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HEADER UNKNOWN FUNCTION 05-OCT-20 7AL6
TITLE CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN PA1622 FROM PSEUDOMONAS
TITLE 2 AERUGINOSA PAO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM
SOURCE 3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 6 / 1C / PRS 101 / PAO1;
SOURCE 7 GENE: PA1622;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PSEUDOMONAS AERUGINOSA, HYPOTHETICAL PROTEIN, ALPHA/BETA HYDROLASE
KEYWDS 2 FOLD, PUTATIVE LIPOLYTIC ENZYME, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.FEILER,W.BLANKENFELDT
REVDAT 1 14-OCT-20 7AL6 0
JRNL AUTH C.G.FEILER,W.BLANKENFELDT
JRNL TITL CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN PA1622 FROM
JRNL TITL 2 PSEUDOMONAS AERUGINOSA PAO1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 91329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4540
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 44.7600 - 6.5200 1.00 2911 175 0.1703 0.1762
REMARK 3 2 6.5200 - 5.1800 1.00 2946 139 0.1648 0.2276
REMARK 3 3 5.1800 - 4.5200 1.00 2905 172 0.1298 0.1542
REMARK 3 4 4.5200 - 4.1100 1.00 2877 154 0.1268 0.1686
REMARK 3 5 4.1100 - 3.8200 1.00 2938 125 0.1359 0.1641
REMARK 3 6 3.8200 - 3.5900 1.00 2904 146 0.1467 0.1721
REMARK 3 7 3.5900 - 3.4100 1.00 2874 161 0.1576 0.2285
REMARK 3 8 3.4100 - 3.2600 1.00 2908 161 0.1711 0.2372
REMARK 3 9 3.2600 - 3.1400 1.00 2899 153 0.1789 0.2376
REMARK 3 10 3.1400 - 3.0300 1.00 2862 175 0.1676 0.2388
REMARK 3 11 3.0300 - 2.9300 1.00 2919 145 0.1763 0.2096
REMARK 3 12 2.9300 - 2.8500 1.00 2825 170 0.1682 0.2096
REMARK 3 13 2.8500 - 2.7800 1.00 2911 175 0.1666 0.2119
REMARK 3 14 2.7700 - 2.7100 1.00 2883 165 0.1707 0.2132
REMARK 3 15 2.7100 - 2.6500 1.00 2880 149 0.1774 0.2409
REMARK 3 16 2.6500 - 2.5900 1.00 2909 122 0.1762 0.2233
REMARK 3 17 2.5900 - 2.5400 1.00 2897 144 0.1671 0.2559
REMARK 3 18 2.5400 - 2.4900 1.00 2870 143 0.1721 0.2447
REMARK 3 19 2.4900 - 2.4500 1.00 2906 149 0.1750 0.2242
REMARK 3 20 2.4500 - 2.4000 1.00 2892 160 0.1718 0.2403
REMARK 3 21 2.4000 - 2.3700 1.00 2889 146 0.1722 0.2070
REMARK 3 22 2.3700 - 2.3300 1.00 2877 151 0.1786 0.2161
REMARK 3 23 2.3300 - 2.2900 1.00 2925 136 0.1791 0.2349
REMARK 3 24 2.2900 - 2.2600 1.00 2922 142 0.1840 0.2422
REMARK 3 25 2.2600 - 2.2300 1.00 2891 121 0.1894 0.2672
REMARK 3 26 2.2300 - 2.2000 1.00 2876 152 0.2026 0.2094
REMARK 3 27 2.2000 - 2.1800 1.00 2896 141 0.2012 0.2715
REMARK 3 28 2.1800 - 2.1500 1.00 2851 169 0.2195 0.2496
REMARK 3 29 2.1500 - 2.1200 1.00 2902 148 0.2155 0.2845
REMARK 3 30 2.1200 - 2.1000 1.00 2844 151 0.2336 0.2772
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.36
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 : 0.013 9101
REMARK 3 ANGLE : 1.463 12332
REMARK 3 CHIRALITY : 0.066 1369
REMARK 3 PLANARITY : 0.010 1604
REMARK 3 DIHEDRAL : 20.754 1290
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 7AL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292111082.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 44.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.7100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.91800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.320
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: 7AL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.24 M MAGNESIUM FORMATE 22% PEG 3350
REMARK 280 20MG/ML PROTEIN CONCENTRATION, PH 7, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 49.37533
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 98.75067
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 74.06300
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 123.43833
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 24.68767
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LEU D 3
REMARK 465 GLN D 4
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 HH11 ARG B 45 OE1 GLU B 270 1.12
REMARK 500 OE1 GLU B 242 H MET B 245 1.39
REMARK 500 OE1 GLU C 255 HH12 ARG C 286 1.39
REMARK 500 OE2 GLU A 235 O HOH A 501 1.79
REMARK 500 NH1 ARG B 45 OE1 GLU B 270 1.90
REMARK 500 OE1 GLU A 235 O HOH A 502 1.96
