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HEADER HYDROLASE 29-MAY-21 7EY3
TITLE DOUBLE CYSTEINE MUTATIONS IN T1 LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS ZALIHAE;
SOURCE 3 ORGANISM_TAXID: 213419;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DISULPHIDE BOND, CYSTEINE, LIPASE, SITE-DIRECTED MUTAGENESIS,
KEYWDS 2 STRUCTURAL PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.HAMDAN,T.C.LEOW,N.M.YAHAYA,M.S.M.ALI,M.A.JONET,S.N.A.MOHAMAD
AUTHOR 2 ARIS,J.MAIANGWA
REVDAT 1 14-DEC-22 7EY3 0
JRNL AUTH S.H.HAMDAN,T.C.LEOW
JRNL TITL DOUBLE CYSTEINE MUTATIONS IN T1 LIPASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.04 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 59541
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.360
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 33.4600 - 4.9100 1.00 4253 148 0.1522 0.1758
REMARK 3 2 4.9100 - 3.9000 1.00 4179 145 0.1345 0.1502
REMARK 3 3 3.9000 - 3.4100 1.00 4155 144 0.1613 0.1915
REMARK 3 4 3.4100 - 3.1000 1.00 4159 145 0.1947 0.2155
REMARK 3 5 3.1000 - 2.8700 1.00 4125 143 0.2198 0.2628
REMARK 3 6 2.8700 - 2.7100 1.00 4146 144 0.2193 0.2834
REMARK 3 7 2.7100 - 2.5700 1.00 4114 142 0.2099 0.2451
REMARK 3 8 2.5700 - 2.4600 1.00 4137 144 0.2031 0.2345
REMARK 3 9 2.4600 - 2.3600 0.99 4132 144 0.1965 0.2247
REMARK 3 10 2.3600 - 2.2800 0.99 4096 142 0.2136 0.2872
REMARK 3 11 2.2800 - 2.2100 0.99 4069 141 0.2355 0.2535
REMARK 3 12 2.2100 - 2.1500 0.98 4047 141 0.2229 0.2867
REMARK 3 13 2.1500 - 2.0900 0.97 3989 138 0.2065 0.2425
REMARK 3 14 2.0900 - 2.0400 0.96 3942 137 0.2178 0.2813
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) : 0.228
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.92
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 6276
REMARK 3 ANGLE : 0.885 8536
REMARK 3 CHIRALITY : 0.052 894
REMARK 3 PLANARITY : 0.005 1124
REMARK 3 DIHEDRAL : 16.003 862
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 7EY3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1300022405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-20
REMARK 200 TEMPERATURE (KELVIN) : 293.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59606
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
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: 2DSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M SODIUM CHLORIDE, 0.1M SODIUM
REMARK 280 CITRATE DIHYDRATE PH 5.6, 2 % ETHYLENE IMINE POLYMER, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 59.08700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.74800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.08700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.74800
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
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 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 634 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 637 LIES ON A SPECIAL POSITION.
