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HEADER HYDROLASE 07-JAN-14 4OB8
TITLE CRYSTAL STRUCTURE OF A NOVEL THERMOSTABLE ESTERASE FROM PSEUDOMONAS
TITLE 2 PUTIDA ECU1011
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-3 DOMAIN PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;
SOURCE 3 ORGANISM_TAXID: 657346;
SOURCE 4 STRAIN: ECU1011;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS A/B HYDROLASE FOLD, ESTERASE, HSL-LIKE FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DOU,X.D.KONG,B.D.MA,J.H.XU,J.H.ZHOU
REVDAT 1 23-JUL-14 4OB8 0
JRNL AUTH S.DOU,X.D.KONG,B.D.MA,Q.CHEN,J.ZHANG,J.H.ZHOU,J.H.XU
JRNL TITL CRYSTAL STRUCTURES OF PSEUDOMONAS PUTIDA ESTERASE REVEAL THE
JRNL TITL 2 FUNCTIONAL ROLE OF RESIDUES 187 AND 287 IN SUBSTRATE BINDING
JRNL TITL 3 AND CHIRAL RECOGNITION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 446 1145 2014
JRNL REFN ISSN 0006-291X
JRNL PMID 24680822
JRNL DOI 10.1016/J.BBRC.2014.03.072
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 38081
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1907
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 42.7804 - 4.3395 0.98 2750 143 0.1555 0.1848
REMARK 3 2 4.3395 - 3.4448 0.98 2637 122 0.1411 0.1924
REMARK 3 3 3.4448 - 3.0095 0.99 2599 141 0.1518 0.1807
REMARK 3 4 3.0095 - 2.7344 1.00 2584 143 0.1545 0.1783
REMARK 3 5 2.7344 - 2.5384 1.00 2592 137 0.1554 0.2036
REMARK 3 6 2.5384 - 2.3888 1.00 2583 137 0.1552 0.1771
REMARK 3 7 2.3888 - 2.2692 1.00 2540 164 0.1485 0.1552
REMARK 3 8 2.2692 - 2.1704 1.00 2560 145 0.1419 0.1947
REMARK 3 9 2.1704 - 2.0868 1.00 2568 117 0.1442 0.1647
REMARK 3 10 2.0868 - 2.0148 1.00 2568 124 0.1375 0.1639
REMARK 3 11 2.0148 - 1.9518 1.00 2559 133 0.1440 0.1942
REMARK 3 12 1.9518 - 1.8960 1.00 2546 136 0.1460 0.1742
REMARK 3 13 1.8960 - 1.8461 1.00 2544 141 0.1379 0.1782
REMARK 3 14 1.8461 - 1.8011 1.00 2544 124 0.1447 0.1868
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.21
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 : 0.006 2523
REMARK 3 ANGLE : 1.074 3431
REMARK 3 CHIRALITY : 0.073 381
REMARK 3 PLANARITY : 0.005 448
REMARK 3 DIHEDRAL : 13.629 921
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 4OB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB084273.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX-HF
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38145
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 42.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 25.500
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
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: PHASER
REMARK 200 STARTING MODEL: 2YH2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES/MOPS-NA, PH 7.5, 12.5% W/V
REMARK 280 PEG 1000, 12.5% W/V PEG 3350, 12.5% V/V MPD, 0.03M MGCL2, 0.03M
REMARK 280 CACL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 43.90300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.81650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.81650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.85450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.81650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.81650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.95150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.81650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.81650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.85450
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.81650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.81650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.95150
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 43.90300
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 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 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A 622 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 647 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 572 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 604 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 MET A -14
REMARK 465 ALA A -13
REMARK 465 SER A -12
REMARK 465 MET A -11
REMARK 465 THR A -10
REMARK 465 GLY A -9
REMARK 465 GLY A -8
REMARK 465 GLN A -7
REMARK 465 GLN A -6
REMARK 465 MET A -5
REMARK 465 GLY A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 LEU A 319
REMARK 465 GLU A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
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 OG SER A 42 O HOH A 663 2.16
REMARK 500 O HOH A 646 O HOH A 833 2.16
REMARK 500 O HOH A 766 O HOH A 836 2.18
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 ASN A 60 54.01 38.74
REMARK 500 TRP A 89 -32.67 71.85
REMARK 500 ASP A 93 -168.77 -179.72
REMARK 500 SER A 159 -125.35 64.61
REMARK 500 PHE A 182 146.34 -170.29
REMARK 500 TRP A 187 61.43 35.82
REMARK 500 PHE A 207 -68.92 75.12
REMARK 500 PHE A 255 73.63 -104.07
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 777 DISTANCE = 5.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OB6 RELATED DB: PDB
REMARK 900 RELATED ID: 4OB7 RELATED DB: PDB
REMARK 900 RELATED ID: 4OU4 RELATED DB: PDB
REMARK 900 RELATED ID: 4OU5 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR STATED THE SEQUENCE DATABASE WAS WRONG AT THIS POSITION.
