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HEADER HYDROLASE 13-JUN-12 4FKB
TITLE AN ORGANIC SOLVENT TOLERANT LIPASE 42
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE ORGANIC SOLVENT TOLERANT 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: BACILLUS SP. 42;
SOURCE 3 ORGANISM_TAXID: 294830;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS A/B CANNONICAL FOLD, HYDROLASE, CLEAVE LIPID
EXPDTA X-RAY DIFFRACTION
AUTHOR R.N.ZALIHA,R.A.RAHMAN,M.S.KHUSAINI
REVDAT 1 19-JUN-13 4FKB 0
JRNL AUTH R.N.ZALIHA,R.N.RAHMAN,M.S.KHUSAINI
JRNL TITL AN ORGANIC SOLVENT TOLERANT LIPASE 42
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 244769
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.129
REMARK 3 R VALUE (WORKING SET) : 0.127
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12959
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16466
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 891
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6102
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 143
REMARK 3 SOLVENT ATOMS : 1015
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : -0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.034
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.025
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.300
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6797 ; 0.025 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9291 ; 2.308 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 889 ; 5.912 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 337 ;33.283 ;22.967
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1058 ;12.487 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;16.315 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 993 ; 0.172 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5350 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4040 ; 2.650 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6550 ; 3.567 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2757 ; 5.325 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2687 ; 7.411 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 6796 ; 9.943 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 287 ;47.343 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 7340 ;14.173 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4FKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.75
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 275120
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.220
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
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: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: COUNTER-DIFFUSION METHOD WITHOUT
REMARK 280 MIXING THE PROTEIN AND PRECIPITANT, PH 8, LIQUID DIFFUSION,
REMARK 280 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 58.91200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.50050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.91200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.50050
REMARK 290 SMTRY3 4 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 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 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 CL CL A 416 LIES ON A SPECIAL POSITION.