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 NH2 ARG B 303 OD1 ASP B 311 2.18
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 SER A 113 -133.42 57.91
REMARK 500 PHE A 154 11.52 -149.19
REMARK 500 VAL A 203 -54.41 64.53
REMARK 500 LEU A 208 39.69 -96.39
REMARK 500 ARG A 271 43.55 -148.45
REMARK 500 ASP A 310 -152.29 -121.15
REMARK 500 ILE A 319 -42.56 -132.48
REMARK 500 LYS A 329 -52.00 -134.73
REMARK 500 ASN A 367 90.06 -161.48
REMARK 500 SER B 113 -135.89 57.32
REMARK 500 VAL B 203 -59.07 71.18
REMARK 500 LEU B 208 38.30 -97.63
REMARK 500 ARG B 271 40.99 -149.93
REMARK 500 LEU B 277 -71.56 -100.29
REMARK 500 ASP B 310 -154.90 -123.13
REMARK 500 ILE B 319 -41.00 -132.94
REMARK 500 LYS B 329 -51.40 -130.25
REMARK 500 ASN B 367 91.60 -165.03
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 A2290 DISTANCE = 5.85 ANGSTROMS
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 A2001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 HIS A 81 NE2 95.2
REMARK 620 3 HIS A 87 NE2 114.2 109.8
REMARK 620 4 ASP A 238 OD2 131.2 102.8 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2003 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 113 OG
REMARK 620 2 HOH A2214 O 88.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 85.9
REMARK 620 3 ASP A 365 OD2 108.0 121.3
REMARK 620 4 PRO A 366 O 158.4 97.4 88.6
REMARK 620 5 HOH A2259 O 81.5 116.4 121.9 77.9
REMARK 620 N 1 2 3 4
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 61 OD1
REMARK 620 2 HIS B 81 NE2 96.4
REMARK 620 3 HIS B 87 NE2 110.9 105.9
REMARK 620 4 ASP B 238 OD2 131.7 106.2 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 113 OG
REMARK 620 2 HOH B 608 O 90.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 286 O
REMARK 620 2 GLU B 360 OE2 84.5
REMARK 620 3 ASP B 365 OD2 111.9 112.2
REMARK 620 4 PRO B 366 O 158.4 88.4 89.6
REMARK 620 N 1 2 3
DBREF 7EY3 A 2 388 UNP Q842J9 Q842J9_9BACI 30 416
DBREF 7EY3 B 2 388 UNP Q842J9 Q842J9_9BACI 30 416
SEQADV 7EY3 CYS A 2 UNP Q842J9 SER 30 ENGINEERED MUTATION
SEQADV 7EY3 CYS A 384 UNP Q842J9 ALA 412 ENGINEERED MUTATION
SEQADV 7EY3 CYS B 2 UNP Q842J9 SER 30 ENGINEERED MUTATION
SEQADV 7EY3 CYS B 384 UNP Q842J9 ALA 412 ENGINEERED MUTATION
SEQRES 1 A 387 CYS LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 A 387 GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE
SEQRES 3 A 387 LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP
SEQRES 4 A 387 LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL
SEQRES 5 A 387 GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA
SEQRES 6 A 387 TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA
SEQRES 7 A 387 ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG
SEQRES 8 A 387 THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY
SEQRES 9 A 387 ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR
SEQRES 10 A 387 ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN
SEQRES 11 A 387 GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU
SEQRES 12 A 387 SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER
SEQRES 13 A 387 VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU
SEQRES 14 A 387 VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU
SEQRES 15 A 387 GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN
SEQRES 16 A 387 VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP
SEQRES 17 A 387 GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP
SEQRES 18 A 387 HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR
SEQRES 19 A 387 SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY
SEQRES 20 A 387 ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN
SEQRES 21 A 387 THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG
SEQRES 22 A 387 GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET
SEQRES 23 A 387 ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY
SEQRES 24 A 387 SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP
SEQRES 25 A 387 LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN
SEQRES 26 A 387 GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR
SEQRES 27 A 387 ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY
SEQRES 28 A 387 THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP
SEQRES 29 A 387 PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG
SEQRES 30 A 387 LEU ALA GLU GLN LEU CYS SER LEU GLN PRO
SEQRES 1 B 387 CYS LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 B 387 GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE
SEQRES 3 B 387 LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP
SEQRES 4 B 387 LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL
SEQRES 5 B 387 GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA
SEQRES 6 B 387 TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA
SEQRES 7 B 387 ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG
SEQRES 8 B 387 THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY
SEQRES 9 B 387 ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR
SEQRES 10 B 387 ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN
SEQRES 11 B 387 GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU
SEQRES 12 B 387 SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER
SEQRES 13 B 387 VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU
SEQRES 14 B 387 VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU
SEQRES 15 B 387 GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN
SEQRES 16 B 387 VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP
SEQRES 17 B 387 GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP
SEQRES 18 B 387 HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR
SEQRES 19 B 387 SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY
SEQRES 20 B 387 ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN
SEQRES 21 B 387 THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG
SEQRES 22 B 387 GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET
SEQRES 23 B 387 ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY
SEQRES 24 B 387 SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP
SEQRES 25 B 387 LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN
SEQRES 26 B 387 GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR
SEQRES 27 B 387 ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY
SEQRES 28 B 387 THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP
SEQRES 29 B 387 PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG
SEQRES 30 B 387 LEU ALA GLU GLN LEU CYS SER LEU GLN PRO
HET ZN A2001 1
HET CA A2002 1
HET NA A2003 1
HET CL A2004 1
HET ZN B 401 1
HET CA B 402 1
HET NA B 403 1
HET CL B 404 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 CL 2(CL 1-)
FORMUL 11 HOH *346(H2 O)
HELIX 1 AA1 GLU A 23 PHE A 27 5 5
HELIX 2 AA2 GLY A 31 GLY A 35 5 5
HELIX 3 AA3 ASP A 36 ASN A 44 1 9
HELIX 4 AA4 SER A 58 GLY A 72 1 15
HELIX 5 AA5 GLY A 78 GLY A 86 1 9
HELIX 6 AA6 LEU A 98 ARG A 103 5 6
HELIX 7 AA7 GLN A 114 GLY A 129 1 16
HELIX 8 AA8 SER A 130 ASN A 141 1 12
HELIX 9 AA9 SER A 145 GLU A 149 5 5
HELIX 10 AB1 THR A 168 MET A 173 5 6
HELIX 11 AB2 ASP A 175 ALA A 191 1 17
HELIX 12 AB3 SER A 220 ARG A 230 1 11
HELIX 13 AB4 SER A 231 SER A 236 1 6