DBREF 4OB8 A 1 316 UNP L7PYQ2 L7PYQ2_9PSED 1 316
SEQADV 4OB8 MET A -14 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 ALA A -13 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 SER A -12 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 MET A -11 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 THR A -10 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLY A -9 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLY A -8 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLN A -7 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLN A -6 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 MET A -5 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLY A -4 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 ARG A -3 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLY A -2 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 SER A -1 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 SER A 0 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLN A 10 UNP L7PYQ2 LYS 10 SEE REMARK 999
SEQADV 4OB8 LEU A 317 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLU A 318 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 LEU A 319 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 GLU A 320 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 HIS A 321 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 HIS A 322 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 HIS A 323 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 HIS A 324 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 HIS A 325 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OB8 HIS A 326 UNP L7PYQ2 EXPRESSION TAG
SEQRES 1 A 341 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 341 SER SER GLY SER PRO GLY VAL GLU GLN HIS THR GLN ALA
SEQRES 3 A 341 PHE LEU GLU ALA LEU GLU GLN GLY GLY GLY LYS PRO LEU
SEQRES 4 A 341 GLU GLN LEU SER PRO LYS ASP ALA ARG ALA VAL LEU THR
SEQRES 5 A 341 GLY ALA GLN ALA SER VAL LYS VAL ASP LEU SER GLY ILE
SEQRES 6 A 341 GLU VAL LYS GLU ARG THR ILE GLN ALA ASN GLY GLN SER
SEQRES 7 A 341 ILE LYS LEU GLN VAL VAL ARG PRO ALA ASN VAL LYS GLY
SEQRES 8 A 341 GLU LEU PRO VAL PHE MET PHE PHE HIS GLY GLY GLY TRP
SEQRES 9 A 341 VAL LEU GLY ASP PHE PRO THR HIS GLN ARG LEU ILE ARG
SEQRES 10 A 341 ASP LEU VAL VAL GLY SER GLY ALA VAL ALA VAL TYR VAL
SEQRES 11 A 341 ASP TYR THR PRO SER PRO GLU SER HIS TYR PRO THR ALA
SEQRES 12 A 341 ILE ASN GLN ALA TYR ALA ALA THR GLN TRP VAL ALA GLU
SEQRES 13 A 341 HIS GLY LYS GLU ILE GLY VAL ASP GLY LYS ARG LEU ALA
