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HEADER HYDROLASE 22-JUN-17 5W95
TITLE MTB RV3802C WITH PEG BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED MEMBRANE PROTEIN OF UNCHARACTERISED FUNCTION;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RV3802C;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: ERS007672_01844, ERS023446_02759, ERS024213_00010,
SOURCE 5 ERS024276_01951, ERS027644_01116, ERS027646_00777, ERS027656_01063,
SOURCE 6 ERS027659_00661, ERS027661_01209, ERS027666_00826, ERS031537_00520,
SOURCE 7 ERS124361_01515, SAMEA2683035_00004;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PEG, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.GOINS,C.M.SCHREIDAH,D.R.RONNING
REVDAT 1 27-DEC-17 5W95 0
JRNL AUTH C.M.GOINS,C.M.SCHREIDAH,S.DAJNOWICZ,D.R.RONNING
JRNL TITL STRUCTURAL BASIS FOR LIPID BINDING AND MECHANISM OF THE
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS RV3802 PHOSPHOLIPASE
JRNL REF J.BIOL.CHEM. 2017
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 56631
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.530
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 44.3360 - 4.1510 1.00 4149 153 0.1460 0.1558
REMARK 3 2 4.1510 - 3.2951 1.00 3998 145 0.1448 0.1484
REMARK 3 3 3.2951 - 2.8786 1.00 3955 146 0.1715 0.2089
REMARK 3 4 2.8786 - 2.6155 1.00 3930 143 0.1701 0.2013
REMARK 3 5 2.6155 - 2.4280 1.00 3914 143 0.1697 0.2085
REMARK 3 6 2.4280 - 2.2849 1.00 3879 143 0.1600 0.1859
REMARK 3 7 2.2849 - 2.1705 1.00 3921 143 0.1605 0.1778
REMARK 3 8 2.1705 - 2.0760 1.00 3882 142 0.1591 0.2112
REMARK 3 9 2.0760 - 1.9961 1.00 3876 142 0.1575 0.1743
REMARK 3 10 1.9961 - 1.9272 1.00 3888 142 0.1606 0.2080
REMARK 3 11 1.9272 - 1.8669 1.00 3864 142 0.1599 0.1688
REMARK 3 12 1.8669 - 1.8136 1.00 3876 141 0.1630 0.2071
REMARK 3 13 1.8136 - 1.7658 1.00 3838 141 0.1615 0.2312
REMARK 3 14 1.7658 - 1.7227 0.95 3661 134 0.1570 0.1843
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.320
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) : 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 : 0.007 4084
REMARK 3 ANGLE : 1.062 5571
REMARK 3 CHIRALITY : 0.041 618
REMARK 3 PLANARITY : 0.006 752
REMARK 3 DIHEDRAL : 13.591 1486
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 5W95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56631
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 44.321
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 14.80
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 25% W/V
REMARK 280 POLYETHYLENE GLYCOL 3,350, EVAPORATION, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 28.59400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.69550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.69550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.59400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.65000
REMARK 290 SMTRY3 4 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 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 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 MET A 52
REMARK 465 HIS A 53
REMARK 465 HIS A 54
REMARK 465 HIS A 55
REMARK 465 HIS A 56
REMARK 465 HIS A 57
REMARK 465 HIS A 58
REMARK 465 SER A 59
REMARK 465 SER A 60
REMARK 465 GLY A 61
