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HEADER BIOSYNTHETIC PROTEIN 17-DEC-19 6VAP
TITLE STRUCTURE OF THE TYPE II THIOESTERASE BORB FROM THE BORRELIDIN
TITLE 2 BIOSYNTHETIC CLUSTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. WAC02707;
SOURCE 3 ORGANISM_TAXID: 2487417;
SOURCE 4 GENE: EF919_13485;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.PEREIRA,S.C.CURRAN,M.-J.BALUYOT,J.LAKE,H.PUTZ,D.ROSENBURG,
AUTHOR 2 J.KEASLING,P.D.ADAMS
REVDAT 1 06-MAY-20 6VAP 0
JRNL AUTH S.C.CURRAN,J.H.PEREIRA,M.J.BALUYOT,J.LAKE,H.PUETZ,
JRNL AUTH 2 D.J.ROSENBURG,P.ADAMS,J.D.KEASLING
JRNL TITL STRUCTURE AND FUNCTION OF BORB, THE TYPE II THIOESTERASE
JRNL TITL 2 FROM THE BORRELIDIN BIOSYNTHETIC GENE CLUSTER.
JRNL REF BIOCHEMISTRY 2020
JRNL REFN ISSN 0006-2960
JRNL PMID 32250597
JRNL DOI 10.1021/ACS.BIOCHEM.0C00126
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 37938
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1883
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 46.1800 - 4.5400 1.00 2939 149 0.1791 0.2162
REMARK 3 2 4.5400 - 3.6000 1.00 2830 159 0.1649 0.1842
REMARK 3 3 3.6000 - 3.1500 1.00 2824 135 0.1774 0.2394
REMARK 3 4 3.1500 - 2.8600 1.00 2805 142 0.1933 0.2175
REMARK 3 5 2.8600 - 2.6500 1.00 2742 170 0.2040 0.2525
REMARK 3 6 2.6500 - 2.5000 1.00 2805 126 0.1967 0.2262
REMARK 3 7 2.5000 - 2.3700 1.00 2762 138 0.2004 0.2201
REMARK 3 8 2.3700 - 2.2700 0.99 2737 145 0.2250 0.3020
REMARK 3 9 2.2700 - 2.1800 0.96 2656 145 0.4217 0.4858
REMARK 3 10 2.1800 - 2.1100 0.99 2737 147 0.2366 0.2956
REMARK 3 11 2.1100 - 2.0400 0.99 2765 136 0.2535 0.2757
REMARK 3 12 2.0400 - 1.9800 0.99 2733 147 0.2724 0.3382
REMARK 3 13 1.9800 - 1.9300 0.99 2720 144 0.3923 0.4514
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) : 0.302
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.312
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.68
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 : 0.011 3846
REMARK 3 ANGLE : 0.983 5240
REMARK 3 CHIRALITY : 0.055 575
REMARK 3 PLANARITY : 0.008 698
REMARK 3 DIHEDRAL : 19.777 1419
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 6VAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1000246099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39997
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 46.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 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: PHENIX
REMARK 200 STARTING MODEL: 3FLA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M HEPES
