HEADER PLASMA PROTEIN 06-JUL-98 1BKE
TITLE HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-
TITLE 2 IODOBENZOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: PLASMA;
SOURCE 6 CELLULAR_LOCATION: PLASMA;
SOURCE 7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS PLASMA PROTEIN, METAL-BINDING, LIPID-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CURRY,H.MANDELKOW,P.BRICK,N.FRANKS
REVDAT 3 02-AUG-23 1BKE 1 REMARK
REVDAT 2 24-FEB-09 1BKE 1 VERSN
REVDAT 1 13-JAN-99 1BKE 0
JRNL AUTH S.CURRY,H.MANDELKOW,P.BRICK,N.FRANKS
JRNL TITL CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH
JRNL TITL 2 FATTY ACID REVEALS AN ASYMMETRIC DISTRIBUTION OF BINDING
JRNL TITL 3 SITES.
JRNL REF NAT.STRUCT.BIOL. V. 5 827 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9731778
JRNL DOI 10.1038/1869
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 11607
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 SET) : 0.177
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.690
REMARK 3 FREE R VALUE TEST SET COUNT : 559
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1393
REMARK 3 BIN R VALUE (WORKING SET) : 0.3032
REMARK 3 BIN FREE R VALUE : 0.3527
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 55
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4445
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 93
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.590
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
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 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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION APPLIED
REMARK 4
REMARK 4 1BKE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171858.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-97
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-21
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : PINHOLE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, CCP4
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11608
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.22200
REMARK 200 R SYM FOR SHELL (I) : 0.22200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1BJ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 93.82500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.43500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 93.82500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.43500
REMARK 290 SMTRY3 4 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 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 LYS A 4 CG CD CE NZ
REMARK 470 LYS A 41 CE NZ
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 ASP A 108 CG OD1 OD2
REMARK 470 ASN A 109 CG OD1 ND2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 148 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 ARG A 197 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 204 CG CD OE1 NE2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 240 CD CE NZ
REMARK 470 GLU A 244 CD OE1 OE2
