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HEADER HYDROLASE 04-FEB-15 5AH0
TITLE STRUCTURE OF LIPASE 1 FROM PELOSINUS FERMENTANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PFL1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PELOSINUS FERMENTANS DSM 17108;
SOURCE 3 ORGANISM_TAXID: 1122947;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET26B(+)
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HROMIC,T.PAVKOV-KELLER,K.GRUBER,A.BIUNDO,D.RIBITSCH,F.QUARTINELLO,
AUTHOR 2 V.PERZ,M.S.ARRELL,F.KALMAN,G.M.GUEBITZ
REVDAT 1 04-NOV-15 5AH0 0
JRNL AUTH A.BIUNDO,A.HROMIC,T.PAVKOV-KELLER,K.GRUBER,F.QUARTINELLO,
JRNL AUTH 2 K.HAERNVALL,V.PERZ,M.S.ARRELL,M.ZINN,D.RIBITSCH,G.M.GUEBITZ
JRNL TITL CHARACTERIZATION OF A POLY(BUTYLENE ADIPATE-CO-
JRNL TITL 2 TEREPHTHALATE)-HYDROLYZING LIPASE FROM PELOSINUS
JRNL TITL 3 FERMENTANS.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2015
JRNL REFN ESSN 1432-0614
JRNL PMID 26490551
JRNL DOI 10.1007/S00253-015-7031-1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.500
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.202
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.01
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.65
REMARK 3 NUMBER OF REFLECTIONS : 31406
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1960
REMARK 3 R VALUE (WORKING SET) : 0.1935
REMARK 3 FREE R VALUE : 0.2428
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1581
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 48.2105 - 5.5570 0.99 3059 151 0.1647 0.2129
REMARK 3 2 5.5570 - 4.4117 1.00 2881 154 0.1455 0.1701
REMARK 3 3 4.4117 - 3.8543 0.99 2855 139 0.1496 0.1996
REMARK 3 4 3.8543 - 3.5020 0.95 2668 151 0.2013 0.2847
REMARK 3 5 3.5020 - 3.2511 0.98 2773 154 0.2333 0.2600
REMARK 3 6 3.2511 - 3.0594 0.97 2709 164 0.2405 0.2869
REMARK 3 7 3.0594 - 2.9062 0.96 2718 134 0.2414 0.2730
REMARK 3 8 2.9062 - 2.7797 0.94 2604 132 0.2543 0.3098
REMARK 3 9 2.7797 - 2.6727 0.93 2599 141 0.2548 0.3095
REMARK 3 10 2.6727 - 2.5805 0.91 2514 146 0.2620 0.3198
REMARK 3 11 2.5805 - 2.4998 0.88 2445 115 0.2624 0.3079
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) : 0.28
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.33
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 : 0.006 6224
REMARK 3 ANGLE : 0.995 8463
REMARK 3 CHIRALITY : 0.039 916
REMARK 3 PLANARITY : 0.005 1075
REMARK 3 DIHEDRAL : 12.461 2179
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR (CHAIN C AND RESNAME ZN AND RESID 2)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6415 -20.9860 90.5804
REMARK 3 T TENSOR
REMARK 3 T11: 0.7335 T22: 0.1894
REMARK 3 T33: 0.4568 T12: -0.0359
REMARK 3 T13: -0.0285 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.9324 L22: 1.4736
REMARK 3 L33: 4.6979 L12: -0.1373
REMARK 3 L13: 0.6059 L23: 0.6206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0797 S12: -0.1093 S13: -0.4608
REMARK 3 S21: -0.1360 S22: 0.0813 S23: 0.1034
REMARK 3 S31: 1.1262 S32: 0.1389 S33: -0.0748
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B OR (CHAIN C AND RESNAME ZN AND RESID 1)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5815 20.9217 75.4203
REMARK 3 T TENSOR
REMARK 3 T11: 1.1842 T22: 0.2032
REMARK 3 T33: 0.5540 T12: -0.1414
REMARK 3 T13: -0.0473 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 1.9386 L22: 1.0906
REMARK 3 L33: 2.5351 L12: -0.2904
REMARK 3 L13: 0.1889 L23: 0.3357
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: 0.0702 S13: 0.4566
REMARK 3 S21: 0.4736 S22: -0.1119 S23: -0.2477
REMARK 3 S31: -1.1242 S32: 0.1418 S33: 0.0569
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 5AH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-15.