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 ALA A 1
REMARK 465 ALA B 1
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 GLN A 216 CG CD OE1 NE2
REMARK 470 GLU B 381 CG CD OE1 OE2
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 O1 GOL A 402 C1 GOL A 411 1.45
REMARK 500 O HOH B 537 O HOH B 717 1.73
REMARK 500 O HOH B 717 O HOH B 935 1.74
REMARK 500 O HOH A 682 O HOH A 968 1.77
REMARK 500 O HOH B 668 O HOH B 909 1.79
REMARK 500 OG SER A 201 O2 GOL A 411 1.81
REMARK 500 NH1 ARG A 378 O HOH A 1010 1.81
REMARK 500 CE2 PHE A 16 O HOH A 710 1.83
REMARK 500 OE2 GLU B 149 O HOH B 938 1.85
REMARK 500 OE1 GLN B 131 O HOH B 977 1.95
REMARK 500 NE2 GLN A 254 O HOH A 935 1.96
REMARK 500 O3 GOL B 407 O HOH B 916 1.97
REMARK 500 O HOH B 799 O HOH B 981 1.97
REMARK 500 CG2 THR A 306 O HOH A 683 1.99
REMARK 500 O HOH B 631 O HOH B 824 2.05
REMARK 500 O HOH A 686 O HOH A 990 2.06
REMARK 500 O HOH A 915 O HOH A 1019 2.08
REMARK 500 O HOH A 655 O HOH A 1015 2.08
REMARK 500 O1 GOL B 410 O HOH B 780 2.09
REMARK 500 O HOH B 811 O HOH B 987 2.09
REMARK 500 OE1 GLU A 250 O HOH A 947 2.11
REMARK 500 O HOH A 713 O HOH A 965 2.12
REMARK 500 O HOH A 996 O HOH A 1022 2.12
REMARK 500 O HOH A 778 O HOH A 1014 2.13
REMARK 500 O HOH A 702 O HOH A 896 2.14
REMARK 500 O HOH A 761 O HOH A 1000 2.14
REMARK 500 O HOH A 728 O HOH A 995 2.16
REMARK 500 O HOH B 970 O HOH B 971 2.17
REMARK 500 OG SER B 201 O HOH B 702 2.17
REMARK 500 CZ PHE A 16 O HOH A 710 2.17
REMARK 500 O HOH A 757 O HOH A 987 2.17
REMARK 500 O HOH A 732 O HOH A 849 2.18
REMARK 500 O HOH B 907 O HOH B 984 2.19
REMARK 500 O HOH B 729 O HOH B 796 2.19
REMARK 500 NH2 ARG B 214 O HOH B 749 2.19
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 683 O HOH B 718 4545 2.03
REMARK 500 O HOH B 736 O HOH B 761 4545 2.09
REMARK 500 O HOH A 684 O HOH B 682 3445 2.16
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 TRP A 40 CE2 TRP A 40 CD2 0.083
REMARK 500 GLU A 100 CD GLU A 100 OE1 0.094
REMARK 500 ARG A 303 CZ ARG A 303 NH1 0.138
REMARK 500 ARG A 303 CZ ARG A 303 NH2 0.109
REMARK 500 GLU B 202 CB GLU B 202 CG -0.130
REMARK 500 GLU B 202 CD GLU B 202 OE2 0.110
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 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU A 277 CB - CG - CD2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 GLY A 279 C - N - CA ANGL. DEV. = -17.3 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TYR A 354 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 357 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 378 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 LEU B 3 CA - CB - CG ANGL. DEV. = -17.5 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG B 214 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 214 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 303 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 330 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 357 CB - CG - OD1 ANGL. DEV. = 8.1 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 SER A 113 -136.14 56.69
REMARK 500 VAL A 203 -59.17 70.18
REMARK 500 LEU A 208 37.29 -99.42
