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HEADER HYDROLASE 26-AUG-10 3OM8
TITLE THE CRYSTAL STRUCTURE OF A HYDROLASE FROM PSEUDOMONAS AERUGINOSA PA01
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PA01;
SOURCE 5 GENE: PA0480;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PPK1037;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19B
KEYWDS STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,G.CHHOR,K.BUCK,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 1 22-SEP-10 3OM8 0
JRNL AUTH K.TAN,G.CHHOR,K.BUCK,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A HYDROLASE FROM PSEUDOMONAS
JRNL TITL 2 AERUGINOSA PA01
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 3 NUMBER OF REFLECTIONS : 50526
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2562
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 48.2420 - 4.8454 0.97 5784 299 0.1817 0.1989
REMARK 3 2 4.8454 - 3.8465 0.98 5491 291 0.1417 0.1687
REMARK 3 3 3.8465 - 3.3604 0.97 5365 306 0.1786 0.2063
REMARK 3 4 3.3604 - 3.0532 0.95 5222 277 0.2057 0.2372
REMARK 3 5 3.0532 - 2.8344 0.90 5010 246 0.2124 0.2378
REMARK 3 6 2.8344 - 2.6673 0.88 4805 266 0.2253 0.2864
REMARK 3 7 2.6673 - 2.5337 0.84 4556 251 0.2254 0.2707
REMARK 3 8 2.5337 - 2.4234 0.78 4288 216 0.2385 0.2857
REMARK 3 9 2.4234 - 2.3301 0.72 3929 189 0.2690 0.3125
REMARK 3 10 2.3301 - 2.2497 0.65 3514 221 0.2959 0.3553
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 : 0.31
REMARK 3 B_SOL : 48.16
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : 14.61500
REMARK 3 B22 (A**2) : 14.61500
REMARK 3 B33 (A**2) : -29.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
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 4123
REMARK 3 ANGLE : 0.977 5619
REMARK 3 CHIRALITY : 0.059 644
REMARK 3 PLANARITY : 0.004 732
REMARK 3 DIHEDRAL : 18.889 1461
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8227 56.1346 21.3082
REMARK 3 T TENSOR
REMARK 3 T11: 0.4501 T22: 0.4349
REMARK 3 T33: 0.2844 T12: -0.0378
REMARK 3 T13: -0.0083 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.8579 L22: 0.6602
REMARK 3 L33: 1.3214 L12: -0.3773
REMARK 3 L13: -0.6040 L23: 0.9317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0835 S12: 0.0271 S13: 0.0242
REMARK 3 S21: -0.1296 S22: -0.0514 S23: -0.0267
REMARK 3 S31: -0.1027 S32: 0.0160 S33: -0.0339
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7511 21.3155 16.8059
REMARK 3 T TENSOR
REMARK 3 T11: 0.3895 T22: 0.5216
REMARK 3 T33: 0.3804 T12: 0.0359
REMARK 3 T13: 0.0046 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.0543 L22: 1.0949
REMARK 3 L33: 1.8552 L12: 0.2373
REMARK 3 L13: -0.1064 L23: -0.8036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: -0.0653 S13: -0.0130
REMARK 3 S21: -0.0393 S22: -0.0441 S23: 0.0145
REMARK 3 S31: -0.0091 S32: 0.0383 S33: 0.0548
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 3OM8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB061292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56314
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 48.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 0.67700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M PROLINE, 0.1M HEPES, 10% W/V