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 GLU A 277 CG CD OE1 OE2
REMARK 470 GLU A 280 CG CD OE1 OE2
REMARK 470 GLU A 292 CD OE1 OE2
REMARK 470 ASP A 301 CG OD1 OD2
REMARK 470 LYS A 313 CG CD CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 HIS A 367 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 368 CG CD OE1 OE2
REMARK 470 LYS A 372 CG CD CE NZ
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 LYS A 402 CD CE NZ
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 LYS A 444 CD CE NZ
REMARK 470 LYS A 466 CE NZ
REMARK 470 LEU A 481 CG CD1 CD2
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 GLU A 505 CG CD OE1 OE2
REMARK 470 LYS A 519 CG CD CE NZ
REMARK 470 LYS A 524 CE NZ
REMARK 470 LYS A 536 CD CE NZ
REMARK 470 LYS A 541 CG CD CE NZ
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 ASP A 549 CG OD1 OD2
REMARK 470 GLU A 556 CG CD OE1 OE2
REMARK 470 LYS A 557 CD CE NZ
REMARK 470 ASP A 562 CG OD1 OD2
REMARK 470 LYS A 564 CG CD CE NZ
REMARK 470 PHE A 568 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 570 CG CD OE1 OE2
REMARK 470 LYS A 573 CD CE NZ
REMARK 470 GLN A 580 CD OE1 NE2
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 GLU A 60 137.33 -35.70
REMARK 500 ASN A 61 -19.21 71.12
REMARK 500 VAL A 77 105.60 -59.88
REMARK 500 GLU A 86 -36.27 -38.74
REMARK 500 GLU A 95 -68.43 12.24
REMARK 500 HIS A 105 21.36 -79.07
REMARK 500 ASN A 130 76.94 -153.70
REMARK 500 TYR A 150 105.62 -57.90
REMARK 500 CYS A 169 1.81 -61.83
REMARK 500 ASP A 173 59.85 -96.14
REMARK 500 CYS A 177 -64.40 -91.08
REMARK 500 PHE A 223 76.72 -110.82
REMARK 500 ILE A 271 -63.57 -126.67
REMARK 500 LYS A 276 -79.48 -46.84
REMARK 500 PRO A 299 -37.73 -28.41
REMARK 500 ALA A 300 -0.94 58.25
REMARK 500 PRO A 303 -106.11 -62.52
REMARK 500 GLU A 311 -98.21 -93.25
REMARK 500 SER A 312 100.08 -8.65
REMARK 500 ASP A 314 27.26 85.99
REMARK 500 ALA A 322 72.21 -161.78
REMARK 500 CYS A 360 -30.87 -135.22
REMARK 500 ALA A 364 -80.61 -40.68
REMARK 500 HIS A 367 -35.18 -39.75
REMARK 500 LYS A 389 -72.23 -46.22
REMARK 500 VAL A 469 -51.12 -133.69
REMARK 500 PRO A 499 144.35 -38.84
REMARK 500 ALA A 511 78.77 -60.38
REMARK 500 LYS A 557 -14.38 -45.66
REMARK 500 LYS A 560 11.25 -140.16
REMARK 500 GLU A 565 -38.46 92.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MYR A 1001
REMARK 610 MYR A 1002
REMARK 610 MYR A 1003
REMARK 610 MYR A 1004
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3I A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3I A 2002
DBREF 1BKE A 4 584 UNP P02768 ALBU_HUMAN 28 608
SEQRES 1 A 581 LYS SER GLU VAL ALA HIS ARG PHE LYS ASP LEU GLY GLU
SEQRES 2 A 581 GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA PHE ALA GLN
SEQRES 3 A 581 TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS VAL LYS LEU
SEQRES 4 A 581 VAL ASN GLU VAL THR GLU PHE ALA LYS THR CYS VAL ALA
SEQRES 5 A 581 ASP GLU SER ALA GLU ASN CYS ASP LYS SER LEU HIS THR
SEQRES 6 A 581 LEU PHE GLY ASP LYS LEU CYS THR VAL ALA THR LEU ARG
