HEADER CYTOKINE 03-SEP-07 2R53
TITLE CRYSTAL STRUCTURE ANALYSIS OF BONE MORPHOGENETIC PROTEIN-6 VARIANT B2
TITLE 2 (B2-BMP-6)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BONE MORPHOGENETIC PROTEIN 6;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BMP-6 VARIANT B2, MATURE PART;
COMPND 5 SYNONYM: BMP-6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BMP6, VGR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PN25
KEYWDS BMP6, VGR, TGF-BETA LIGAND, CHONDROGENESIS, CLEAVAGE ON PAIR OF BASIC
KEYWDS 2 RESIDUES, CYTOKINE, DEVELOPMENTAL PROTEIN, DIFFERENTIATION,
KEYWDS 3 GLYCOPROTEIN, GROWTH FACTOR, OSTEOGENESIS, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.MUELLER,W.SEBALD
REVDAT 4 30-AUG-23 2R53 1 REMARK
REVDAT 3 25-OCT-17 2R53 1 REMARK
REVDAT 2 24-FEB-09 2R53 1 VERSN
REVDAT 1 15-JAN-08 2R53 0
JRNL AUTH S.SAREMBA,J.NICKEL,A.SEHER,A.KOTZSCH,W.SEBALD,T.D.MUELLER
JRNL TITL TYPE I RECEPTOR BINDING OF BONE MORPHOGENETIC PROTEIN 6 IS
JRNL TITL 2 DEPENDENT ON N-GLYCOSYLATION OF THE LIGAND.
JRNL REF FEBS J. V. 275 172 2007
JRNL REFN ISSN 1742-464X
JRNL PMID 18070108
JRNL DOI 10.1111/J.1742-4658.2007.06187.X
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 28518
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) : 0.259
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1426
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 : 1700
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.70
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) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.475
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.883
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 2R53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9183
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28518
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
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: 1BMP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% 2-METHYL-2,4-PENTANDIOL, 0.1M
REMARK 280 SODIUM CITRATE PH 4.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 28.92000
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 57.84000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.84000
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 28.92000
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS THE BIOLOGICAL HOMODIMER
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: 3380 ANGSTROM**2
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 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 17
REMARK 465 ALA A 18
REMARK 465 GLN A 19
REMARK 465 ALA A 20
REMARK 465 LYS A 21
REMARK 465 HIS A 22
REMARK 465 LYS A 23
REMARK 465 GLN A 24
REMARK 465 ARG A 25
REMARK 465 MET B 17
REMARK 465 ALA B 18
REMARK 465 GLN B 19
REMARK 465 ALA B 20
REMARK 465 LYS B 21
REMARK 465 HIS B 22
REMARK 465 LYS B 23
REMARK 465 GLN B 24
REMARK 465 ARG B 25
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 ARG B 27 CG CD NE CZ NH1 NH2
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 ASN A 73 N - CA - C ANGL. DEV. = 19.9 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 ALA A 51 148.09 -174.37
REMARK 500 ASN A 58 -175.01 68.19
REMARK 500 MET A 72 -152.59 -118.56
REMARK 500 ASN A 73 -15.48 -43.05
REMARK 500 ASP A 111 -168.45 -109.04
REMARK 500 LEU B 28 -73.30 -50.97
REMARK 500 ASN B 58 -179.20 68.62
REMARK 500 CYS B 64 78.99 -116.56
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 MPD B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BMP RELATED DB: PDB
REMARK 900 BMP-2 LIGAND STRUCTURE
REMARK 900 RELATED ID: 1REW RELATED DB: PDB
REMARK 900 BINARY LIGAND-RECEPTOR COMPLEX BMP-2 AND ITS TYPE I RECEPTOR BMPR-IA
REMARK 900 RELATED ID: 2H62 RELATED DB: PDB
REMARK 900 TERNARY LIGAND-RECEPTOR COMPLEX OF BMP-2 BOUND TO ITS TYPE I
REMARK 900 RECEPTOR BMPR-IA AND ITS TYPE II RECEPTOR ACTR-IIB
REMARK 900 RELATED ID: 2H64 RELATED DB: PDB
REMARK 900 TERNARY LIGAND-RECEPTOR COMPLEX OF A BMP-2 VARIANT BOUND TO ITS
REMARK 900 TYPE I RECEPTOR BMPR-IA AND ITS TYPE II RECEPTOR ACTR-IIB
REMARK 900 RELATED ID: 2R52 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 375 TO 410 OF BMP-6 ARE REPLACED BY MAQAKHKQEKRLK.
