HEADER CELL INVASION/INHIBITOR 07-JUL-11 3SRJ
TITLE PFAMA1 IN COMPLEX WITH INVASION-INHIBITORY PEPTIDE R1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APICAL MEMBRANE ANTIGEN 1, AMA1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: AMA1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: R1 PEPTIDE;
COMPND 9 CHAIN: C, D, E, F;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: 3D7;
SOURCE 5 GENE: AMA1, PF11_0344;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES
KEYWDS AMA1, PLASMODIUM FALCIPARUM, INHIBITORY PEPTIDE, MALARIA, CELL
KEYWDS 2 INVASION, CELL INVASION-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.VULLIEZ-LE NORMAND,F.A.SAUL,G.A.BENTLEY
REVDAT 2 13-SEP-23 3SRJ 1 SEQADV
REVDAT 1 11-JUL-12 3SRJ 0
JRNL AUTH B.VULLIEZ-LE NORMAND,M.L.TONKIN,M.H.LAMARQUE,S.LANGER,
JRNL AUTH 2 S.HOOS,M.ROQUES,F.A.SAUL,B.W.FABER,G.A.BENTLEY,
JRNL AUTH 3 M.J.BOULANGER,M.LEBRUN
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS INTO THE MALARIA PARASITE
JRNL TITL 2 MOVING JUNCTION COMPLEX.
JRNL REF PLOS PATHOG. V. 8 02755 2012
JRNL REFN ISSN 1553-7366
JRNL PMID 22737069
JRNL DOI 10.1371/JOURNAL.PPAT.1002755
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 42736
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1297
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.75
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2291
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2162
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2222
REMARK 3 BIN R VALUE (WORKING SET) : 0.2153
REMARK 3 BIN FREE R VALUE : 0.2486
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 69
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 : 5155
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.96170
REMARK 3 B22 (A**2) : -8.99930
REMARK 3 B33 (A**2) : 4.03760
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.228
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.198
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 148 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 761 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5342 ; 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 : 669 ; 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 : 6288 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.37
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.82
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 3SRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97911
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42798
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 40.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 1Z40
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.1M TRIS/HCL, 0.1M
REMARK 280 SODIUM ACETATE, 10% ISOPROPANOL, PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 19.16000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.82000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.82000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.16000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.16000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F
