HEADER CELL INVASION 04-AUG-14 4UV6
TITLE CRYSTAL STRUCTURE OF APICAL MEMBRANE ANTIGEN 1 FROM PLASMODIUM
TITLE 2 KNOWLESI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APICAL MEROZOITE ANTIGEN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 43-387;
COMPND 5 SYNONYM: AMA1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM KNOWLESI;
SOURCE 3 ORGANISM_TAXID: 5851;
SOURCE 4 STRAIN: H;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KM71H;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PPICZALPHAA
KEYWDS CELL INVASION, MALARIA, VACCINE CANDIDATE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.VULLIEZ-LE NORMAND,F.A.SAUL,G.A.BENTLEY
REVDAT 2 10-JAN-24 4UV6 1 REMARK
REVDAT 1 29-APR-15 4UV6 0
JRNL AUTH B.VULLIEZ-LE NORMAND,B.W.FABER,F.A.SAUL,M.VAN DER EIJK,
JRNL AUTH 2 A.W.THOMAS,B.SINGH,C.H.M.KOCKEN,G.A.BENTLEY
JRNL TITL CRYSTAL STRUCTURE OF PLASMODIUM KNOWLESI APICAL MEMBRANE
JRNL TITL 2 ANTIGEN 1 AND ITS COMPLEX WITH AN INVASION-INHIBITORY
JRNL TITL 3 MONOCLONAL ANTIBODY.
JRNL REF PLOS ONE V. 10 23567 2015
JRNL REFN ESSN 1932-6203
JRNL PMID 25886591
JRNL DOI 10.1371/JOURNAL.PONE.0123567
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 34846
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.420
REMARK 3 FREE R VALUE TEST SET COUNT : 843
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.52
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.11
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2833
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2538
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2755
REMARK 3 BIN R VALUE (WORKING SET) : 0.2525
REMARK 3 BIN FREE R VALUE : 0.3018
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.75
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78
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 : 5407
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 386
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.14180
REMARK 3 B22 (A**2) : -6.09570
REMARK 3 B33 (A**2) : 15.23750
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.24510
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.281
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.307
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.228
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.299
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.228
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5554 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7501 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1969 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 183 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 787 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5554 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 696 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6649 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.22
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.20
