| content |
HEADER HYDROLASE 03-APR-24 8YYE
TITLE CRYSTAL STRUCTURE OF LIPASE CTL (CALDIBACILLUS THERMOAMYLOVORANS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDIBACILLUS THERMOAMYLOVORANS;
SOURCE 3 ORGANISM_TAXID: 35841;
SOURCE 4 GENE: BT1A1_2518;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.PAN,D.M.LAN,Y.H.WANG
REVDAT 1 09-APR-25 8YYE 0
JRNL AUTH S.Y.PAN,D.M.LAN,Y.H.WANG
JRNL TITL CRYSTAL STRUCTURE OF LIPASE CTL (CALDIBACILLUS
JRNL TITL 2 THERMOAMYLOVORANS)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 27702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.220
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 6.0600 - 4.8100 0.99 1864 144 0.1700 0.2264
REMARK 3 2 4.8100 - 4.2000 0.99 1837 144 0.1652 0.2014
REMARK 3 3 4.2000 - 3.8200 0.99 1823 141 0.1758 0.2227
REMARK 3 4 3.8200 - 3.5400 0.99 1867 145 0.1893 0.2553
REMARK 3 5 3.5400 - 3.3400 0.99 1817 142 0.2083 0.2562
REMARK 3 6 3.3400 - 3.1700 0.99 1843 142 0.2122 0.2374
REMARK 3 7 3.1700 - 3.0300 0.99 1824 143 0.2144 0.3381
REMARK 3 8 3.0300 - 2.9100 0.99 1848 143 0.2363 0.2858
REMARK 3 9 2.9100 - 2.8100 0.99 1826 142 0.2290 0.2835
REMARK 3 10 2.8100 - 2.7300 0.98 1807 140 0.2111 0.2809
REMARK 3 11 2.7300 - 2.6500 0.98 1838 144 0.2201 0.2675
REMARK 3 12 2.6500 - 2.5800 0.99 1793 138 0.2302 0.2953
REMARK 3 13 2.5800 - 2.5200 0.98 1856 145 0.2554 0.3521
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) : 0.303
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.953
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.90
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 : 0.008 6319
REMARK 3 ANGLE : 0.912 8600
REMARK 3 CHIRALITY : 0.053 856
REMARK 3 PLANARITY : 0.008 1115
REMARK 3 DIHEDRAL : 4.944 849
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 8YYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-APR-24.
REMARK 100 THE DEPOSITION ID IS D_1300046643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JAN-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27750
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 57.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM ZINC ACETATE, 100 MM SODIUM
REMARK 280 ACETATE/ACETIC ACID (PH 4.9), 11% POLYETHYLENE GLYCOL 3000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 74.48250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 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 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 GLU A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 GLU B 1
