HEADER IMMUNE SYSTEM 31-AUG-11 3TM6
TITLE CRYSTAL STRUCTURE OF THE BETA-2 MICROGLOBULIN DIMC50 DISULPHIDE-LINKED
TITLE 2 HOMODIMER MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: FULL-LENGTH BETA-2 MICROGLOBULIN;
COMPND 5 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IMMUNOGLOBULIN-LIKE FOLD, MHC CLASS I, LIGHT CHAIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.COLOMBO,S.RICAGNO,M.BOLOGNESI
REVDAT 3 13-SEP-23 3TM6 1 REMARK SEQADV
REVDAT 2 28-AUG-13 3TM6 1 JRNL
REVDAT 1 05-SEP-12 3TM6 0
JRNL AUTH M.COLOMBO,M.DE ROSA,V.BELLOTTI,S.RICAGNO,M.BOLOGNESI
JRNL TITL A RECURRENT D-STRAND ASSOCIATION INTERFACE IS OBSERVED IN
JRNL TITL 2 BETA-2 MICROGLOBULIN OLIGOMERS.
JRNL REF FEBS J. V. 279 1131 2012
JRNL REFN ISSN 1742-464X
JRNL PMID 22289140
JRNL DOI 10.1111/J.1742-4658.2012.08510.X
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 23013
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1160
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.86
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2846
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2548
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2710
REMARK 3 BIN R VALUE (WORKING SET) : 0.2531
REMARK 3 BIN FREE R VALUE : 0.2888
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.78
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
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 : 6560
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 112
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.70780
REMARK 3 B22 (A**2) : 1.18420
REMARK 3 B33 (A**2) : 0.52360
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.72500
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.419
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) : NULL
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 : 0.874
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.838
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6802 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9203 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2348 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 170 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 954 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6802 ; 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 : 842 ; 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 : 6210 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.29
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.25
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 3TM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 0.93950
REMARK 200 MONOCHROMATOR : CHANNEL CUT ESRF MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23049
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2Z9T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: IMIDAZOLE-MALATE 0.2 M, PH 5.5, PEG
REMARK 280 600 24%, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.13600
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 MET A 99
REMARK 465 MET B 99
REMARK 465 ASP C 98
REMARK 465 MET C 99
REMARK 465 MET D 99
REMARK 465 ASP E 98
REMARK 465 MET E 99
REMARK 465 ASP F 98
REMARK 465 MET F 99
REMARK 465 ASP G 98
REMARK 465 MET G 99
REMARK 465 ASP H 98
REMARK 465 MET H 99
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 ASP A 34 109.40 -58.42
REMARK 500 ARG A 97 59.84 -101.86
REMARK 500 ASP B 34 108.80 -58.67
REMARK 500 ARG B 97 -3.56 -50.96
REMARK 500 ASP C 34 106.35 -58.12
REMARK 500 ASP D 34 108.09 -57.60
REMARK 500 ASP E 34 108.73 -57.91
REMARK 500 ASP F 34 108.60 -57.79
REMARK 500 LYS F 48 58.50 -93.51
REMARK 500 ASP G 34 109.92 -59.02
REMARK 500 ASN H 21 -162.10 -129.97
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 RESIDUE PEG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG G 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG G 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X89 RELATED DB: PDB
REMARK 900 RELATED ID: 3CIQ RELATED DB: PDB
DBREF 3TM6 A 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 C 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 E 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 G 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3TM6 H 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 3TM6 MET A 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS A 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET B 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS B 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET C 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS C 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET D 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS D 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET E 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS E 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET F 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS F 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET G 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS G 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQADV 3TM6 MET H 0 UNP P61769 EXPRESSION TAG
