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HEADER HYDROLASE 23-AUG-01 1JU4
TITLE BACTERIAL COCAINE ESTERASE COMPLEX WITH PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCAINE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. MB1;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.LARSEN,J.M.TURNER,J.STEVENS,S.J.ROSSER,A.BASRAN,
AUTHOR 2 R.A.LERNER,N.C.BRUCE,I.A.WILSON
REVDAT 2 09-JAN-02 1JU4 1 AUTHOR
REVDAT 1 21-DEC-01 1JU4 0
JRNL AUTH N.A.LARSEN,J.M.TURNER,J.STEVENS,S.J.ROSSER,
JRNL AUTH 2 A.BASRAN,R.A.LERNER,N.C.BRUCE,I.A.WILSON
JRNL TITL CRYSTAL STRUCTURE OF A BACTERIAL COCAINE ESTERASE
JRNL REF NAT.STRUCT.BIOL. V. 9 17 2002
JRNL REFN ASTM NSBIEW US ISSN 1072-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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) : 0.190
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4783
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 95669
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 : 4351
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 436
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) : 0.008
REMARK 3 ANGLE DISTANCES (A) : 2.100
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 1JU4 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-2001.
REMARK 100 THE RCSB ID CODE IS RCSB014187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-2000; 07-JAN-2001
REMARK 200 TEMPERATURE (KELVIN) : 120; 120
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS ; SSRL
REMARK 200 BEAMLINE : 5.0.2; 9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1; 1.07167,1.07198,0.86095
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95669
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE AND ARP/WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM DTT, 10MM TRIS PH 7.5, 25 MM
REMARK 280 NACL, 1.6 M AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,-X+Y,1/6+Z
REMARK 290 6555 X-Y,X,5/6+Z
REMARK 290 7555 Y,X,2/3-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,1/3-Z
REMARK 290 10555 -Y,-X,1/6-Z
REMARK 290 11555 -X+Y,Y,1/2-Z
REMARK 290 12555 X,X-Y,5/6-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 -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 148.14000
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 74.07000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.10500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.03500
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 185.17500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 148.14000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 74.07000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.03500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 111.10500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 185.17500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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 1
REMARK 465 VAL A 2
REMARK 465 ASP A 3
REMARK 465 GLY A 4
REMARK 465 PRO A 575
REMARK 465 LEU A 576
REMARK 465 GLU A 577
REMARK 465 HIS A 578
REMARK 465 HIS A 579
REMARK 465 HIS A 580
REMARK 465 HIS A 581
REMARK 465 HIS A 582
REMARK 465 HIS A 583
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 A 573 CG CD CE NZ
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 151 NE1 TRP A 151 CD1 -0.053