REMARK 465 THR B 2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 24 CG CD1 CD2
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 OD1 ASN A 378 O HOH A 501 2.06
REMARK 500 OE1 GLU A 173 O HOH A 502 2.07
REMARK 500 OE1 GLU B 36 O HOH B 501 2.09
REMARK 500 NE2 HIS A 83 O HOH A 503 2.11
REMARK 500 O HOH A 524 O HOH A 565 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ASP A 34 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
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 TYR A 96 66.81 -153.99
REMARK 500 ASP A 100 -152.20 -155.65
REMARK 500 SER A 111 -130.75 57.08
REMARK 500 ASN A 152 73.77 -104.76
REMARK 500 LEU A 208 61.94 -114.86
REMARK 500 VAL A 272 -62.52 -90.64
REMARK 500 ILE A 315 -9.94 -149.53
REMARK 500 ASP B 100 -155.07 -170.41
REMARK 500 SER B 111 -130.76 58.06
REMARK 500 VAL B 272 -71.11 -79.63
REMARK 500 ASP B 306 -168.08 -101.20
REMARK 500 ILE B 315 -13.25 -146.84
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 59 OD1
REMARK 620 2 HIS A 79 NE2 104.0
REMARK 620 3 HIS A 85 NE2 118.5 98.1
REMARK 620 4 ASP A 233 OD1 99.3 77.2 141.7
REMARK 620 5 ASP A 233 OD2 129.0 110.5 92.7 55.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 181 OD1
REMARK 620 2 ASP A 181 OD2 49.1
REMARK 620 3 ASP B 181 OD1 165.3 142.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 351 OD2
REMARK 620 2 ASP A 354 OD1 91.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 59 OD1
REMARK 620 2 HIS B 85 NE2 114.8
REMARK 620 3 ASP B 233 OD2 109.8 123.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 82 OE2
REMARK 620 2 HIS B 83 NE2 77.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 283 ND1
REMARK 620 2 ASP B 351 OD2 63.6
REMARK 620 N 1
DBREF1 8YYE A 1 385 UNP A0A090IW71_9BACI
DBREF2 8YYE A A0A090IW71 33 417
DBREF1 8YYE B 1 385 UNP A0A090IW71_9BACI
DBREF2 8YYE B A0A090IW71 33 417
SEQRES 1 A 385 GLU THR SER GLY ASN ASP TYR PRO ILE VAL LEU VAL HIS
SEQRES 2 A 385 GLY LEU GLY GLY TRP GLY LYS GLY GLU PHE LEU GLY TYR
SEQRES 3 A 385 ARG TYR TRP GLY GLY LEU LYS ASP ILE GLU PHE TYR LEU
SEQRES 4 A 385 ASN GLN THR GLY HIS ARG THR TYR VAL ALA THR VAL GLY
SEQRES 5 A 385 PRO VAL SER SER ASN TRP ASP ARG ALA VAL GLU LEU TYR
SEQRES 6 A 385 TYR TYR ILE LYS GLY GLY THR VAL ASP TYR GLY ALA ALA
SEQRES 7 A 385 HIS ALA LYS GLU HIS GLY HIS ALA ARG PHE GLY ARG THR
SEQRES 8 A 385 TYR PRO GLY ILE TYR GLY GLN TRP ASP GLU THR ASN LYS
SEQRES 9 A 385 ILE HIS LEU ILE GLY HIS SER MET GLY GLY GLN THR SER
SEQRES 10 A 385 ARG MET LEU VAL GLU LEU LEU LYS SER GLY SER GLN LYS
SEQRES 11 A 385 GLU GLN GLU TYR TYR SER GLN HIS PRO GLU GLU GLY ILE