REMARK 280 PH 7.5, 22% POLY (ACRYLIC ACID SODIUM SALT) 5100, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.07000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.07000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.18000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.18000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.07000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.18000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.07000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.18000
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 338 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 377 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 HIS A 2
REMARK 465 MET A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 ASN A 7
REMARK 465 THR A 152
REMARK 465 LEU A 153
REMARK 465 ASP A 154
REMARK 465 GLY A 155
REMARK 465 THR A 156
REMARK 465 ALA A 157
REMARK 465 GLU A 158
REMARK 465 GLN A 159
REMARK 465 VAL A 160
REMARK 465 PHE A 161
REMARK 465 HIS A 162
REMARK 465 ASP A 163
REMARK 465 GLU A 164
REMARK 465 GLU A 165
REMARK 465 ALA A 256
REMARK 465 PRO A 257
REMARK 465 GLY A 258
REMARK 465 ASP A 259
REMARK 465 ARG A 260
REMARK 465 SER A 261
REMARK 465 GLY A 262
REMARK 465 LEU A 263
REMARK 465 THR A 264
REMARK 465 ARG A 265
REMARK 465 GLU A 266
REMARK 465 GLY B 1
REMARK 465 HIS B 2
REMARK 465 MET B 3
REMARK 465 THR B 4
REMARK 465 GLY B 5
REMARK 465 THR B 6
REMARK 465 THR B 252
REMARK 465 CYS B 253
REMARK 465 SER B 254
REMARK 465 ARG B 255
REMARK 465 ALA B 256
REMARK 465 PRO B 257
REMARK 465 GLY B 258
REMARK 465 ASP B 259
REMARK 465 ARG B 260
REMARK 465 SER B 261
REMARK 465 GLY B 262
REMARK 465 LEU B 263
REMARK 465 THR B 264
REMARK 465 ARG B 265
REMARK 465 GLU B 266
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 CYS A 194 C PRO A 195 N 0.161
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 GLN A 62 -120.63 52.71
REMARK 500 SER A 98 -121.67 56.23
REMARK 500 GLN B 62 -130.21 54.40
REMARK 500 SER B 98 -125.49 52.05
REMARK 500 LEU B 153 -38.76 65.68
REMARK 500 ALA B 157 -157.39 -105.10
REMARK 500 GLU B 158 56.21 -113.16
REMARK 500 GLN B 159 92.11 103.09
REMARK 500 VAL B 160 -66.76 -104.02
REMARK 500 PHE B 161 72.54 -102.60
REMARK 500 ASP B 163 74.80 -68.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 476 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A 477 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 478 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH B 488 DISTANCE = 6.39 ANGSTROMS
DBREF1 6VAP A 3 266 UNP A0A454WD44_9ACTN
DBREF2 6VAP A A0A454WD44 1 264
DBREF1 6VAP B 3 266 UNP A0A454WD44_9ACTN
DBREF2 6VAP B A0A454WD44 1 264