REMARK 500 ARG A 271 44.15 -147.18
REMARK 500 LEU A 277 -71.73 -87.71
REMARK 500 ASP A 310 -155.77 -130.29
REMARK 500 ILE A 319 -41.32 -138.89
REMARK 500 LYS A 329 -46.40 -133.66
REMARK 500 ASN A 367 90.21 -164.99
REMARK 500 SER B 113 -138.16 59.87
REMARK 500 ASP B 175 37.39 -95.03
REMARK 500 VAL B 203 -55.82 72.17
REMARK 500 LEU B 208 35.31 -99.57
REMARK 500 ARG B 271 45.74 -152.67
REMARK 500 LEU B 277 -66.62 -93.31
REMARK 500 ASN B 304 82.83 -151.11
REMARK 500 ASP B 310 -158.54 -127.55
REMARK 500 ILE B 319 -36.14 -137.35
REMARK 500 LYS B 329 -51.73 -133.22
REMARK 500 ASN B 367 91.64 -169.91
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 PHE A 16 THR A 17 149.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 294 21.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GOL A 402
REMARK 610 GOL A 411
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 B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 238 OD2
REMARK 620 2 ASP B 61 OD1 124.8
REMARK 620 3 HIS B 87 NE2 97.6 120.2
REMARK 620 4 HIS B 81 NE2 107.4 98.7 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 202 OE1
REMARK 620 2 GLU A 202 OE2 41.6
REMARK 620 N 1
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 238 OD2
REMARK 620 2 ASP A 61 OD1 129.4
REMARK 620 3 HIS A 81 NE2 107.8 98.4
REMARK 620 4 HIS A 87 NE2 96.6 116.0 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 693 O
REMARK 620 2 LYS A 329 O 94.1
REMARK 620 3 HOH A 766 O 178.0 87.9
REMARK 620 4 SER A 332 O 90.3 95.3 89.9
REMARK 620 5 HOH A 861 O 55.9 146.9 122.2 73.4
REMARK 620 6 HOH A 826 O 95.7 76.4 84.5 170.1 116.5
REMARK 620 N 1 2 3 4 5
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 HOH B 910 O
REMARK 620 2 HOH B 575 O 76.9
REMARK 620 3 SER B 369 OG 108.9 84.3
REMARK 620 4 HOH B 724 O 100.0 91.1 148.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 742 O
REMARK 620 2 HOH A 743 O 172.5
REMARK 620 3 HOH A 760 O 85.4 92.6
REMARK 620 4 HOH A 578 O 83.5 89.1 83.4
REMARK 620 5 HOH A 967 O 76.3 110.6 81.0 155.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 578 O
REMARK 620 2 THR A 272 O 170.7
REMARK 620 3 HOH A 760 O 91.5 89.6
REMARK 620 4 GLU A 270 OE1 91.4 92.9 145.5
REMARK 620 5 GLU A 284 OE2 76.2 94.6 104.1 109.9
REMARK 620 6 HOH A 577 O 126.3 62.9 75.8 74.8 157.4
REMARK 620 7 HOH A 684 O 89.7 83.9 50.4 163.9 54.9 116.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 816 O
REMARK 620 2 HOH B 730 O 80.8
REMARK 620 3 LYS B 329 O 165.3 93.9
REMARK 620 4 HOH B 757 O 93.5 172.1 92.9
REMARK 620 5 SER B 332 O 71.5 91.1 95.0 92.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 272 O
REMARK 620 2 HOH B 726 O 150.0
REMARK 620 3 GLU B 270 OE1 96.2 90.4
REMARK 620 4 HOH B 621 O 69.0 140.8 76.7
REMARK 620 5 HOH B 653 O 79.9 83.0 157.6 121.1
REMARK 620 6 HOH B 900 O 135.7 71.2 99.2 74.6 98.8
REMARK 620 7 GLU B 284 OE2 85.1 64.9 102.3 153.7 55.6 130.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 918 O
REMARK 620 2 HOH B 929 O 87.5
REMARK 620 3 HOH A 884 O 171.4 98.3
REMARK 620 4 HOH A 727 O 94.2 161.1 78.3
REMARK 620 5 HOH B 746 O 89.9 79.8 85.0 81.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 424 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 360 OE2