SEQRES 12 A 385 SER PRO LEU PHE THR GLY GLY LYS ASN TRP VAL HIS SER
SEQRES 13 A 385 VAL THR SER LEU ALA THR PRO HIS ASN GLY SER THR PHE
SEQRES 14 A 385 ALA ASP GLN GLU GLN ILE VAL SER PHE ILE LYS ASP PHE
SEQRES 15 A 385 ILE ILE HIS LEU ALA SER ALA ALA GLY GLN LYS GLN GLU
SEQRES 16 A 385 SER LEU ILE TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU
SEQRES 17 A 385 LYS ARG GLN PRO GLY GLU SER PHE HIS ALA TYR MET ASN
SEQRES 18 A 385 ARG VAL MET THR SER PRO ILE TRP GLN SER ASN ASP ILE
SEQRES 19 A 385 SER ALA TYR ASP LEU THR THR PHE GLY ALA GLN GLU LEU
SEQRES 20 A 385 ASN GLN TRP MET LYS THR TYR PRO ASP VAL TYR TYR LEU
SEQRES 21 A 385 SER TYR THR GLY ASN ALA SER TYR ARG GLY VAL VAL THR
SEQRES 22 A 385 GLY ASN TYR TYR PRO ILE GLY THR MET HIS PRO LEU PHE
SEQRES 23 A 385 THR LEU ILE SER MET GLN MET GLY SER TYR THR ARG GLN
SEQRES 24 A 385 SER PRO ALA PRO VAL ILE ASP ARG SER TRP LEU PRO ASN
SEQRES 25 A 385 ASP GLY ILE VAL ASN VAL VAL SER ALA LYS TYR PRO PHE
SEQRES 26 A 385 GLY HIS PRO ASN SER PRO TYR ASP GLY ALA ILE LYS GLN
SEQRES 27 A 385 GLY VAL TRP ASN SER PHE PRO VAL MET GLU GLY TRP ASP
SEQRES 28 A 385 HIS MET ASP PHE ILE ASN PHE ILE GLY SER ASN THR PRO
SEQRES 29 A 385 GLY TYR PHE SER ILE TYR GLY TYR TYR ASN ASP VAL ALA
SEQRES 30 A 385 ASN ARG VAL HIS SER LEU PRO LYS
SEQRES 1 B 385 GLU THR SER GLY ASN ASP TYR PRO ILE VAL LEU VAL HIS
SEQRES 2 B 385 GLY LEU GLY GLY TRP GLY LYS GLY GLU PHE LEU GLY TYR
SEQRES 3 B 385 ARG TYR TRP GLY GLY LEU LYS ASP ILE GLU PHE TYR LEU
SEQRES 4 B 385 ASN GLN THR GLY HIS ARG THR TYR VAL ALA THR VAL GLY
SEQRES 5 B 385 PRO VAL SER SER ASN TRP ASP ARG ALA VAL GLU LEU TYR
SEQRES 6 B 385 TYR TYR ILE LYS GLY GLY THR VAL ASP TYR GLY ALA ALA
SEQRES 7 B 385 HIS ALA LYS GLU HIS GLY HIS ALA ARG PHE GLY ARG THR
SEQRES 8 B 385 TYR PRO GLY ILE TYR GLY GLN TRP ASP GLU THR ASN LYS
SEQRES 9 B 385 ILE HIS LEU ILE GLY HIS SER MET GLY GLY GLN THR SER
SEQRES 10 B 385 ARG MET LEU VAL GLU LEU LEU LYS SER GLY SER GLN LYS
SEQRES 11 B 385 GLU GLN GLU TYR TYR SER GLN HIS PRO GLU GLU GLY ILE
SEQRES 12 B 385 SER PRO LEU PHE THR GLY GLY LYS ASN TRP VAL HIS SER
SEQRES 13 B 385 VAL THR SER LEU ALA THR PRO HIS ASN GLY SER THR PHE
SEQRES 14 B 385 ALA ASP GLN GLU GLN ILE VAL SER PHE ILE LYS ASP PHE
SEQRES 15 B 385 ILE ILE HIS LEU ALA SER ALA ALA GLY GLN LYS GLN GLU
SEQRES 16 B 385 SER LEU ILE TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU
SEQRES 17 B 385 LYS ARG GLN PRO GLY GLU SER PHE HIS ALA TYR MET ASN
SEQRES 18 B 385 ARG VAL MET THR SER PRO ILE TRP GLN SER ASN ASP ILE