SEQADV 6VAP GLY A 1 UNP A0A454WD4 EXPRESSION TAG
SEQADV 6VAP HIS A 2 UNP A0A454WD4 EXPRESSION TAG
SEQADV 6VAP GLY B 1 UNP A0A454WD4 EXPRESSION TAG
SEQADV 6VAP HIS B 2 UNP A0A454WD4 EXPRESSION TAG
SEQRES 1 A 266 GLY HIS MET THR GLY THR ASN THR HIS SER ASP VAL TRP
SEQRES 2 A 266 ILE ARG GLN TYR ARG PRO ALA HIS PRO THR ALA PRO GLN
SEQRES 3 A 266 LEU ILE CYS LEU PRO HIS ALA GLY GLY SER ALA THR PHE
SEQRES 4 A 266 TYR HIS PRO VAL ALA ALA ALA LEU ALA PRO ARG CYS ASP
SEQRES 5 A 266 VAL LEU ALA VAL GLN TYR PRO GLY ARG GLN ASP ARG ARG
SEQRES 6 A 266 ALA GLU LYS PRO LEU GLU ASP ILE ASP GLU LEU ALA ASN
SEQRES 7 A 266 GLN LEU PHE PRO VAL LEU ARG ALA ARG VAL HIS GLN PRO
SEQRES 8 A 266 VAL ALA LEU PHE GLY HIS SER MET GLY ALA THR LEU ALA
SEQRES 9 A 266 PHE GLU LEU ALA ARG ARG PHE GLU SER ALA GLY ILE SER
SEQRES 10 A 266 LEU GLU ALA LEU LEU VAL SER ALA ARG PRO ALA PRO SER
SEQRES 11 A 266 ARG GLN ARG THR GLY GLY THR VAL HIS LEU LEU SER ASP
SEQRES 12 A 266 GLU GLU LEU VAL ALA GLU LEU ARG THR LEU ASP GLY THR
SEQRES 13 A 266 ALA GLU GLN VAL PHE HIS ASP GLU GLU LEU VAL ARG MET
SEQRES 14 A 266 ALA LEU PRO ALA ILE ARG GLY ASP TYR ARG ALA ALA GLU
SEQRES 15 A 266 THR TYR ARG TYR ARG PRO GLY PRO LYS LEU ARG CYS PRO
SEQRES 16 A 266 ILE HIS ALA LEU THR GLY ASP ASP ASP PRO MET VAL THR
SEQRES 17 A 266 PRO VAL GLU ALA ARG ALA TRP SER GLU HIS THR ASP GLY
SEQRES 18 A 266 PRO PHE THR LEU ASP THR PHE ALA GLY GLY HIS PHE TYR
SEQRES 19 A 266 LEU LEU GLU HIS ARG ASP ALA ILE LEU GLY ILE ILE ALA
SEQRES 20 A 266 GLU HIS LEU ARG THR CYS SER ARG ALA PRO GLY ASP ARG
SEQRES 21 A 266 SER GLY LEU THR ARG GLU
SEQRES 1 B 266 GLY HIS MET THR GLY THR ASN THR HIS SER ASP VAL TRP
SEQRES 2 B 266 ILE ARG GLN TYR ARG PRO ALA HIS PRO THR ALA PRO GLN
SEQRES 3 B 266 LEU ILE CYS LEU PRO HIS ALA GLY GLY SER ALA THR PHE
SEQRES 4 B 266 TYR HIS PRO VAL ALA ALA ALA LEU ALA PRO ARG CYS ASP
SEQRES 5 B 266 VAL LEU ALA VAL GLN TYR PRO GLY ARG GLN ASP ARG ARG
SEQRES 6 B 266 ALA GLU LYS PRO LEU GLU ASP ILE ASP GLU LEU ALA ASN
SEQRES 7 B 266 GLN LEU PHE PRO VAL LEU ARG ALA ARG VAL HIS GLN PRO
SEQRES 8 B 266 VAL ALA LEU PHE GLY HIS SER MET GLY ALA THR LEU ALA
SEQRES 9 B 266 PHE GLU LEU ALA ARG ARG PHE GLU SER ALA GLY ILE SER
SEQRES 10 B 266 LEU GLU ALA LEU LEU VAL SER ALA ARG PRO ALA PRO SER
SEQRES 11 B 266 ARG GLN ARG THR GLY GLY THR VAL HIS LEU LEU SER ASP
SEQRES 12 B 266 GLU GLU LEU VAL ALA GLU LEU ARG THR LEU ASP GLY THR
SEQRES 13 B 266 ALA GLU GLN VAL PHE HIS ASP GLU GLU LEU VAL ARG MET
SEQRES 14 B 266 ALA LEU PRO ALA ILE ARG GLY ASP TYR ARG ALA ALA GLU
SEQRES 15 B 266 THR TYR ARG TYR ARG PRO GLY PRO LYS LEU ARG CYS PRO