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4UV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1290061392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
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) : 0.9760
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34848
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 47.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: PDB ENTRY 1W81
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.86M SODIUM CITRATE, 0.1M HEPES PH
REMARK 280 8.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.16000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.16000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 GLU A 41
REMARK 465 PHE A 42
REMARK 465 PRO A 43
REMARK 465 ILE A 44
REMARK 465 ILE A 45
REMARK 465 GLU A 46
REMARK 465 ARG A 47
REMARK 465 SER A 48
REMARK 465 ILE A 49
REMARK 465 ARG A 50
REMARK 465 MET A 51
REMARK 465 ALA A 131
REMARK 465 ASP A 132
REMARK 465 SER A 212
REMARK 465 GLN A 213
REMARK 465 ASN A 214
REMARK 465 LYS A 215
REMARK 465 GLY A 328
REMARK 465 ALA A 329
REMARK 465 PHE A 330
REMARK 465 ASN A 331
REMARK 465 ASP A 398
REMARK 465 LEU A 399
REMARK 465 ASN A 400
REMARK 465 SER A 401
REMARK 465 ALA A 402
REMARK 465 VAL A 403
REMARK 465 ASP A 404
REMARK 465 HIS A 405
REMARK 465 HIS A 406
REMARK 465 HIS A 407
REMARK 465 HIS A 408
REMARK 465 HIS A 409
REMARK 465 HIS A 410
REMARK 465 GLU B 41
REMARK 465 PHE B 42
REMARK 465 PRO B 43
REMARK 465 ILE B 44
REMARK 465 ILE B 45
REMARK 465 GLU B 46
REMARK 465 ARG B 47
REMARK 465 SER B 48
REMARK 465 ILE B 49
REMARK 465 ARG B 50
REMARK 465 MET B 51
REMARK 465 SER B 212
REMARK 465 GLN B 213
REMARK 465 ASN B 214
REMARK 465 LYS B 215
REMARK 465 ASP B 216
REMARK 465 ALA B 217
REMARK 465 GLY B 328
REMARK 465 ALA B 329
REMARK 465 PHE B 330
REMARK 465 ASN B 331
REMARK 465 SER B 332
REMARK 465 LEU B 399
REMARK 465 ASN B 400
REMARK 465 SER B 401
REMARK 465 ALA B 402
REMARK 465 VAL B 403
REMARK 465 ASP B 404
REMARK 465 HIS B 405
REMARK 465 HIS B 406
REMARK 465 HIS B 407
REMARK 465 HIS B 408
REMARK 465 HIS B 409
REMARK 465 HIS B 410
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 GLU A 397 CG CD OE1 OE2
REMARK 470 MET B 218 CG SD CE
REMARK 470 GLU B 397 CG CD OE1 OE2
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 LEU A 76 56.26 -143.66
REMARK 500 LYS A 122 -8.87 -59.16
REMARK 500 HIS A 134 82.41 58.62
REMARK 500 GLU A 173 8.91 -67.54
REMARK 500 ASN A 176 84.78 -11.60
REMARK 500 ARG A 206 -70.94 -69.00
REMARK 500 CYS A 208 47.00 -109.68
REMARK 500 PRO A 210 96.05 -48.33
REMARK 500 ASP A 242 33.81 -92.16
REMARK 500 ARG A 249 -64.34 -150.74
REMARK 500 GLN A 380 -44.09 -135.08
REMARK 500 GLU A 385 90.37 -66.04
REMARK 500 LEU B 76 62.72 -154.84
REMARK 500 LYS B 122 -9.74 -58.58
REMARK 500 ALA B 131 -155.42 -93.25
REMARK 500 HIS B 134 83.12 44.15
REMARK 500 GLU B 173 6.24 -65.44
REMARK 500 ASN B 176 86.45 -15.29
REMARK 500 CYS B 208 46.73 -93.92
REMARK 500 PRO B 210 97.71 -51.75
REMARK 500 ASP B 242 32.99 -90.72
REMARK 500 ARG B 249 -66.35 -152.11
REMARK 500 GLN B 380 -41.16 -134.11
