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HEADER HYDROLASE 01-NOV-25 9XHM
TITLE CRYSTAL STRUCTURE OF ACVB FROM AGROBACTERIUM TUMEFACIENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACVB;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: THE SEQUENCE ALSO FOUR ADDITIONAL RESIDUES (GLY-PRO-
COMPND 6 HIS-MET) DERIVED FROM THE EXPRESSION TAG AT THE N TERMINUS.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS;
SOURCE 3 ORGANISM_TAXID: 358;
SOURCE 4 STRAIN: NBRC15193;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C43
KEYWDS LYSYL-PHOSPHATIDYLGLYCEROL HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HOSHI,Y.WATANABE
REVDAT 1 15-APR-26 9XHM 0
JRNL AUTH M.HOSHI,Y.WATANABE
JRNL TITL STRUCTURAL BASIS OF SUBSTRATE RECOGNITION AND MEMBRANE
JRNL TITL 2 ASSOCIATION BY THE BACTERIAL LYSYL-PHOSPHATIDYLGLYCEROL
JRNL TITL 3 HYDROLASE ACVB
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 22037
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 1084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.6000 - 6.2600 0.99 2647 136 0.2052 0.2552
REMARK 3 2 6.2600 - 4.9700 0.99 2601 159 0.2187 0.2780
REMARK 3 3 4.9700 - 4.3400 0.99 2676 114 0.1812 0.2074
REMARK 3 4 4.3400 - 3.9400 0.99 2599 153 0.2128 0.2954
REMARK 3 5 3.9400 - 3.6600 0.99 2615 131 0.2458 0.3044
REMARK 3 6 3.6600 - 3.4500 0.98 2635 140 0.2484 0.3075
REMARK 3 7 3.4500 - 3.2700 0.98 2590 121 0.2876 0.2910
REMARK 3 8 3.2700 - 3.1300 0.97 2590 130 0.3415 0.4241
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.880
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 6294
REMARK 3 ANGLE : 0.533 8571
REMARK 3 CHIRALITY : 0.044 1029
REMARK 3 PLANARITY : 0.007 1105
REMARK 3 DIHEDRAL : 9.704 890
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9XHM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-25.
REMARK 100 THE DEPOSITION ID IS D_1300065407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-22
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 : SPRING-8
REMARK 200 BEAMLINE : BL32XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43700
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.130
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12600
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.99400
REMARK 200 FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M SODIUM MALONATE (PH 7.0), VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 21
REMARK 465 PRO A 22
REMARK 465 HIS A 23
REMARK 465 MET A 24
REMARK 465 GLN A 25
REMARK 465 ASP A 26
REMARK 465 LYS A 27
REMARK 465 PRO A 28
REMARK 465 ALA A 115
REMARK 465 GLY A 116
REMARK 465 THR A 117
REMARK 465 GLY A 118
REMARK 465 GLY B 21
REMARK 465 PRO B 22