SEQRES 16 B 266 ILE HIS ALA LEU THR GLY ASP ASP ASP PRO MET VAL THR
SEQRES 17 B 266 PRO VAL GLU ALA ARG ALA TRP SER GLU HIS THR ASP GLY
SEQRES 18 B 266 PRO PHE THR LEU ASP THR PHE ALA GLY GLY HIS PHE TYR
SEQRES 19 B 266 LEU LEU GLU HIS ARG ASP ALA ILE LEU GLY ILE ILE ALA
SEQRES 20 B 266 GLU HIS LEU ARG THR CYS SER ARG ALA PRO GLY ASP ARG
SEQRES 21 B 266 SER GLY LEU THR ARG GLU
FORMUL 3 HOH *366(H2 O)
HELIX 1 AA1 SER A 36 PHE A 39 5 4
HELIX 2 AA2 TYR A 40 ALA A 48 1 9
HELIX 3 AA3 ARG A 61 ARG A 65 5 5
HELIX 4 AA4 ASP A 72 VAL A 88 1 17
HELIX 5 AA5 SER A 98 ALA A 114 1 17
HELIX 6 AA6 ALA A 128 GLN A 132 5 5
HELIX 7 AA7 THR A 137 LEU A 141 5 5
HELIX 8 AA8 SER A 142 LEU A 150 1 9
HELIX 9 AA9 VAL A 167 THR A 183 1 17
HELIX 10 AB1 THR A 208 ALA A 214 1 7
HELIX 11 AB2 TRP A 215 THR A 219 5 5
HELIX 12 AB3 PHE A 233 GLU A 237 5 5
HELIX 13 AB4 HIS A 238 ARG A 251 1 14
HELIX 14 AB5 SER B 36 PHE B 39 5 4
HELIX 15 AB6 TYR B 40 ALA B 48 1 9
HELIX 16 AB7 ARG B 61 ARG B 65 5 5
HELIX 17 AB8 ASP B 72 VAL B 88 1 17
HELIX 18 AB9 SER B 98 ALA B 114 1 17
HELIX 19 AC1 ALA B 128 GLN B 132 5 5
HELIX 20 AC2 THR B 137 LEU B 141 5 5
HELIX 21 AC3 SER B 142 GLY B 155 1 14
HELIX 22 AC4 ASP B 163 ALA B 170 1 8
HELIX 23 AC5 ALA B 170 TYR B 184 1 15
HELIX 24 AC6 THR B 208 ALA B 214 1 7
HELIX 25 AC7 TRP B 215 THR B 219 5 5
HELIX 26 AC8 PHE B 233 HIS B 238 1 6
HELIX 27 AC9 HIS B 238 LEU B 250 1 13
SHEET 1 AA1 7 ILE A 14 ARG A 15 0
SHEET 2 AA1 7 ASP A 52 VAL A 56 -1 O ALA A 55 N ARG A 15
SHEET 3 AA1 7 GLN A 26 LEU A 30 1 N LEU A 27 O LEU A 54
SHEET 4 AA1 7 VAL A 92 HIS A 97 1 O PHE A 95 N LEU A 30
SHEET 5 AA1 7 ALA A 120 SER A 124 1 O LEU A 122 N LEU A 94
SHEET 6 AA1 7 ILE A 196 GLY A 201 1 O HIS A 197 N LEU A 121
SHEET 7 AA1 7 PHE A 223 PHE A 228 1 O THR A 224 N ALA A 198
SHEET 1 AA2 7 ILE B 14 ARG B 15 0
SHEET 2 AA2 7 ASP B 52 VAL B 56 -1 O ALA B 55 N ARG B 15
SHEET 3 AA2 7 GLN B 26 LEU B 30 1 N LEU B 27 O LEU B 54
SHEET 4 AA2 7 VAL B 92 HIS B 97 1 O PHE B 95 N ILE B 28
SHEET 5 AA2 7 ALA B 120 SER B 124 1 O LEU B 122 N LEU B 94
SHEET 6 AA2 7 ILE B 196 GLY B 201 1 O HIS B 197 N LEU B 121
SHEET 7 AA2 7 PHE B 223 PHE B 228 1 O THR B 224 N ALA B 198
CISPEP 1 ALA A 48 PRO A 49 0 0.66
CISPEP 2 GLN A 90 PRO A 91 0 1.48
CISPEP 3 ALA B 48 PRO B 49 0 1.39
CISPEP 4 GLN B 90 PRO B 91 0 2.96
CRYST1 72.450 92.360 150.140 90.00 90.00 90.00 C 2 2 21 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 0.013803 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006660 0.00000
TER 3639 ARG A 255
TER 7435 ARG B 251
MASTER 359 0 0 27 14 0 0 6 4113 2 0 42
END |