SEQADV 3TM6 CYS H 50 UNP P61769 GLU 70 ENGINEERED MUTATION
SEQRES 1 A 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 A 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 A 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 A 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 A 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 A 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 A 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 A 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 C 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 C 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 C 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 C 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 C 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 C 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 C 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 D 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 D 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 D 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 D 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 D 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 D 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 D 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 D 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 E 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 E 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 E 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 E 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 E 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 E 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 E 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 E 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 F 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 F 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 F 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 F 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 F 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 F 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 F 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 F 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 G 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 G 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 G 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 G 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 G 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 G 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 G 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 G 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 H 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 H 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 H 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 H 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL CYS HIS
SEQRES 5 H 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 H 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 H 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 H 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
HET PEG A 201 7
HET PEG B 200 7
HET PO4 B 100 5
HET PO4 C 100 5
HET PO4 C 101 5
HET PEG D 200 7
HET PO4 E 100 5
HET PO4 F 100 5
HET PEG G 200 7
HET PEG G 100 7
HET PO4 H 100 5
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PO4 PHOSPHATE ION
FORMUL 9 PEG 5(C4 H10 O3)
FORMUL 11 PO4 6(O4 P 3-)
FORMUL 20 HOH *112(H2 O)
SHEET 1 A 4 LYS A 6 SER A 11 0
SHEET 2 A 4 ASN A 21 PHE A 30 -1 O ASN A 24 N TYR A 10
SHEET 3 A 4 PHE A 62 PHE A 70 -1 O PHE A 62 N PHE A 30
SHEET 4 A 4 CYS A 50 HIS A 51 -1 N CYS A 50 O TYR A 67
SHEET 1 B 4 LYS A 6 SER A 11 0
SHEET 2 B 4 ASN A 21 PHE A 30 -1 O ASN A 24 N TYR A 10
SHEET 3 B 4 PHE A 62 PHE A 70 -1 O PHE A 62 N PHE A 30
SHEET 4 B 4 SER A 55 PHE A 56 -1 N SER A 55 O TYR A 63
SHEET 1 C 4 GLU A 44 ARG A 45 0
SHEET 2 C 4 GLU A 36 LYS A 41 -1 N LYS A 41 O GLU A 44
SHEET 3 C 4 TYR A 78 ASN A 83 -1 O ARG A 81 N ASP A 38
SHEET 4 C 4 LYS A 91 LYS A 94 -1 O LYS A 91 N VAL A 82
SHEET 1 D 4 LYS B 6 SER B 11 0
SHEET 2 D 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 D 4 PHE B 62 PHE B 70 -1 O PHE B 62 N PHE B 30
SHEET 4 D 4 CYS B 50 HIS B 51 -1 N CYS B 50 O TYR B 67
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O PHE B 62 N PHE B 30
SHEET 4 E 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 F 4 GLU B 44 ARG B 45 0
SHEET 2 F 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 F 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 F 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 G 4 LYS C 6 SER C 11 0
SHEET 2 G 4 ASN C 21 PHE C 30 -1 O ASN C 24 N TYR C 10
SHEET 3 G 4 PHE C 62 PHE C 70 -1 O PHE C 62 N PHE C 30
SHEET 4 G 4 CYS C 50 HIS C 51 -1 N CYS C 50 O TYR C 67
SHEET 1 H 4 LYS C 6 SER C 11 0