SEQRES 19 B 385 SER ALA TYR ASP LEU THR THR PHE GLY ALA GLN GLU LEU
SEQRES 20 B 385 ASN GLN TRP MET LYS THR TYR PRO ASP VAL TYR TYR LEU
SEQRES 21 B 385 SER TYR THR GLY ASN ALA SER TYR ARG GLY VAL VAL THR
SEQRES 22 B 385 GLY ASN TYR TYR PRO ILE GLY THR MET HIS PRO LEU PHE
SEQRES 23 B 385 THR LEU ILE SER MET GLN MET GLY SER TYR THR ARG GLN
SEQRES 24 B 385 SER PRO ALA PRO VAL ILE ASP ARG SER TRP LEU PRO ASN
SEQRES 25 B 385 ASP GLY ILE VAL ASN VAL VAL SER ALA LYS TYR PRO PHE
SEQRES 26 B 385 GLY HIS PRO ASN SER PRO TYR ASP GLY ALA ILE LYS GLN
SEQRES 27 B 385 GLY VAL TRP ASN SER PHE PRO VAL MET GLU GLY TRP ASP
SEQRES 28 B 385 HIS MET ASP PHE ILE ASN PHE ILE GLY SER ASN THR PRO
SEQRES 29 B 385 GLY TYR PHE SER ILE TYR GLY TYR TYR ASN ASP VAL ALA
SEQRES 30 B 385 ASN ARG VAL HIS SER LEU PRO LYS
HET ZN A 401 1
HET ZN A 402 1
HET ZN A 403 1
HET ZN B 401 1
HET ZN B 402 1
HET ZN B 403 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 6(ZN 2+)
FORMUL 9 HOH *127(H2 O)
HELIX 1 AA1 ASP A 34 THR A 42 1 9
HELIX 2 AA2 SER A 56 GLY A 70 1 15
HELIX 3 AA3 GLY A 76 GLY A 84 1 9
HELIX 4 AA4 SER A 111 GLY A 127 1 17
HELIX 5 AA5 SER A 128 HIS A 138 1 11
HELIX 6 AA6 PRO A 139 GLY A 142 5 4
HELIX 7 AA7 SER A 144 THR A 148 5 5
HELIX 8 AA8 PHE A 169 GLU A 173 5 5
HELIX 9 AA9 GLN A 174 ALA A 190 1 17
HELIX 10 AB1 LYS A 193 LEU A 197 5 5
HELIX 11 AB2 LEU A 203 GLY A 207 5 5
HELIX 12 AB3 SER A 215 SER A 226 1 12
HELIX 13 AB4 PRO A 227 SER A 231 5 5
HELIX 14 AB5 ILE A 234 THR A 240 1 7
HELIX 15 AB6 THR A 240 GLN A 249 1 10
HELIX 16 AB7 PHE A 286 TYR A 296 1 11
HELIX 17 AB8 ASP A 306 LEU A 310 5 5
HELIX 18 AB9 ASN A 317 LYS A 322 1 6
HELIX 19 AC1 MET A 353 ASN A 357 5 5
HELIX 20 AC2 SER A 368 SER A 382 1 15
HELIX 21 AC3 ASP B 34 THR B 42 1 9
HELIX 22 AC4 SER B 56 GLY B 70 1 15
HELIX 23 AC5 GLY B 76 GLY B 84 1 9
HELIX 24 AC6 SER B 111 GLY B 127 1 17
HELIX 25 AC7 SER B 128 HIS B 138 1 11
HELIX 26 AC8 PRO B 139 GLY B 142 5 4
HELIX 27 AC9 SER B 144 GLY B 149 1 6
HELIX 28 AD1 PHE B 169 GLU B 173 5 5
HELIX 29 AD2 GLN B 174 ALA B 190 1 17
HELIX 30 AD3 LYS B 193 LEU B 197 5 5
HELIX 31 AD4 LEU B 203 GLY B 207 5 5
HELIX 32 AD5 SER B 215 SER B 226 1 12
HELIX 33 AD6 PRO B 227 SER B 231 5 5
HELIX 34 AD7 ILE B 234 LEU B 239 1 6
HELIX 35 AD8 THR B 240 GLN B 249 1 10
HELIX 36 AD9 HIS B 283 LEU B 285 5 3
HELIX 37 AE1 PHE B 286 GLY B 294 1 9
HELIX 38 AE2 ASP B 306 LEU B 310 5 5
HELIX 39 AE3 ASN B 317 LYS B 322 1 6
HELIX 40 AE4 ASP B 351 ASN B 357 5 7
HELIX 41 AE5 SER B 368 SER B 382 1 15
SHEET 1 AA1 7 THR A 46 ALA A 49 0