REMARK 620 2 GLY B 286 O 85.1
REMARK 620 3 HOH B 660 O 147.7 86.9
REMARK 620 4 PRO B 366 O 91.9 165.3 88.0
REMARK 620 5 ASP B 365 OD2 111.5 104.2 100.8 90.3
REMARK 620 6 HOH B 691 O 91.6 88.3 56.9 77.3 154.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 420 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 666 O
REMARK 620 2 PRO A 366 O 89.1
REMARK 620 3 GLY A 286 O 87.8 165.0
REMARK 620 4 GLU A 360 OE2 145.6 90.3 83.9
REMARK 620 5 ASP A 365 OD2 101.3 91.8 103.2 113.0
REMARK 620 6 HOH A 747 O 57.6 80.5 85.5 88.4 157.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 733 O
REMARK 620 2 HOH B 519 O 113.8
REMARK 620 3 ALA B 192 O 78.0 88.3
REMARK 620 4 HOH B 543 O 72.0 162.4 76.5
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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 421
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 424
DBREF 4FKB A 1 388 UNP Q5U780 Q5U780_9BACI 29 416
DBREF 4FKB B 1 388 UNP Q5U780 Q5U780_9BACI 29 416
SEQADV 4FKB LEU A 147 UNP Q5U780 TRP 175 ENGINEERED MUTATION
SEQADV 4FKB GLU A 202 UNP Q5U780 GLN 230 ENGINEERED MUTATION
SEQADV 4FKB LEU B 147 UNP Q5U780 TRP 175 ENGINEERED MUTATION
SEQADV 4FKB GLU B 202 UNP Q5U780 GLN 230 ENGINEERED MUTATION
SEQRES 1 A 388 ALA SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU
SEQRES 2 A 388 HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY
SEQRES 3 A 388 PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN
SEQRES 4 A 388 TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA
SEQRES 5 A 388 VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU
SEQRES 6 A 388 ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY
SEQRES 7 A 388 ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY
SEQRES 8 A 388 ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY
SEQRES 9 A 388 GLY ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN
SEQRES 10 A 388 THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER
SEQRES 11 A 388 GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER
SEQRES 12 A 388 LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU
SEQRES 13 A 388 SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR
SEQRES 14 A 388 LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP
SEQRES 15 A 388 LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER
SEQRES 16 A 388 ASN VAL PRO TYR THR SER GLU VAL TYR ASP PHE LYS LEU
SEQRES 17 A 388 ASP GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE
SEQRES 18 A 388 ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP
SEQRES 19 A 388 THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER
SEQRES 20 A 388 GLY ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO
SEQRES 21 A 388 ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR
SEQRES 22 A 388 ARG GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY
SEQRES 23 A 388 MET ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU
SEQRES 24 A 388 GLY SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG
SEQRES 25 A 388 TRP LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET
SEQRES 26 A 388 ASN GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO
SEQRES 27 A 388 TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET
SEQRES 28 A 388 GLY THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL
SEQRES 29 A 388 ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU
SEQRES 30 A 388 ARG LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
SEQRES 1 B 388 ALA SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU
SEQRES 2 B 388 HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY
SEQRES 3 B 388 PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN
SEQRES 4 B 388 TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA
SEQRES 5 B 388 VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU
SEQRES 6 B 388 ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY
SEQRES 7 B 388 ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY
SEQRES 8 B 388 ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY
SEQRES 9 B 388 GLY ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN
SEQRES 10 B 388 THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER
SEQRES 11 B 388 GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER
SEQRES 12 B 388 LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU
SEQRES 13 B 388 SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR
SEQRES 14 B 388 LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP
SEQRES 15 B 388 LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER
SEQRES 16 B 388 ASN VAL PRO TYR THR SER GLU VAL TYR ASP PHE LYS LEU
SEQRES 17 B 388 ASP GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE
SEQRES 18 B 388 ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP
SEQRES 19 B 388 THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER
SEQRES 20 B 388 GLY ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO
SEQRES 21 B 388 ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR
SEQRES 22 B 388 ARG GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY
SEQRES 23 B 388 MET ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU
SEQRES 24 B 388 GLY SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG
SEQRES 25 B 388 TRP LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET
SEQRES 26 B 388 ASN GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO
SEQRES 27 B 388 TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET
SEQRES 28 B 388 GLY THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL
SEQRES 29 B 388 ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU
SEQRES 30 B 388 ARG LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
HET ZN A 401 1
HET GOL A 402 1
HET GOL A 403 12
HET NA A 404 1
HET NA A 405 1
HET NA A 406 1
HET NA A 407 1
HET GOL A 408 6
HET GOL A 409 6
HET GOL A 410 6
HET GOL A 411 5
HET GOL A 412 6
HET GOL A 413 6
HET GOL A 414 6
HET CL A 415 1
HET CL A 416 1
HET CL A 417 1
HET CL A 418 1
HET CL A 419 1
HET CA A 420 1
HET ZN B 401 1
HET NA B 402 1
HET NA B 403 1
HET NA B 404 1
HET NA B 405 1
HET NA B 406 1
HET GOL B 407 6
HET GOL B 408 18
HET GOL B 409 6
HET GOL B 410 6
HET GOL B 411 6
HET GOL B 412 6
HET GOL B 413 12
HET GOL B 414 6
HET GOL B 415 6
HET GOL B 416 6
HET GOL B 417 6
HET GOL B 418 6
HET CL B 419 1
HET CL B 420 1
HET CL B 421 1
HET CL B 422 1
HET CL B 423 1
HET CA B 424 1
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 GOL 21(C3 H8 O3)
FORMUL 6 NA 9(NA 1+)
FORMUL 17 CL 10(CL 1-)