SEQRES 14 A 341 VAL ALA GLY ASN SER VAL GLY GLY ASN MET ALA ALA VAL
SEQRES 15 A 341 VAL ALA LEU LYS ALA LYS GLU ALA GLY THR PRO ALA LEU
SEQRES 16 A 341 ARG PHE GLN LEU LEU LEU TRP PRO VAL THR ASP ALA SER
SEQRES 17 A 341 PHE GLU THR ALA SER TYR LYS GLN PHE ALA ASP GLY HIS
SEQRES 18 A 341 PHE LEU THR THR GLY MET MET LYS TRP PHE TRP ASP ASN
SEQRES 19 A 341 TYR THR THR ASP ALA LYS ALA ARG GLU GLN ILE TYR ALA
SEQRES 20 A 341 SER PRO LEU ARG ALA SER SER GLU GLN LEU LYS GLY LEU
SEQRES 21 A 341 PRO PRO ALA LEU VAL GLN THR ALA GLU PHE ASP VAL LEU
SEQRES 22 A 341 ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ASN ALA
SEQRES 23 A 341 ALA GLY VAL THR VAL THR SER VAL ARG TYR ASN GLY MET
SEQRES 24 A 341 ILE HIS ASP TYR GLY LEU LEU ASN PRO LEU SER GLN VAL
SEQRES 25 A 341 PRO ALA VAL LYS ALA ALA MET ARG GLN ALA GLY THR GLU
SEQRES 26 A 341 LEU LYS VAL HIS LEU GLN LEU GLU LEU GLU HIS HIS HIS
SEQRES 27 A 341 HIS HIS HIS
HET MPD A 401 8
HET PEG A 402 7
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 MPD C6 H14 O2
FORMUL 3 PEG C4 H10 O3
FORMUL 4 HOH *365(H2 O)
HELIX 1 1 GLU A 6 GLY A 20 1 15
HELIX 2 2 PRO A 23 LEU A 27 5 5
HELIX 3 3 SER A 28 SER A 42 1 15
HELIX 4 4 ASP A 93 GLY A 109 1 17
HELIX 5 5 PRO A 126 GLY A 143 1 18
HELIX 6 6 LYS A 144 ILE A 146 5 3
HELIX 7 7 SER A 159 GLY A 176 1 18
HELIX 8 8 THR A 196 PHE A 202 1 7
HELIX 9 9 THR A 209 THR A 221 1 13
HELIX 10 10 ASP A 223 GLU A 228 1 6
HELIX 11 11 SER A 233 ALA A 237 5 5
HELIX 12 12 SER A 238 LYS A 243 1 6
HELIX 13 13 LEU A 258 ALA A 272 1 15
HELIX 14 14 LEU A 291 SER A 295 5 5
HELIX 15 15 VAL A 297 LEU A 315 1 19
SHEET 1 A 8 ILE A 50 ALA A 59 0
SHEET 2 A 8 GLN A 62 PRO A 71 -1 O LEU A 66 N ARG A 55
SHEET 3 A 8 VAL A 111 VAL A 115 -1 O ALA A 112 N VAL A 69
SHEET 4 A 8 LEU A 78 PHE A 84 1 N PHE A 81 O VAL A 111
SHEET 5 A 8 VAL A 148 ASN A 158 1 O ALA A 154 N MET A 82
SHEET 6 A 8 PHE A 182 LEU A 186 1 O LEU A 184 N VAL A 155
SHEET 7 A 8 ALA A 248 PHE A 255 1 O LEU A 249 N LEU A 185
SHEET 8 A 8 VAL A 276 ILE A 285 1 O TYR A 281 N THR A 252
CISPEP 1 SER A 120 PRO A 121 0 4.15
CISPEP 2 TYR A 125 PRO A 126 0 6.50
CISPEP 3 THR A 177 PRO A 178 0 -4.30
SITE 1 AC1 6 LEU A 36 GLY A 87 LEU A 91 PHE A 207
SITE 2 AC1 6 ASP A 287 HOH A 558
SITE 1 AC2 4 GLY A 107 GLY A 109 THR A 309 LYS A 312
CRYST1 95.633 95.633 87.806 90.00 90.00 90.00 P 43 21 2 8
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 0.010457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011389 0.00000
TER 2453 GLU A 318
MASTER 329 0 2 15 8 0 3 6 2807 1 15 27
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