| content |
HEADER HYDROLASE 13-NOV-11 3UMJ
TITLE CRYSTAL STRUCTURE OF D311E LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 30-416;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 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;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX/T1S
KEYWDS THERMOSTABLE D311E LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.RUSLAN,R.N.Z.R.A.RAHMAN,T.C.LEOW,M.S.M.ALI,M.BASRI,A.B.SALLEH
REVDAT 1 22-FEB-12 3UMJ 0
JRNL AUTH R.RUSLAN,R.N.Z.R.A.RAHMAN,T.C.LEOW,M.S.M.ALI,M.BASRI,
JRNL AUTH 2 A.B.SALLEH
JRNL TITL IMPROVEMENT OF THERMAL STABILITY VIA OUTER-LOOP ION PAIR
JRNL TITL 2 INTERACTION OF MUTATED T1 LIPASE FROM GEOBACILLUS ZALIHAE
JRNL TITL 3 STRAIN T1
JRNL REF INT J MOL SCI V. 13 943 2012
JRNL REFN ESSN 1422-0067
JRNL PMID 22312296
JRNL DOI 10.3390/IJMS13010943
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 50139
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2677
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3443
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 185
REMARK 3 BIN FREE R VALUE : 0.2680
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 : 26
REMARK 3 SOLVENT ATOMS : 622
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.106
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6285 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8543 ; 1.786 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 771 ; 6.430 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 314 ;33.822 ;23.121
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 951 ;14.681 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;19.483 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 893 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4956 ; 0.010 ; 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): 3825 ; 1.064 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6124 ; 1.817 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2460 ; 3.108 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2419 ; 4.822 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3UMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-NOV-11.
REMARK 100 THE RCSB ID CODE IS RCSB068940.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.540
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88705
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 37.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 2.930
REMARK 200 R MERGE (I) : 0.08330
REMARK 200 R SYM (I) : 0.09200
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.15
REMARK 200 R MERGE FOR SHELL (I) : 0.19460
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.010
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XPREP
REMARK 200 STARTING MODEL: PDB ENTRY 2DSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.1M SODIUM PHOSPHATE, 0.1M
REMARK 280 POTASSIUM PHOSPHATE, 1.5M NACL, PH 5.5, VAPOR DIFFUSION, SITTING
REMARK 280 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 58.66150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.58100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.66150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.58100
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 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 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 389 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 620 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 SER A 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 415 O HOH A 559 1.69
REMARK 500 O GLY A 32 O1 GOL A 1001 1.86
REMARK 500 O HOH A 414 O HOH A 502 1.93
REMARK 500 OE1 GLN A 387 O HOH A 683 1.95
REMARK 500 NH1 ARG B 47 O HOH B 658 1.96