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 95
REMARK 465 PHE A 96
REMARK 465 ILE A 97
REMARK 465 GLU A 98
REMARK 465 ILE A 99
REMARK 465 VAL A 100
REMARK 465 GLU A 101
REMARK 465 ARG A 102
REMARK 465 SER A 103
REMARK 465 ASN A 104
REMARK 465 TYR A 105
REMARK 465 ASN A 264
REMARK 465 LYS A 265
REMARK 465 ASP A 266
REMARK 465 GLU A 267
REMARK 465 SER A 268
REMARK 465 LYS A 269
REMARK 465 ARG A 270
REMARK 465 TYR A 353
REMARK 465 GLU A 354
REMARK 465 GLN A 355
REMARK 465 HIS A 356
REMARK 465 LEU A 357
REMARK 465 THR A 358
REMARK 465 ASP A 359
REMARK 465 TYR A 360
REMARK 465 GLU A 361
REMARK 465 LYS A 362
REMARK 465 ILE A 363
REMARK 465 LYS A 364
REMARK 465 GLU A 365
REMARK 465 GLY A 366
REMARK 465 PHE A 367
REMARK 465 LYS A 368
REMARK 465 ASN A 369
REMARK 465 LYS A 370
REMARK 465 ASN A 371
REMARK 465 ALA A 372
REMARK 465 ASP A 373
REMARK 465 MET A 374
REMARK 465 ILE A 375
REMARK 465 LYS A 376
REMARK 465 SER A 377
REMARK 465 ALA A 378
REMARK 465 PHE A 379
REMARK 465 LEU A 380
REMARK 465 PRO A 381
REMARK 465 THR A 382
REMARK 465 GLY A 383
REMARK 465 ALA A 384
REMARK 465 PHE A 385
REMARK 465 LYS A 386
REMARK 465 ALA A 387
REMARK 465 ARG A 446
REMARK 465 ALA A 447
REMARK 465 ALA A 448
REMARK 465 ALA A 449
REMARK 465 ALA A 450
REMARK 465 ALA A 451
REMARK 465 SER A 452
REMARK 465 PHE A 453
REMARK 465 LEU A 454
REMARK 465 GLU A 455
REMARK 465 GLN A 456
REMARK 465 LYS A 457
REMARK 465 LEU A 458
REMARK 465 ILE A 459
REMARK 465 SER A 460
REMARK 465 GLU A 461
REMARK 465 GLU A 462
REMARK 465 ASP A 463
REMARK 465 LEU A 464
REMARK 465 ASN A 465
REMARK 465 SER A 466
REMARK 465 ALA A 467
REMARK 465 VAL A 468
REMARK 465 ASP A 469
REMARK 465 HIS A 470
REMARK 465 HIS A 471
REMARK 465 HIS A 472
REMARK 465 HIS A 473
REMARK 465 HIS A 474
REMARK 465 HIS A 475
REMARK 465 GLU B 95
REMARK 465 PHE B 96
REMARK 465 ILE B 97
REMARK 465 GLU B 98
REMARK 465 ILE B 99
REMARK 465 VAL B 100
REMARK 465 GLU B 101
REMARK 465 ARG B 102
REMARK 465 SER B 103
REMARK 465 ASN B 104
REMARK 465 TYR B 105
REMARK 465 ASN B 264
REMARK 465 LYS B 265
REMARK 465 ASP B 266
REMARK 465 GLU B 267
REMARK 465 SER B 268
REMARK 465 LYS B 269
REMARK 465 ARG B 270
REMARK 465 ASN B 271
REMARK 465 TYR B 353
REMARK 465 GLU B 354
REMARK 465 GLN B 355
REMARK 465 HIS B 356
REMARK 465 LEU B 357
REMARK 465 THR B 358
REMARK 465 ASP B 359
REMARK 465 TYR B 360
REMARK 465 GLU B 361
REMARK 465 LYS B 362
REMARK 465 ILE B 363
REMARK 465 LYS B 364
REMARK 465 GLU B 365
REMARK 465 GLY B 366
REMARK 465 PHE B 367
REMARK 465 LYS B 368
REMARK 465 ASN B 369
REMARK 465 LYS B 370
REMARK 465 ASN B 371
REMARK 465 ALA B 372
REMARK 465 ASP B 373
REMARK 465 MET B 374
REMARK 465 ILE B 375
REMARK 465 LYS B 376
REMARK 465 SER B 377
REMARK 465 ALA B 378
REMARK 465 PHE B 379
REMARK 465 LEU B 380
REMARK 465 PRO B 381