REMARK 100 THE PDBE ID CODE IS EBI-62928.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-14
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97242
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (225 MM MARMOSAIC)
REMARK 200 DETECTOR MANUFACTURER : NMARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33116
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.49
REMARK 200 RESOLUTION RANGE LOW (A) : 60.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 12.7
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 12.6
REMARK 200 R MERGE FOR SHELL (I) : 0.74
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.50
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: 1KU0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M POTASSIUM SODIUM TARTRATE
REMARK 280 TETRAHYDRATE, 0.1 M TRIS, PH 8.5 AND 0.5 % W/V
REMARK 280 POLYETHYLENE GLYCOL MONOMETHYL ETHER 5000
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 107.95000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.90000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.97500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.90000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 161.92500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.90000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.90000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 53.97500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.90000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.90000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 161.92500
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 107.95000
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 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 401
REMARK 465 ASN A 402
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 GLY A 88 OG SER A 92 2.16
REMARK 500 OG SER A 166 OD2 ASP A 271 2.19
REMARK 500 NZ LYS B 143 OD1 ASP B 271 2.18
REMARK 500 O ILE B 336 NZ LYS B 342 2.11
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 17 134.81 179.55
REMARK 500 SER A 129 -135.04 55.85
REMARK 500 ILE A 187 -65.98 55.81
REMARK 500 LEU A 222 57.53 -94.90
REMARK 500 VAL A 332 -35.36 -131.03
REMARK 500 ASN B 17 132.15 -179.79
REMARK 500 VAL B 35 70.77 50.15
REMARK 500 SER B 129 -136.03 55.26
REMARK 500 ILE B 187 -70.51 58.69
REMARK 500 LEU B 222 56.49 -93.39
REMARK 500 VAL B 332 -34.77 -132.89
REMARK 500 SER B 401 -164.39 -70.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 97 SER A 98 144.69
REMARK 500 HIS B 97 SER B 98 144.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1405 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 371 OD2
REMARK 620 2 HOH B2007 O 81.6
REMARK 620 3 ASP B 374 OD1 84.7 143.4
REMARK 620 4 THR B 380 OG1 148.7 73.9 103.5
REMARK 620 5 HOH B2009 O 74.9 68.9 74.8 78.2
REMARK 620 6 ASP B 374 OD2 70.4 151.4 41.4 134.3 107.8