SEQRES 7 A 581 GLU THR TYR GLY GLU MET ALA ASP CYS CYS ALA LYS GLN
SEQRES 8 A 581 GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN HIS LYS ASP
SEQRES 9 A 581 ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG PRO GLU VAL
SEQRES 10 A 581 ASP VAL MET CYS THR ALA PHE HIS ASP ASN GLU GLU THR
SEQRES 11 A 581 PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA ARG ARG HIS
SEQRES 12 A 581 PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE PHE ALA LYS
SEQRES 13 A 581 ARG TYR LYS ALA ALA PHE THR GLU CYS CYS GLN ALA ALA
SEQRES 14 A 581 ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU ASP GLU LEU
SEQRES 15 A 581 ARG ASP GLU GLY LYS ALA SER SER ALA LYS GLN ARG LEU
SEQRES 16 A 581 LYS CYS ALA SER LEU GLN LYS PHE GLY GLU ARG ALA PHE
SEQRES 17 A 581 LYS ALA TRP ALA VAL ALA ARG LEU SER GLN ARG PHE PRO
SEQRES 18 A 581 LYS ALA GLU PHE ALA GLU VAL SER LYS LEU VAL THR ASP
SEQRES 19 A 581 LEU THR LYS VAL HIS THR GLU CYS CYS HIS GLY ASP LEU
SEQRES 20 A 581 LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA LYS TYR
SEQRES 21 A 581 ILE CYS GLU ASN GLN ASP SER ILE SER SER LYS LEU LYS
SEQRES 22 A 581 GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS SER HIS CYS
SEQRES 23 A 581 ILE ALA GLU VAL GLU ASN ASP GLU MET PRO ALA ASP LEU
SEQRES 24 A 581 PRO SER LEU ALA ALA ASP PHE VAL GLU SER LYS ASP VAL
SEQRES 25 A 581 CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL PHE LEU GLY
SEQRES 26 A 581 MET PHE LEU TYR GLU TYR ALA ARG ARG HIS PRO ASP TYR
SEQRES 27 A 581 SER VAL VAL LEU LEU LEU ARG LEU ALA LYS THR TYR GLU
SEQRES 28 A 581 THR THR LEU GLU LYS CYS CYS ALA ALA ALA ASP PRO HIS
SEQRES 29 A 581 GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE LYS PRO LEU
SEQRES 30 A 581 VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN ASN CYS GLU
SEQRES 31 A 581 LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE GLN ASN ALA
SEQRES 32 A 581 LEU LEU VAL ARG TYR THR LYS LYS VAL PRO GLN VAL SER
SEQRES 33 A 581 THR PRO THR LEU VAL GLU VAL SER ARG ASN LEU GLY LYS
SEQRES 34 A 581 VAL GLY SER LYS CYS CYS LYS HIS PRO GLU ALA LYS ARG
SEQRES 35 A 581 MET PRO CYS ALA GLU ASP TYR LEU SER VAL VAL LEU ASN
SEQRES 36 A 581 GLN LEU CYS VAL LEU HIS GLU LYS THR PRO VAL SER ASP
SEQRES 37 A 581 ARG VAL THR LYS CYS CYS THR GLU SER LEU VAL ASN ARG
SEQRES 38 A 581 ARG PRO CYS PHE SER ALA LEU GLU VAL ASP GLU THR TYR
SEQRES 39 A 581 VAL PRO LYS GLU PHE ASN ALA GLU THR PHE THR PHE HIS
SEQRES 40 A 581 ALA ASP ILE CYS THR LEU SER GLU LYS GLU ARG GLN ILE
SEQRES 41 A 581 LYS LYS GLN THR ALA LEU VAL GLU LEU VAL LYS HIS LYS
SEQRES 42 A 581 PRO LYS ALA THR LYS GLU GLN LEU LYS ALA VAL MET ASP
SEQRES 43 A 581 ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS LYS ALA ASP
SEQRES 44 A 581 ASP LYS GLU THR CYS PHE ALA GLU GLU GLY LYS LYS LEU
SEQRES 45 A 581 VAL ALA ALA SER GLN ALA ALA LEU GLY
HET MYR A1001 14
HET MYR A1002 13
HET MYR A1003 13
HET MYR A1004 13
HET MYR A1005 16
HET B3I A2001 24
HET B3I A2002 24