REMARK 500 O GLY A 32 C1 GOL A 1001 1.96
REMARK 500 O HOH A 406 O HOH A 407 1.99
REMARK 500 O HOH A 612 O HOH B 666 2.00
REMARK 500 O HOH A 612 O HOH A 705 2.07
REMARK 500 O HOH B 432 O HOH B 627 2.08
REMARK 500 N HIS A 153 O HOH A 609 2.08
REMARK 500 O GLY A 35 O1 GOL A 1001 2.08
REMARK 500 O THR A 272 O HOH A 542 2.09
REMARK 500 OD1 ASP B 182 O HOH B 526 2.12
REMARK 500 O HOH A 404 O HOH A 584 2.13
REMARK 500 O HOH A 402 O HOH A 598 2.14
REMARK 500 O HOH A 479 O HOH A 537 2.15
REMARK 500 O HOH A 542 O HOH A 591 2.15
REMARK 500 O HIS A 153 O HOH A 708 2.17
REMARK 500 O HOH A 708 O HOH A 710 2.18
REMARK 500 O HOH B 431 O HOH B 503 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 391 O HOH A 706 4446 1.17
REMARK 500 O HOH A 392 O HOH A 609 4446 1.28
REMARK 500 O3 GOL A 1001 O HOH A 686 4446 1.39
REMARK 500 O HOH A 389 O HOH A 559 4456 1.43
REMARK 500 O HOH A 390 O HOH A 707 4446 1.66
REMARK 500 C3 GOL A 1001 O HOH A 686 4446 1.97
REMARK 500 O1 GOL A 1001 C1 GOL A 1002 4446 2.02
REMARK 500 O HOH A 665 O HOH B 664 4456 2.06
REMARK 500 O HOH A 396 O HOH A 605 4446 2.12
REMARK 500 O HOH A 393 O HOH A 710 4446 2.17
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 103 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU A 307 CA - CB - CG ANGL. DEV. = 19.1 DEGREES
REMARK 500 LEU B 285 CB - CG - CD2 ANGL. DEV. = -12.1 DEGREES
REMARK 500 ASP B 317 CB - CG - OD2 ANGL. DEV. = -5.7 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 -135.96 61.18
REMARK 500 VAL A 203 -56.59 67.67
REMARK 500 ARG A 271 41.07 -149.21
REMARK 500 LEU A 277 -75.98 -89.25
REMARK 500 ASN A 304 83.43 -155.51
REMARK 500 ASP A 310 -152.48 -114.09
REMARK 500 ILE A 319 -37.36 -138.65
REMARK 500 LYS A 329 -48.46 -133.07
REMARK 500 ASN A 367 91.97 -164.36
REMARK 500 SER B 113 -136.17 66.28
REMARK 500 VAL B 203 -60.36 70.17
REMARK 500 LEU B 208 39.05 -98.85
REMARK 500 ARG B 271 38.61 -142.00
REMARK 500 LEU B 277 -62.85 -98.48
REMARK 500 ASP B 310 -155.93 -130.85
REMARK 500 ILE B 319 -47.24 -142.53
REMARK 500 LYS B 329 -52.48 -126.62
REMARK 500 ASN B 367 91.82 -163.71
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 PHE A 154 24.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 470 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH A 529 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 533 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A 600 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH A 655 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH A 675 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B 678 DISTANCE = 6.96 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 B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 238 OD2
REMARK 620 2 ASP B 61 OD1 126.9
REMARK 620 3 HIS B 81 NE2 113.3 99.0
REMARK 620 4 HIS B 87 NE2 99.7 115.3 100.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 238 OD2
REMARK 620 2 HIS A 81 NE2 106.1
REMARK 620 3 ASP A 61 OD1 129.7 95.1
REMARK 620 4 HIS A 87 NE2 98.8 108.0 117.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 902 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 84.6
REMARK 620 3 PRO A 366 O 173.6 95.2
REMARK 620 4 ASP A 365 OD2 99.0 106.8 87.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 902 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 286 O
REMARK 620 2 GLU B 360 OE2 85.9
REMARK 620 3 ASP B 365 OD2 105.2 106.2
REMARK 620 4 PRO B 366 O 167.8 94.3 86.5
REMARK 620 5 HOH B 516 O 87.6 86.3 162.5 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 904 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 113 OG
REMARK 620 2 HOH B 550 O 112.3
REMARK 620 N 1
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 904