REMARK 280 PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 141.87250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.76450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.76450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.93625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.76450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.76450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 212.80875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.76450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.76450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 70.93625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.76450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.76450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 212.80875
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 141.87250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: EXPERIMENTALLY UNKNOWN. IT IS PREDICTED THAT THE MOLECULE
REMARK 300 IS MONOMERIC.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 45.76450
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 45.76450
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.93625
REMARK 350
REMARK 350 BIOMOLECULE: 4
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: 5
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 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 SER A -1
REMARK 465 ASN A 0
REMARK 465 SER B -1
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 ARG A 60 125.89 -37.18
REMARK 500 SER A 99 -114.28 58.34
REMARK 500 ALA A 112 53.10 -140.63
REMARK 500 GLU A 117 -95.63 -96.92
REMARK 500 ASN A 123 61.23 33.00
REMARK 500 PRO A 241 48.03 -78.82
REMARK 500 VAL A 243 -130.38 -84.46
REMARK 500 ALA B 1 -115.70 50.61
REMARK 500 SER B 99 -118.56 57.74
REMARK 500 GLU B 117 -94.79 -84.94
REMARK 500 ASN B 123 63.85 39.01
REMARK 500 TRP B 127 116.28 -168.53
REMARK 500 ALA B 167 102.97 -38.10
REMARK 500 PRO B 241 49.94 -77.67
REMARK 500 VAL B 243 -92.00 -88.20
REMARK 500 LEU B 245 75.68 -102.21
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 MES A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 266
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC37789.1 RELATED DB: TARGETDB
DBREF 3OM8 A 2 264 UNP Q9I638 Q9I638_PSEAE 2 264
DBREF 3OM8 B 2 264 UNP Q9I638 Q9I638_PSEAE 2 264
SEQADV 3OM8 SER A -1 UNP Q9I638 EXPRESSION TAG
SEQADV 3OM8 ASN A 0 UNP Q9I638 EXPRESSION TAG
SEQADV 3OM8 ALA A 1 UNP Q9I638 EXPRESSION TAG
SEQADV 3OM8 SER B -1 UNP Q9I638 EXPRESSION TAG
SEQADV 3OM8 ASN B 0 UNP Q9I638 EXPRESSION TAG
SEQADV 3OM8 ALA B 1 UNP Q9I638 EXPRESSION TAG
SEQRES 1 A 266 SER ASN ALA GLY ASN LEU SER PHE LEU ALA THR SER ASP
SEQRES 2 A 266 GLY ALA SER LEU ALA TYR ARG LEU ASP GLY ALA ALA GLU
SEQRES 3 A 266 LYS PRO LEU LEU ALA LEU SER ASN SER ILE GLY THR THR
SEQRES 4 A 266 LEU HIS MSE TRP ASP ALA GLN LEU PRO ALA LEU THR ARG
SEQRES 5 A 266 HIS PHE ARG VAL LEU ARG TYR ASP ALA ARG GLY HIS GLY
SEQRES 6 A 266 ALA SER SER VAL PRO PRO GLY PRO TYR THR LEU ALA ARG
SEQRES 7 A 266 LEU GLY GLU ASP VAL LEU GLU LEU LEU ASP ALA LEU GLU