REMARK 500 OE2 GLU C 94 O HOH C 401 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HE1 MET B 171 HB3 HIS D 154 5554 1.25
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 226 CD GLU A 226 OE1 -0.073
REMARK 500 GLU A 235 N GLU A 235 CA 0.168
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 ASP A 38 -154.21 -95.81
REMARK 500 TYR A 75 57.02 -118.90
REMARK 500 SER A 102 -121.18 53.42
REMARK 500 LEU A 128 -62.29 -149.54
REMARK 500 VAL A 174 -139.26 54.08
REMARK 500 GLU A 242 86.41 -155.18
REMARK 500 ASP B 38 -153.07 -95.06
REMARK 500 LEU B 50 70.96 -114.33
REMARK 500 TYR B 75 62.80 -112.38
REMARK 500 SER B 102 -120.15 57.37
REMARK 500 LEU B 128 -57.16 -154.03
REMARK 500 GLN B 236 39.33 -93.33
REMARK 500 HIS B 264 41.42 -99.58
REMARK 500 ASP C 38 -153.90 -90.10
REMARK 500 TYR C 75 56.21 -117.47
REMARK 500 SER C 102 -116.03 51.67
REMARK 500 LEU C 128 -62.98 -151.28
REMARK 500 VAL C 174 -135.52 49.45
REMARK 500 ASP D 38 -152.07 -89.96
REMARK 500 TYR D 75 53.54 -111.04
REMARK 500 SER D 102 -118.65 54.56
REMARK 500 LEU D 128 -61.61 -149.93
REMARK 500 HIS D 264 41.28 -105.30
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 PEG 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 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 304
DBREF 7AL6 A 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
DBREF 7AL6 B 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
DBREF 7AL6 C 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
DBREF 7AL6 D 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
SEQRES 1 A 286 MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 A 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 A 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 A 286 ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 A 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 A 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 A 286 ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU
SEQRES 8 A 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY
SEQRES 9 A 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 A 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 A 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 A 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 A 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 A 286 ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 A 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 A 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 A 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 A 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 A 286 GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA
SEQRES 20 A 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 A 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 A 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
SEQRES 1 B 286 MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 B 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 B 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 B 286 ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 B 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 B 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 B 286 ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU
SEQRES 8 B 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY
SEQRES 9 B 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 B 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 B 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 B 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 B 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 B 286 ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 B 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 B 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 B 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 B 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 B 286 GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA
SEQRES 20 B 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 B 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 B 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