REMARK 620 7 HOH A2018 O 111.9 95.7 120.9 90.1 162.6 89.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 71 OD1
REMARK 620 2 HIS A 91 NE2 108.5
REMARK 620 3 HIS A 97 NE2 108.6 110.9
REMARK 620 4 ASP A 248 OD2 129.5 107.4 90.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 71 OD1
REMARK 620 2 ASP B 248 OD2 115.0
REMARK 620 3 HIS B 91 NE2 107.0 100.5
REMARK 620 4 HIS B 97 NE2 111.2 105.1 118.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1405
DBREF 5AH0 A 16 402 UNP I8S946 I8S946_9FIRM 16 402
DBREF 5AH0 B 16 402 UNP I8S946 I8S946_9FIRM 16 402
SEQADV 5AH0 MET A 16 UNP I8S946 VAL 16 EXPRESSION TAG
SEQADV 5AH0 MET B 16 UNP I8S946 VAL 16 EXPRESSION TAG
SEQRES 1 A 387 MET ASN SER TYR PRO ILE VAL LEU VAL HIS GLY PHE MET
SEQRES 2 A 387 GLY TRP GLY ARG ASN GLU VAL LEU GLY LEU LYS TYR TRP
SEQRES 3 A 387 GLY GLY ILE THR ASP TYR GLU GLN GLU LEU SER SER TYR
SEQRES 4 A 387 GLY TYR THR ALA TYR THR ALA THR VAL GLY PRO VAL SER
SEQRES 5 A 387 SER ASN TRP ASP ARG ALA CYS GLU LEU TYR ALA TYR ILE
SEQRES 6 A 387 LYS GLY GLY THR VAL ASP TYR GLY HIS ALA HIS SER THR
SEQRES 7 A 387 GLN LYS GLY HIS SER ARG TYR GLY ARG THR TYR PRO GLY
SEQRES 8 A 387 LEU TYR PRO GLU TRP GLY ASN LEU THR THR GLU GLY LYS
SEQRES 9 A 387 VAL ASN LYS ILE HIS LEU VAL ALA HIS SER MET GLY GLY
SEQRES 10 A 387 GLN THR VAL ARG THR LEU VAL GLN LEU LEU LYS GLU GLY
SEQRES 11 A 387 SER GLU GLU GLU ARG ASN THR THR PRO SER GLN LEU SER
SEQRES 12 A 387 SER LEU PHE ALA GLY GLY LYS SER TRP VAL HIS SER ILE
SEQRES 13 A 387 THR THR ILE ALA SER PRO HIS ASP GLY THR THR LEU ALA
SEQRES 14 A 387 ASP GLY ILE ASN ILE PHE GLY ASP PHE ALA LYS ASN LEU
SEQRES 15 A 387 VAL ALA SER LEU ALA SER PHE THR GLY ALA GLY GLU LYS
SEQRES 16 A 387 LEU ILE TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ASN
SEQRES 17 A 387 ARG LYS SER GLY GLU SER LEU THR ASP TYR THR ASN ARG
SEQRES 18 A 387 VAL PHE ASN SER ALA ILE TRP ASN SER THR ASN ASP LEU
SEQRES 19 A 387 ALA ASN TRP ASP LEU SER THR ASP GLY ALA ARG VAL LEU
SEQRES 20 A 387 ASN GLN TRP VAL LYS ALA GLN SER ASP ILE TYR TYR PHE
SEQRES 21 A 387 SER TYR SER THR CYS ALA THR VAL PRO SER ILE LEU THR
SEQRES 22 A 387 SER ASN GLU LEU PRO HIS VAL ILE TYR MET THR PRO LEU
SEQRES 23 A 387 LEU TYR PRO PHE GLY ARG PHE ILE GLY SER TYR THR ARG
SEQRES 24 A 387 ASN GLU GLN GLY ARG VAL ILE ILE ASP ASN SER TRP LYS
SEQRES 25 A 387 PRO ASN ASP GLY VAL VAL ASN THR ILE SER GLN ASN GLY
SEQRES 26 A 387 PRO LYS ILE TRP SER SER ASP LYS ILE VAL ASN TYR ASN
SEQRES 27 A 387 GLY VAL PRO GLN ILE GLY LYS TRP ASN SER MET PRO LEU
SEQRES 28 A 387 LEU ASP THR ILE ASP HIS MET ASP ALA CYS GLY ILE GLY
SEQRES 29 A 387 THR ASN ALA LEU THR LEU SER TRP TYR LYS GLY LEU ALA
SEQRES 30 A 387 GLU LYS LEU SER GLN LEU THR ILE SER ASN
SEQRES 1 B 387 MET ASN SER TYR PRO ILE VAL LEU VAL HIS GLY PHE MET
SEQRES 2 B 387 GLY TRP GLY ARG ASN GLU VAL LEU GLY LEU LYS TYR TRP
SEQRES 3 B 387 GLY GLY ILE THR ASP TYR GLU GLN GLU LEU SER SER TYR