SEQRES 8 A 266 VAL ARG ARG ALA HIS PHE LEU GLY LEU SER LEU GLY GLY
SEQRES 9 A 266 ILE VAL GLY GLN TRP LEU ALA LEU HIS ALA PRO GLN ARG
SEQRES 10 A 266 ILE GLU ARG LEU VAL LEU ALA ASN THR SER ALA TRP LEU
SEQRES 11 A 266 GLY PRO ALA ALA GLN TRP ASP GLU ARG ILE ALA ALA VAL
SEQRES 12 A 266 LEU GLN ALA GLU ASP MSE SER GLU THR ALA ALA GLY PHE
SEQRES 13 A 266 LEU GLY ASN TRP PHE PRO PRO ALA LEU LEU GLU ARG ALA
SEQRES 14 A 266 GLU PRO VAL VAL GLU ARG PHE ARG ALA MSE LEU MSE ALA
SEQRES 15 A 266 THR ASN ARG HIS GLY LEU ALA GLY SER PHE ALA ALA VAL
SEQRES 16 A 266 ARG ASP THR ASP LEU ARG ALA GLN LEU ALA ARG ILE GLU
SEQRES 17 A 266 ARG PRO THR LEU VAL ILE ALA GLY ALA TYR ASP THR VAL
SEQRES 18 A 266 THR ALA ALA SER HIS GLY GLU LEU ILE ALA ALA SER ILE
SEQRES 19 A 266 ALA GLY ALA ARG LEU VAL THR LEU PRO ALA VAL HIS LEU
SEQRES 20 A 266 SER ASN VAL GLU PHE PRO GLN ALA PHE GLU GLY ALA VAL
SEQRES 21 A 266 LEU SER PHE LEU GLY ALA
SEQRES 1 B 266 SER ASN ALA GLY ASN LEU SER PHE LEU ALA THR SER ASP
SEQRES 2 B 266 GLY ALA SER LEU ALA TYR ARG LEU ASP GLY ALA ALA GLU
SEQRES 3 B 266 LYS PRO LEU LEU ALA LEU SER ASN SER ILE GLY THR THR
SEQRES 4 B 266 LEU HIS MSE TRP ASP ALA GLN LEU PRO ALA LEU THR ARG
SEQRES 5 B 266 HIS PHE ARG VAL LEU ARG TYR ASP ALA ARG GLY HIS GLY
SEQRES 6 B 266 ALA SER SER VAL PRO PRO GLY PRO TYR THR LEU ALA ARG
SEQRES 7 B 266 LEU GLY GLU ASP VAL LEU GLU LEU LEU ASP ALA LEU GLU
SEQRES 8 B 266 VAL ARG ARG ALA HIS PHE LEU GLY LEU SER LEU GLY GLY
SEQRES 9 B 266 ILE VAL GLY GLN TRP LEU ALA LEU HIS ALA PRO GLN ARG
SEQRES 10 B 266 ILE GLU ARG LEU VAL LEU ALA ASN THR SER ALA TRP LEU
SEQRES 11 B 266 GLY PRO ALA ALA GLN TRP ASP GLU ARG ILE ALA ALA VAL
SEQRES 12 B 266 LEU GLN ALA GLU ASP MSE SER GLU THR ALA ALA GLY PHE
SEQRES 13 B 266 LEU GLY ASN TRP PHE PRO PRO ALA LEU LEU GLU ARG ALA
SEQRES 14 B 266 GLU PRO VAL VAL GLU ARG PHE ARG ALA MSE LEU MSE ALA
SEQRES 15 B 266 THR ASN ARG HIS GLY LEU ALA GLY SER PHE ALA ALA VAL
SEQRES 16 B 266 ARG ASP THR ASP LEU ARG ALA GLN LEU ALA ARG ILE GLU
SEQRES 17 B 266 ARG PRO THR LEU VAL ILE ALA GLY ALA TYR ASP THR VAL
SEQRES 18 B 266 THR ALA ALA SER HIS GLY GLU LEU ILE ALA ALA SER ILE
SEQRES 19 B 266 ALA GLY ALA ARG LEU VAL THR LEU PRO ALA VAL HIS LEU
SEQRES 20 B 266 SER ASN VAL GLU PHE PRO GLN ALA PHE GLU GLY ALA VAL
SEQRES 21 B 266 LEU SER PHE LEU GLY ALA
MODRES 3OM8 MSE A 40 MET SELENOMETHIONINE
MODRES 3OM8 MSE A 147 MET SELENOMETHIONINE
MODRES 3OM8 MSE A 177 MET SELENOMETHIONINE
MODRES 3OM8 MSE A 179 MET SELENOMETHIONINE
MODRES 3OM8 MSE B 40 MET SELENOMETHIONINE
MODRES 3OM8 MSE B 147 MET SELENOMETHIONINE
MODRES 3OM8 MSE B 177 MET SELENOMETHIONINE
MODRES 3OM8 MSE B 179 MET SELENOMETHIONINE
HET MSE A 40 8
HET MSE A 147 8
HET MSE A 177 8
HET MSE A 179 8
HET MSE B 40 8
HET MSE B 147 8
HET MSE B 177 8
HET MSE B 179 8
HET MES A 265 12
HET EDO A 266 4
HET MES B 265 12
HET EDO B 266 4
HETNAM MSE SELENOMETHIONINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 MES 2(C6 H13 N O4 S)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 7 HOH *118(H2 O)
HELIX 1 1 THR A 37 ALA A 43 5 7
HELIX 2 2 GLN A 44 ARG A 50 1 7
HELIX 3 3 THR A 73 LEU A 88 1 16
HELIX 4 4 SER A 99 ALA A 112 1 14