REMARK 500 GLU B 385 89.35 -69.72
REMARK 500 GLU B 396 -4.04 -59.69
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 A2097 DISTANCE = 5.94 ANGSTROMS
DBREF 4UV6 A 43 387 UNP B3L5E1 B3L5E1_PLAKH 43 387
DBREF 4UV6 B 43 387 UNP B3L5E1 B3L5E1_PLAKH 43 387
SEQADV 4UV6 GLU A 41 UNP B3L5E1 CLONING ARTIFACT
SEQADV 4UV6 PHE A 42 UNP B3L5E1 CLONING ARTIFACT
SEQADV 4UV6 GLY A 388 UNP B3L5E1 CLONING ARTIFACT
SEQADV 4UV6 LEU A 389 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLU A 390 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLN A 391 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LYS A 392 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LEU A 393 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ILE A 394 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 SER A 395 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLU A 396 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLU A 397 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ASP A 398 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LEU A 399 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ASN A 400 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 SER A 401 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ALA A 402 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 VAL A 403 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ASP A 404 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS A 405 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS A 406 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS A 407 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS A 408 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS A 409 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS A 410 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LYS A 107 UNP B3L5E1 ASN 107 ENGINEERED MUTATION
SEQADV 4UV6 ASN A 178 UNP B3L5E1 SER 178 ENGINEERED MUTATION
SEQADV 4UV6 GLU A 189 UNP B3L5E1 ASN 189 ENGINEERED MUTATION
SEQADV 4UV6 ARG A 240 UNP B3L5E1 SER 240 ENGINEERED MUTATION
SEQADV 4UV6 GLU B 41 UNP B3L5E1 CLONING ARTIFACT
SEQADV 4UV6 PHE B 42 UNP B3L5E1 CLONING ARTIFACT
SEQADV 4UV6 GLY B 388 UNP B3L5E1 CLONING ARTIFACT
SEQADV 4UV6 LEU B 389 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLU B 390 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLN B 391 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LYS B 392 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LEU B 393 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ILE B 394 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 SER B 395 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLU B 396 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 GLU B 397 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ASP B 398 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LEU B 399 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ASN B 400 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 SER B 401 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ALA