SEQRES 4 B 387 GLY TYR THR ALA TYR THR ALA THR VAL GLY PRO VAL SER
SEQRES 5 B 387 SER ASN TRP ASP ARG ALA CYS GLU LEU TYR ALA TYR ILE
SEQRES 6 B 387 LYS GLY GLY THR VAL ASP TYR GLY HIS ALA HIS SER THR
SEQRES 7 B 387 GLN LYS GLY HIS SER ARG TYR GLY ARG THR TYR PRO GLY
SEQRES 8 B 387 LEU TYR PRO GLU TRP GLY ASN LEU THR THR GLU GLY LYS
SEQRES 9 B 387 VAL ASN LYS ILE HIS LEU VAL ALA HIS SER MET GLY GLY
SEQRES 10 B 387 GLN THR VAL ARG THR LEU VAL GLN LEU LEU LYS GLU GLY
SEQRES 11 B 387 SER GLU GLU GLU ARG ASN THR THR PRO SER GLN LEU SER
SEQRES 12 B 387 SER LEU PHE ALA GLY GLY LYS SER TRP VAL HIS SER ILE
SEQRES 13 B 387 THR THR ILE ALA SER PRO HIS ASP GLY THR THR LEU ALA
SEQRES 14 B 387 ASP GLY ILE ASN ILE PHE GLY ASP PHE ALA LYS ASN LEU
SEQRES 15 B 387 VAL ALA SER LEU ALA SER PHE THR GLY ALA GLY GLU LYS
SEQRES 16 B 387 LEU ILE TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ASN
SEQRES 17 B 387 ARG LYS SER GLY GLU SER LEU THR ASP TYR THR ASN ARG
SEQRES 18 B 387 VAL PHE ASN SER ALA ILE TRP ASN SER THR ASN ASP LEU
SEQRES 19 B 387 ALA ASN TRP ASP LEU SER THR ASP GLY ALA ARG VAL LEU
SEQRES 20 B 387 ASN GLN TRP VAL LYS ALA GLN SER ASP ILE TYR TYR PHE
SEQRES 21 B 387 SER TYR SER THR CYS ALA THR VAL PRO SER ILE LEU THR
SEQRES 22 B 387 SER ASN GLU LEU PRO HIS VAL ILE TYR MET THR PRO LEU
SEQRES 23 B 387 LEU TYR PRO PHE GLY ARG PHE ILE GLY SER TYR THR ARG
SEQRES 24 B 387 ASN GLU GLN GLY ARG VAL ILE ILE ASP ASN SER TRP LYS
SEQRES 25 B 387 PRO ASN ASP GLY VAL VAL ASN THR ILE SER GLN ASN GLY
SEQRES 26 B 387 PRO LYS ILE TRP SER SER ASP LYS ILE VAL ASN TYR ASN
SEQRES 27 B 387 GLY VAL PRO GLN ILE GLY LYS TRP ASN SER MET PRO LEU
SEQRES 28 B 387 LEU ASP THR ILE ASP HIS MET ASP ALA CYS GLY ILE GLY
SEQRES 29 B 387 THR ASN ALA LEU THR LEU SER TRP TYR LYS GLY LEU ALA
SEQRES 30 B 387 GLU LYS LEU SER GLN LEU THR ILE SER ASN
HET ZN B1403 1
HET ZN A1401 1
HET PEG B1404 7
HET PEG A1402 7
HET K B1405 1
HETNAM K POTASSIUM ION
HETNAM ZN ZINC ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 5 K K 1+
FORMUL 6 HOH *31(H2 O)
HELIX 1 1 ASP A 46 TYR A 54 1 9
HELIX 2 2 SER A 68 GLY A 82 1 15
HELIX 3 3 GLY A 88 GLY A 96 1 9
HELIX 4 4 MET A 130 GLY A 145 1 16
HELIX 5 5 SER A 146 THR A 152 1 7
HELIX 6 6 SER A 158 ALA A 162 5 5
HELIX 7 7 THR A 181 GLY A 186 1 6
HELIX 8 8 ILE A 187 GLY A 206 1 20
HELIX 9 9 ALA A 207 LEU A 211 5 5
HELIX 10 10 LEU A 217 GLY A 221 5 5
HELIX 11 11 SER A 229 ASN A 239 1 11
HELIX 12 12 ALA A 241 THR A 246 1 6
HELIX 13 13 LEU A 249 LEU A 254 1 6
HELIX 14 14 SER A 255 VAL A 266 1 12
HELIX 15 15 LEU A 302 GLY A 310 1 9
HELIX 16 16 ASP A 323 LYS A 327 5 5
HELIX 17 17 THR A 335 GLN A 338 5 4
HELIX 18 18 MET A 373 GLY A 377 5 5
HELIX 19 19 THR A 384 SER A 396 1 13
HELIX 20 20 ASP B 46 TYR B 54 1 9
HELIX 21 21 SER B 68 GLY B 82 1 15
HELIX 22 22 GLY B 88 GLY B 96 1 9
HELIX 23 23 MET B 130 GLY B 145 1 16
HELIX 24 24 SER B 146 THR B 152 1 7
HELIX 25 25 SER B 158 ALA B 162 5 5