SHEET 2 AA1 7 ILE A 9 VAL A 12 1 N LEU A 11 O TYR A 47
SHEET 3 AA1 7 ILE A 105 HIS A 110 1 O ILE A 108 N VAL A 10
SHEET 4 AA1 7 VAL A 154 LEU A 160 1 O SER A 156 N LEU A 107
SHEET 5 AA1 7 TYR A 258 TYR A 262 1 O TYR A 258 N VAL A 157
SHEET 6 AA1 7 TRP A 341 SER A 343 1 O ASN A 342 N TYR A 259
SHEET 7 AA1 7 ASN A 329 PRO A 331 1 N SER A 330 O TRP A 341
SHEET 1 AA2 2 GLY A 71 ASP A 74 0
SHEET 2 AA2 2 PHE A 88 TYR A 92 -1 O ARG A 90 N VAL A 73
SHEET 1 AA3 2 GLY A 264 ASN A 265 0
SHEET 2 AA3 2 MET A 347 GLU A 348 1 O MET A 347 N ASN A 265
SHEET 1 AA4 2 SER A 267 ARG A 269 0
SHEET 2 AA4 2 TYR A 276 PRO A 278 -1 O TYR A 277 N TYR A 268
SHEET 1 AA5 7 THR B 46 ALA B 49 0
SHEET 2 AA5 7 ILE B 9 VAL B 12 1 N ILE B 9 O TYR B 47
SHEET 3 AA5 7 ILE B 105 HIS B 110 1 O HIS B 106 N VAL B 10
SHEET 4 AA5 7 VAL B 154 LEU B 160 1 O SER B 156 N LEU B 107
SHEET 5 AA5 7 TYR B 258 TYR B 262 1 O LEU B 260 N SER B 159
SHEET 6 AA5 7 TRP B 341 SER B 343 1 O ASN B 342 N TYR B 259
SHEET 7 AA5 7 ASN B 329 PRO B 331 1 N SER B 330 O TRP B 341
SHEET 1 AA6 2 GLY B 71 ASP B 74 0
SHEET 2 AA6 2 PHE B 88 TYR B 92 -1 O ARG B 90 N VAL B 73
SHEET 1 AA7 2 GLY B 264 ASN B 265 0
SHEET 2 AA7 2 MET B 347 GLU B 348 1 O MET B 347 N ASN B 265
SHEET 1 AA8 2 SER B 267 ARG B 269 0
SHEET 2 AA8 2 TYR B 276 PRO B 278 -1 O TYR B 277 N TYR B 268
LINK OD1 ASP A 59 ZN ZN A 401 1555 1555 2.04
LINK NE2 HIS A 79 ZN ZN A 401 1555 1555 2.18
LINK NE2 HIS A 85 ZN ZN A 401 1555 1555 2.30
LINK OD1 ASP A 181 ZN ZN A 402 1555 1555 2.59
LINK OD2 ASP A 181 ZN ZN A 402 1555 1555 2.64
LINK OD1 ASP A 233 ZN ZN A 401 1555 1555 2.64
LINK OD2 ASP A 233 ZN ZN A 401 1555 1555 1.87
LINK OD2 ASP A 351 ZN ZN A 403 1555 1555 1.83
LINK OD1 ASP A 354 ZN ZN A 403 1555 1555 1.99
LINK ZN ZN A 402 OD1 ASP B 181 1555 1555 2.42
LINK OD1 ASP B 59 ZN ZN B 401 1555 1555 2.05
LINK OE2 GLU B 82 ZN ZN B 402 1555 1555 1.92
LINK NE2 HIS B 83 ZN ZN B 402 1555 1555 2.28
LINK NE2 HIS B 85 ZN ZN B 401 1555 1555 2.29
LINK OD2 ASP B 233 ZN ZN B 401 1555 1555 1.78
LINK ND1 HIS B 283 ZN ZN B 403 1555 1555 2.34
LINK OD2 ASP B 351 ZN ZN B 403 1555 1555 2.20
CISPEP 1 SER A 300 PRO A 301 0 -8.57
CISPEP 2 ALA A 302 PRO A 303 0 4.47
CISPEP 3 SER B 300 PRO B 301 0 -4.40
CISPEP 4 ALA B 302 PRO B 303 0 0.55
CRYST1 48.859 148.965 58.884 90.00 100.95 90.00 P 1 21 1 4
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 0.020467 0.000000 0.003959 0.00000
SCALE2 0.000000 0.006713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017297 0.00000
TER 3053 LYS A 385
TER 6115 LYS B 385
MASTER 329 0 6 41 26 0 0 6 6246 2 24 60
END |