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLN A 236 CB - CG - CD ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG A 293 C - N - CA ANGL. DEV. = 20.3 DEGREES
REMARK 500 ALA A 455 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 ASN A 537 C - N - CA ANGL. DEV. = 19.8 DEGREES
REMARK 500 GLY A 540 C - N - CA ANGL. DEV. = 19.0 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 HIS A 87 -33.47 70.15
REMARK 500 SER A 117 -112.52 55.74
REMARK 500 THR A 371 163.83 66.62
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JU3 RELATED DB: PDB
REMARK 900 BACTERIAL COCAINE ESTERASE COMPLEX WITH TRANSITION STATE
REMARK 900 ANALOG
DBREF 1JU4 A 1 574 GB 7229394 AAF42807 1 574
SEQADV 1JU4 PRO A 575 GB 7229394 CLONING ARTIFACT
SEQADV 1JU4 LEU A 576 GB 7229394 CLONING ARTIFACT
SEQADV 1JU4 GLU A 577 GB 7229394 CLONING ARTIFACT
SEQADV 1JU4 HIS A 578 GB 7229394 HIS TAG
SEQADV 1JU4 HIS A 579 GB 7229394 HIS TAG
SEQADV 1JU4 HIS A 580 GB 7229394 HIS TAG
SEQADV 1JU4 HIS A 581 GB 7229394 HIS TAG
SEQADV 1JU4 HIS A 582 GB 7229394 HIS TAG
SEQADV 1JU4 HIS A 583 GB 7229394 HIS TAG
SEQRES 1 A 583 MET VAL ASP GLY ASN TYR SER VAL ALA SER ASN VAL MET
SEQRES 2 A 583 VAL PRO MET ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU
SEQRES 3 A 583 TYR ARG PRO ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU
SEQRES 4 A 583 VAL ARG ASN PRO TYR ASP LYS PHE ASP VAL PHE ALA TRP
SEQRES 5 A 583 SER THR GLN SER THR ASN TRP LEU GLU PHE VAL ARG ASP
SEQRES 6 A 583 GLY TYR ALA VAL VAL ILE GLN ASP THR ARG GLY LEU PHE
SEQRES 7 A 583 ALA SER GLU GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU
SEQRES 8 A 583 ALA ASP ALA GLU ASP THR LEU SER TRP ILE LEU GLU GLN
SEQRES 9 A 583 ALA TRP CYS ASP GLY ASN VAL GLY MET PHE GLY VAL SER
SEQRES 10 A 583 TYR LEU GLY VAL THR GLN TRP GLN ALA ALA VAL SER GLY
SEQRES 11 A 583 VAL GLY GLY LEU LYS ALA ILE ALA PRO SER MET ALA SER
SEQRES 12 A 583 ALA ASP LEU TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY
SEQRES 13 A 583 ALA LEU SER VAL GLU ALA LEU LEU GLY TRP SER ALA LEU
SEQRES 14 A 583 ILE GLY THR GLY LEU ILE THR SER ARG SER ASP ALA ARG
SEQRES 15 A 583 PRO GLU ASP ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE
SEQRES 16 A 583 LEU ASN ASP VAL ALA GLY ALA ALA SER VAL THR PRO LEU
SEQRES 17 A 583 ALA GLU GLN PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL
SEQRES 18 A 583 ILE ASP GLN VAL VAL ASP HIS PRO ASP ASN ASP GLU SER
SEQRES 19 A 583 TRP GLN SER ILE SER LEU PHE GLU ARG LEU GLY GLY LEU
SEQRES 20 A 583 ALA THR PRO ALA LEU ILE THR ALA GLY TRP TYR ASP GLY
SEQRES 21 A 583 PHE VAL GLY GLU SER LEU ARG THR PHE VAL ALA VAL LYS
SEQRES 22 A 583 ASP ASN ALA ASP ALA ARG LEU VAL VAL GLY PRO TRP SER
SEQRES 23 A 583 HIS SER ASN LEU THR GLY ARG ASN ALA ASP ARG LYS PHE
SEQRES 24 A 583 GLY ILE ALA ALA THR TYR PRO ILE GLN GLU ALA THR THR
SEQRES 25 A 583 MET HIS LYS ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU
SEQRES 26 A 583 THR ASP ALA LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE
SEQRES 27 A 583 VAL MET GLY ILE ASP GLU TRP ARG ASP GLU THR ASP TRP
SEQRES 28 A 583 PRO LEU PRO ASP THR ALA TYR THR PRO PHE TYR LEU GLY
SEQRES 29 A 583 GLY SER GLY ALA ALA ASN THR SER THR GLY GLY GLY THR
SEQRES 30 A 583 LEU SER THR SER ILE SER GLY THR GLU SER ALA ASP THR
SEQRES 31 A 583 TYR LEU TYR ASP PRO ALA ASP PRO VAL PRO SER LEU GLY
SEQRES 32 A 583 GLY THR LEU LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA
