HEADER TRANSPORT PROTEIN 21-OCT-01 1K7S
TITLE FHUD COMPLEXED WITH ALBOMYCIN-DELTA 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERRICHROME-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: N;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMR21
KEYWDS TWO MIXED DOMAINS CONNECTED BY AN ALPHA HELIX, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.E.CLARKE,V.BRAUN,G.WINKELMANN,L.W.TARI,H.J.VOGEL
REVDAT 5 16-AUG-23 1K7S 1 REMARK SEQADV
REVDAT 4 28-SEP-11 1K7S 1 VERSN
REVDAT 3 24-FEB-09 1K7S 1 VERSN
REVDAT 2 15-MAY-02 1K7S 1 REMARK
REVDAT 1 17-APR-02 1K7S 0
JRNL AUTH T.E.CLARKE,V.BRAUN,G.WINKELMANN,L.W.TARI,H.J.VOGEL
JRNL TITL X-RAY CRYSTALLOGRAPHIC STRUCTURES OF THE ESCHERICHIA COLI
JRNL TITL 2 PERIPLASMIC PROTEIN FHUD BOUND TO HYDROXAMATE-TYPE
JRNL TITL 3 SIDEROPHORES AND THE ANTIBIOTIC ALBOMYCIN.
JRNL REF J.BIOL.CHEM. V. 277 13966 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11805094
JRNL DOI 10.1074/JBC.M109385200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.E.CLARKE,S.-Y.KU,D.R.DOUGAN,H.J.VOGEL,L.W.TARI
REMARK 1 TITL THE STRUCTURE OF THE FERRIC SIDEROPHORE BINDING PROTEIN FHUD
REMARK 1 TITL 2 COMPLEXED WITH GALLICHROME
REMARK 1 REF NAT.STRUCT.BIOL. V. 7 287 2000
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/74048
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 10715
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) : 0.194
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 484
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 : 2013
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 38
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) : 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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
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 1K7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014667.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
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 : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : OSMIC CONFOCAL MULTILAYER OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 10715
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 94.80
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 95.50
REMARK 200 R MERGE FOR SHELL (I) : 0.64600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1EFD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 0.1M NA ACETATE, PH 5.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.80000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 45.80000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.80000
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: N
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 GLY N 294
REMARK 465 LYS N 295
REMARK 465 ALA N 296
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 N 86 CG CD OE1 OE2
REMARK 470 GLU N 111 CG CD OE1 OE2
REMARK 470 ARG N 115 CG CD NE CZ NH1 NH2
REMARK 470 LYS N 136 CG CD CE NZ
REMARK 470 VAL N 170 CG1 CG2
REMARK 470 LYS N 171 CB CG CD CE NZ
REMARK 470 ARG N 172 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG N 186 CG CD NE CZ NH1 NH2
REMARK 470 ARG N 226 CG CD NE CZ NH1 NH2
REMARK 470 LYS N 231 CG CD CE NZ
REMARK 470 SER N 243 OG
REMARK 470 LYS N 244 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ASP N 76 NH2 ARG N 262 6554 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE N 33 -86.39 16.19
REMARK 500 ASP N 61 62.51 65.23
REMARK 500 SER N 70 -48.21 64.72
REMARK 500 GLU N 71 -161.87 -64.11
REMARK 500 PRO N 72 62.10 19.86
REMARK 500 VAL N 78 132.09 -38.86
