HEADER IMMUNE SYSTEM 01-NOV-02 1J05
TITLE THE CRYSTAL STRUCTURE OF ANTI-CARCINOEMBRYONIC ANTIGEN MONOCLONAL
TITLE 2 ANTIBODY T84.66 FV FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTI-CEA MAB T84.66, LIGHT CHAIN;
COMPND 3 CHAIN: L, A;
COMPND 4 FRAGMENT: FV FRAGMENT;
COMPND 5 SYNONYM: T84.66 ANTIBODY;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ANTI-CEA MAB T84.66, HEAVY CHAIN;
COMPND 9 CHAIN: H, B;
COMPND 10 FRAGMENT: FV FRAGMENT;
COMPND 11 SYNONYM: T84.66 ANTIBODY;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS IMMUNOGLOBULIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KONDO,Y.NISHIMURA,M.SHIROISHI,R.ASANO,N.NORO,K.TSUMOTO,I.KUMAGAI
REVDAT 4 27-DEC-23 1J05 1 REMARK SHEET
REVDAT 3 13-JUL-11 1J05 1 VERSN
REVDAT 2 24-FEB-09 1J05 1 VERSN
REVDAT 1 16-DEC-03 1J05 0
JRNL AUTH H.KONDO,Y.NISHIMURA,M.SHIROISHI,R.ASANO,N.NORO,K.TSUMOTO,
JRNL AUTH 2 I.KUMAGAI
JRNL TITL THE CRYSTAL STRUCTURE OF ANTI-CARCINOEMBRYONIC ANTIGEN
JRNL TITL 2 MONOCLONAL ANTIBODY T84.66 FV FRAGMENT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.190
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.185
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 8909
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 91647
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3562
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 ANGLE DISTANCES (A) : NULL
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000005463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91647
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 23.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.32500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA, K PHOSPHATE, NA HEPES, GLYCEROL,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING 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 37.51650
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, 3
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 BIOLOGICAL ASSEMBLIES ARE FORMED BETWEEN CHAIN L AND H
REMARK 300 AND BETWEEN A AND B.
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: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, 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 350
REMARK 350 BIOMOLECULE: 2
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: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 350 APPLY THE FOLLOWING TO CHAINS: L, H
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 51.16912
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -37.51650
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 125.76367
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 L 107 O
REMARK 470 SER H 113 O
REMARK 470 LYS A 107 O
REMARK 470 SER B 113 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER L 7 CB SER L 7 OG -0.095
REMARK 500
REMARK 500 REMARK: NULL
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 ARG L 24 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG L 68 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG L 68 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG H 40 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG H 50 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG H 50 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 40 CD - NE - CZ ANGL. DEV. = 33.8 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 50 CD - NE - CZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG B 50 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 50 NE - CZ - NH2 ANGL. DEV. = -4.5 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 L 51 -40.96 74.64