REMARK 465 LEU A 62
REMARK 465 GLU A 63
REMARK 465 VAL A 64
REMARK 465 LEU A 65
REMARK 465 PHE A 66
REMARK 465 GLN A 67
REMARK 465 GLY A 68
REMARK 465 PRO A 69
REMARK 465 ALA A 70
REMARK 465 GLY A 293
REMARK 465 ALA A 294
REMARK 465 GLY A 295
REMARK 465 GLN A 296
REMARK 465 LYS A 334
REMARK 465 HIS A 335
REMARK 465 ARG A 336
REMARK 465 MET B 52
REMARK 465 HIS B 53
REMARK 465 HIS B 54
REMARK 465 HIS B 55
REMARK 465 HIS B 56
REMARK 465 HIS B 57
REMARK 465 HIS B 58
REMARK 465 SER B 59
REMARK 465 SER B 60
REMARK 465 GLY B 61
REMARK 465 LEU B 62
REMARK 465 GLU B 63
REMARK 465 VAL B 64
REMARK 465 GLY B 292
REMARK 465 GLY B 293
REMARK 465 ALA B 294
REMARK 465 GLY B 295
REMARK 465 GLN B 296
REMARK 465 LYS B 334
REMARK 465 HIS B 335
REMARK 465 ARG B 336
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 O HOH A 504 O HOH A 666 2.01
REMARK 500 O HOH A 502 O HOH A 694 2.02
REMARK 500 O HOH B 705 O HOH B 749 2.11
REMARK 500 O HOH A 511 O HOH A 715 2.13
REMARK 500 O HOH A 504 O HOH A 739 2.13
REMARK 500 NH1 ARG A 163 O HOH A 501 2.14
REMARK 500 OE1 GLU A 313 O HOH A 502 2.14
REMARK 500 OD2 ASP A 198 O HOH A 503 2.15
REMARK 500 O HOH A 533 O HOH A 596 2.18
REMARK 500 OE2 GLU A 313 ND2 ASN A 321 2.18
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 O HOH A 739 O HOH B 780 1554 2.14
REMARK 500 O HOH B 746 O HOH B 806 4458 2.17
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 94 73.43 -150.63
REMARK 500 SER A 175 -119.61 61.30
REMARK 500 VAL A 237 -41.35 76.03
REMARK 500 PRO B 69 151.73 -49.16
REMARK 500 SER B 175 -119.40 58.16
REMARK 500 VAL B 237 -39.00 78.93
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 822 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH B 826 DISTANCE = 7.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 402
DBREF1 5W95 A 70 336 UNP A0A045KEI3_MYCTX
DBREF2 5W95 A A0A045KEI3 70 336
DBREF1 5W95 B 70 336 UNP A0A045KEI3_MYCTX
DBREF2 5W95 B A0A045KEI3 70 336
SEQADV 5W95 MET A 52 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS A 53 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS A 54 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS A 55 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS A 56 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS A 57 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS A 58 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 SER A 59 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 SER A 60 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLY A 61 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 LEU A 62 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLU A 63 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 VAL A 64 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 LEU A 65 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 PHE A 66 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLN A 67 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLY A 68 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 PRO A 69 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 MET B 52 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS B 53 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS B 54 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS B 55 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS B 56 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS B 57 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 HIS B 58 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 SER B 59 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 SER B 60 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLY B 61 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 LEU B 62 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLU B 63 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 VAL B 64 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 LEU B 65 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 PHE B 66 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLN B 67 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 GLY B 68 UNP A0A045KEI EXPRESSION TAG
SEQADV 5W95 PRO B 69 UNP A0A045KEI EXPRESSION TAG
SEQRES 1 A 285 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 A 285 LEU PHE GLN GLY PRO ALA SER CYS PRO ASP VAL GLN MET
SEQRES 3 A 285 ILE SER VAL PRO GLY THR TRP GLU SER SER PRO GLN GLN
SEQRES 4 A 285 ASN PRO LEU ASN PRO VAL GLN PHE PRO LYS ALA LEU LEU
SEQRES 5 A 285 LEU LYS VAL THR GLY PRO ILE ALA GLN GLN PHE ALA PRO
SEQRES 6 A 285 ALA ARG VAL GLN THR TYR THR VAL ALA TYR THR ALA GLN
SEQRES 7 A 285 PHE HIS ASN PRO LEU THR THR ASP ASN GLN MET SER TYR
SEQRES 8 A 285 ASN ASP SER ARG ALA GLU GLY THR ARG ALA MET VAL ALA
SEQRES 9 A 285 ALA MET THR ASP MET ASN ASN ARG CYS PRO LEU THR SER
SEQRES 10 A 285 TYR VAL LEU ILE GLY PHE SER GLN GLY ALA VAL ILE ALA
SEQRES 11 A 285 GLY ASP VAL ALA SER ASP ILE GLY ASN GLY ARG GLY PRO
SEQRES 12 A 285 VAL ASP GLU ASP LEU VAL LEU GLY VAL THR LEU ILE ALA
SEQRES 13 A 285 ASP GLY ARG ARG GLN GLN GLY VAL GLY ASN GLN VAL PRO
SEQRES 14 A 285 PRO SER PRO ARG GLY GLU GLY ALA GLU ILE THR LEU HIS
SEQRES 15 A 285 GLU VAL PRO VAL LEU SER GLY LEU GLY LEU THR MET THR
SEQRES 16 A 285 GLY PRO ARG PRO GLY GLY PHE GLY ALA LEU ASP GLY ARG
SEQRES 17 A 285 THR ASN GLU ILE CYS ALA GLN GLY ASP LEU ILE CYS ALA
SEQRES 18 A 285 ALA PRO ALA GLN ALA PHE SER PRO ALA ASN LEU PRO THR
SEQRES 19 A 285 THR LEU ASN THR LEU ALA GLY GLY ALA GLY GLN PRO VAL
SEQRES 20 A 285 HIS ALA MET TYR ALA THR PRO GLU PHE TRP ASN SER ASP
SEQRES 21 A 285 GLY GLU PRO ALA THR GLU TRP THR LEU ASN TRP ALA HIS
SEQRES 22 A 285 GLN LEU ILE GLU ASN ALA PRO HIS PRO LYS HIS ARG
SEQRES 1 B 285 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 B 285 LEU PHE GLN GLY PRO ALA SER CYS PRO ASP VAL GLN MET
SEQRES 3 B 285 ILE SER VAL PRO GLY THR TRP GLU SER SER PRO GLN GLN
SEQRES 4 B 285 ASN PRO LEU ASN PRO VAL GLN PHE PRO LYS ALA LEU LEU
SEQRES 5 B 285 LEU LYS VAL THR GLY PRO ILE ALA GLN GLN PHE ALA PRO
SEQRES 6 B 285 ALA ARG VAL GLN THR TYR THR VAL ALA TYR THR ALA GLN
SEQRES 7 B 285 PHE HIS ASN PRO LEU THR THR ASP ASN GLN MET SER TYR
SEQRES 8 B 285 ASN ASP SER ARG ALA GLU GLY THR ARG ALA MET VAL ALA
SEQRES 9 B 285 ALA MET THR ASP MET ASN ASN ARG CYS PRO LEU THR SER
SEQRES 10 B 285 TYR VAL LEU ILE GLY PHE SER GLN GLY ALA VAL ILE ALA
SEQRES 11 B 285 GLY ASP VAL ALA SER ASP ILE GLY ASN GLY ARG GLY PRO
SEQRES 12 B 285 VAL ASP GLU ASP LEU VAL LEU GLY VAL THR LEU ILE ALA
SEQRES 13 B 285 ASP GLY ARG ARG GLN GLN GLY VAL GLY ASN GLN VAL PRO