HETNAM MYR MYRISTIC ACID
HETNAM B3I 2,3,5-TRIIODOBENZOIC ACID
FORMUL 2 MYR 5(C14 H28 O2)
FORMUL 7 B3I 2(C7 H3 I3 O2)
HELIX 1 1 GLU A 6 LEU A 14 1 9
HELIX 2 2 GLU A 16 TYR A 30 1 15
HELIX 3 3 PHE A 36 ALA A 55 1 20
HELIX 4 4 LEU A 66 THR A 76 1 11
HELIX 5 5 ALA A 78 THR A 83 5 6
HELIX 6 6 GLY A 85 ALA A 92 5 8
HELIX 7 7 PRO A 96 GLN A 104 1 9
HELIX 8 8 VAL A 120 ASP A 129 1 10
HELIX 9 9 GLU A 131 ARG A 145 1 15
HELIX 10 10 ALA A 151 CYS A 168 1 18
HELIX 11 11 LYS A 174 LYS A 205 1 32
HELIX 12 12 GLY A 207 ARG A 222 1 16
HELIX 13 13 PHE A 228 HIS A 247 1 20
HELIX 14 14 LEU A 250 GLU A 266 1 17
HELIX 15 15 GLN A 268 SER A 270 5 3
HELIX 16 16 LYS A 276 GLU A 280 1 5
HELIX 17 17 LEU A 283 GLU A 292 1 10
HELIX 18 18 ALA A 306 PHE A 309 1 4
HELIX 19 19 VAL A 315 GLU A 321 1 7
HELIX 20 20 LYS A 323 ARG A 336 1 14
HELIX 21 21 VAL A 343 LYS A 359 1 17
HELIX 22 22 PRO A 366 GLU A 368 5 3
HELIX 23 23 VAL A 373 GLN A 397 1 25
HELIX 24 24 GLU A 400 LYS A 414 1 15
HELIX 25 25 THR A 420 CYS A 438 1 19
HELIX 26 26 GLU A 442 LYS A 466 1 25
HELIX 27 27 ASP A 471 THR A 478 1 8
HELIX 28 28 PRO A 486 ALA A 490 1 5
HELIX 29 29 ALA A 504 PHE A 507 5 4
HELIX 30 30 ILE A 513 THR A 515 5 3
HELIX 31 31 GLU A 518 HIS A 535 1 18
HELIX 32 32 LYS A 541 CYS A 559 1 19
HELIX 33 33 CYS A 567 ALA A 582 1 16
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.03
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.03
SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.02
SSBOND 4 CYS A 124 CYS A 169 1555 1555 2.03
SSBOND 5 CYS A 168 CYS A 177 1555 1555 2.03
SSBOND 6 CYS A 200 CYS A 246 1555 1555 2.02
SSBOND 7 CYS A 245 CYS A 253 1555 1555 2.03
SSBOND 8 CYS A 265 CYS A 279 1555 1555 2.02
SSBOND 9 CYS A 278 CYS A 289 1555 1555 2.03
SSBOND 10 CYS A 316 CYS A 361 1555 1555 2.03
SSBOND 11 CYS A 360 CYS A 369 1555 1555 2.03
SSBOND 12 CYS A 392 CYS A 438 1555 1555 2.03
SSBOND 13 CYS A 437 CYS A 448 1555 1555 2.03
SSBOND 14 CYS A 461 CYS A 477 1555 1555 2.03
SSBOND 15 CYS A 476 CYS A 487 1555 1555 2.02
SSBOND 16 CYS A 514 CYS A 559 1555 1555 2.03
SSBOND 17 CYS A 558 CYS A 567 1555 1555 2.02
SITE 1 AC1 5 ARG A 117 MET A 123 TYR A 138 TYR A 161
SITE 2 AC1 5 B3I A2002
SITE 1 AC2 5 TYR A 150 ALA A 254 ARG A 257 LEU A 283
SITE 2 AC2 5 SER A 287
SITE 1 AC3 7 SER A 342 VAL A 344 ARG A 348 ILE A 388
SITE 2 AC3 7 LEU A 430 LEU A 453 ARG A 485
SITE 1 AC4 7 LEU A 387 ARG A 410 TYR A 411 VAL A 415
SITE 2 AC4 7 LEU A 460 PHE A 488 SER A 489
SITE 1 AC5 7 TYR A 401 PHE A 502 PHE A 507 LYS A 525
SITE 2 AC5 7 MET A 548 PHE A 551 SER A 579
SITE 1 AC6 5 LEU A 219 PHE A 223 HIS A 242 ARG A 257
SITE 2 AC6 5 ALA A 291
SITE 1 AC7 7 HIS A 146 PHE A 149 TYR A 161 GLY A 189
SITE 2 AC7 7 LYS A 190 SER A 193 MYR A1001
CRYST1 187.650 38.870 95.910 90.00 105.49 90.00 C 1 2 1 4
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 0.005329 0.000000 0.001477 0.00000
SCALE2 0.000000 0.025727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010819 0.00000
(ATOM LINES ARE NOT SHOWN.)
END