REMARK 500 ARG L 68 -93.96 47.48
REMARK 500 ALA L 84 168.53 178.24
REMARK 500 VAL H 99 -52.99 -128.70
REMARK 500 ALA A 51 -41.59 72.67
REMARK 500 SER A 67 -23.74 -145.45
REMARK 500 ALA A 84 175.63 175.48
REMARK 500 VAL B 99 -53.08 -122.80
REMARK 500 ALA B 101B -156.00 -149.22
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 PO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 1202
DBREF 1J05 L 1 107 UNP P01660 KV3H_MOUSE 1 111
DBREF 1J05 H 1 113 UNP Q9JL85 Q9JL85_MOUSE 1 103
DBREF 1J05 A 1 107 UNP P01660 KV3H_MOUSE 1 111
DBREF 1J05 B 1 113 UNP Q9JL85 Q9JL85_MOUSE 1 103
SEQRES 1 L 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL
SEQRES 2 L 111 SER LEU GLY GLN ARG ALA THR MET SER CYS ARG ALA GLY
SEQRES 3 L 111 GLU SER VAL ASP ILE PHE GLY VAL GLY PHE LEU HIS TRP
SEQRES 4 L 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE
SEQRES 5 L 111 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO VAL ARG
SEQRES 6 L 111 PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU ILE
SEQRES 7 L 111 ILE ASP PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR
SEQRES 8 L 111 CYS GLN GLN THR ASN GLU ASP PRO TYR THR PHE GLY GLY
SEQRES 9 L 111 GLY THR LYS LEU GLU ILE LYS
SEQRES 1 H 121 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL GLU
SEQRES 2 H 121 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 H 121 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 H 121 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 H 121 PRO ALA ASN GLY ASN SER LYS TYR VAL PRO LYS PHE GLN
SEQRES 6 H 121 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 H 121 ALA TYR LEU GLN LEU THR SER LEU THR SER GLU ASP THR
SEQRES 8 H 121 ALA VAL TYR TYR CYS ALA PRO PHE GLY TYR TYR VAL SER
SEQRES 9 H 121 ASP TYR ALA MET ALA TYR TRP GLY GLN GLY THR SER VAL
SEQRES 10 H 121 THR VAL SER SER
SEQRES 1 A 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL
SEQRES 2 A 111 SER LEU GLY GLN ARG ALA THR MET SER CYS ARG ALA GLY
SEQRES 3 A 111 GLU SER VAL ASP ILE PHE GLY VAL GLY PHE LEU HIS TRP
SEQRES 4 A 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE
SEQRES 5 A 111 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO VAL ARG
SEQRES 6 A 111 PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU ILE
SEQRES 7 A 111 ILE ASP PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR
SEQRES 8 A 111 CYS GLN GLN THR ASN GLU ASP PRO TYR THR PHE GLY GLY
SEQRES 9 A 111 GLY THR LYS LEU GLU ILE LYS
SEQRES 1 B 121 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL GLU
SEQRES 2 B 121 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 B 121 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 B 121 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 B 121 PRO ALA ASN GLY ASN SER LYS TYR VAL PRO LYS PHE GLN
SEQRES 6 B 121 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 B 121 ALA TYR LEU GLN LEU THR SER LEU THR SER GLU ASP THR
SEQRES 8 B 121 ALA VAL TYR TYR CYS ALA PRO PHE GLY TYR TYR VAL SER
SEQRES 9 B 121 ASP TYR ALA MET ALA TYR TRP GLY GLN GLY THR SER VAL
SEQRES 10 B 121 THR VAL SER SER
HET GOL L1202 6
HET PO4 H 502 5
HET GOL A1201 6
HET PO4 B 501 5
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 9 HOH *256(H2 O)
HELIX 1 1 GLU L 79 VAL L 83 5 5
HELIX 2 2 ASN H 28 THR H 32 5 5
HELIX 3 3 PRO H 61 GLN H 64 5 4
HELIX 4 4 THR H 73 SER H 75 5 3
HELIX 5 5 THR H 83 THR H 87 5 5
HELIX 6 6 GLU A 79 VAL A 83 5 5
HELIX 7 7 ASN B 28 THR B 32 5 5
HELIX 8 8 PRO B 61 GLN B 64 5 4
HELIX 9 9 THR B 73 SER B 75 5 3
HELIX 10 10 THR B 83 THR B 87 5 5
SHEET 1 A 4 LEU L 4 SER L 7 0