REMARK 465 THR B 382
REMARK 465 GLY B 383
REMARK 465 ALA B 384
REMARK 465 PHE B 385
REMARK 465 LYS B 386
REMARK 465 ALA B 387
REMARK 465 ARG B 446
REMARK 465 ALA B 447
REMARK 465 ALA B 448
REMARK 465 ALA B 449
REMARK 465 ALA B 450
REMARK 465 ALA B 451
REMARK 465 SER B 452
REMARK 465 PHE B 453
REMARK 465 LEU B 454
REMARK 465 GLU B 455
REMARK 465 GLN B 456
REMARK 465 LYS B 457
REMARK 465 LEU B 458
REMARK 465 ILE B 459
REMARK 465 SER B 460
REMARK 465 GLU B 461
REMARK 465 GLU B 462
REMARK 465 ASP B 463
REMARK 465 LEU B 464
REMARK 465 ASN B 465
REMARK 465 SER B 466
REMARK 465 ALA B 467
REMARK 465 VAL B 468
REMARK 465 ASP B 469
REMARK 465 HIS B 470
REMARK 465 HIS B 471
REMARK 465 HIS B 472
REMARK 465 HIS B 473
REMARK 465 HIS B 474
REMARK 465 HIS B 475
REMARK 465 LEU C 19
REMARK 465 LYS C 20
REMARK 465 VAL D 1
REMARK 465 PHE D 2
REMARK 465 ALA D 3
REMARK 465 LYS D 11
REMARK 465 PHE D 12
REMARK 465 GLY D 13
REMARK 465 SER D 14
REMARK 465 ARG D 15
REMARK 465 MET D 16
REMARK 465 HIS D 17
REMARK 465 ILE D 18
REMARK 465 LEU D 19
REMARK 465 LYS D 20
REMARK 465 ILE E 18
REMARK 465 LEU E 19
REMARK 465 LYS E 20
REMARK 465 LYS F 11
REMARK 465 PHE F 12
REMARK 465 GLY F 13
REMARK 465 SER F 14
REMARK 465 ARG F 15
REMARK 465 MET F 16
REMARK 465 HIS F 17
REMARK 465 ILE F 18
REMARK 465 LEU F 19
REMARK 465 LYS F 20
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 TYR A 262 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 351 CG CD CE NZ
REMARK 470 GLN A 352 CG CD OE1 NE2
REMARK 470 LYS B 209 CG CD CE NZ
REMARK 470 ARG B 261 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 351 CG CD CE NZ
REMARK 470 GLN B 352 CG CD OE1 NE2
REMARK 470 ASN B 439 CG OD1 ND2
REMARK 470 ILE C 18 CG1 CG2 CD1
REMARK 470 VAL E 1 CG1 CG2
REMARK 470 HIS E 17 CG ND1 CD2 CE1 NE2
REMARK 470 PHE F 2 CG CD1 CD2 CE1 CE2 CZ
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 131 45.65 -144.35
REMARK 500 SER A 146 13.74 -148.95
REMARK 500 ASP A 227 11.32 58.88
REMARK 500 ASN A 258 35.70 -144.44
REMARK 500 ARG A 261 -80.56 -50.99
REMARK 500 ASN A 297 31.79 -94.67
REMARK 500 ARG A 304 -69.65 -138.51
REMARK 500 ARG A 389 -72.36 -77.17
REMARK 500 LEU B 131 50.41 -146.20
REMARK 500 ASP B 227 18.41 52.32
REMARK 500 ASN B 228 19.48 55.88
REMARK 500 ARG B 304 -67.26 -147.16
REMARK 500 MET C 16 -35.86 -35.60
REMARK 500 MET C 16 -35.46 -35.60
REMARK 500 HIS C 17 30.55 -89.44
REMARK 500 PHE F 2 -10.75 63.42
REMARK 500 ALA F 3 73.74 -158.95
REMARK 500 GLU F 4 -131.88 59.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF R1 PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF R1 PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF R1 PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF R1 PEPTIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z40 RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM AMA1
REMARK 900 RELATED ID: 3SRI RELATED DB: PDB
DBREF 3SRJ A 97 442 UNP Q7KQK5 Q7KQK5_PLAF7 97 442
DBREF 3SRJ B 97 442 UNP Q7KQK5 Q7KQK5_PLAF7 97 442