B 402 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 VAL B 403 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 ASP B 404 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS B 405 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS B 406 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS B 407 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS B 408 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS B 409 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 HIS B 410 UNP B3L5E1 EXPRESSION TAG
SEQADV 4UV6 LYS B 107 UNP B3L5E1 ASN 107 ENGINEERED MUTATION
SEQADV 4UV6 ASN B 178 UNP B3L5E1 SER 178 ENGINEERED MUTATION
SEQADV 4UV6 GLU B 189 UNP B3L5E1 ASN 189 ENGINEERED MUTATION
SEQADV 4UV6 ARG B 240 UNP B3L5E1 SER 240 ENGINEERED MUTATION
SEQRES 1 A 370 GLU PHE PRO ILE ILE GLU ARG SER ILE ARG MET SER ASN
SEQRES 2 A 370 PRO TRP LYS ALA PHE MET GLU LYS TYR ASP LEU GLU ARG
SEQRES 3 A 370 ALA HIS ASN SER GLY ILE ARG ILE ASP LEU GLY GLU ASP
SEQRES 4 A 370 ALA GLU VAL GLY ASN SER LYS TYR ARG ILE PRO ALA GLY
SEQRES 5 A 370 LYS CYS PRO VAL PHE GLY LYS GLY ILE VAL ILE GLU ASN
SEQRES 6 A 370 SER LYS VAL SER PHE LEU THR PRO VAL ALA THR GLY ALA
SEQRES 7 A 370 GLN ARG LEU LYS GLU GLY GLY PHE ALA PHE PRO ASN ALA
SEQRES 8 A 370 ASP ASP HIS ILE SER PRO ILE THR ILE ALA ASN LEU LYS
SEQRES 9 A 370 GLU ARG TYR LYS GLU ASN ALA ASP LEU MET LYS LEU ASN
SEQRES 10 A 370 ASP ILE ALA LEU CYS LYS THR HIS ALA ALA SER PHE VAL
SEQRES 11 A 370 ILE ALA GLU ASP GLN ASN THR ASN TYR ARG HIS PRO ALA
SEQRES 12 A 370 VAL TYR ASP GLU LYS GLU LYS THR CYS TYR MET LEU TYR
SEQRES 13 A 370 LEU SER ALA GLN GLU ASN MET GLY PRO ARG TYR CYS SER
SEQRES 14 A 370 PRO ASP SER GLN ASN LYS ASP ALA MET PHE CYS PHE LYS
SEQRES 15 A 370 PRO ASP LYS ASN GLU LYS PHE ASP ASN LEU VAL TYR LEU
SEQRES 16 A 370 SER LYS ASN VAL ARG ASN ASP TRP GLU ASN LYS CYS PRO
SEQRES 17 A 370 ARG LYS ASN LEU GLY ASN ALA LYS PHE GLY LEU TRP VAL
SEQRES 18 A 370 ASP GLY ASN CYS GLU GLU ILE PRO TYR VAL ASN GLU VAL
SEQRES 19 A 370 GLU ALA ARG SER LEU ARG GLU CYS ASN ARG ILE VAL PHE
SEQRES 20 A 370 GLU ALA SER ALA SER ASP GLN PRO ARG GLN TYR GLU GLU
SEQRES 21 A 370 GLU LEU THR ASP TYR GLU LYS ILE GLN GLU GLY PHE ARG
SEQRES 22 A 370 GLN ASN ASN ARG ASP MET ILE LYS SER ALA PHE LEU PRO
SEQRES 23 A 370 VAL GLY ALA PHE ASN SER ASP ASN PHE LYS SER LYS GLY
SEQRES 24 A 370 ARG GLY TYR ASN TRP ALA ASN PHE ASP SER VAL ASN ASN
SEQRES 25 A 370 LYS CYS TYR ILE PHE ASN THR LYS PRO THR CYS LEU ILE
SEQRES 26 A 370 ASN ASP LYS ASN PHE PHE ALA THR THR ALA LEU SER HIS
SEQRES 27 A 370 PRO GLN GLU VAL ASP ASN GLU PHE PRO GLY LEU GLU GLN
SEQRES 28 A 370 LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP
SEQRES 29 A 370 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 370 GLU PHE PRO ILE ILE GLU ARG SER ILE ARG MET SER ASN
SEQRES 2 B 370 PRO TRP LYS ALA PHE MET GLU LYS TYR ASP LEU GLU ARG
SEQRES 3 B 370 ALA HIS ASN SER GLY ILE ARG ILE ASP LEU GLY GLU ASP
SEQRES 4 B 370 ALA GLU VAL GLY ASN SER LYS TYR ARG ILE PRO ALA GLY
