HEADER PEPTIDE BINDING PROTEIN 11-NOV-98 1B4H
TITLE OLIGO-PEPTIDE BINDING PROTEIN COMPLEXED WITH LYSYL-DIAMINOBUTYRIC
TITLE 2 ACID-LYSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC OLIGO-PEPTIDE BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OPPA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LYS-DAB-LYS PEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES
KEYWDS PERIPLASMIC PEPTIDE BINDING PROTEIN, PEPTIDE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.G.DAVIES,J.R.H.TAME
REVDAT 5 27-DEC-23 1B4H 1 REMARK LINK
REVDAT 4 24-FEB-09 1B4H 1 VERSN
REVDAT 3 01-APR-03 1B4H 1 JRNL
REVDAT 2 15-DEC-99 1B4H 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 18-NOV-98 1B4H 0
JRNL AUTH T.G.DAVIES,R.E.HUBBARD,J.R.TAME
JRNL TITL RELATING STRUCTURE TO THERMODYNAMICS: THE CRYSTAL STRUCTURES
JRNL TITL 2 AND BINDING AFFINITY OF EIGHT OPPA-PEPTIDE COMPLEXES.
JRNL REF PROTEIN SCI. V. 8 1432 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10422831
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.R.TAME,E.J.DODSON,G.MURSHUDOV,C.F.HIGGINS,A.J.WILKINSON
REMARK 1 TITL THE CRYSTAL STRUCTURES OF THE OLIGOPEPTIDE-BINDING PROTEIN
REMARK 1 TITL 2 OPPA COMPLEXED WITH TRIPEPTIDE AND TETRAPEPTIDE LIGANDS
REMARK 1 REF STRUCTURE V. 3 1395 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 45354
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4191
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 373
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.50
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.029 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.032 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.176 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.247 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.136 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 3.700 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 14.100; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.371 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.935 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.674 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.484 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-98.
REMARK 100 THE DEPOSITION ID IS D_1000000074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 5.5
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 : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47784
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5
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 54.86100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.21200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.97650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.21200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.86100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.97650
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 12 CE NZ
REMARK 480 LYS A 178 CE NZ