FORMUL 22 CA 2(CA 2+)
FORMUL 47 HOH *1015(H2 O)
HELIX 1 1 GLU A 23 PHE A 27 5 5
HELIX 2 2 GLY A 31 GLY A 35 5 5
HELIX 3 3 ASP A 36 ASN A 44 1 9
HELIX 4 4 SER A 58 GLY A 72 1 15
HELIX 5 5 GLY A 78 GLY A 86 1 9
HELIX 6 6 LEU A 98 ARG A 103 5 6
HELIX 7 7 GLN A 114 GLY A 129 1 16
HELIX 8 8 SER A 130 ASN A 141 1 12
HELIX 9 9 SER A 145 GLU A 149 5 5
HELIX 10 10 THR A 168 MET A 173 5 6
HELIX 11 11 ASP A 175 ALA A 191 1 17
HELIX 12 12 LEU A 208 GLY A 212 5 5
HELIX 13 13 SER A 220 ARG A 230 1 11
HELIX 14 14 SER A 231 SER A 236 1 6
HELIX 15 15 THR A 239 SER A 245 1 7
HELIX 16 16 SER A 245 VAL A 256 1 12
HELIX 17 17 ASN A 288 CYS A 295 1 8
HELIX 18 18 CYS A 295 GLY A 300 1 6
HELIX 19 19 ASN A 304 GLY A 308 5 5
HELIX 20 20 ASP A 310 LEU A 314 5 5
HELIX 21 21 ASN A 321 ASN A 326 5 6
HELIX 22 22 ASP A 371 SER A 385 1 15
HELIX 23 23 GLU B 23 PHE B 27 5 5
HELIX 24 24 GLY B 31 GLY B 35 5 5
HELIX 25 25 ASP B 36 ASN B 44 1 9
HELIX 26 26 SER B 58 GLY B 72 1 15
HELIX 27 27 GLY B 78 GLY B 86 1 9
HELIX 28 28 LEU B 98 GLY B 104 5 7
HELIX 29 29 GLN B 114 GLY B 129 1 16
HELIX 30 30 SER B 130 ASN B 141 1 12
HELIX 31 31 SER B 145 GLU B 149 5 5
HELIX 32 32 THR B 168 MET B 173 5 6
HELIX 33 33 ASP B 175 ALA B 191 1 17
HELIX 34 34 LEU B 208 GLY B 212 5 5
HELIX 35 35 SER B 220 ARG B 230 1 11
HELIX 36 36 SER B 231 SER B 236 1 6
HELIX 37 37 THR B 239 SER B 245 1 7
HELIX 38 38 SER B 245 VAL B 256 1 12
HELIX 39 39 ASN B 288 CYS B 295 1 8
HELIX 40 40 CYS B 295 GLY B 300 1 6
HELIX 41 41 ASN B 304 GLY B 308 5 5
HELIX 42 42 ASP B 310 LEU B 314 5 5
HELIX 43 43 ASN B 321 MET B 325 5 5
HELIX 44 44 ASP B 371 SER B 385 1 15
SHEET 1 A 7 THR A 48 THR A 50 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 N LEU A 12 O TYR A 49
SHEET 3 A 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 A 7 VAL A 155 ILE A 161 1 O THR A 159 N ILE A 109
SHEET 5 A 7 TYR A 263 THR A 269 1 O TYR A 263 N LEU A 156
SHEET 6 A 7 TRP A 348 TYR A 354 1 O ASN A 349 N TYR A 264
SHEET 7 A 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 B 2 GLY A 73 ASP A 76 0
SHEET 2 B 2 PHE A 90 TYR A 94 -1 O TYR A 94 N GLY A 73
SHEET 1 C 2 THR A 272 ARG A 274 0
SHEET 2 C 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 D 7 THR B 48 THR B 50 0
SHEET 2 D 7 ILE B 10 LEU B 13 1 N LEU B 12 O TYR B 49
SHEET 3 D 7 ILE B 107 HIS B 112 1 O HIS B 108 N VAL B 11
SHEET 4 D 7 VAL B 155 ILE B 161 1 O THR B 159 N ALA B 111
SHEET 5 D 7 TYR B 263 THR B 269 1 O LEU B 265 N VAL B 158
SHEET 6 D 7 TRP B 348 TYR B 354 1 O MET B 351 N SER B 266
SHEET 7 D 7 ILE B 336 PRO B 338 1 N VAL B 337 O TRP B 348
SHEET 1 E 2 GLY B 73 ASP B 76 0
SHEET 2 E 2 PHE B 90 TYR B 94 -1 O ARG B 92 N VAL B 75
SHEET 1 F 2 THR B 272 ARG B 274 0
SHEET 2 F 2 HIS B 281 PRO B 283 -1 O TYR B 282 N TYR B 273
LINK OD2 ASP B 238 ZN ZN B 401 1555 1555 1.96
LINK OE1 GLU A 202 NA NA A 407 1555 1555 1.97
LINK OD1 ASP B 61 ZN ZN B 401 1555 1555 1.98
LINK OD2 ASP A 238 ZN ZN A 401 1555 1555 1.99
LINK NE2 HIS B 87 ZN ZN B 401 1555 1555 2.00
LINK OD1 ASP A 61 ZN ZN A 401 1555 1555 2.00
LINK NE2 HIS A 81 ZN ZN A 401 1555 1555 2.00
LINK NE2 HIS A 87 ZN ZN A 401 1555 1555 2.01
LINK NA NA A 404 O HOH A 693 1555 1555 2.02
LINK NE2 HIS B 81 ZN ZN B 401 1555 1555 2.03