SEQRES 1 C 286 MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 C 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 C 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 C 286 ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 C 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 C 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 C 286 ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU
SEQRES 8 C 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY
SEQRES 9 C 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 C 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 C 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 C 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 C 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 C 286 ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 C 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 C 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 C 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 C 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 C 286 GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA
SEQRES 20 C 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 C 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 C 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
SEQRES 1 D 286 MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 D 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 D 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 D 286 ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 D 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 D 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 D 286 ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU
SEQRES 8 D 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY
SEQRES 9 D 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 D 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 D 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 D 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 D 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 D 286 ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 D 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 D 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 D 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 D 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 D 286 GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA
SEQRES 20 D 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 D 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 D 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
HET PEG A 401 17
HET PEG A 402 17
HET PGE A 403 24
HET EDO A 404 10
HET PEG C 301 17
HET PEG C 302 17
HET PGE C 303 24
HET PEG D 301 17
HET EDO D 302 10
HET EDO D 303 10
HET EDO D 304 10
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 PEG 5(C4 H10 O3)
FORMUL 7 PGE 2(C6 H14 O4)
FORMUL 8 EDO 4(C2 H6 O2)
FORMUL 16 HOH *665(H2 O)
HELIX 1 AA1 ASN A 39 SER A 44 5 6
HELIX 2 AA2 LEU A 46 LEU A 50 5 5
HELIX 3 AA3 LEU A 76 GLY A 92 1 17
HELIX 4 AA4 SER A 102 LEU A 115 1 14
HELIX 5 AA5 GLU A 134 ASP A 136 5 3
HELIX 6 AA6 LYS A 137 ALA A 151 1 15
HELIX 7 AA7 LEU A 152 LYS A 155 5 4
HELIX 8 AA8 GLU A 162 GLY A 173 1 12
HELIX 9 AA9 SER A 178 GLY A 189 1 12
HELIX 10 AB1 ASP A 202 LEU A 207 5 6
HELIX 11 AB2 THR A 214 SER A 224 1 11
HELIX 12 AB3 GLY A 237 GLU A 242 1 6
HELIX 13 AB4 ARG A 244 THR A 251 1 8
HELIX 14 AB5 HIS A 264 ASP A 269 1 6
HELIX 15 AB6 ASP A 269 ALA A 285 1 17
HELIX 16 AB7 ASN B 39 SER B 44 5 6
HELIX 17 AB8 LEU B 46 LEU B 50 5 5
HELIX 18 AB9 LEU B 76 GLY B 92 1 17
HELIX 19 AC1 SER B 102 LEU B 115 1 14
HELIX 20 AC2 GLU B 134 ASP B 136 5 3
HELIX 21 AC3 LYS B 137 LEU B 152 1 16
HELIX 22 AC4 ARG B 153 LYS B 155 5 3
HELIX 23 AC5 GLU B 162 ARG B 172 1 11
HELIX 24 AC6 SER B 178 GLY B 189 1 12
HELIX 25 AC7 ASP B 202 LEU B 207 5 6
HELIX 26 AC8 THR B 214 ARG B 223 1 10
HELIX 27 AC9 GLY B 237 GLU B 242 1 6
HELIX 28 AD1 GLU B 242 THR B 251 1 10
HELIX 29 AD2 HIS B 264 ASP B 269 1 6
HELIX 30 AD3 ASP B 269 ARG B 286 1 18
HELIX 31 AD4 ASN C 39 SER C 44 5 6
HELIX 32 AD5 ARG C 45 LEU C 50 1 6