REMARK 500 LYS N 96 60.15 60.41
REMARK 500 ARG N 172 87.83 -68.06
REMARK 500 ALA N 174 23.60 -75.90
REMARK 500 LYS N 231 -85.57 -66.47
REMARK 500 HIS N 240 58.19 -160.23
REMARK 500 ALA N 277 -127.48 -131.99
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 ALB N 500
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALB N 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EFD RELATED DB: PDB
REMARK 900 FHUD COMPLEXED WITH GALLICHROME
REMARK 900 RELATED ID: 1ESZ RELATED DB: PDB
REMARK 900 FHUD COMPLEXED WITH COPROGEN
REMARK 900 RELATED ID: 1K2V RELATED DB: PDB
REMARK 900 FHUD COMPLEXED WITH DESFERAL
DBREF 1K7S N 33 296 UNP P07822 FHUD_ECOLI 33 296
SEQADV 1K7S GLY N 32 UNP P07822 EXPRESSION TAG
SEQRES 1 N 265 GLY ILE ASP PRO ASN ARG ILE VAL ALA LEU GLU TRP LEU
SEQRES 2 N 265 PRO VAL GLU LEU LEU LEU ALA LEU GLY ILE VAL PRO TYR
SEQRES 3 N 265 GLY VAL ALA ASP THR ILE ASN TYR ARG LEU TRP VAL SER
SEQRES 4 N 265 GLU PRO PRO LEU PRO ASP SER VAL ILE ASP VAL GLY LEU
SEQRES 5 N 265 ARG THR GLU PRO ASN LEU GLU LEU LEU THR GLU MET LYS
SEQRES 6 N 265 PRO SER PHE MET VAL TRP SER ALA GLY TYR GLY PRO SER
SEQRES 7 N 265 PRO GLU MET LEU ALA ARG ILE ALA PRO GLY ARG GLY PHE
SEQRES 8 N 265 ASN PHE SER ASP GLY LYS GLN PRO LEU ALA MET ALA ARG
SEQRES 9 N 265 LYS SER LEU THR GLU MET ALA ASP LEU LEU ASN LEU GLN
SEQRES 10 N 265 SER ALA ALA GLU THR HIS LEU ALA GLN TYR GLU ASP PHE
SEQRES 11 N 265 ILE ARG SER MET LYS PRO ARG PHE VAL LYS ARG GLY ALA
SEQRES 12 N 265 ARG PRO LEU LEU LEU THR THR LEU ILE ASP PRO ARG HIS
SEQRES 13 N 265 MET LEU VAL PHE GLY PRO ASN SER LEU PHE GLN GLU ILE
SEQRES 14 N 265 LEU ASP GLU TYR GLY ILE PRO ASN ALA TRP GLN GLY GLU
SEQRES 15 N 265 THR ASN PHE TRP GLY SER THR ALA VAL SER ILE ASP ARG
SEQRES 16 N 265 LEU ALA ALA TYR LYS ASP VAL ASP VAL LEU CYS PHE ASP
SEQRES 17 N 265 HIS ASP ASN SER LYS ASP MET ASP ALA LEU MET ALA THR
SEQRES 18 N 265 PRO LEU TRP GLN ALA MET PRO PHE VAL ARG ALA GLY ARG
SEQRES 19 N 265 PHE GLN ARG VAL PRO ALA VAL TRP PHE TYR GLY ALA THR
SEQRES 20 N 265 LEU SER ALA MET HIS PHE VAL ARG VAL LEU ASP ASN ALA
SEQRES 21 N 265 ILE GLY GLY LYS ALA
HET ALB N 500 41
HETNAM ALB DELTA-2-ALBOMYCIN A1
FORMUL 2 ALB C37 H57 FE N12 O18 S
FORMUL 3 HOH *38(H2 O)
HELIX 1 1 GLU N 42 LEU N 52 1 11
HELIX 2 2 ASP N 61 VAL N 69 1 9
HELIX 3 3 ASN N 88 LYS N 96 1 9
HELIX 4 4 SER N 109 ALA N 114 1 6
HELIX 5 5 GLN N 129 ASN N 146 1 18
HELIX 6 6 LEU N 147 MET N 165 1 19
HELIX 7 8 LEU N 196 GLY N 205 1 10
HELIX 8 9 ASP N 225 TYR N 230 5 6
HELIX 9 10 ASN N 242 THR N 252 1 11
HELIX 10 11 THR N 252 MET N 258 1 7
HELIX 11 12 MET N 258 ALA N 263 1 6
HELIX 12 13 ALA N 277 GLY N 293 1 17
SHEET 1 A 5 ILE N 79 ASP N 80 0
SHEET 2 A 5 GLY N 58 VAL N 59 1 N VAL N 59 O ILE N 79
SHEET 3 A 5 ILE N 38 ALA N 40 1 N ALA N 40 O GLY N 58
SHEET 4 A 5 PHE N 99 SER N 103 1 O VAL N 101 N VAL N 39
SHEET 5 A 5 GLY N 119 PHE N 122 1 O PHE N 122 N TRP N 102
SHEET 1 B 5 SER N 219 SER N 223 0
SHEET 2 B 5 HIS N 187 PHE N 191 -1 N MET N 188 O VAL N 222
SHEET 3 B 5 LEU N 177 ASP N 184 -1 N THR N 181 O LEU N 189
SHEET 4 B 5 ASP N 234 PHE N 238 1 O ASP N 234 N LEU N 178
SHEET 5 B 5 PHE N 266 VAL N 269 1 O GLN N 267 N VAL N 235
SITE 1 AC1 9 TRP N 68 ARG N 84 THR N 85 TYR N 106
SITE 2 AC1 9 ILE N 183 LEU N 189 TRP N 217 TRP N 273
SITE 3 AC1 9 TYR N 275
CRYST1 85.570 85.570 91.600 90.00 90.00 120.00 P 63 6
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 0.011686 0.006747 0.000000 0.00000
SCALE2 0.000000 0.013494 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010917 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