SHEET 2 A 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 A 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O ILE L 74
SHEET 1 B 5 ASN L 53 LEU L 54 0
SHEET 2 B 5 PRO L 44 TYR L 49 -1 N TYR L 49 O ASN L 53
SHEET 3 B 5 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45
SHEET 4 B 5 ALA L 84 GLN L 90 -1 O THR L 85 N GLN L 38
SHEET 5 B 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 C 6 ASN L 53 LEU L 54 0
SHEET 2 C 6 PRO L 44 TYR L 49 -1 N TYR L 49 O ASN L 53
SHEET 3 C 6 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45
SHEET 4 C 6 ALA L 84 GLN L 90 -1 O THR L 85 N GLN L 38
SHEET 5 C 6 THR L 102 ILE L 106 -1 O LEU L 104 N ALA L 84
SHEET 6 C 6 SER L 10 VAL L 13 1 N LEU L 11 O LYS L 103
SHEET 1 D 1 VAL L 30 GLY L 31 0
SHEET 1 E 4 GLN H 3 GLN H 6 0
SHEET 2 E 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5
SHEET 3 E 4 THR H 77 LEU H 82 -1 O LEU H 80 N LEU H 20
SHEET 4 E 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79
SHEET 1 F 6 GLU H 10 VAL H 12 0
SHEET 2 F 6 THR H 107 VAL H 111 1 O SER H 108 N GLU H 10
SHEET 3 F 6 ALA H 88 PHE H 95 -1 N ALA H 88 O VAL H 109
SHEET 4 F 6 TYR H 33 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 F 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34
SHEET 6 F 6 SER H 57 TYR H 59 -1 O LYS H 58 N ARG H 50
SHEET 1 G 4 LEU A 4 SER A 7 0
SHEET 2 G 4 ALA A 19 ALA A 25 -1 O ARG A 24 N THR A 5
SHEET 3 G 4 ASP A 70 ILE A 75 -1 O LEU A 73 N MET A 21
SHEET 4 G 4 PHE A 62 THR A 65 -1 N SER A 63 O ILE A 74
SHEET 1 H 5 ASN A 53 LEU A 54 0
SHEET 2 H 5 LYS A 45 TYR A 49 -1 N TYR A 49 O ASN A 53
SHEET 3 H 5 LEU A 33 GLN A 38 -1 N TRP A 35 O LEU A 47
SHEET 4 H 5 ALA A 84 GLN A 90 -1 O GLN A 89 N HIS A 34
SHEET 5 H 5 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90
SHEET 1 I 6 ASN A 53 LEU A 54 0
SHEET 2 I 6 LYS A 45 TYR A 49 -1 N TYR A 49 O ASN A 53
SHEET 3 I 6 LEU A 33 GLN A 38 -1 N TRP A 35 O LEU A 47
SHEET 4 I 6 ALA A 84 GLN A 90 -1 O GLN A 89 N HIS A 34
SHEET 5 I 6 THR A 102 ILE A 106 -1 O LEU A 104 N ALA A 84
SHEET 6 I 6 SER A 10 VAL A 13 1 N LEU A 11 O GLU A 105
SHEET 1 J 4 GLN B 3 GLN B 6 0
SHEET 2 J 4 VAL B 18 SER B 25 -1 O THR B 23 N GLN B 5
SHEET 3 J 4 THR B 77 LEU B 82 -1 O LEU B 80 N LEU B 20
SHEET 4 J 4 ALA B 67 ASP B 72 -1 N ASP B 72 O THR B 77
SHEET 1 K 6 GLU B 10 VAL B 12 0
SHEET 2 K 6 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10
SHEET 3 K 6 ALA B 88 PHE B 95 -1 N ALA B 88 O VAL B 109
SHEET 4 K 6 TYR B 33 GLN B 39 -1 N TYR B 33 O PHE B 95
SHEET 5 K 6 GLU B 46 ILE B 51 -1 O GLU B 46 N LYS B 38
SHEET 6 K 6 SER B 57 TYR B 59 -1 O LYS B 58 N ARG B 50
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.07
SSBOND 2 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 3 CYS A 23 CYS A 88 1555 1555 2.07
SSBOND 4 CYS B 22 CYS B 92 1555 1555 2.05
CISPEP 1 SER L 7 PRO L 8 0 -0.36
CISPEP 2 ASP L 76 PRO L 77 0 1.06
CISPEP 3 ASP L 94 PRO L 95 0 -1.65
CISPEP 4 SER A 7 PRO A 8 0 -9.58
CISPEP 5 ASP A 76 PRO A 77 0 6.46
CISPEP 6 ASP A 94 PRO A 95 0 -8.81
SITE 1 AC1 7 TYR B 33 ARG B 50 ASP B 52 ASN B 54
SITE 2 AC1 7 ASN B 56 HOH B 539 ASN H 28
SITE 1 AC2 6 TYR H 33 ARG H 50 ASP H 52 ASN H 54
SITE 2 AC2 6 ASN H 56 HOH H 542
SITE 1 AC3 7 GLN A 37 LYS A 45 PHE A 62 ASP A 81
SITE 2 AC3 7 ASP A 82 HOH A1207 HOH A1237
SITE 1 AC4 5 GLY L 66 SER L 67 ARG L 68 THR L 69
SITE 2 AC4 5 ASP L 70
CRYST1 61.774 75.033 63.105 90.00 94.82 90.00 P 1 21 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 0.016188 0.000000 0.001365 0.00000
SCALE2 0.000000 0.013327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015903 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