REMARK 465 HIS B 23
REMARK 465 MET B 24
REMARK 465 GLN B 25
REMARK 465 ASP B 26
REMARK 465 LYS B 27
REMARK 465 PRO B 28
REMARK 465 THR B 114
REMARK 465 ALA B 115
REMARK 465 GLY B 116
REMARK 465 THR B 117
REMARK 465 GLY B 118
REMARK 465 ALA B 382
REMARK 465 GLY B 383
REMARK 465 GLU B 384
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 A 62 CG CD OE1 OE2
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 LYS A 69 CG CD CE NZ
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 ASP A 93 CG OD1 OD2
REMARK 470 ASP A 94 CG OD1 OD2
REMARK 470 GLN A 112 CG CD OE1 NE2
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 LYS A 163 CG CD CE NZ
REMARK 470 ASP A 175 CG OD1 OD2
REMARK 470 ASP A 198 CG OD1 OD2
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 ASN A 246 CG OD1 ND2
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 ASP A 271 CG OD1 OD2
REMARK 470 GLU A 279 CG CD OE1 OE2
REMARK 470 ASP A 306 CG OD1 OD2
REMARK 470 LYS A 308 CG CD CE NZ
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 ARG A 352 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 368 CG CD OE1 OE2
REMARK 470 LYS A 386 CG CD CE NZ
REMARK 470 HIS A 433 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 456 CG CD CE NZ
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 LYS B 69 CG CD CE NZ
REMARK 470 GLU B 73 CG CD OE1 OE2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 ASP B 93 CG OD1 OD2
REMARK 470 ASP B 94 CG OD1 OD2
REMARK 470 ASP B 103 CG OD1 OD2
REMARK 470 GLU B 149 CG CD OE1 OE2
REMARK 470 VAL B 174 CG1 CG2
REMARK 470 ASP B 175 CG OD1 OD2
REMARK 470 ASP B 184 CG OD1 OD2
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 GLU B 228 CG CD OE1 OE2
REMARK 470 ASP B 236 CG OD1 OD2
REMARK 470 GLU B 256 CG CD OE1 OE2
REMARK 470 LYS B 287 CG CD CE NZ
REMARK 470 ASP B 306 CG OD1 OD2
REMARK 470 LYS B 308 CG CD CE NZ
REMARK 470 ASP B 351 CG OD1 OD2
REMARK 470 GLU B 368 CG CD OE1 OE2
REMARK 470 LYS B 386 CG CD CE NZ
REMARK 470 ASP B 398 CG OD1 OD2
REMARK 470 GLU B 409 CG CD OE1 OE2
REMARK 470 LYS B 420 CG CD CE NZ
REMARK 470 GLU B 430 CG CD OE1 OE2
REMARK 470 HIS B 433 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS B 130 O GLY B 158 2.09
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 GLU A 149 148.30 -170.16
REMARK 500 PRO A 197 -4.56 -56.63
REMARK 500 ARG A 275 -169.15 -102.92
REMARK 500 SER A 336 -112.54 59.33
REMARK 500 PHE A 435 -134.66 63.11
REMARK 500 GLU A 437 17.05 58.59
REMARK 500 ARG B 275 -167.08 -118.47
REMARK 500 SER B 336 -106.88 52.96
REMARK 500 PHE B 435 -145.60 63.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 148 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9XHM A 21 456 PDB 9XHM 9XHM 21 456