DBREF 3SRJ C 1 20 PDB 3SRJ 3SRJ 1 20
DBREF 3SRJ D 1 20 PDB 3SRJ 3SRJ 1 20
DBREF 3SRJ E 1 20 PDB 3SRJ 3SRJ 1 20
DBREF 3SRJ F 1 20 PDB 3SRJ 3SRJ 1 20
SEQADV 3SRJ GLU A 95 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ PHE A 96 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LYS A 162 UNP Q7KQK5 ASN 162 ENGINEERED MUTATION
SEQADV 3SRJ VAL A 288 UNP Q7KQK5 THR 288 ENGINEERED MUTATION
SEQADV 3SRJ ASP A 373 UNP Q7KQK5 SER 373 ENGINEERED MUTATION
SEQADV 3SRJ ASP A 422 UNP Q7KQK5 ASN 422 ENGINEERED MUTATION
SEQADV 3SRJ LYS A 423 UNP Q7KQK5 SER 423 ENGINEERED MUTATION
SEQADV 3SRJ SER A 443 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ VAL A 444 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ PRO A 445 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ARG A 446 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA A 447 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA A 448 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA A 449 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA A 450 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA A 451 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ SER A 452 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ PHE A 453 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LEU A 454 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU A 455 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLN A 456 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LYS A 457 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LEU A 458 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ILE A 459 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ SER A 460 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU A 461 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU A 462 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ASP A 463 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LEU A 464 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ASN A 465 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ SER A 466 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA A 467 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ VAL A 468 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ASP A 469 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS A 470 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS A 471 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS A 472 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS A 473 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS A 474 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS A 475 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU B 95 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ PHE B 96 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LYS B 162 UNP Q7KQK5 ASN 162 ENGINEERED MUTATION
SEQADV 3SRJ VAL B 288 UNP Q7KQK5 THR 288 ENGINEERED MUTATION
SEQADV 3SRJ ASP B 373 UNP Q7KQK5 SER 373 ENGINEERED MUTATION