SEQRES 5 B 370 LYS CYS PRO VAL PHE GLY LYS GLY ILE VAL ILE GLU ASN
SEQRES 6 B 370 SER LYS VAL SER PHE LEU THR PRO VAL ALA THR GLY ALA
SEQRES 7 B 370 GLN ARG LEU LYS GLU GLY GLY PHE ALA PHE PRO ASN ALA
SEQRES 8 B 370 ASP ASP HIS ILE SER PRO ILE THR ILE ALA ASN LEU LYS
SEQRES 9 B 370 GLU ARG TYR LYS GLU ASN ALA ASP LEU MET LYS LEU ASN
SEQRES 10 B 370 ASP ILE ALA LEU CYS LYS THR HIS ALA ALA SER PHE VAL
SEQRES 11 B 370 ILE ALA GLU ASP GLN ASN THR ASN TYR ARG HIS PRO ALA
SEQRES 12 B 370 VAL TYR ASP GLU LYS GLU LYS THR CYS TYR MET LEU TYR
SEQRES 13 B 370 LEU SER ALA GLN GLU ASN MET GLY PRO ARG TYR CYS SER
SEQRES 14 B 370 PRO ASP SER GLN ASN LYS ASP ALA MET PHE CYS PHE LYS
SEQRES 15 B 370 PRO ASP LYS ASN GLU LYS PHE ASP ASN LEU VAL TYR LEU
SEQRES 16 B 370 SER LYS ASN VAL ARG ASN ASP TRP GLU ASN LYS CYS PRO
SEQRES 17 B 370 ARG LYS ASN LEU GLY ASN ALA LYS PHE GLY LEU TRP VAL
SEQRES 18 B 370 ASP GLY ASN CYS GLU GLU ILE PRO TYR VAL ASN GLU VAL
SEQRES 19 B 370 GLU ALA ARG SER LEU ARG GLU CYS ASN ARG ILE VAL PHE
SEQRES 20 B 370 GLU ALA SER ALA SER ASP GLN PRO ARG GLN TYR GLU GLU
SEQRES 21 B 370 GLU LEU THR ASP TYR GLU LYS ILE GLN GLU GLY PHE ARG
SEQRES 22 B 370 GLN ASN ASN ARG ASP MET ILE LYS SER ALA PHE LEU PRO
SEQRES 23 B 370 VAL GLY ALA PHE ASN SER ASP ASN PHE LYS SER LYS GLY
SEQRES 24 B 370 ARG GLY TYR ASN TRP ALA ASN PHE ASP SER VAL ASN ASN
SEQRES 25 B 370 LYS CYS TYR ILE PHE ASN THR LYS PRO THR CYS LEU ILE
SEQRES 26 B 370 ASN ASP LYS ASN PHE PHE ALA THR THR ALA LEU SER HIS
SEQRES 27 B 370 PRO GLN GLU VAL ASP ASN GLU PHE PRO GLY LEU GLU GLN
SEQRES 28 B 370 LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP
SEQRES 29 B 370 HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *386(H2 O)
HELIX 1 1 ALA A 57 TYR A 62 5 6
HELIX 2 2 ASP A 63 HIS A 68 1 6
HELIX 3 3 ARG A 120 GLY A 124 5 5
HELIX 4 4 ILE A 140 TYR A 147 1 8
HELIX 5 5 ASN A 150 LYS A 155 1 6
HELIX 6 6 ASN A 157 ALA A 167 1 11
HELIX 7 7 GLU A 227 ASP A 230 5 4
HELIX 8 8 ASP A 242 CYS A 247 1 6
HELIX 9 9 SER A 278 SER A 290 1 13
HELIX 10 10 ASP A 304 GLN A 314 1 11
HELIX 11 11 ASN A 316 ALA A 323 1 8
HELIX 12 12 SER A 332 LYS A 336 5 5
HELIX 13 13 ALA B 57 TYR B 62 5 6
HELIX 14 14 ASP B 63 HIS B 68 1 6
HELIX 15 15 ARG B 120 GLY B 124 5 5
HELIX 16 16 ILE B 140 TYR B 147 1 8
HELIX 17 17 ASN B 150 LYS B 155 1 6
HELIX 18 18 ASN B 157 ALA B 167 1 11
HELIX 19 19 GLU B 227 ASP B 230 5 4
HELIX 20 20 ASP B 242 CYS B 247 1 6
HELIX 21 21 SER B 278 SER B 290 1 13
HELIX 22 22 ASP B 304 GLN B 314 1 11
HELIX 23 23 ASN B 316 SER B 322 1 7
SHEET 1 AA 2 GLU A 78 VAL A 82 0
SHEET 2 AA 2 SER A 85 ILE A 89 -1 O SER A 85 N VAL A 82
SHEET 1 AB 5 VAL A 96 PHE A 97 0
SHEET 2 AB 5 LEU A 232 LEU A 235 -1 O TYR A 234 N VAL A 96
SHEET 3 AB 5 ALA A 183 ASP A 186 -1 O ALA A 183 N LEU A 235
SHEET 4 AB 5 THR A 191 MET A 194 -1 O THR A 191 N ASP A 186
SHEET 5 AB 5 ILE A 138 THR A 139 -1 O ILE A 138 N CYS A 192
SHEET 1 AC 2 LYS A 99 ILE A 103 0
SHEET 2 AC 2 PHE A 221 LYS A 225 -1 O LYS A 222 N VAL A 102