DBREF 3UMJ A 2 388 UNP Q842J9 Q842J9_9BACI 30 416
DBREF 3UMJ B 2 388 UNP Q842J9 Q842J9_9BACI 30 416
SEQADV 3UMJ GLU A 311 UNP Q842J9 ASP 339 ENGINEERED MUTATION
SEQADV 3UMJ GLU B 311 UNP Q842J9 ASP 339 ENGINEERED MUTATION
SEQRES 1 A 387 SER 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 GLU 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 ALA SER LEU GLN PRO
SEQRES 1 B 387 SER 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 GLU 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 ALA SER LEU GLN PRO
HET ZN A 901 1
HET GOL A1001 6
HET GOL A1002 6
HET CL A 903 1
HET NA A 904 1
HET CA A 902 1
HET CA B 902 1
HET ZN B 901 1
HET GOL B1001 6
HET CL B 903 1
HET NA B 904 1
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 6 CL 2(CL 1-)
FORMUL 7 NA 2(NA 1+)
FORMUL 8 CA 2(CA 2+)
FORMUL 14 HOH *622(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 SER A 220 ARG A 230 1 11
HELIX 13 13 SER A 231 SER A 236 1 6
HELIX 14 14 THR A 239 SER A 245 1 7
HELIX 15 15 SER A 245 VAL A 256 1 12
HELIX 16 16 ASN A 288 CYS A 295 1 8
HELIX 17 17 CYS A 295 GLY A 300 1 6
HELIX 18 18 ASN A 304 GLY A 308 5 5
HELIX 19 19 ASP A 310 LEU A 314 5 5
HELIX 20 20 ASN A 321 ASN A 326 5 6
HELIX 21 21 LEU A 359 GLY A 363 5 5
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 ARG B 103 5 6
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 SER A 157 N ILE A 109
SHEET 5 A 7 TYR A 263 THR A 269 1 O LEU A 265 N THR A 160
SHEET 6 A 7 TRP A 348 TYR A 354 1 O MET A 351 N SER A 266
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 ILE B 109
SHEET 5 D 7 TYR B 263 THR B 269 1 O LEU B 265 N THR B 160
SHEET 6 D 7 TRP B 348 TYR B 354 1 O TYR B 354 N SER B 268
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 901 1555 1555 2.04
LINK OD1 ASP B 61 ZN ZN B 901 1555 1555 2.05
LINK NE2 HIS B 81 ZN ZN B 901 1555 1555 2.07
LINK OD2 ASP A 238 ZN ZN A 901 1555 1555 2.08
LINK NE2 HIS A 81 ZN ZN A 901 1555 1555 2.12
LINK OD1 ASP A 61 ZN ZN A 901 1555 1555 2.13
LINK NE2 HIS B 87 ZN ZN B 901 1555 1555 2.24
LINK O GLY A 286 CA CA A 902 1555 1555 2.25
LINK OE2 GLU A 360 CA CA A 902 1555 1555 2.27
LINK NE2 HIS A 87 ZN ZN A 901 1555 1555 2.28
LINK O GLY B 286 CA CA B 902 1555 1555 2.29
LINK OE2 GLU B 360 CA CA B 902 1555 1555 2.34
LINK OD2 ASP B 365 CA CA B 902 1555 1555 2.37
LINK O PRO B 366 CA CA B 902 1555 1555 2.37
LINK OG SER B 113 NA NA B 904 1555 1555 2.40
LINK O PRO A 366 CA CA A 902 1555 1555 2.42
LINK OD2 ASP A 365 CA CA A 902 1555 1555 2.58
LINK OH TYR A 29 NA NA A 904 1555 1555 2.85
LINK NA NA B 904 O HOH B 550 1555 1555 2.19
LINK CA CA B 902 O HOH B 516 1555 1555 2.98
SITE 1 AC1 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
SITE 1 AC2 9 GLY A 31 GLY A 32 VAL A 33 ARG A 34
SITE 2 AC2 9 GLY A 35 GLU A 149 HIS A 152 HOH A 686
SITE 3 AC2 9 GOL A1002
SITE 1 AC3 9 GLY A 26 PHE A 27 LYS A 28 GLY A 32
SITE 2 AC3 9 GLY A 35 ASP A 36 GLY A 150 HIS A 152
SITE 3 AC3 9 GOL A1001
SITE 1 AC4 3 ARG A 214 GLN A 216 ARG A 227
SITE 1 AC5 4 GLY A 15 PHE A 16 THR A 17 TYR A 29
SITE 1 AC6 4 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 1 AC7 5 GLY B 286 GLU B 360 ASP B 365 PRO B 366
SITE 2 AC7 5 HOH B 516
SITE 1 AC8 4 ASP B 61 HIS B 81 HIS B 87 ASP B 238
SITE 1 AC9 7 TRP B 60 HIS B 81 HIS B 85 HOH B 430
SITE 2 AC9 7 HOH B 505 HOH B 532 HOH B 687
SITE 1 BC1 4 LEU B 213 ARG B 214 GLN B 216 ARG B 227
SITE 1 BC2 4 PHE B 16 SER B 113 HIS B 358 HOH B 550
CRYST1 117.323 81.162 100.140 90.00 96.49 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 0.008523 0.000000 0.000969 0.00000
SCALE2 0.000000 0.012321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010050 0.00000
TER 3049 PRO A 388
TER 6104 PRO B 388
MASTER 502 0 11 44 22 0 17 6 6750 2 45 60
END |