SEQADV 3SRJ ASP B 422 UNP Q7KQK5 ASN 422 ENGINEERED MUTATION
SEQADV 3SRJ LYS B 423 UNP Q7KQK5 SER 423 ENGINEERED MUTATION
SEQADV 3SRJ SER B 443 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ VAL B 444 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ PRO B 445 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ARG B 446 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA B 447 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA B 448 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA B 449 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA B 450 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA B 451 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ SER B 452 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ PHE B 453 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LEU B 454 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU B 455 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLN B 456 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LYS B 457 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LEU B 458 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ILE B 459 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ SER B 460 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU B 461 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ GLU B 462 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ASP B 463 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ LEU B 464 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ASN B 465 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ SER B 466 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ALA B 467 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ VAL B 468 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ ASP B 469 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS B 470 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS B 471 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS B 472 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS B 473 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS B 474 UNP Q7KQK5 EXPRESSION TAG
SEQADV 3SRJ HIS B 475 UNP Q7KQK5 EXPRESSION TAG
SEQRES 1 A 381 GLU PHE ILE GLU ILE VAL GLU ARG SER ASN TYR MET GLY
SEQRES 2 A 381 ASN PRO TRP THR GLU TYR MET ALA LYS TYR ASP ILE GLU
SEQRES 3 A 381 GLU VAL HIS GLY SER GLY ILE ARG VAL ASP LEU GLY GLU
SEQRES 4 A 381 ASP ALA GLU VAL ALA GLY THR GLN TYR ARG LEU PRO SER
SEQRES 5 A 381 GLY LYS CYS PRO VAL PHE GLY LYS GLY ILE ILE ILE GLU
SEQRES 6 A 381 ASN SER LYS THR THR PHE LEU THR PRO VAL ALA THR GLY
SEQRES 7 A 381 ASN GLN TYR LEU LYS ASP GLY GLY PHE ALA PHE PRO PRO
SEQRES 8 A 381 THR GLU PRO LEU MET SER PRO MET THR LEU ASP GLU MET
SEQRES 9 A 381 ARG HIS PHE TYR LYS ASP ASN LYS TYR VAL LYS ASN LEU
SEQRES 10 A 381 ASP GLU LEU THR LEU CYS SER ARG HIS ALA GLY ASN MET
SEQRES 11 A 381 ILE PRO ASP ASN ASP LYS ASN SER ASN TYR LYS TYR PRO