HELIX 33 AD6 LEU C 76 GLY C 92 1 17
HELIX 34 AD7 SER C 102 LEU C 115 1 14
HELIX 35 AD8 GLU C 134 ASP C 136 5 3
HELIX 36 AD9 LYS C 137 LEU C 152 1 16
HELIX 37 AE1 GLU C 162 ARG C 172 1 11
HELIX 38 AE2 SER C 178 GLY C 189 1 12
HELIX 39 AE3 ASP C 202 LEU C 207 5 6
HELIX 40 AE4 THR C 214 SER C 224 1 11
HELIX 41 AE5 MET C 238 VAL C 241 5 4
HELIX 42 AE6 GLU C 242 THR C 251 1 10
HELIX 43 AE7 HIS C 264 ASP C 269 1 6
HELIX 44 AE8 ASP C 269 ARG C 286 1 18
HELIX 45 AE9 ASN D 39 SER D 44 5 6
HELIX 46 AF1 LEU D 46 LEU D 50 5 5
HELIX 47 AF2 LEU D 76 GLY D 92 1 17
HELIX 48 AF3 SER D 102 LEU D 115 1 14
HELIX 49 AF4 GLU D 134 ASP D 136 5 3
HELIX 50 AF5 LYS D 137 LEU D 152 1 16
HELIX 51 AF6 GLU D 162 ARG D 172 1 11
HELIX 52 AF7 SER D 178 GLY D 189 1 12
HELIX 53 AF8 ASP D 202 LEU D 207 5 6
HELIX 54 AF9 THR D 214 SER D 224 1 11
HELIX 55 AG1 GLY D 237 GLU D 242 1 6
HELIX 56 AG2 GLU D 242 THR D 251 1 10
HELIX 57 AG3 HIS D 264 ASP D 269 1 6
HELIX 58 AG4 ASP D 269 ARG D 286 1 18
SHEET 1 AA1 8 GLU A 7 SER A 11 0
SHEET 2 AA1 8 GLU A 16 PHE A 22 -1 O LEU A 17 N ILE A 10
SHEET 3 AA1 8 LEU A 53 LEU A 58 -1 O ALA A 57 N HIS A 20
SHEET 4 AA1 8 LYS A 28 LEU A 33 1 N LYS A 28 O ARG A 54
SHEET 5 AA1 8 PHE A 96 HIS A 101 1 O LEU A 99 N LEU A 33
SHEET 6 AA1 8 ILE A 119 ILE A 125 1 O ILE A 125 N GLY A 100
SHEET 7 AA1 8 VAL A 229 ALA A 234 1 O SER A 230 N LEU A 124
SHEET 8 AA1 8 GLU A 255 LEU A 259 1 O GLU A 255 N LEU A 231
SHEET 1 AA2 2 LEU A 190 VAL A 193 0
SHEET 2 AA2 2 GLY A 196 TRP A 199 -1 O GLY A 196 N VAL A 193
SHEET 1 AA3 8 GLU B 7 SER B 11 0
SHEET 2 AA3 8 GLU B 16 PHE B 22 -1 O LEU B 17 N ILE B 10
SHEET 3 AA3 8 LEU B 53 LEU B 58 -1 O ALA B 57 N HIS B 20
SHEET 4 AA3 8 LYS B 28 LEU B 33 1 N LYS B 28 O ARG B 54
SHEET 5 AA3 8 PHE B 96 HIS B 101 1 O HIS B 101 N LEU B 33
SHEET 6 AA3 8 ILE B 119 ILE B 125 1 O ALA B 123 N LEU B 98
SHEET 7 AA3 8 VAL B 229 ALA B 234 1 O SER B 230 N LEU B 122
SHEET 8 AA3 8 GLU B 255 LEU B 259 1 O GLU B 255 N LEU B 231
SHEET 1 AA4 2 LEU B 190 VAL B 193 0
SHEET 2 AA4 2 GLY B 196 TRP B 199 -1 O GLY B 196 N VAL B 193
SHEET 1 AA5 8 GLU C 7 SER C 11 0
SHEET 2 AA5 8 GLU C 16 PHE C 22 -1 O LEU C 17 N ILE C 10
SHEET 3 AA5 8 LEU C 53 LEU C 58 -1 O ALA C 57 N HIS C 20
SHEET 4 AA5 8 LYS C 28 LEU C 33 1 N VAL C 30 O VAL C 56
SHEET 5 AA5 8 PHE C 96 HIS C 101 1 O LEU C 99 N LEU C 33
SHEET 6 AA5 8 ILE C 119 ILE C 125 1 O ILE C 125 N GLY C 100
SHEET 7 AA5 8 VAL C 229 ALA C 234 1 O SER C 230 N LEU C 124
SHEET 8 AA5 8 GLU C 255 LEU C 259 1 O HIS C 257 N LEU C 233
SHEET 1 AA6 2 LEU C 190 VAL C 193 0
SHEET 2 AA6 2 GLY C 196 TRP C 199 -1 O GLY C 196 N VAL C 193
SHEET 1 AA7 8 GLU D 7 SER D 11 0
SHEET 2 AA7 8 GLU D 16 PHE D 22 -1 O LEU D 17 N ILE D 10
SHEET 3 AA7 8 LEU D 53 LEU D 58 -1 O ALA D 57 N HIS D 20
SHEET 4 AA7 8 LYS D 28 LEU D 33 1 N VAL D 30 O VAL D 56
SHEET 5 AA7 8 PHE D 96 HIS D 101 1 O LEU D 99 N LEU D 33
SHEET 6 AA7 8 ILE D 119 ILE D 125 1 O ALA D 123 N LEU D 98
SHEET 7 AA7 8 VAL D 229 ALA D 234 1 O SER D 230 N LEU D 124
SHEET 8 AA7 8 GLU D 255 LEU D 259 1 O GLU D 255 N LEU D 231
SHEET 1 AA8 2 LEU D 190 VAL D 193 0
SHEET 2 AA8 2 GLY D 196 TRP D 199 -1 O GLY D 196 N VAL D 193
SITE 1 AC1 3 LEU A 77 SER A 209 ARG A 212
SITE 1 AC2 5 ARG A 95 GLU A 117 HOH A 665 GLU C 235
SITE 2 AC2 5 HIS C 258
SITE 1 AC3 2 LYS A 28 ALA A 285
SITE 1 AC4 7 PRO A 228 VAL A 229 PRO A 253 GLU A 255
SITE 2 AC4 7 HOH A 563 HOH A 609 ARG C 278
SITE 1 AC5 3 ARG A 54 TRP A 93 TYR C 197
SITE 1 AC6 7 GLU C 176 SER C 178 GLN C 236 GLY C 261
SITE 2 AC6 7 GLY C 262 ASP C 268 HOH C 553
SITE 1 AC7 1 LEU C 3
SITE 1 AC8 4 LEU C 184 GLU D 250 HOH D 513 HOH D 515
SITE 1 AC9 2 LEU D 21 ARG D 54
SITE 1 AD1 3 SER D 209 ARG D 212 HOH D 444
SITE 1 AD2 3 ILE D 129 PRO D 130 TYR D 131
CRYST1 136.758 136.758 148.126 90.00 90.00 120.00 P 61 24
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 0.007312 0.004222 0.000000 0.00000
SCALE2 0.000000 0.008443 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006751 0.00000
TER 4472 ARG A 286
TER 8905 ARG B 286
TER 13357 ARG C 286
TER 17768 ARG D 286
MASTER 384 0 11 58 40 0 14 6 9513 4 173 88
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