SEQRES 33 A 583 ASP GLN ARG PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS
SEQRES 34 A 583 TYR SER THR GLU VAL LEU THR ASP PRO VAL GLU VAL THR
SEQRES 35 A 583 GLY THR VAL SER ALA ARG LEU PHE VAL SER SER SER ALA
SEQRES 36 A 583 VAL ASP THR ASP PHE THR ALA LYS LEU VAL ASP VAL PHE
SEQRES 37 A 583 PRO ASP GLY ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL
SEQRES 38 A 583 ARG MET ARG TYR ARG GLU THR LEU VAL ASN PRO THR LEU
SEQRES 39 A 583 ILE GLU ALA GLY GLU ILE TYR GLU VAL ALA ILE ASP MET
SEQRES 40 A 583 LEU ALA THR SER ASN VAL PHE LEU PRO GLY HIS ARG ILE
SEQRES 41 A 583 MET VAL GLN VAL SER SER SER ASN PHE PRO LYS TYR ASP
SEQRES 42 A 583 ARG ASN SER ASN THR GLY GLY VAL ILE ALA ARG GLU GLN
SEQRES 43 A 583 LEU GLU GLU MET CYS THR ALA VAL ASN ARG ILE HIS ARG
SEQRES 44 A 583 GLY PRO GLU HIS PRO SER HIS ILE VAL LEU PRO ILE ILE
SEQRES 45 A 583 LYS ARG PRO LEU GLU HIS HIS HIS HIS HIS HIS
HET BEZ 1 9
HETNAM BEZ BENZOIC ACID
FORMUL 2 BEZ C7 H6 O2
FORMUL 3 HOH *436(H2 O1)
HELIX 1 1 ASP A 48 THR A 54 1 7
HELIX 2 2 TRP A 59 ASP A 65 1 7
HELIX 3 3 ASP A 89 GLN A 104 1 16
HELIX 4 4 SER A 117 VAL A 128 1 12
HELIX 5 5 SER A 159 ARG A 178 1 20
HELIX 6 6 GLU A 184 ASP A 198 1 15
HELIX 7 7 ASP A 198 ALA A 203 1 6
HELIX 8 8 GLN A 211 ILE A 218 1 8
HELIX 9 9 PRO A 219 GLN A 224 1 6
HELIX 10 10 ASP A 232 SER A 237 1 6
HELIX 11 11 LEU A 240 GLY A 245 1 6
HELIX 12 12 PHE A 261 LYS A 273 1 13
HELIX 13 13 GLY A 300 THR A 304 5 5
HELIX 14 14 PRO A 306 ARG A 323 1 18
HELIX 15 15 GLN A 418 HIS A 422 5 5
HELIX 16 16 ARG A 484 ARG A 486 5 3
HELIX 17 17 VAL A 541 GLU A 545 5 5
HELIX 18 18 GLN A 546 MET A 550 5 5
SHEET 1 A 6 TYR A 6 PRO A 15 0
SHEET 2 A 6 ARG A 21 PRO A 29 -1 O LEU A 22 N VAL A 14
SHEET 3 A 6 ALA A 68 ASP A 73 -1 O VAL A 69 N TYR A 27
SHEET 4 A 6 VAL A 35 ASN A 42 1 N LEU A 38 O VAL A 70
SHEET 5 A 6 CYS A 107 VAL A 116 1 O GLY A 112 N LEU A 39
SHEET 6 A 6 LEU A 134 SER A 140 1 O LYS A 135 N VAL A 111
SHEET 1 B 4 ALA A 251 TYR A 258 0
SHEET 2 B 4 ALA A 278 SER A 286 1 O ARG A 279 N ILE A 253
SHEET 3 B 4 VAL A 335 VAL A 339 1 O PHE A 338 N VAL A 282
SHEET 4 B 4 GLU A 344 GLU A 348 -1 O GLU A 344 N VAL A 339
SHEET 1 C 2 ARG A 293 ASN A 294 0
SHEET 2 C 2 ARG A 297 LYS A 298 -1 O ARG A 297 N ASN A 294
SHEET 1 D 4 TYR A 501 PHE A 514 0
SHEET 2 D 4 VAL A 439 SER A 453 -1 N VAL A 441 O ASN A 512
SHEET 3 D 4 ALA A 553 ARG A 559 0
SHEET 4 D 4 SER A 387 TYR A 393 -1 N SER A 387 O ARG A 559
SHEET 1 E 5 TYR A 501 PHE A 514 0
SHEET 2 E 5 VAL A 439 SER A 453 -1 N VAL A 441 O ASN A 512
SHEET 3 E 5 HIS A 566 ILE A 572 0
SHEET 4 E 5 ALA A 357 GLY A 364 -1 N PHE A 361 O ILE A 567
SHEET 5 E 5 THR A 377 SER A 379 -1 O SER A 379 N TYR A 362
SHEET 1 F 4 LEU A 428 SER A 431 0
SHEET 2 F 4 ARG A 519 SER A 525 -1 O VAL A 522 N TYR A 430
SHEET 3 F 4 ASP A 459 VAL A 467 -1 N THR A 461 O SER A 525
SHEET 4 F 4 ALA A 473 ARG A 482 -1 O ILE A 474 N ASP A 466
CISPEP 1 ALA A 149 PRO A 150 0 6.45
CISPEP 2 THR A 206 PRO A 207 0 -13.22
CISPEP 3 TRP A 351 PRO A 352 0 -11.39
CISPEP 4 PHE A 529 PRO A 530 0 3.04
CRYST1 106.216 106.216 222.210 90.00 90.00 120.00 P 65 2 2 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 0.009415 0.005435 0.000000 0.00000
SCALE2 0.000000 0.010871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004500 0.00000
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