LINK NA NA B 403 O HOH B 910 1555 1555 2.07
LINK NA NA A 406 O HOH A 742 1555 1555 2.11
LINK NA NA A 405 O HOH A 578 1555 1555 2.12
LINK NA NA B 402 O HOH B 816 1555 1555 2.12
LINK NA NA B 402 O HOH B 730 1555 1555 2.13
LINK O THR B 272 NA NA B 404 1555 1555 2.16
LINK NA NA B 404 O HOH B 726 1555 1555 2.17
LINK O THR A 272 NA NA A 405 1555 1555 2.19
LINK NA NA A 406 O HOH A 743 1555 1555 2.22
LINK NA NA B 405 O HOH B 918 1555 1555 2.23
LINK NA NA A 405 O HOH A 760 1555 1555 2.29
LINK OE2 GLU B 360 CA CA B 424 1555 1555 2.29
LINK O LYS B 329 NA NA B 402 1555 1555 2.31
LINK O GLY B 286 CA CA B 424 1555 1555 2.31
LINK CA CA B 424 O HOH B 660 1555 1555 2.31
LINK CA CA A 420 O HOH A 666 1555 1555 2.31
LINK O PRO A 366 CA CA A 420 1555 1555 2.32
LINK O LYS A 329 NA NA A 404 1555 1555 2.34
LINK O GLY A 286 CA CA A 420 1555 1555 2.34
LINK NA NA B 406 O HOH B 733 1555 1555 2.35
LINK O PRO B 366 CA CA B 424 1555 1555 2.35
LINK NA NA B 406 O HOH B 519 1555 1555 2.35
LINK O ALA B 192 NA NA B 406 1555 1555 2.35
LINK OE2 GLU A 360 CA CA A 420 1555 1555 2.35
LINK NA NA B 405 O HOH B 929 1555 1555 2.36
LINK OD2 ASP A 365 CA CA A 420 1555 1555 2.36
LINK NA NA A 406 O HOH A 760 1555 1555 2.37
LINK OE1 GLU A 270 NA NA A 405 1555 1555 2.37
LINK NA NA B 406 O HOH B 543 1555 1555 2.37
LINK NA NA A 406 O HOH A 578 1555 1555 2.38
LINK NA NA B 402 O HOH B 757 1555 1555 2.39
LINK OD2 ASP B 365 CA CA B 424 1555 1555 2.39
LINK OE1 GLU B 270 NA NA B 404 1555 1555 2.39
LINK O SER B 332 NA NA B 402 1555 1555 2.43
LINK NA NA B 403 O HOH B 575 1555 1555 2.45
LINK NA NA A 404 O HOH A 766 1555 1555 2.47
LINK NA NA B 405 O HOH A 884 1555 1555 2.49
LINK O SER A 332 NA NA A 404 1555 1555 2.51
LINK OG ASER B 369 NA NA B 403 1555 1555 2.55
LINK NA NA B 405 O HOH A 727 1555 1555 2.56
LINK NA NA B 405 O HOH B 746 1555 1555 2.58
LINK NA NA B 404 O HOH B 621 1555 1555 2.64
LINK NA NA B 404 O HOH B 653 1555 1555 2.65
LINK CA CA B 424 O HOH B 691 1555 1555 2.67
LINK NA NA A 404 O HOH A 861 1555 1555 2.70
LINK NA NA B 403 O HOH B 724 1555 1555 2.72
LINK OE2 GLU A 284 NA NA A 405 1555 1555 2.75
LINK NA NA A 406 O HOH A 967 1555 1555 2.82
LINK NA NA B 404 O HOH B 900 1555 1555 2.82
LINK CA CA A 420 O HOH A 747 1555 1555 2.83
LINK NA NA A 404 O HOH A 826 1555 1555 2.87
LINK NA NA A 405 O HOH A 577 1555 1555 3.02
LINK NA NA A 405 O HOH A 684 1555 1555 3.04
LINK OE2 GLU B 284 NA NA B 404 1555 1555 3.10
LINK OE2 GLU A 202 NA NA A 407 1555 1555 3.18
SITE 1 AC1 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
SITE 1 AC2 5 GLU A 22 GLU A 23 MET A 24 PHE A 25
SITE 2 AC2 5 GOL A 411
SITE 1 AC3 8 HOH A 570 HOH A 765 HIS B 85 THR B 237
SITE 2 AC3 8 TYR B 242 LYS B 251 GOL B 411 HOH B 604
SITE 1 AC4 6 LYS A 329 SER A 332 HOH A 693 HOH A 766
SITE 2 AC4 6 HOH A 826 HOH A 861
SITE 1 AC5 8 GLU A 270 THR A 272 GLU A 284 NA A 406
SITE 2 AC5 8 HOH A 577 HOH A 578 HOH A 684 HOH A 760
SITE 1 AC6 6 NA A 405 HOH A 578 HOH A 742 HOH A 743
SITE 2 AC6 6 HOH A 760 HOH A 967
SITE 1 AC7 4 GLU A 202 ARG A 214 ARG A 215 CL A 417
SITE 1 AC8 3 THR A 353 TYR A 354 HOH A 546
SITE 1 AC9 8 TRP A 60 HIS A 81 HIS A 85 HOH A 509
SITE 2 AC9 8 HOH A 514 HOH A 534 HOH A 592 HOH A 779
SITE 1 BC1 7 THR A 50 GLN A 69 LEU A 97 HOH A 579
