG ALA ARG LEU PRO
SEQRES 7 A 439 GLN GLN PRO GLY SER ALA GLN GLU VAL GLN PRO ALA ALA
SEQRES 8 A 439 TRP SER ALA LEU GLY ILE ASP ALA VAL VAL VAL GLY GLN
SEQRES 9 A 439 VAL THR PRO ASN PRO ASP GLY SER TYR ASN VAL ALA TYR
SEQRES 10 A 439 GLN LEU VAL ASP THR GLY GLY ALA PRO GLY THR VAL LEU
SEQRES 11 A 439 ALA GLN ASN SER TYR LYS VAL ASN LYS GLN TRP LEU ARG
SEQRES 12 A 439 TYR ALA GLY HIS THR ALA SER ASP GLU VAL PHE GLU LYS
SEQRES 13 A 439 LEU THR GLY ILE LYS GLY ALA PHE ARG THR ARG ILE ALA
SEQRES 14 A 439 TYR VAL VAL GLN THR ASN GLY GLY GLN PHE PRO TYR GLU
SEQRES 15 A 439 LEU ARG VAL SER ASP TYR ASP GLY TYR ASN GLN PHE VAL
SEQRES 16 A 439 VAL HIS ARG SER PRO GLN PRO LEU MET SER PRO ALA TRP
SEQRES 17 A 439 SER PRO ASP GLY SER LYS LEU ALA TYR VAL THR PHE GLU
SEQRES 18 A 439 SER GLY ARG SER ALA LEU VAL ILE GLN THR LEU ALA ASN
SEQRES 19 A 439 GLY ALA VAL ARG GLN VAL ALA SER PHE PRO ARG HIS ASN
SEQRES 20 A 439 GLY ALA PRO ALA PHE SER PRO ASP GLY SER LYS LEU ALA
SEQRES 21 A 439 PHE ALA LEU SER LYS THR GLY SER LEU ASN LEU TYR VAL
SEQRES 22 A 439 MET ASP LEU ALA SER GLY GLN ILE ARG GLN VAL THR ASP
SEQRES 23 A 439 GLY ARG SER ASN ASN THR GLU PRO THR TRP PHE PRO ASP
SEQRES 24 A 439 SER GLN ASN LEU ALA PHE THR SER ASP GLN ALA GLY ARG
SEQRES 25 A 439 PRO GLN VAL TYR LYS VAL ASN ILE ASN GLY GLY ALA PRO
SEQRES 26 A 439 GLN ARG ILE THR TRP GLU GLY SER GLN ASN GLN ASP ALA
SEQRES 27 A 439 ASP VAL SER SER ASP GLY LYS PHE MET VAL MET VAL SER
SEQRES 28 A 439 SER ASN GLY GLY GLN GLN HIS ILE ALA LYS GLN ASP LEU
SEQRES 29 A 439 ALA THR GLY GLY VAL GLN VAL LEU SER SER THR PHE LEU
SEQRES 30 A 439 ASP GLU THR PRO SER LEU ALA PRO ASN GLY THR MET VAL
SEQRES 31 A 439 ILE TYR SER SER SER GLN GLY MET GLY SER VAL LEU ASN
SEQRES 32 A 439 LEU VAL SER THR ASP GLY ARG PHE LYS ALA ARG LEU PRO
SEQRES 33 A 439 ALA THR ASP GLY GLN VAL LYS PHE PRO ALA TRP SER PRO
SEQRES 34 A 439 TYR LEU LEU GLU HIS HIS HIS HIS HIS HIS
HET YB A 501 1
HETNAM YB YTTERBIUM (III) ION
FORMUL 2 YB YB 3+
FORMUL 3 HOH *230(H2 O)
HELIX 1 1 ILE A 55 ASN A 65 1 11
HELIX 2 2 ARG A 74 ARG A 76 5 3
HELIX 3 3 PRO A 89 TRP A 92 1 4
HELIX 4 4 LYS A 139 THR A 158 5 20
SHEET 1 A 2 ARG A 36 ILE A 38 0
SHEET 2 A 2 PHE A 69 PRO A 71 1 N ASN A 70 O ARG A 36
SHEET 1 B 4 GLN A 44 ALA A 46 0
SHEET 2 B 4 VAL A 100 PRO A 107 1 N VAL A 105 O GLN A 44
SHEET 3 B 4 TYR A 113 ASP A 121 -1 N VAL A 120 O VAL A 100
SHEET 4 B 4 THR A 128 VAL A 137 -1 N VAL A 137 O TYR A 113
SHEET 1 C 4 GLN A 421 LYS A 423 0
SHEET 2 C 4 ARG A 167 GLN A 173 -1 N GLN A 173 O GLN A 421
SHEET 3 C 4 TYR A 181 ASP A 187 -1 N SER A 186 O ILE A 168
SHEET 4 C 4 PHE A 194 SER A 199 -1 N SER A 199 O TYR A 181
SHEET 1 D 3 LYS A 214 THR A 219 0
SHEET 2 D 3 ALA A 226 THR A 231 -1 N GLN A 230 O LEU A 215
SHEET 3 D 3 VAL A 237 ALA A 241 -1 N ALA A 241 O LEU A 227
SHEET 1 E 3 LYS A 258 LEU A 263 0
SHEET 2 E 3 ASN A 270 ASP A 275 -1 N MET A 274 O LEU A 259
SHEET 3 E 3 GLN A 280 GLN A 283 -1 N ARG A 282 O VAL A 273
SHEET 1 F 2 ASN A 302 SER A 307 0
SHEET 2 F 2 GLN A 314 ASN A 319 -1 N VAL A 318 O LEU A 303
SHEET 1 G 4 GLN A 334 GLN A 336 0
SHEET 2 G 4 PHE A 346 ASN A 353 -1 N SER A 352 O GLN A 334
SHEET 3 G 4 GLN A 356 ASP A 363 -1 N GLN A 362 O MET A 347
SHEET 4 G 4 VAL A 369 VAL A 371 -1 N GLN A 370 O LYS A 361
SHEET 1 H 3 MET A 389 GLN A 396 0
SHEET 2 H 3 GLY A 399 SER A 406 -1 N VAL A 405 O VAL A 390
SHEET 3 H 3 LYS A 412 ARG A 414 -1 N ALA A 413 O LEU A 404
LINK OD1 ASP A 337 YB YB A 501 1555 1555 2.35
LINK YB YB A 501 O HOH A 611 1555 1555 2.40
LINK YB YB A 501 O HOH A 616 1555 1555 2.39
LINK YB YB A 501 O HOH A 622 1555 1555 2.37
LINK YB YB A 501 O HOH A 651 1555 1555 2.96
LINK YB YB A 501 O HOH A 721 1555 1555 2.56
SITE 1 AC1 6 ASP A 337 HOH A 611 HOH A 616 HOH A 622
SITE 2 AC1 6 HOH A 651 HOH A 721
CRYST1 63.580 40.190 77.660 90.00 110.22 90.00 P 1 21 1 2
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 0.015728 0.000000 0.005793 0.00000
SCALE2 0.000000 0.024882 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013722 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