SEQRES 14 B 285 PRO SER PRO ARG GLY GLU GLY ALA GLU ILE THR LEU HIS
SEQRES 15 B 285 GLU VAL PRO VAL LEU SER GLY LEU GLY LEU THR MET THR
SEQRES 16 B 285 GLY PRO ARG PRO GLY GLY PHE GLY ALA LEU ASP GLY ARG
SEQRES 17 B 285 THR ASN GLU ILE CYS ALA GLN GLY ASP LEU ILE CYS ALA
SEQRES 18 B 285 ALA PRO ALA GLN ALA PHE SER PRO ALA ASN LEU PRO THR
SEQRES 19 B 285 THR LEU ASN THR LEU ALA GLY GLY ALA GLY GLN PRO VAL
SEQRES 20 B 285 HIS ALA MET TYR ALA THR PRO GLU PHE TRP ASN SER ASP
SEQRES 21 B 285 GLY GLU PRO ALA THR GLU TRP THR LEU ASN TRP ALA HIS
SEQRES 22 B 285 GLN LEU ILE GLU ASN ALA PRO HIS PRO LYS HIS ARG
HET 1PE A 401 16
HET 1PE A 402 16
HET 1PE B 401 16
HET 1PE B 402 16
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 1PE 4(C10 H22 O6)
FORMUL 7 HOH *648(H2 O)
HELIX 1 AA1 LEU A 103 PHE A 114 1 12
HELIX 2 AA2 SER A 141 CYS A 164 1 24
HELIX 3 AA3 SER A 175 ASN A 190 1 16
HELIX 4 AA4 ASP A 196 ASP A 198 5 3
HELIX 5 AA5 GLY A 227 LEU A 232 1 6
HELIX 6 AA6 PHE A 253 GLY A 258 5 6
HELIX 7 AA7 PRO A 274 SER A 279 5 6
HELIX 8 AA8 ASN A 282 GLY A 292 1 11
HELIX 9 AA9 PRO A 297 MET A 301 5 5
HELIX 10 AB1 PRO A 314 ASN A 329 1 16
HELIX 11 AB2 LEU B 103 PHE B 114 1 12
HELIX 12 AB3 SER B 141 CYS B 164 1 24
HELIX 13 AB4 SER B 175 ASN B 190 1 16
HELIX 14 AB5 ASP B 196 ASP B 198 5 3
HELIX 15 AB6 GLY B 227 LEU B 232 1 6
HELIX 16 AB7 LEU B 238 GLY B 242 5 5
HELIX 17 AB8 PHE B 253 GLY B 258 5 6
HELIX 18 AB9 PRO B 274 SER B 279 5 6
HELIX 19 AC1 ASN B 282 ALA B 291 1 10
HELIX 20 AC2 PRO B 297 MET B 301 5 5
HELIX 21 AC3 PRO B 314 ASN B 329 1 16
SHEET 1 AA1 6 VAL A 119 THR A 123 0
SHEET 2 AA1 6 VAL A 75 VAL A 80 1 N MET A 77 O GLN A 120
SHEET 3 AA1 6 SER A 168 PHE A 174 1 O SER A 168 N GLN A 76
SHEET 4 AA1 6 VAL A 200 ILE A 206 1 O LEU A 201 N TYR A 169
SHEET 5 AA1 6 THR A 260 ILE A 263 1 O ASN A 261 N LEU A 205
SHEET 6 AA1 6 ASN A 217 GLN A 218 1 N ASN A 217 O THR A 260
SHEET 1 AA2 6 VAL B 119 THR B 123 0
SHEET 2 AA2 6 VAL B 75 VAL B 80 1 N SER B 79 O TYR B 122
SHEET 3 AA2 6 SER B 168 PHE B 174 1 O SER B 168 N GLN B 76
SHEET 4 AA2 6 VAL B 200 ILE B 206 1 O ILE B 206 N GLY B 173
SHEET 5 AA2 6 THR B 260 ILE B 263 1 O ASN B 261 N LEU B 205
SHEET 6 AA2 6 ASN B 217 GLN B 218 1 N ASN B 217 O GLU B 262
SSBOND 1 CYS A 72 CYS A 164 1555 1555 2.04
SSBOND 2 CYS A 264 CYS A 271 1555 1555 2.06
SSBOND 3 CYS B 72 CYS B 164 1555 1555 2.03
SSBOND 4 CYS B 264 CYS B 271 1555 1555 2.06
CISPEP 1 GLY A 193 PRO A 194 0 9.84
CISPEP 2 PRO A 220 PRO A 221 0 3.04
CISPEP 3 GLY B 193 PRO B 194 0 8.68
CISPEP 4 PRO B 220 PRO B 221 0 1.38
SITE 1 AC1 3 TYR A 142 ILE A 270 1PE A 402
SITE 1 AC2 9 THR A 83 PHE A 130 ASN A 132 SER A 175
SITE 2 AC2 9 LEU A 241 LEU A 290 ALA A 291 1PE A 401
SITE 3 AC2 9 HOH A 558
SITE 1 AC3 7 TYR B 142 GLN B 176 VAL B 179 GLU B 229
SITE 2 AC3 7 ILE B 270 LEU B 287 LEU B 290
SITE 1 AC4 8 THR B 83 PHE B 130 ASN B 132 PRO B 133
SITE 2 AC4 8 SER B 175 GLN B 176 LEU B 290 HOH B 519
CRYST1 57.188 91.300 101.391 90.00 90.00 90.00 P 21 21 21 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 0.017486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009863 0.00000
TER 1925 PRO A 333
TER 3890 PRO B 333
MASTER 354 0 4 21 12 0 8 6 4600 2 72 44
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