DBREF 9XHM B 21 456 PDB 9XHM 9XHM 21 456
SEQRES 1 A 436 GLY PRO HIS MET GLN ASP LYS PRO ALA TYR GLU THR GLY
SEQRES 2 A 436 MET ILE PRO ALA ASP HIS ILE MET VAL PRO ASP GLY ASP
SEQRES 3 A 436 ILE GLN ALA SER ILE PHE LEU ILE SER ASP ALA ASN GLY
SEQRES 4 A 436 TRP THR GLU ALA ASP GLU THR ARG ALA LYS ALA LEU VAL
SEQRES 5 A 436 GLU LYS GLY ALA ALA VAL VAL GLY ILE ASP PHE LYS GLU
SEQRES 6 A 436 TYR LEU LYS ALA LEU GLU ALA ASP ASP ASP GLU CYS ILE
SEQRES 7 A 436 TYR MET ILE SER ASP ILE GLU SER LEU SER GLN GLN ILE
SEQRES 8 A 436 GLN ARG THR ALA GLY THR GLY SER TYR ARG LEU PRO ILE
SEQRES 9 A 436 VAL THR GLY ILE GLY LYS GLY GLY THR LEU ALA LEU ALA
SEQRES 10 A 436 MET ILE ALA GLN SER PRO VAL SER THR VAL ARG GLU ALA
SEQRES 11 A 436 VAL ALA VAL ASP PRO LYS ALA GLY LEU PRO LEU GLU LYS
SEQRES 12 A 436 ILE LEU CYS THR PRO ALA THR LYS ASP LYS VAL ASP GLY
SEQRES 13 A 436 GLU THR LEU TYR GLY LEU THR ASP GLY ALA LEU PRO ALA
SEQRES 14 A 436 PRO VAL SER VAL ILE PHE THR PRO ASP ALA ASP GLN LYS
SEQRES 15 A 436 GLY ARG ASP HIS VAL ASN ALA LEU VAL LYS LEU HIS SER
SEQRES 16 A 436 ASP ILE GLU VAL THR ASP VAL THR ASP LYS ALA ASP GLU
SEQRES 17 A 436 VAL LEU THR GLN THR LEU SER ASP LYS VAL ASP ALA ALA
SEQRES 18 A 436 GLY ASP SER GLY ASN PRO LEU GLY LEU PRO ILE THR VAL
SEQRES 19 A 436 LEU GLU ALA LYS PRO VAL MET ASP THR MET ALA VAL ILE
SEQRES 20 A 436 TYR SER GLY ASP GLY GLY TRP ARG ASP LEU ASP GLU GLU
SEQRES 21 A 436 VAL GLY SER ALA LEU GLN LYS GLN GLY VAL PRO VAL ILE
SEQRES 22 A 436 GLY VAL ASP ALA LEU ARG TYR PHE TRP LYS GLU LYS ASP
SEQRES 23 A 436 PRO LYS GLU VAL ALA GLY ASP LEU ALA ARG ILE ILE ASP
SEQRES 24 A 436 THR TYR ARG LYS GLU TRP GLU VAL LYS ASN VAL VAL LEU
SEQRES 25 A 436 ILE GLY TYR SER PHE GLY ALA ASP ILE ILE PRO ALA THR
SEQRES 26 A 436 TYR ASN LEU LEU PRO ASP ARG VAL LYS SER SER VAL ALA
SEQRES 27 A 436 GLN LEU SER LEU LEU GLY LEU SER ASN GLU VAL ASP PHE
SEQRES 28 A 436 GLU ILE SER VAL GLN GLY TRP LEU GLY VAL ALA GLY GLU
SEQRES 29 A 436 GLY LYS GLY GLY LYS THR VAL ASP ASP ILE ALA LYS ILE
SEQRES 30 A 436 ASP PRO LYS LEU VAL GLN CYS VAL TYR GLY THR GLU GLU
SEQRES 31 A 436 GLU ASP GLU ASP PRO CYS PRO GLY LEU LYS ALA LYS GLY
SEQRES 32 A 436 VAL GLU THR ILE GLY ILE GLU GLY GLY HIS HIS PHE ASP
SEQRES 33 A 436 GLU ASP TYR GLU ALA LEU ALA LYS ARG ILE VAL THR SER
SEQRES 34 A 436 LEU LYS THR ARG LEU ALA LYS
SEQRES 1 B 436 GLY PRO HIS MET GLN ASP LYS PRO ALA TYR GLU THR GLY
SEQRES 2 B 436 MET ILE PRO ALA ASP HIS ILE MET VAL PRO ASP GLY ASP
SEQRES 3 B 436 ILE GLN ALA SER ILE PHE LEU ILE SER ASP ALA ASN GLY
SEQRES 4 B 436 TRP THR GLU ALA ASP GLU THR ARG ALA LYS ALA LEU VAL
SEQRES 5 B 436 GLU LYS GLY ALA ALA VAL VAL GLY ILE ASP PHE LYS GLU