REMARK 480 GLN A 338 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 27 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 GLU A 53 OE1 - CD - OE2 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASP A 102 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 102 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 133 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 269 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 273 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 362 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 402 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 410 CB - CG - OD1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP A 410 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 413 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 413 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 413 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TYR A 485 CA - CB - CG ANGL. DEV. = 11.6 DEGREES
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 GLN A 13 74.59 -103.86
REMARK 500 GLU A 32 -3.94 -143.66
REMARK 500 GLU A 200 -64.35 -127.78
REMARK 500 ASN A 246 61.41 -103.78
REMARK 500 ASN A 308 58.31 38.93
REMARK 500 THR A 367 119.42 -36.89
REMARK 500 SER A 368 143.12 -177.48
REMARK 500 ASP A 410 -72.61 -105.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE SOLVENT STRUCTURE AROUND THE URANIUM IONS IS TENTATIVE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 A 908
DBREF 1B4H A 1 517 UNP P06202 OPPA_SALTY 26 542
DBREF 1B4H B 1 3 PDB 1B4H 1B4H 1 3
SEQRES 1 A 517 ALA ASP VAL PRO ALA GLY VAL GLN LEU ALA ASP LYS GLN
SEQRES 2 A 517 THR LEU VAL ARG ASN ASN GLY SER GLU VAL GLN SER LEU
SEQRES 3 A 517 ASP PRO HIS LYS ILE GLU GLY VAL PRO GLU SER ASN VAL
SEQRES 4 A 517 SER ARG ASP LEU PHE GLU GLY LEU LEU ILE SER ASP VAL
SEQRES 5 A 517 GLU GLY HIS PRO SER PRO GLY VAL ALA GLU LYS TRP GLU
SEQRES 6 A 517 ASN LYS ASP PHE LYS VAL TRP THR PHE HIS LEU ARG GLU
SEQRES 7 A 517 ASN ALA LYS TRP SER ASP GLY THR PRO VAL THR ALA HIS
SEQRES 8 A 517 ASP PHE VAL TYR SER TRP GLN ARG LEU ALA ASP PRO ASN
SEQRES 9 A 517 THR ALA SER PRO TYR ALA SER TYR LEU GLN TYR GLY HIS
SEQRES 10 A 517 ILE ALA ASN ILE ASP ASP ILE ILE ALA GLY LYS LYS PRO
SEQRES 11 A 517 ALA THR ASP LEU GLY VAL LYS ALA LEU ASP ASP HIS THR
SEQRES 12 A 517 PHE GLU VAL THR LEU SER GLU PRO VAL PRO TYR PHE TYR
SEQRES 13 A 517 LYS LEU LEU VAL HIS PRO SER VAL SER PRO VAL PRO LYS
SEQRES 14 A 517 SER ALA VAL GLU LYS PHE GLY ASP LYS TRP THR GLN PRO
SEQRES 15 A 517 ALA ASN ILE VAL THR ASN GLY ALA TYR LYS LEU LYS ASN
SEQRES 16 A 517 TRP VAL VAL ASN GLU ARG ILE VAL LEU GLU ARG ASN PRO
SEQRES 17 A 517 GLN TYR TRP ASP ASN ALA LYS THR VAL ILE ASN GLN VAL
SEQRES 18 A 517 THR TYR LEU PRO ILE SER SER GLU VAL THR ASP VAL ASN
SEQRES 19 A 517 ARG TYR ARG SER GLY GLU ILE ASP MET THR TYR ASN ASN
SEQRES 20 A 517 MET PRO ILE GLU LEU PHE GLN LYS LEU LYS LYS GLU ILE
SEQRES 21 A 517 PRO ASN GLU VAL ARG VAL ASP PRO TYR LEU CYS THR TYR
SEQRES 22 A 517 TYR TYR GLU ILE ASN ASN GLN LYS ALA PRO PHE ASN ASP
SEQRES 23 A 517 VAL ARG VAL ARG THR ALA LEU LYS LEU ALA LEU ASP ARG
SEQRES 24 A 517 ASP ILE ILE VAL ASN LYS VAL LYS ASN GLN GLY ASP LEU
SEQRES 25 A 517 PRO ALA TYR SER TYR THR PRO PRO TYR THR ASP GLY ALA
SEQRES 26 A 517 LYS LEU VAL GLU PRO GLU TRP PHE LYS TRP SER GLN GLN
SEQRES 27 A 517 LYS ARG ASN GLU GLU ALA LYS LYS LEU LEU ALA GLU ALA
SEQRES 28 A 517 GLY PHE THR ALA ASP LYS PRO LEU THR PHE ASP LEU LEU
SEQRES 29 A 517 TYR ASN THR SER ASP LEU HIS LYS LYS LEU ALA ILE ALA
SEQRES 30 A 517 VAL ALA SER ILE TRP LYS LYS ASN LEU GLY VAL ASN VAL