SITE 2 BC1 7 HOH A 629 HOH A 718 HOH A 816
SITE 1 BC2 7 GLU A 22 PHE A 25 SER A 201 GLU A 202
SITE 2 BC2 7 VAL A 203 GOL A 402 HOH A 585
SITE 1 BC3 5 GLU A 127 GLY A 151 HIS A 152 HIS A 153
SITE 2 BC3 5 ASN A 261
SITE 1 BC4 8 ARG A 303 ASP A 310 ASP A 311 HOH A 507
SITE 2 BC4 8 HOH A 617 HOH A 858 PHE B 90 GLY B 91
SITE 1 BC5 3 PHE A 25 ALA A 192 SER A 201
SITE 1 BC6 6 GLY A 275 LEU A 277 THR A 278 GLY A 279
SITE 2 BC6 6 ASN A 280 TYR A 282
SITE 1 BC7 2 THR A 200 SER A 201
SITE 1 BC8 4 PHE A 206 ARG A 215 TYR A 224 NA A 407
SITE 1 BC9 2 ARG A 214 ARG A 227
SITE 1 CC1 5 ARG A 34 PRO A 366 ASN A 367 PRO A 368
SITE 2 CC1 5 HOH A 875
SITE 1 CC2 6 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 2 CC2 6 HOH A 666 HOH A 747
SITE 1 CC3 4 ASP B 61 HIS B 81 HIS B 87 ASP B 238
SITE 1 CC4 5 LYS B 329 SER B 332 HOH B 730 HOH B 757
SITE 2 CC4 5 HOH B 816
SITE 1 CC5 4 SER B 369 HOH B 575 HOH B 724 HOH B 910
SITE 1 CC6 7 GLU B 270 THR B 272 GLU B 284 HOH B 621
SITE 2 CC6 7 HOH B 653 HOH B 726 HOH B 900
SITE 1 CC7 5 HOH A 727 HOH A 884 HOH B 746 HOH B 918
SITE 2 CC7 5 HOH B 929
SITE 1 CC8 6 HIS B 153 ALA B 192 HOH B 519 HOH B 529
SITE 2 CC8 6 HOH B 543 HOH B 733
SITE 1 CC9 7 THR B 50 GLN B 69 TYR B 94 GOL B 413
SITE 2 CC9 7 HOH B 620 HOH B 646 HOH B 916
SITE 1 DC1 12 GLY B 26 PHE B 27 LYS B 28 GLY B 32
SITE 2 DC1 12 GLY B 35 ASP B 36 GLU B 149 GLY B 150
SITE 3 DC1 12 GLY B 151 HIS B 152 HOH B 776 HOH B 938
SITE 1 DC2 9 TYR B 199 THR B 200 GLU B 202 ARG B 214
SITE 2 DC2 9 ARG B 215 GLN B 216 PRO B 217 HOH B 598
SITE 3 DC2 9 HOH B 868
SITE 1 DC3 10 ASP B 7 ALA B 8 GLY B 105 ARG B 106
SITE 2 DC3 10 CL B 420 HOH B 654 HOH B 756 HOH B 780
SITE 3 DC3 10 HOH B 870 HOH B 936
SITE 1 DC4 9 GOL A 403 HOH A 570 HOH A 765 TRP B 60
SITE 2 DC4 9 HIS B 81 HIS B 85 HOH B 506 HOH B 541
SITE 3 DC4 9 HOH B 584
SITE 1 DC5 7 TYR B 67 LYS B 102 HIS B 152 HOH B 549
SITE 2 DC5 7 HOH B 578 HOH B 643 HOH B 775
SITE 1 DC6 10 ARG B 21 GLU B 38 TYR B 49 THR B 50
SITE 2 DC6 10 LEU B 97 GOL B 407 HOH B 700 HOH B 708
SITE 3 DC6 10 HOH B 762 HOH B 826
SITE 1 DC7 2 THR B 353 HOH B 527
SITE 1 DC8 4 ARG B 34 ARG B 373 HOH B 611 HOH B 808
SITE 1 DC9 7 TRP B 60 SER B 130 GLU B 132 TRP B 255
SITE 2 DC9 7 HOH B 584 HOH B 640 HOH B 932
SITE 1 EC1 6 PHE B 267 TYR B 354 PHE B 375 ARG B 378
SITE 2 EC1 6 GLN B 382 HOH B 915
SITE 1 EC2 9 LYS B 185 GLU B 189 SER B 195 HOH B 571
SITE 2 EC2 9 HOH B 608 HOH B 627 HOH B 841 HOH B 880
SITE 3 EC2 9 HOH B 890
SITE 1 EC3 6 GLY B 275 LEU B 277 THR B 278 GLY B 279
SITE 2 EC3 6 ASN B 280 TYR B 282
SITE 1 EC4 2 ARG B 106 GOL B 410
SITE 1 EC5 4 LEU B 213 ARG B 214 GLN B 216 ARG B 227
SITE 1 EC6 6 ARG B 34 PRO B 366 ASN B 367 PRO B 368
SITE 2 EC6 6 HOH B 648 HOH B 810
SITE 1 EC7 5 LEU B 126 HIS B 153 PHE B 154 VAL B 155
SITE 2 EC7 5 HOH B 725
SITE 1 EC8 6 GLY B 286 GLU B 360 ASP B 365 PRO B 366
SITE 2 EC8 6 HOH B 660 HOH B 691
CRYST1 117.824 81.001 99.529 90.00 96.69 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 0.008487 0.000000 0.000996 0.00000
SCALE2 0.000000 0.012346 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010116 0.00000
TER 3155 PRO A 388
TER 6442 PRO B 388
MASTER 771 0 44 44 22 0 81 6 7260 2 227 60
END |