SEQRES 6 B 436 TYR LEU LYS ALA LEU GLU ALA ASP ASP ASP GLU CYS ILE
SEQRES 7 B 436 TYR MET ILE SER ASP ILE GLU SER LEU SER GLN GLN ILE
SEQRES 8 B 436 GLN ARG THR ALA GLY THR GLY SER TYR ARG LEU PRO ILE
SEQRES 9 B 436 VAL THR GLY ILE GLY LYS GLY GLY THR LEU ALA LEU ALA
SEQRES 10 B 436 MET ILE ALA GLN SER PRO VAL SER THR VAL ARG GLU ALA
SEQRES 11 B 436 VAL ALA VAL ASP PRO LYS ALA GLY LEU PRO LEU GLU LYS
SEQRES 12 B 436 ILE LEU CYS THR PRO ALA THR LYS ASP LYS VAL ASP GLY
SEQRES 13 B 436 GLU THR LEU TYR GLY LEU THR ASP GLY ALA LEU PRO ALA
SEQRES 14 B 436 PRO VAL SER VAL ILE PHE THR PRO ASP ALA ASP GLN LYS
SEQRES 15 B 436 GLY ARG ASP HIS VAL ASN ALA LEU VAL LYS LEU HIS SER
SEQRES 16 B 436 ASP ILE GLU VAL THR ASP VAL THR ASP LYS ALA ASP GLU
SEQRES 17 B 436 VAL LEU THR GLN THR LEU SER ASP LYS VAL ASP ALA ALA
SEQRES 18 B 436 GLY ASP SER GLY ASN PRO LEU GLY LEU PRO ILE THR VAL
SEQRES 19 B 436 LEU GLU ALA LYS PRO VAL MET ASP THR MET ALA VAL ILE
SEQRES 20 B 436 TYR SER GLY ASP GLY GLY TRP ARG ASP LEU ASP GLU GLU
SEQRES 21 B 436 VAL GLY SER ALA LEU GLN LYS GLN GLY VAL PRO VAL ILE
SEQRES 22 B 436 GLY VAL ASP ALA LEU ARG TYR PHE TRP LYS GLU LYS ASP
SEQRES 23 B 436 PRO LYS GLU VAL ALA GLY ASP LEU ALA ARG ILE ILE ASP
SEQRES 24 B 436 THR TYR ARG LYS GLU TRP GLU VAL LYS ASN VAL VAL LEU
SEQRES 25 B 436 ILE GLY TYR SER PHE GLY ALA ASP ILE ILE PRO ALA THR
SEQRES 26 B 436 TYR ASN LEU LEU PRO ASP ARG VAL LYS SER SER VAL ALA
SEQRES 27 B 436 GLN LEU SER LEU LEU GLY LEU SER ASN GLU VAL ASP PHE
SEQRES 28 B 436 GLU ILE SER VAL GLN GLY TRP LEU GLY VAL ALA GLY GLU
SEQRES 29 B 436 GLY LYS GLY GLY LYS THR VAL ASP ASP ILE ALA LYS ILE
SEQRES 30 B 436 ASP PRO LYS LEU VAL GLN CYS VAL TYR GLY THR GLU GLU
SEQRES 31 B 436 GLU ASP GLU ASP PRO CYS PRO GLY LEU LYS ALA LYS GLY
SEQRES 32 B 436 VAL GLU THR ILE GLY ILE GLU GLY GLY HIS HIS PHE ASP
SEQRES 33 B 436 GLU ASP TYR GLU ALA LEU ALA LYS ARG ILE VAL THR SER
SEQRES 34 B 436 LEU LYS THR ARG LEU ALA LYS
HET EDO A 501 4
HET EDO B 501 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
HELIX 1 AA1 THR A 61 GLU A 73 1 13
HELIX 2 AA2 ASP A 82 ALA A 92 1 11
HELIX 3 AA3 MET A 100 THR A 114 1 15
HELIX 4 AA4 GLY A 129 ALA A 140 1 12
HELIX 5 AA5 ASP A 200 HIS A 214 1 15
HELIX 6 AA6 LYS A 225 GLY A 242 1 18
HELIX 7 AA7 ARG A 275 GLN A 288 1 14
HELIX 8 AA8 ASP A 296 PHE A 301 1 6
HELIX 9 AA9 ASP A 306 TRP A 325 1 20
HELIX 10 AB1 SER A 336 LEU A 349 1 14
HELIX 11 AB2 PRO A 350 SER A 355 1 6
HELIX 12 AB3 LYS A 389 LYS A 396 1 8
HELIX 13 AB4 GLU A 409 GLU A 411 5 3
HELIX 14 AB5 LEU A 419 GLY A 423 5 5
HELIX 15 AB6 ASP A 438 ALA A 455 1 18
HELIX 16 AB7 THR B 61 GLU B 73 1 13
HELIX 17 AB8 ASP B 82 ALA B 92 1 11