SEQRES 12 A 381 ALA VAL TYR ASP ASP LYS ASP LYS LYS CYS HIS ILE LEU
SEQRES 13 A 381 TYR ILE ALA ALA GLN GLU ASN ASN GLY PRO ARG TYR CYS
SEQRES 14 A 381 ASN LYS ASP GLU SER LYS ARG ASN SER MET PHE CYS PHE
SEQRES 15 A 381 ARG PRO ALA LYS ASP ILE SER PHE GLN ASN TYR VAL TYR
SEQRES 16 A 381 LEU SER LYS ASN VAL VAL ASP ASN TRP GLU LYS VAL CYS
SEQRES 17 A 381 PRO ARG LYS ASN LEU GLN ASN ALA LYS PHE GLY LEU TRP
SEQRES 18 A 381 VAL ASP GLY ASN CYS GLU ASP ILE PRO HIS VAL ASN GLU
SEQRES 19 A 381 PHE PRO ALA ILE ASP LEU PHE GLU CYS ASN LYS LEU VAL
SEQRES 20 A 381 PHE GLU LEU SER ALA SER ASP GLN PRO LYS GLN TYR GLU
SEQRES 21 A 381 GLN HIS LEU THR ASP TYR GLU LYS ILE LYS GLU GLY PHE
SEQRES 22 A 381 LYS ASN LYS ASN ALA ASP MET ILE LYS SER ALA PHE LEU
SEQRES 23 A 381 PRO THR GLY ALA PHE LYS ALA ASP ARG TYR LYS SER HIS
SEQRES 24 A 381 GLY LYS GLY TYR ASN TRP GLY ASN TYR ASN THR GLU THR
SEQRES 25 A 381 GLN LYS CYS GLU ILE PHE ASN VAL LYS PRO THR CYS LEU
SEQRES 26 A 381 ILE ASN ASP LYS SER TYR ILE ALA THR THR ALA LEU SER
SEQRES 27 A 381 HIS PRO ILE GLU VAL GLU ASN ASN PHE PRO SER VAL PRO
SEQRES 28 A 381 ARG ALA ALA ALA ALA ALA SER PHE LEU GLU GLN LYS LEU
SEQRES 29 A 381 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 30 A 381 HIS HIS HIS HIS
SEQRES 1 B 381 GLU PHE ILE GLU ILE VAL GLU ARG SER ASN TYR MET GLY
SEQRES 2 B 381 ASN PRO TRP THR GLU TYR MET ALA LYS TYR ASP ILE GLU
SEQRES 3 B 381 GLU VAL HIS GLY SER GLY ILE ARG VAL ASP LEU GLY GLU
SEQRES 4 B 381 ASP ALA GLU VAL ALA GLY THR GLN TYR ARG LEU PRO SER
SEQRES 5 B 381 GLY LYS CYS PRO VAL PHE GLY LYS GLY ILE ILE ILE GLU
SEQRES 6 B 381 ASN SER LYS THR THR PHE LEU THR PRO VAL ALA THR GLY
SEQRES 7 B 381 ASN GLN TYR LEU LYS ASP GLY GLY PHE ALA PHE PRO PRO
SEQRES 8 B 381 THR GLU PRO LEU MET SER PRO MET THR LEU ASP GLU MET
SEQRES 9 B 381 ARG HIS PHE TYR LYS ASP ASN LYS TYR VAL LYS ASN LEU
SEQRES 10 B 381 ASP GLU LEU THR LEU CYS SER ARG HIS ALA GLY ASN MET
SEQRES 11 B 381 ILE PRO ASP ASN ASP LYS ASN SER ASN TYR LYS TYR PRO
SEQRES 12 B 381 ALA VAL TYR ASP ASP LYS ASP LYS LYS CYS HIS ILE LEU
SEQRES 13 B 381 TYR ILE ALA ALA GLN GLU ASN ASN GLY PRO ARG TYR CYS
SEQRES 14 B 381 ASN LYS ASP GLU SER LYS ARG ASN SER MET PHE CYS PHE
SEQRES 15 B 381 ARG PRO ALA LYS ASP ILE SER PHE GLN ASN TYR VAL TYR
SEQRES 16 B 381 LEU SER LYS ASN VAL VAL ASP ASN TRP GLU LYS VAL CYS
SEQRES 17 B 381 PRO ARG LYS ASN LEU GLN ASN ALA LYS PHE GLY LEU TRP
SEQRES 18 B 381 VAL ASP GLY ASN CYS GLU ASP ILE PRO HIS VAL ASN GLU
SEQRES 19 B 381 PHE PRO ALA ILE ASP LEU PHE GLU CYS ASN LYS LEU VAL
SEQRES 20 B 381 PHE GLU LEU SER ALA SER ASP GLN PRO LYS GLN TYR GLU
SEQRES 21 B 381 GLN HIS LEU THR ASP TYR GLU LYS ILE LYS GLU GLY PHE
SEQRES 22 B 381 LYS ASN LYS ASN ALA ASP MET ILE LYS SER ALA PHE LEU
SEQRES 23 B 381 PRO THR GLY ALA PHE LYS ALA ASP ARG TYR LYS SER HIS
SEQRES 24 B 381 GLY LYS GLY TYR ASN TRP GLY ASN TYR ASN THR GLU THR
SEQRES 25 B 381 GLN LYS CYS GLU ILE PHE ASN VAL LYS PRO THR CYS LEU