HELIX 26 26 THR B 181 GLY B 186 1 6
HELIX 27 27 ILE B 187 GLY B 206 1 20
HELIX 28 28 ALA B 207 LEU B 211 5 5
HELIX 29 29 LEU B 217 GLY B 221 5 5
HELIX 30 30 SER B 229 ASN B 239 1 11
HELIX 31 31 ALA B 241 THR B 246 1 6
HELIX 32 32 LEU B 249 LEU B 254 1 6
HELIX 33 33 SER B 255 VAL B 266 1 12
HELIX 34 34 LEU B 302 GLY B 310 1 9
HELIX 35 35 ASP B 323 LYS B 327 5 5
HELIX 36 36 THR B 335 GLN B 338 5 4
HELIX 37 37 MET B 373 GLY B 377 5 5
HELIX 38 38 THR B 384 SER B 396 1 13
SHEET 1 AA 7 ALA A 58 ALA A 61 0
SHEET 2 AA 7 ILE A 21 VAL A 24 1 O ILE A 21 N TYR A 59
SHEET 3 AA 7 ILE A 123 HIS A 128 1 O HIS A 124 N VAL A 22
SHEET 4 AA 7 VAL A 168 ILE A 174 1 N HIS A 169 O ILE A 123
SHEET 5 AA 7 TYR A 273 TYR A 277 1 O TYR A 273 N ILE A 171
SHEET 6 AA 7 TRP A 361 SER A 363 1 O ASN A 362 N SER A 276
SHEET 7 AA 7 ILE A 349 ASN A 351 1 O VAL A 350 N SER A 363
SHEET 1 AB 2 GLY A 83 ASP A 86 0
SHEET 2 AB 2 TYR A 100 TYR A 104 -1 N GLY A 101 O VAL A 85
SHEET 1 AC 2 THR A 279 CYS A 280 0
SHEET 2 AC 2 LEU A 367 ASP A 368 1 O LEU A 367 N CYS A 280
SHEET 1 BA 7 ALA B 58 ALA B 61 0
SHEET 2 BA 7 ILE B 21 VAL B 24 1 O ILE B 21 N TYR B 59
SHEET 3 BA 7 ILE B 123 HIS B 128 1 O HIS B 124 N VAL B 22
SHEET 4 BA 7 VAL B 168 ILE B 174 1 N HIS B 169 O ILE B 123
SHEET 5 BA 7 TYR B 273 TYR B 277 1 O TYR B 273 N ILE B 171
SHEET 6 BA 7 TRP B 361 SER B 363 1 O ASN B 362 N SER B 276
SHEET 7 BA 7 ILE B 349 ASN B 351 1 O VAL B 350 N SER B 363
SHEET 1 BB 2 GLY B 83 ASP B 86 0
SHEET 2 BB 2 TYR B 100 TYR B 104 -1 N GLY B 101 O VAL B 85
SHEET 1 BC 2 THR B 279 CYS B 280 0
SHEET 2 BC 2 LEU B 367 ASP B 368 1 O LEU B 367 N CYS B 280
LINK ZN ZN A1401 OD1 ASP A 71 1555 1555 1.94
LINK ZN ZN A1401 NE2 HIS A 91 1555 1555 2.08
LINK ZN ZN A1401 NE2 HIS A 97 1555 1555 2.07
LINK ZN ZN A1401 OD2 ASP A 248 1555 1555 1.98
LINK ZN ZN B1403 NE2 HIS B 97 1555 1555 2.07
LINK ZN ZN B1403 OD1 ASP B 71 1555 1555 1.94
LINK ZN ZN B1403 OD2 ASP B 248 1555 1555 1.98
LINK ZN ZN B1403 NE2 HIS B 91 1555 1555 2.08
LINK K K B1405 O HOH A2018 1555 1555 2.81
LINK K K B1405 OD2 ASP B 374 1555 1555 2.74
LINK K K B1405 O HOH B2009 1555 1555 2.59
LINK K K B1405 OG1 THR B 380 1555 1555 2.93
LINK K K B1405 OD1 ASP B 374 1555 1555 3.35
LINK K K B1405 O HOH B2007 1555 1555 3.03
LINK K K B1405 OD2 ASP B 371 1555 1555 3.01
SITE 1 AC1 4 ASP B 71 HIS B 91 HIS B 97 ASP B 248
SITE 1 AC2 4 ASP A 71 HIS A 91 HIS A 97 ASP A 248
SITE 1 AC3 3 ARG A 307 SER A 311 PEG A1402
SITE 1 AC4 4 PRO B 304 ARG B 307 SER B 311 PEG B1404
SITE 1 AC5 6 HOH A2018 ASP B 371 ASP B 374 THR B 380
SITE 2 AC5 6 HOH B2007 HOH B2009
CRYST1 91.800 91.800 215.900 90.00 90.00 90.00 P 41 21 2 1
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 0.010893 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010893 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004632 0.00000
TER 3015 ILE A 400
TER 6044 ASN B 402
MASTER 374 0 5 38 22 0 6 6 6090 2 33 60
END |