SEQRES 31 A 517 ASN LEU GLU ASN GLN GLU TRP LYS THR PHE LEU ASP THR
SEQRES 32 A 517 ARG HIS GLN GLY THR PHE ASP VAL ALA ARG ALA GLY TRP
SEQRES 33 A 517 CYS ALA ASP TYR ASN GLU PRO THR SER PHE LEU ASN THR
SEQRES 34 A 517 MET LEU SER ASP SER SER ASN ASN THR ALA HIS TYR LYS
SEQRES 35 A 517 SER PRO ALA PHE ASP LYS LEU ILE ALA ASP THR LEU LYS
SEQRES 36 A 517 VAL ALA ASP ASP THR GLN ARG SER GLU LEU TYR ALA LYS
SEQRES 37 A 517 ALA GLU GLN GLN LEU ASP LYS ASP SER ALA ILE VAL PRO
SEQRES 38 A 517 VAL TYR TYR TYR VAL ASN ALA ARG LEU VAL LYS PRO TRP
SEQRES 39 A 517 VAL GLY GLY TYR THR GLY LYS ASP PRO LEU ASP ASN ILE
SEQRES 40 A 517 TYR VAL LYS ASN LEU TYR ILE ILE LYS HIS
SEQRES 1 B 3 LYS DAB LYS
MODRES 1B4H DAB B 2 ALA 2,4-DIAMINOBUTYRIC ACID
HET DAB B 2 8
HET U1 A 901 1
HET U1 A 902 1
HET U1 A 903 1
HET U1 A 904 1
HET U1 A 905 1
HET U1 A 906 1
HET U1 A 907 1
HET U1 A 908 1
HETNAM DAB 2,4-DIAMINOBUTYRIC ACID
HETNAM U1 URANIUM ATOM
FORMUL 2 DAB C4 H10 N2 O2
FORMUL 3 U1 8(U)
FORMUL 11 HOH *373(H2 O)
HELIX 1 1 VAL A 34 LEU A 43 1 10
HELIX 2 2 ALA A 90 ALA A 101 1 12
HELIX 3 3 PRO A 103 THR A 105 5 3
HELIX 4 4 ALA A 110 GLY A 116 5 7
HELIX 5 5 ILE A 121 ILE A 125 1 5
HELIX 6 6 ALA A 131 ASP A 133 5 3
HELIX 7 7 PHE A 155 VAL A 160 5 6
HELIX 8 8 PRO A 162 VAL A 164 5 3
HELIX 9 9 LYS A 169 LYS A 178 1 10
HELIX 10 10 ASN A 213 LYS A 215 5 3
HELIX 11 11 GLU A 229 ARG A 237 1 9
HELIX 12 12 PHE A 253 GLU A 259 1 7
HELIX 13 13 PRO A 261 GLU A 263 5 3
HELIX 14 14 VAL A 287 ALA A 296 1 10
HELIX 15 15 ARG A 299 ASN A 304 1 6
HELIX 16 16 GLU A 331 LYS A 334 1 4
HELIX 17 17 GLN A 337 ALA A 351 1 15
HELIX 18 18 ASP A 369 LEU A 386 1 18
HELIX 19 19 TRP A 397 GLN A 406 1 10
HELIX 20 20 PRO A 423 MET A 430 5 8
HELIX 21 21 PRO A 444 LEU A 454 1 11
HELIX 22 22 ASP A 459 LYS A 475 1 17
HELIX 23 23 VAL A 509 ASN A 511 5 3
SHEET 1 A 4 THR A 14 ASN A 18 0
SHEET 2 A 4 GLN A 220 LEU A 224 1 N GLN A 220 O LEU A 15
SHEET 3 A 4 ARG A 201 ARG A 206 -1 N LEU A 204 O VAL A 221
SHEET 4 A 4 TYR A 191 VAL A 197 -1 N VAL A 197 O ARG A 201
SHEET 1 B 2 LEU A 48 SER A 50 0
SHEET 2 B 2 PRO A 56 PRO A 58 -1 N SER A 57 O ILE A 49
SHEET 1 C 4 ALA A 61 LYS A 67 0
SHEET 2 C 4 VAL A 71 LEU A 76 -1 N HIS A 75 O GLU A 62
SHEET 3 C 4 THR A 143 THR A 147 -1 N VAL A 146 O TRP A 72
SHEET 4 C 4 VAL A 136 ASP A 140 -1 N ASP A 140 O THR A 143
SHEET 1 D 2 VAL A 264 PRO A 268 0
SHEET 2 D 2 VAL A 486 LEU A 490 -1 N ARG A 489 O ARG A 265
SHEET 1 E 3 VAL A 411 CYS A 417 0
SHEET 2 E 3 CYS A 271 ILE A 277 -1 N GLU A 276 O ALA A 412
SHEET 3 E 3 ILE A 479 TYR A 484 -1 N TYR A 483 O TYR A 273
SHEET 1 F 2 THR A 360 ASN A 366 0
SHEET 2 F 2 ASN A 389 GLN A 395 1 N ASN A 389 O PHE A 361
SSBOND 1 CYS A 271 CYS A 417 1555 1555 2.08
LINK C LYS B 1 N DAB B 2 1555 1555 1.33
LINK C DAB B 2 N LYS B 3 1555 1555 1.34
CISPEP 1 ALA A 282 PRO A 283 0 1.92
SITE 1 AC1 2 ASP A 323 ASN A 394
SITE 1 AC2 2 GLU A 251 ASP A 369
SITE 1 AC3 3 GLU A 53 ASP A 362 ASP A 410
SITE 1 AC4 2 ASP A 133 HIS A 517
SITE 1 AC5 2 ASP A 11 HOH A1232
CRYST1 109.722 75.953 70.424 90.00 90.00 90.00 P 21 21 21 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 0.009114 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014200 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