HELIX 14 AB5 THR A 239 SER A 245 1 7
HELIX 15 AB6 SER A 245 VAL A 256 1 12
HELIX 16 AB7 ASN A 288 CYS A 295 1 8
HELIX 17 AB8 CYS A 295 GLY A 300 1 6
HELIX 18 AB9 ASP A 310 LEU A 314 5 5
HELIX 19 AC1 ASN A 321 ASN A 326 5 6
HELIX 20 AC2 ASP A 371 SER A 385 1 15
HELIX 21 AC3 GLU B 23 PHE B 27 5 5
HELIX 22 AC4 GLY B 31 GLY B 35 5 5
HELIX 23 AC5 ASP B 36 ASN B 44 1 9
HELIX 24 AC6 SER B 58 GLY B 72 1 15
HELIX 25 AC7 GLY B 78 GLY B 86 1 9
HELIX 26 AC8 LEU B 98 GLY B 104 5 7
HELIX 27 AC9 GLN B 114 GLY B 129 1 16
HELIX 28 AD1 SER B 130 ASN B 141 1 12
HELIX 29 AD2 SER B 145 GLU B 149 5 5
HELIX 30 AD3 THR B 168 MET B 173 5 6
HELIX 31 AD4 ASP B 175 ALA B 191 1 17
HELIX 32 AD5 LEU B 208 GLY B 212 5 5
HELIX 33 AD6 SER B 220 ARG B 230 1 11
HELIX 34 AD7 SER B 231 SER B 236 1 6
HELIX 35 AD8 THR B 239 SER B 245 1 7
HELIX 36 AD9 SER B 245 VAL B 256 1 12
HELIX 37 AE1 ASN B 288 CYS B 295 1 8
HELIX 38 AE2 CYS B 295 GLY B 300 1 6
HELIX 39 AE3 ASN B 304 GLY B 308 5 5
HELIX 40 AE4 ASP B 310 LEU B 314 5 5
HELIX 41 AE5 ASN B 321 MET B 325 5 5
HELIX 42 AE6 ASP B 371 SER B 385 1 15
SHEET 1 AA1 7 THR A 48 LEU A 51 0
SHEET 2 AA1 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 AA1 7 ILE A 107 HIS A 112 1 O ILE A 110 N VAL A 11
SHEET 4 AA1 7 VAL A 155 ILE A 161 1 O THR A 159 N ALA A 111
SHEET 5 AA1 7 TYR A 263 THR A 269 1 O TYR A 263 N VAL A 158
SHEET 6 AA1 7 TRP A 348 TYR A 354 1 O ASN A 349 N TYR A 264
SHEET 7 AA1 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 AA2 2 GLY A 73 ASP A 76 0
SHEET 2 AA2 2 PHE A 90 TYR A 94 -1 O ARG A 92 N VAL A 75
SHEET 1 AA3 2 THR A 272 ARG A 274 0
SHEET 2 AA3 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 AA4 7 THR B 48 THR B 50 0
SHEET 2 AA4 7 ILE B 10 LEU B 13 1 N LEU B 12 O TYR B 49
SHEET 3 AA4 7 ILE B 107 HIS B 112 1 O HIS B 108 N VAL B 11
SHEET 4 AA4 7 VAL B 155 ILE B 161 1 O THR B 159 N ILE B 109
SHEET 5 AA4 7 TYR B 263 THR B 269 1 O LEU B 265 N THR B 160
SHEET 6 AA4 7 TRP B 348 TYR B 354 1 O ASN B 349 N TYR B 264
SHEET 7 AA4 7 ILE B 336 PRO B 338 1 N VAL B 337 O TRP B 348
SHEET 1 AA5 2 GLY B 73 ASP B 76 0
SHEET 2 AA5 2 PHE B 90 TYR B 94 -1 O ARG B 92 N VAL B 75
SHEET 1 AA6 2 THR B 272 ARG B 274 0
SHEET 2 AA6 2 HIS B 281 PRO B 283 -1 O TYR B 282 N TYR B 273
SSBOND 1 CYS A 2 CYS A 384 1555 1555 2.05
SSBOND 2 CYS B 2 CYS B 384 1555 1555 2.05
LINK OD1 ASP A 61 ZN ZN A2001 1555 1555 2.12
LINK NE2 HIS A 81 ZN ZN A2001 1555 1555 2.24
LINK NE2 HIS A 87 ZN ZN A2001 1555 1555 2.24
LINK OG SER A 113 NA NA A2003 1555 1555 2.61
LINK OD2 ASP A 238 ZN ZN A2001 1555 1555 1.98
LINK O GLY A 286 CA CA A2002 1555 1555 2.31
LINK OE2 GLU A 360 CA CA A2002 1555 1555 2.31
LINK OD2 ASP A 365 CA CA A2002 1555 1555 2.43
LINK O PRO A 366 CA CA A2002 1555 1555 2.40
LINK CA CA A2002 O HOH A2259 1555 1555 2.61
LINK NA NA A2003 O HOH A2214 1555 1555 2.51
LINK OD1 ASP B 61 ZN ZN B 401 1555 1555 2.09
LINK NE2 HIS B 81 ZN ZN B 401 1555 1555 2.19
LINK NE2 HIS B 87 ZN ZN B 401 1555 1555 2.27
LINK OG SER B 113 NA NA B 403 1555 1555 2.45
LINK OD2 ASP B 238 ZN ZN B 401 1555 1555 2.00
LINK O GLY B 286 CA CA B 402 1555 1555 2.31
LINK OE2 GLU B 360 CA CA B 402 1555 1555 2.47
LINK OD2 ASP B 365 CA CA B 402 1555 1555 2.32
LINK O PRO B 366 CA CA B 402 1555 1555 2.48
LINK NA NA B 403 O HOH B 608 1555 1555 2.48
CRYST1 118.174 81.496 100.046 90.00 96.94 90.00 C 1 2 1 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 0.008462 0.000000 0.001030 0.00000
SCALE2 0.000000 0.012271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010069 0.00000
TER 3055 PRO A 388
TER 6110 PRO B 388
MASTER 340 0 8 42 22 0 0 6 6462 2 32 60
END |