SHEET 2 H 4 ASN C 21 PHE C 30 -1 O ASN C 24 N TYR C 10
SHEET 3 H 4 PHE C 62 PHE C 70 -1 O PHE C 62 N PHE C 30
SHEET 4 H 4 SER C 55 PHE C 56 -1 N SER C 55 O TYR C 63
SHEET 1 I 4 GLU C 44 ARG C 45 0
SHEET 2 I 4 GLU C 36 LYS C 41 -1 N LYS C 41 O GLU C 44
SHEET 3 I 4 TYR C 78 ASN C 83 -1 O ALA C 79 N LEU C 40
SHEET 4 I 4 LYS C 91 LYS C 94 -1 O LYS C 91 N VAL C 82
SHEET 1 J 4 LYS D 6 SER D 11 0
SHEET 2 J 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 J 4 PHE D 62 PHE D 70 -1 O PHE D 62 N PHE D 30
SHEET 4 J 4 CYS D 50 HIS D 51 -1 N CYS D 50 O TYR D 67
SHEET 1 K 4 LYS D 6 SER D 11 0
SHEET 2 K 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 K 4 PHE D 62 PHE D 70 -1 O PHE D 62 N PHE D 30
SHEET 4 K 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 L 4 GLU D 44 ARG D 45 0
SHEET 2 L 4 GLU D 36 LYS D 41 -1 N LYS D 41 O GLU D 44
SHEET 3 L 4 TYR D 78 ASN D 83 -1 O ALA D 79 N LEU D 40
SHEET 4 L 4 LYS D 91 LYS D 94 -1 O LYS D 91 N VAL D 82
SHEET 1 M 4 LYS E 6 SER E 11 0
SHEET 2 M 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 M 4 PHE E 62 PHE E 70 -1 O PHE E 62 N PHE E 30
SHEET 4 M 4 CYS E 50 HIS E 51 -1 N CYS E 50 O TYR E 67
SHEET 1 N 4 LYS E 6 SER E 11 0
SHEET 2 N 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 N 4 PHE E 62 PHE E 70 -1 O PHE E 62 N PHE E 30
SHEET 4 N 4 SER E 55 PHE E 56 -1 N SER E 55 O TYR E 63
SHEET 1 O 4 GLU E 44 ARG E 45 0
SHEET 2 O 4 GLU E 36 LYS E 41 -1 N LYS E 41 O GLU E 44
SHEET 3 O 4 TYR E 78 ASN E 83 -1 O ALA E 79 N LEU E 40
SHEET 4 O 4 LYS E 91 LYS E 94 -1 O LYS E 91 N VAL E 82
SHEET 1 P 4 LYS F 6 SER F 11 0
SHEET 2 P 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 P 4 PHE F 62 PHE F 70 -1 O PHE F 62 N PHE F 30
SHEET 4 P 4 CYS F 50 HIS F 51 -1 N CYS F 50 O TYR F 67
SHEET 1 Q 4 LYS F 6 SER F 11 0
SHEET 2 Q 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 Q 4 PHE F 62 PHE F 70 -1 O PHE F 62 N PHE F 30
SHEET 4 Q 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 R 4 GLU F 44 ARG F 45 0
SHEET 2 R 4 GLU F 36 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 R 4 TYR F 78 ASN F 83 -1 O ALA F 79 N LEU F 40
SHEET 4 R 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SHEET 1 S 4 LYS G 6 SER G 11 0
SHEET 2 S 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10
SHEET 3 S 4 PHE G 62 PHE G 70 -1 O PHE G 62 N PHE G 30
SHEET 4 S 4 CYS G 50 HIS G 51 -1 N CYS G 50 O TYR G 67
SHEET 1 T 4 LYS G 6 SER G 11 0
SHEET 2 T 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10
SHEET 3 T 4 PHE G 62 PHE G 70 -1 O PHE G 62 N PHE G 30
SHEET 4 T 4 SER G 55 PHE G 56 -1 N SER G 55 O TYR G 63
SHEET 1 U 4 GLU G 44 ARG G 45 0
SHEET 2 U 4 GLU G 36 LYS G 41 -1 N LYS G 41 O GLU G 44
SHEET 3 U 4 TYR G 78 ASN G 83 -1 O ARG G 81 N ASP G 38
SHEET 4 U 4 LYS G 91 LYS G 94 -1 O LYS G 91 N VAL G 82
SHEET 1 V 4 LYS H 6 SER H 11 0
SHEET 2 V 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 V 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 V 4 CYS H 50 HIS H 51 -1 N CYS H 50 O TYR H 67
SHEET 1 W 4 LYS H 6 SER H 11 0
SHEET 2 W 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 W 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 W 4 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 X 4 GLU H 44 ARG H 45 0
SHEET 2 X 4 GLU H 36 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 X 4 TYR H 78 ASN H 83 -1 O ARG H 81 N ASP H 38
SHEET 4 X 4 LYS H 91 LYS H 94 -1 O LYS H 91 N VAL H 82
SSBOND 1 CYS A 25 CYS A 80 1555 1555 2.04
SSBOND 2 CYS A 50 CYS B 50 1555 1555 2.02
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS C 25 CYS C 80 1555 1555 2.04
SSBOND 5 CYS C 50 CYS D 50 1555 1555 2.05
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.04
SSBOND 7 CYS E 25 CYS E 80 1555 1555 2.04
SSBOND 8 CYS E 50 CYS F 50 1555 1555 2.03
SSBOND 9 CYS F 25 CYS F 80 1555 1555 2.04
SSBOND 10 CYS G 25 CYS G 80 1555 1555 2.03
SSBOND 11 CYS G 50 CYS H 50 1555 1555 2.05
SSBOND 12 CYS H 25 CYS H 80 1555 1555 2.04
CISPEP 1 HIS A 31 PRO A 32 0 2.43
CISPEP 2 HIS B 31 PRO B 32 0 2.76
CISPEP 3 HIS C 31 PRO C 32 0 2.16
CISPEP 4 HIS D 31 PRO D 32 0 2.62
CISPEP 5 HIS E 31 PRO E 32 0 2.58
CISPEP 6 HIS F 31 PRO F 32 0 2.72
CISPEP 7 HIS G 31 PRO G 32 0 2.80
CISPEP 8 HIS H 31 PRO H 32 0 1.46
SITE 1 AC1 1 TYR A 10
SITE 1 AC2 5 ASP A 53 SER B 52 SER B 55 TYR B 67
SITE 2 AC2 5 ASP C 53
SITE 1 AC3 4 ARG B 12 HIS B 13 SER D 57 LYS D 58
SITE 1 AC4 3 HIS A 13 SER C 57 LYS C 58
SITE 1 AC5 6 SER A 57 LYS A 58 ARG C 12 HIS C 13
SITE 2 AC5 6 PHE C 22 HOH C 108
SITE 1 AC6 1 ARG D 12
SITE 1 AC7 4 ARG E 12 HIS E 13 SER H 57 LYS H 58
SITE 1 AC8 4 ARG F 12 HIS F 13 SER G 57 LYS G 58
SITE 1 AC9 4 TYR E 67 ASP F 53 ASP G 53 HOH G 109
SITE 1 BC1 3 SER F 55 TYR F 63 ARG G 12
SITE 1 BC2 4 SER E 57 LYS E 58 ARG H 12 HIS H 13
CRYST1 90.102 56.272 96.374 90.00 115.67 90.00 P 1 21 1 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 0.011099 0.000000 0.005334 0.00000
SCALE2 0.000000 0.017771 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011512 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