SEQRES 26 B 381 ILE ASN ASP LYS SER TYR ILE ALA THR THR ALA LEU SER
SEQRES 27 B 381 HIS PRO ILE GLU VAL GLU ASN ASN PHE PRO SER VAL PRO
SEQRES 28 B 381 ARG ALA ALA ALA ALA ALA SER PHE LEU GLU GLN LYS LEU
SEQRES 29 B 381 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 30 B 381 HIS HIS HIS HIS
SEQRES 1 C 20 VAL PHE ALA GLU PHE LEU PRO LEU PHE SER LYS PHE GLY
SEQRES 2 C 20 SER ARG MET HIS ILE LEU LYS
SEQRES 1 D 20 VAL PHE ALA GLU PHE LEU PRO LEU PHE SER LYS PHE GLY
SEQRES 2 D 20 SER ARG MET HIS ILE LEU LYS
SEQRES 1 E 20 VAL PHE ALA GLU PHE LEU PRO LEU PHE SER LYS PHE GLY
SEQRES 2 E 20 SER ARG MET HIS ILE LEU LYS
SEQRES 1 F 20 VAL PHE ALA GLU PHE LEU PRO LEU PHE SER LYS PHE GLY
SEQRES 2 F 20 SER ARG MET HIS ILE LEU LYS
FORMUL 7 HOH *450(H2 O)
HELIX 1 1 TRP A 110 ALA A 115 1 6
HELIX 2 2 ASP A 118 HIS A 123 1 6
HELIX 3 3 THR A 171 TYR A 175 5 5
HELIX 4 4 LEU A 195 TYR A 202 1 8
HELIX 5 5 ASP A 212 GLY A 222 1 11
HELIX 6 6 ASP A 281 GLN A 285 5 5
HELIX 7 7 ASN A 297 CYS A 302 1 6
HELIX 8 8 ASP A 333 SER A 345 1 13
HELIX 9 9 MET B 114 TYR B 117 5 4
HELIX 10 10 ASP B 118 HIS B 123 1 6
HELIX 11 11 THR B 171 TYR B 175 5 5
HELIX 12 12 LEU B 195 TYR B 202 1 8
HELIX 13 13 ASN B 205 ASN B 210 1 6
HELIX 14 14 ASP B 212 ASN B 223 1 12
HELIX 15 15 ILE B 282 GLN B 285 5 4
HELIX 16 16 ASN B 297 CYS B 302 1 6
HELIX 17 17 ASP B 333 SER B 345 1 13
SHEET 1 A 2 GLU A 133 VAL A 137 0
SHEET 2 A 2 THR A 140 LEU A 144 -1 O TYR A 142 N ALA A 135
SHEET 1 B 5 VAL A 151 PHE A 152 0
SHEET 2 B 5 TYR A 287 LEU A 290 -1 O TYR A 289 N VAL A 151
SHEET 3 B 5 ALA A 238 ASP A 241 -1 N ALA A 238 O LEU A 290
SHEET 4 B 5 LYS A 246 ILE A 249 -1 O LYS A 246 N ASP A 241
SHEET 5 B 5 MET A 193 THR A 194 -1 N MET A 193 O CYS A 247
SHEET 1 C 2 GLY A 155 ILE A 158 0
SHEET 2 C 2 PHE A 276 ALA A 279 -1 O ARG A 277 N ILE A 157
SHEET 1 D 4 THR A 186 GLU A 187 0
SHEET 2 D 4 LEU D 6 PHE D 9 1 O LEU D 6 N GLU A 187
SHEET 3 D 4 PHE C 12 SER C 14 1 N PHE C 12 O PHE D 9
SHEET 4 D 4 MET A 224 PRO A 226 -1 N ILE A 225 O GLY C 13
SHEET 1 E 6 ASN A 319 ASP A 322 0
SHEET 2 E 6 ASN A 306 VAL A 316 -1 N VAL A 316 O ASN A 319
SHEET 3 E 6 CYS A 418 THR A 429 -1 O ILE A 420 N LYS A 311
SHEET 4 E 6 TRP A 399 ASN A 403 -1 N TYR A 402 O ILE A 426
SHEET 5 E 6 LYS A 408 PHE A 412 -1 O LYS A 408 N ASN A 403
SHEET 6 E 6 ASN A 327 PRO A 330 -1 N PHE A 329 O CYS A 409
SHEET 1 F 3 ASN A 319 ASP A 322 0
SHEET 2 F 3 ASN A 306 VAL A 316 -1 N VAL A 316 O ASN A 319
SHEET 3 F 3 VAL A 437 GLU A 438 1 O GLU A 438 N ASN A 306
SHEET 1 G 2 GLU B 133 VAL B 137 0
SHEET 2 G 2 THR B 140 LEU B 144 -1 O TYR B 142 N ALA B 135
SHEET 1 H 5 VAL B 151 PHE B 152 0
SHEET 2 H 5 TYR B 287 LEU B 290 -1 O TYR B 289 N VAL B 151
SHEET 3 H 5 ALA B 238 ASP B 241 -1 N ALA B 238 O LEU B 290
SHEET 4 H 5 LYS B 246 ILE B 249 -1 O HIS B 248 N VAL B 239
SHEET 5 H 5 MET B 193 THR B 194 -1 N MET B 193 O CYS B 247
SHEET 1 I 2 LYS B 154 ILE B 158 0
SHEET 2 I 2 PHE B 276 LYS B 280 -1 O ARG B 277 N ILE B 157