HELIX 18 AB9 TYR B 99 ARG B 113 1 15
HELIX 19 AC1 GLY B 129 ALA B 140 1 12
HELIX 20 AC2 ASP B 200 HIS B 214 1 15
HELIX 21 AC3 LYS B 225 ASP B 243 1 19
HELIX 22 AC4 ARG B 275 GLN B 288 1 14
HELIX 23 AC5 ASP B 296 PHE B 301 1 6
HELIX 24 AC6 ASP B 306 GLU B 326 1 21
HELIX 25 AC7 SER B 336 LEU B 348 1 13
HELIX 26 AC8 PRO B 350 SER B 356 1 7
HELIX 27 AC9 GLN B 376 GLY B 380 5 5
HELIX 28 AD1 LYS B 389 ALA B 395 1 7
HELIX 29 AD2 CYS B 416 GLY B 423 5 8
HELIX 30 AD3 ASP B 438 LYS B 456 1 19
SHEET 1 AA1 7 HIS A 39 MET A 41 0
SHEET 2 AA1 7 ALA A 76 ILE A 81 -1 O GLY A 80 N HIS A 39
SHEET 3 AA1 7 ALA A 49 ILE A 54 1 N LEU A 53 O ILE A 81
SHEET 4 AA1 7 PRO A 123 ILE A 128 1 O ILE A 124 N PHE A 52
SHEET 5 AA1 7 GLU A 149 VAL A 153 1 O GLU A 149 N VAL A 125
SHEET 6 AA1 7 VAL A 191 PHE A 195 1 O ILE A 194 N ALA A 152
SHEET 7 AA1 7 GLU A 218 ASP A 221 1 O THR A 220 N PHE A 195
SHEET 1 AA2 2 LYS A 173 VAL A 174 0
SHEET 2 AA2 2 GLU A 177 THR A 178 -1 O GLU A 177 N VAL A 174
SHEET 1 AA3 7 ILE A 252 LEU A 255 0
SHEET 2 AA3 7 VAL A 292 VAL A 295 -1 O VAL A 292 N LEU A 255
SHEET 3 AA3 7 THR A 263 TYR A 268 1 N ILE A 267 O VAL A 295
SHEET 4 AA3 7 ASN A 329 TYR A 335 1 O ILE A 333 N VAL A 266
SHEET 5 AA3 7 VAL A 357 LEU A 363 1 O SER A 361 N LEU A 332
SHEET 6 AA3 7 VAL A 402 GLY A 407 1 O GLN A 403 N LEU A 360
SHEET 7 AA3 7 GLU A 425 ILE A 429 1 O ILE A 427 N TYR A 406
SHEET 1 AA4 7 ILE B 40 MET B 41 0
SHEET 2 AA4 7 ALA B 76 VAL B 79 -1 O VAL B 78 N MET B 41
SHEET 3 AA4 7 ALA B 49 ILE B 54 1 N ILE B 51 O VAL B 79
SHEET 4 AA4 7 PRO B 123 ILE B 128 1 O ILE B 124 N SER B 50
SHEET 5 AA4 7 GLU B 149 VAL B 153 1 O GLU B 149 N VAL B 125
SHEET 6 AA4 7 VAL B 191 PHE B 195 1 O SER B 192 N ALA B 150
SHEET 7 AA4 7 GLU B 218 ASP B 221 1 O GLU B 218 N VAL B 193
SHEET 1 AA5 7 ILE B 252 LEU B 255 0
SHEET 2 AA5 7 VAL B 292 VAL B 295 -1 O VAL B 292 N LEU B 255
SHEET 3 AA5 7 THR B 263 TYR B 268 1 N ILE B 267 O VAL B 295
SHEET 4 AA5 7 ASN B 329 TYR B 335 1 O ILE B 333 N VAL B 266
SHEET 5 AA5 7 VAL B 357 LEU B 363 1 O SER B 361 N LEU B 332
SHEET 6 AA5 7 VAL B 402 GLY B 407 1 O GLN B 403 N LEU B 360
SHEET 7 AA5 7 GLU B 425 ILE B 429 1 O ILE B 427 N TYR B 406
SSBOND 1 CYS A 97 CYS A 166 1555 1555 2.03
SSBOND 2 CYS A 404 CYS A 416 1555 1555 2.02
SSBOND 3 CYS B 97 CYS B 166 1555 1555 2.03
SSBOND 4 CYS B 404 CYS B 416 1555 1555 2.03
CRYST1 66.565 76.273 77.219 113.86 98.35 106.78 P 1 2
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 0.015023 0.004530 0.004921 0.00000
SCALE2 0.000000 0.013694 0.007317 0.00000
SCALE3 0.000000 0.000000 0.014840 0.00000
TER 3106 LYS A 456
TER 6189 LYS B 456
MASTER 333 0 2 30 30 0 0 6 6195 2 16 68
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