DBREF 2R53 A 30 132 UNP P22004 BMP6_HUMAN 411 513
DBREF 2R53 B 30 132 UNP P22004 BMP6_HUMAN 411 513
SEQADV 2R53 MET A 17 UNP P22004 SEE REMARK 999
SEQADV 2R53 ALA A 18 UNP P22004 SEE REMARK 999
SEQADV 2R53 GLN A 19 UNP P22004 SEE REMARK 999
SEQADV 2R53 ALA A 20 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS A 21 UNP P22004 SEE REMARK 999
SEQADV 2R53 HIS A 22 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS A 23 UNP P22004 SEE REMARK 999
SEQADV 2R53 GLN A 24 UNP P22004 SEE REMARK 999
SEQADV 2R53 ARG A 25 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS A 26 UNP P22004 SEE REMARK 999
SEQADV 2R53 ARG A 27 UNP P22004 SEE REMARK 999
SEQADV 2R53 LEU A 28 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS A 29 UNP P22004 SEE REMARK 999
SEQADV 2R53 MET B 17 UNP P22004 SEE REMARK 999
SEQADV 2R53 ALA B 18 UNP P22004 SEE REMARK 999
SEQADV 2R53 GLN B 19 UNP P22004 SEE REMARK 999
SEQADV 2R53 ALA B 20 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS B 21 UNP P22004 SEE REMARK 999
SEQADV 2R53 HIS B 22 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS B 23 UNP P22004 SEE REMARK 999
SEQADV 2R53 GLN B 24 UNP P22004 SEE REMARK 999
SEQADV 2R53 ARG B 25 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS B 26 UNP P22004 SEE REMARK 999
SEQADV 2R53 ARG B 27 UNP P22004 SEE REMARK 999
SEQADV 2R53 LEU B 28 UNP P22004 SEE REMARK 999
SEQADV 2R53 LYS B 29 UNP P22004 SEE REMARK 999
SEQRES 1 A 116 MET ALA GLN ALA LYS HIS LYS GLN ARG LYS ARG LEU LYS
SEQRES 2 A 116 ALA CYS ARG LYS HIS GLU LEU TYR VAL SER PHE GLN ASP
SEQRES 3 A 116 LEU GLY TRP GLN ASP TRP ILE ILE ALA PRO LYS GLY TYR
SEQRES 4 A 116 ALA ALA ASN TYR CYS ASP GLY GLU CYS SER PHE PRO LEU
SEQRES 5 A 116 ASN ALA HIS MET ASN ALA THR ASN HIS ALA ILE VAL GLN
SEQRES 6 A 116 THR LEU VAL HIS LEU MET ASN PRO GLU TYR VAL PRO LYS
SEQRES 7 A 116 PRO CYS CYS ALA PRO THR LYS LEU ASN ALA ILE SER VAL
SEQRES 8 A 116 LEU TYR PHE ASP ASP ASN SER ASN VAL ILE LEU LYS LYS
SEQRES 9 A 116 TYR ARG ASN MET VAL VAL ARG ALA CYS GLY CYS HIS
SEQRES 1 B 116 MET ALA GLN ALA LYS HIS LYS GLN ARG LYS ARG LEU LYS
SEQRES 2 B 116 ALA CYS ARG LYS HIS GLU LEU TYR VAL SER PHE GLN ASP
SEQRES 3 B 116 LEU GLY TRP GLN ASP TRP ILE ILE ALA PRO LYS GLY TYR