HELIX 5 5 ALA A 131 ALA A 144 1 14
HELIX 6 6 MSE A 147 PHE A 159 1 13
HELIX 7 7 PRO A 160 ARG A 166 1 7
HELIX 8 8 GLU A 168 ALA A 180 1 13
HELIX 9 9 ASN A 182 ASP A 195 1 14
HELIX 10 10 GLN A 201 ILE A 205 5 5
HELIX 11 11 ALA A 221 ILE A 232 1 12
HELIX 12 12 LEU A 245 PHE A 250 1 6
HELIX 13 13 PHE A 250 GLY A 263 1 14
HELIX 14 14 THR B 37 ALA B 43 5 7
HELIX 15 15 GLN B 44 ARG B 50 1 7
HELIX 16 16 THR B 73 GLU B 89 1 17
HELIX 17 17 SER B 99 ALA B 112 1 14
HELIX 18 18 ALA B 131 ALA B 144 1 14
HELIX 19 19 MSE B 147 PHE B 159 1 13
HELIX 20 20 PRO B 160 ARG B 166 1 7
HELIX 21 21 GLU B 168 ALA B 180 1 13
HELIX 22 22 ASN B 182 ASP B 195 1 14
HELIX 23 23 LEU B 198 ILE B 205 5 8
HELIX 24 24 ALA B 221 ILE B 232 1 12
HELIX 25 25 LEU B 245 PHE B 250 1 6
HELIX 26 26 PHE B 250 GLY B 263 1 14
SHEET 1 A 8 SER A 5 ALA A 8 0
SHEET 2 A 8 SER A 14 ASP A 20 -1 O LEU A 15 N LEU A 7
SHEET 3 A 8 ARG A 53 TYR A 57 -1 O VAL A 54 N ASP A 20
SHEET 4 A 8 LEU A 27 SER A 31 1 N LEU A 28 O ARG A 53
SHEET 5 A 8 ALA A 93 LEU A 98 1 O LEU A 96 N ALA A 29
SHEET 6 A 8 ILE A 116 ALA A 122 1 O VAL A 120 N PHE A 95
SHEET 7 A 8 THR A 209 GLY A 214 1 O ILE A 212 N LEU A 121
SHEET 8 A 8 ARG A 236 LEU A 240 1 O LEU A 240 N ALA A 213
SHEET 1 B 8 SER B 5 ALA B 8 0
SHEET 2 B 8 SER B 14 ASP B 20 -1 O TYR B 17 N SER B 5
SHEET 3 B 8 ARG B 53 TYR B 57 -1 O VAL B 54 N ASP B 20
SHEET 4 B 8 LEU B 27 SER B 31 1 N LEU B 28 O ARG B 53
SHEET 5 B 8 ALA B 93 LEU B 98 1 O LEU B 96 N ALA B 29
SHEET 6 B 8 ILE B 116 ALA B 122 1 O GLU B 117 N ALA B 93
SHEET 7 B 8 THR B 209 GLY B 214 1 O LEU B 210 N LEU B 119
SHEET 8 B 8 ARG B 236 LEU B 240 1 O VAL B 238 N VAL B 211
LINK C HIS A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N TRP A 41 1555 1555 1.33
LINK C ASP A 146 N MSE A 147 1555 1555 1.33
LINK C MSE A 147 N SER A 148 1555 1555 1.33
LINK C ALA A 176 N MSE A 177 1555 1555 1.33
LINK C MSE A 177 N LEU A 178 1555 1555 1.33
LINK C LEU A 178 N MSE A 179 1555 1555 1.33
LINK C MSE A 179 N ALA A 180 1555 1555 1.33
LINK C HIS B 39 N MSE B 40 1555 1555 1.33
LINK C MSE B 40 N TRP B 41 1555 1555 1.33
LINK C ASP B 146 N MSE B 147 1555 1555 1.33
LINK C MSE B 147 N SER B 148 1555 1555 1.33
LINK C ALA B 176 N MSE B 177 1555 1555 1.33
LINK C MSE B 177 N LEU B 178 1555 1555 1.33
LINK C LEU B 178 N MSE B 179 1555 1555 1.33
LINK C MSE B 179 N ALA B 180 1555 1555 1.33
CISPEP 1 GLY A 70 PRO A 71 0 -2.66
CISPEP 2 GLY A 129 PRO A 130 0 -2.68
CISPEP 3 GLY B 70 PRO B 71 0 -0.55
CISPEP 4 GLY B 129 PRO B 130 0 0.54
SITE 1 AC1 6 ASP A 195 THR A 196 ASP A 197 LEU A 198
SITE 2 AC1 6 GLN A 201 HOH A 322
SITE 1 AC2 4 SER A 33 ILE A 34 SER A 99 LEU A 100
SITE 1 AC3 5 ASP B 195 THR B 196 ASP B 197 LEU B 198
SITE 2 AC3 5 GLN B 201
SITE 1 AC4 5 SER B 33 ILE B 34 SER B 99 LEU B 100
SITE 2 AC4 5 LEU B 128
CRYST1 91.529 91.529 283.745 90.00 90.00 90.00 P 41 21 2 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 0.010925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010925 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003524 0.00000
TER 1998 ALA A 264
TER 4004 ALA B 264
MASTER 357 0 12 26 16 0 7 6 4136 2 112 42
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