SHEET 1 AD 2 ASN A 264 GLU A 266 0
SHEET 2 AD 2 ASN A 251 VAL A 261 -1 O LEU A 259 N GLU A 266
SHEET 1 AE 6 ASN A 272 GLU A 275 0
SHEET 2 AE 6 LYS A 353 PHE A 357 -1 O CYS A 354 N VAL A 274
SHEET 3 AE 6 TRP A 344 ASP A 348 -1 O TRP A 344 N PHE A 357
SHEET 4 AE 6 CYS A 363 THR A 374 -1 O PHE A 371 N PHE A 347
SHEET 5 AE 6 ASN A 251 VAL A 261 -1 O LEU A 252 N ALA A 372
SHEET 6 AE 6 ASN A 264 GLU A 266 -1 O ASN A 264 N VAL A 261
SHEET 1 AF 6 ASN A 272 GLU A 275 0
SHEET 2 AF 6 LYS A 353 PHE A 357 -1 O CYS A 354 N VAL A 274
SHEET 3 AF 6 TRP A 344 ASP A 348 -1 O TRP A 344 N PHE A 357
SHEET 4 AF 6 CYS A 363 THR A 374 -1 O PHE A 371 N PHE A 347
SHEET 5 AF 6 ASN A 251 VAL A 261 -1 O LEU A 252 N ALA A 372
SHEET 6 AF 6 VAL A 382 ASP A 383 1 O ASP A 383 N GLY A 253
SHEET 1 AG 2 ILE A 394 SER A 395 0
SHEET 2 AG 2 PHE B 169 VAL B 170 -1 O VAL B 170 N ILE A 394
SHEET 1 BA 2 GLU B 78 VAL B 82 0
SHEET 2 BA 2 SER B 85 ILE B 89 -1 O SER B 85 N VAL B 82
SHEET 1 BB 5 VAL B 96 PHE B 97 0
SHEET 2 BB 5 LEU B 232 LEU B 235 -1 O TYR B 234 N VAL B 96
SHEET 3 BB 5 ALA B 183 ASP B 186 -1 O ALA B 183 N LEU B 235
SHEET 4 BB 5 THR B 191 MET B 194 -1 O THR B 191 N ASP B 186
SHEET 5 BB 5 ILE B 138 THR B 139 -1 O ILE B 138 N CYS B 192
SHEET 1 BC 2 LYS B 99 ILE B 103 0
SHEET 2 BC 2 PHE B 221 LYS B 225 -1 O LYS B 222 N VAL B 102
SHEET 1 BD 2 ASN B 264 GLU B 266 0
SHEET 2 BD 2 ASN B 251 VAL B 261 -1 O LEU B 259 N GLU B 266
SHEET 1 BE 6 ASN B 272 GLU B 275 0
SHEET 2 BE 6 LYS B 353 PHE B 357 -1 O CYS B 354 N VAL B 274
SHEET 3 BE 6 TRP B 344 ASP B 348 -1 O TRP B 344 N PHE B 357
SHEET 4 BE 6 CYS B 363 THR B 374 -1 O PHE B 371 N PHE B 347
SHEET 5 BE 6 ASN B 251 VAL B 261 -1 O LEU B 252 N ALA B 372
SHEET 6 BE 6 ASN B 264 GLU B 266 -1 O ASN B 264 N VAL B 261
SHEET 1 BF 6 ASN B 272 GLU B 275 0
SHEET 2 BF 6 LYS B 353 PHE B 357 -1 O CYS B 354 N VAL B 274
SHEET 3 BF 6 TRP B 344 ASP B 348 -1 O TRP B 344 N PHE B 357
SHEET 4 BF 6 CYS B 363 THR B 374 -1 O PHE B 371 N PHE B 347
SHEET 5 BF 6 ASN B 251 VAL B 261 -1 O LEU B 252 N ALA B 372
SHEET 6 BF 6 VAL B 382 ASP B 383 1 O ASP B 383 N GLY B 253
SSBOND 1 CYS A 94 CYS A 247 1555 1555 2.05
SSBOND 2 CYS A 162 CYS A 192 1555 1555 2.03
SSBOND 3 CYS A 208 CYS A 220 1555 1555 2.04
SSBOND 4 CYS A 265 CYS A 363 1555 1555 2.01
SSBOND 5 CYS A 282 CYS A 354 1555 1555 2.05
SSBOND 6 CYS B 94 CYS B 247 1555 1555 2.02
SSBOND 7 CYS B 162 CYS B 192 1555 1555 2.06
SSBOND 8 CYS B 208 CYS B 220 1555 1555 2.03
SSBOND 9 CYS B 265 CYS B 363 1555 1555 2.02
SSBOND 10 CYS B 282 CYS B 354 1555 1555 2.06
CISPEP 1 SER A 136 PRO A 137 0 -5.90
CISPEP 2 SER B 136 PRO B 137 0 -6.90
CRYST1 90.320 105.700 104.750 90.00 98.04 90.00 C 1 2 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 0.011072 0.000000 0.001564 0.00000
SCALE2 0.000000 0.009461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009641 0.00000
MTRIX1 1 -0.953060 0.046090 -0.299260 51.59998 1
MTRIX2 1 -0.041280 -0.998900 -0.022390 60.96933 1
MTRIX3 1 -0.299960 -0.008990 0.953910 -44.41268 1
(ATOM LINES ARE NOT SHOWN.)
END