SEQRES 4 B 116 ALA ALA ASN TYR CYS ASP GLY GLU CYS SER PHE PRO LEU
SEQRES 5 B 116 ASN ALA HIS MET ASN ALA THR ASN HIS ALA ILE VAL GLN
SEQRES 6 B 116 THR LEU VAL HIS LEU MET ASN PRO GLU TYR VAL PRO LYS
SEQRES 7 B 116 PRO CYS CYS ALA PRO THR LYS LEU ASN ALA ILE SER VAL
SEQRES 8 B 116 LEU TYR PHE ASP ASP ASN SER ASN VAL ILE LEU LYS LYS
SEQRES 9 B 116 TYR ARG ASN MET VAL VAL ARG ALA CYS GLY CYS HIS
HET MPD A 3 8
HET MPD A 4 8
HET MPD B 1 8
HET MPD B 2 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 MPD 4(C6 H14 O2)
FORMUL 7 HOH *78(H2 O)
HELIX 1 1 THR A 75 ASN A 88 1 14
HELIX 2 2 PHE B 40 GLY B 44 1 5
HELIX 3 3 ASN B 69 ASN B 73 5 5
HELIX 4 4 THR B 75 ASN B 88 1 14
SHEET 1 A 2 ARG A 32 HIS A 34 0
SHEET 2 A 2 TYR A 59 ASP A 61 -1 O TYR A 59 N HIS A 34
SHEET 1 B 2 TYR A 37 SER A 39 0
SHEET 2 B 2 GLY A 54 ALA A 56 -1 O TYR A 55 N VAL A 38
SHEET 1 C 3 ILE A 49 ALA A 51 0
SHEET 2 C 3 CYS A 96 PHE A 110 -1 O LEU A 108 N ALA A 51
SHEET 3 C 3 VAL A 116 HIS A 132 -1 O TYR A 121 N ILE A 105
SHEET 1 D 2 ARG B 32 HIS B 34 0
SHEET 2 D 2 TYR B 59 ASP B 61 -1 O TYR B 59 N HIS B 34
SHEET 1 E 2 TYR B 37 SER B 39 0
SHEET 2 E 2 GLY B 54 ALA B 56 -1 O TYR B 55 N VAL B 38
SHEET 1 F 3 ILE B 49 ALA B 51 0
SHEET 2 F 3 CYS B 96 PHE B 110 -1 O LEU B 108 N ALA B 51
SHEET 3 F 3 VAL B 116 HIS B 132 -1 O TYR B 121 N ILE B 105
SSBOND 1 CYS A 31 CYS A 97 1555 1555 2.04
SSBOND 2 CYS A 60 CYS A 129 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 131 1555 1555 2.04
SSBOND 4 CYS A 96 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 31 CYS B 97 1555 1555 2.03
SSBOND 6 CYS B 60 CYS B 129 1555 1555 2.04
SSBOND 7 CYS B 64 CYS B 131 1555 1555 2.03
CISPEP 1 ALA A 51 PRO A 52 0 -0.16
CISPEP 2 PHE A 66 PRO A 67 0 0.14
CISPEP 3 ALA B 51 PRO B 52 0 -0.17
CISPEP 4 PHE B 66 PRO B 67 0 0.48
SITE 1 AC1 4 ASP A 42 LEU A 43 PRO B 52 HOH B 166
SITE 1 AC2 2 TRP A 45 ASN B 76
SITE 1 AC3 3 ASN A 76 ILE A 79 MET B 124
CRYST1 99.780 99.780 86.760 90.00 90.00 120.00 P 31 2 1 12
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 0.010022 0.005786 0.000000 0.00000
SCALE2 0.000000 0.011572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011526 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