SHEET 1 J 4 THR B 186 GLU B 187 0
SHEET 2 J 4 LEU F 6 PHE F 9 1 O LEU F 6 N GLU B 187
SHEET 3 J 4 PHE E 12 SER E 14 1 N PHE E 12 O PHE F 9
SHEET 4 J 4 MET B 224 PRO B 226 -1 N ILE B 225 O GLY E 13
SHEET 1 K 6 ASN B 319 ASP B 322 0
SHEET 2 K 6 ASN B 306 VAL B 316 -1 N VAL B 316 O ASN B 319
SHEET 3 K 6 CYS B 418 THR B 429 -1 O ILE B 420 N LYS B 311
SHEET 4 K 6 TRP B 399 ASN B 403 -1 N TYR B 402 O ILE B 426
SHEET 5 K 6 LYS B 408 PHE B 412 -1 O LYS B 408 N ASN B 403
SHEET 6 K 6 ASN B 327 PRO B 330 -1 N PHE B 329 O CYS B 409
SHEET 1 L 3 ASN B 319 ASP B 322 0
SHEET 2 L 3 ASN B 306 VAL B 316 -1 N VAL B 316 O ASN B 319
SHEET 3 L 3 VAL B 437 GLU B 438 1 O GLU B 438 N ASN B 306
SSBOND 1 CYS A 149 CYS A 302 1555 1555 2.05
SSBOND 2 CYS A 217 CYS A 247 1555 1555 2.06
SSBOND 3 CYS A 263 CYS A 275 1555 1555 2.03
SSBOND 4 CYS A 320 CYS A 418 1555 1555 2.02
SSBOND 5 CYS A 337 CYS A 409 1555 1555 2.04
SSBOND 6 CYS B 149 CYS B 302 1555 1555 2.04
SSBOND 7 CYS B 217 CYS B 247 1555 1555 2.05
SSBOND 8 CYS B 263 CYS B 275 1555 1555 2.03
SSBOND 9 CYS B 320 CYS B 418 1555 1555 2.01
SSBOND 10 CYS B 337 CYS B 409 1555 1555 2.05
CISPEP 1 GLU A 187 PRO A 188 0 1.35
CISPEP 2 SER A 191 PRO A 192 0 -7.68
CISPEP 3 GLU B 187 PRO B 188 0 -0.99
CISPEP 4 SER B 191 PRO B 192 0 -7.23
CISPEP 5 ALA F 3 GLU F 4 0 8.78
SITE 1 AC1 40 ASP A 134 VAL A 137 THR A 140 GLN A 141
SITE 2 AC1 40 TYR A 142 ALA A 170 TYR A 175 PHE A 183
SITE 3 AC1 40 PHE A 201 GLY A 222 ASN A 223 MET A 224
SITE 4 AC1 40 ILE A 225 ASP A 227 ASN A 228 SER A 232
SITE 5 AC1 40 TYR A 234 LYS A 235 TYR A 236 TYR A 251
SITE 6 AC1 40 ALA A 254 MET A 273 GLY B 139 HOH C 33
SITE 7 AC1 40 HOH C 181 HOH C 184 HOH C 219 HOH C 248
SITE 8 AC1 40 HOH C 277 HOH C 300 HOH C 365 HOH C 438
SITE 9 AC1 40 HOH C 440 HOH C 666 LEU D 6 PRO D 7
SITE 10 AC1 40 LEU D 8 PHE D 9 SER D 10 VAL F 1
SITE 1 AC2 18 THR A 171 PRO A 184 PRO A 185 THR A 186
SITE 2 AC2 18 GLU A 187 MET A 190 ASN A 228 LYS A 230
SITE 3 AC2 18 PHE C 9 SER C 10 LYS C 11 PHE C 12
SITE 4 AC2 18 GLY C 13 SER C 14 HIS C 17 HOH D 287
SITE 5 AC2 18 VAL F 1 PHE F 2
SITE 1 AC3 31 ASN A 173 GLN A 174 ASP B 134 GLN B 141
SITE 2 AC3 31 TYR B 142 ALA B 170 TYR B 175 LEU B 176
SITE 3 AC3 31 GLY B 222 ASN B 223 MET B 224 ILE B 225
SITE 4 AC3 31 PRO B 226 ASP B 227 ASN B 228 SER B 232
SITE 5 AC3 31 TYR B 234 LYS B 235 TYR B 236 TYR B 251
SITE 6 AC3 31 ALA B 254 TYR B 262 MET B 273 HOH B 626
SITE 7 AC3 31 HOH E 86 HOH E 192 HOH E 364 LEU F 6
SITE 8 AC3 31 PRO F 7 LEU F 8 PHE F 9
SITE 1 AC4 18 THR A 171 GLY A 172 ASN A 173 PRO B 184
SITE 2 AC4 18 PRO B 185 THR B 186 GLU B 187 ASN B 228
SITE 3 AC4 18 LYS B 230 SER C 10 GLU D 4 PHE E 9
SITE 4 AC4 18 SER E 10 LYS E 11 PHE E 12 GLY E 13
SITE 5 AC4 18 SER E 14 HOH F 341
CRYST1 38.320 144.320 145.640 90.00 90.00 90.00 P 21 21 21 16
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 0.026096 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006866 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
