| content |
HEADER HYDROLASE 09-SEP-14 4WDR
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB 140A+143L+177W+211L
TITLE 2 MUTANT (LINB86) FROM SPHINGOBIUM JAPONICUM UT26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 4-296;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM JAPONICUM UT26S;
SOURCE 3 ORGANISM_TAXID: 452662;
SOURCE 4 GENE: LINB, DHAA, SJA_C1-19590;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, PROTEIN ENGINEERING, TERTIARY, SPHINGOBIOUM
EXPDTA X-RAY DIFFRACTION
AUTHOR O.DEGTJARIK,P.REZACOVA,I.IERMAK,R.CHALOUPKOVA,J.DAMBORSKY,I.KUTA-
AUTHOR 2 SMATANOVA
REVDAT 1 23-DEC-15 4WDR 0
JRNL AUTH O.DEGTJARIK,P.REZACOVA,I.IERMAK,R.CHALOUPKOVA,J.DAMBORSKY,
JRNL AUTH 2 I.KUTA-SMATANOVA
JRNL TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB
JRNL TITL 2 140A+143L+177W+211L MUTANT (LINB86) FROM SPHINGOBIUM
JRNL TITL 3 JAPONICUM UT26
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1144
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1549
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4609
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.57000
REMARK 3 B12 (A**2) : 0.09000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.521
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.081
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4733 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4435 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6427 ; 1.602 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10177 ; 1.058 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 583 ; 5.827 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;34.770 ;22.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 740 ;15.837 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;19.475 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 671 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5393 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1129 ; 0.005 ; 0.020
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): 2338 ; 2.018 ; 2.976
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2337 ; 2.018 ; 2.977
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2919 ; 3.023 ; 4.470
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 294 B 4 294 18036 0.080 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 13
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8790 25.8570 50.3610
REMARK 3 T TENSOR
REMARK 3 T11: 0.3669 T22: 0.5599
REMARK 3 T33: 0.6485 T12: 0.1243
REMARK 3 T13: 0.0098 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 6.1545 L22: 4.3741
REMARK 3 L33: 22.5251 L12: -4.9028
REMARK 3 L13: 11.2071 L23: -9.9223
REMARK 3 S TENSOR
REMARK 3 S11: 0.2821 S12: 0.9580 S13: 0.4805
REMARK 3 S21: -0.2173 S22: -0.8871 S23: -0.2709
REMARK 3 S31: 0.4929 S32: 2.0591 S33: 0.6050
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1790 23.6310 54.4740
REMARK 3 T TENSOR
REMARK 3 T11: 0.0524 T22: 0.1157
REMARK 3 T33: 0.1419 T12: 0.0353
REMARK 3 T13: -0.0633 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.4058 L22: 2.3397
REMARK 3 L33: 1.3902 L12: -0.4753
REMARK 3 L13: -0.3321 L23: 0.5573
REMARK 3 S TENSOR
REMARK 3 S11: -0.0444 S12: -0.1979 S13: 0.1191
REMARK 3 S21: 0.1848 S22: 0.0461 S23: -0.3150
REMARK 3 S31: 0.0901 S32: 0.1934 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 109 A 224
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6120 19.9860 42.3800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1004 T22: 0.0796
REMARK 3 T33: 0.0808 T12: 0.0005
REMARK 3 T13: 0.0031 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.0457 L22: 1.9525
REMARK 3 L33: 0.7726 L12: -0.4019
REMARK 3 L13: 0.1676 L23: 0.4306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: 0.0277 S13: -0.0596
REMARK 3 S21: -0.1622 S22: -0.0083 S23: -0.1078
REMARK 3 S31: 0.0356 S32: 0.0024 S33: -0.0062
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 225 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0280 37.2980 45.8360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1283 T22: 0.0989
REMARK 3 T33: 0.1049 T12: 0.0267
REMARK 3 T13: -0.0049 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.1731 L22: 2.7812
REMARK 3 L33: 1.8958 L12: -0.4252
REMARK 3 L13: -0.5635 L23: 0.0016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0376 S12: 0.0945 S13: 0.2596
REMARK 3 S21: -0.1767 S22: 0.0732 S23: -0.1455
REMARK 3 S31: -0.1269 S32: -0.0641 S33: -0.0357
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 71
REMARK 3 ORIGIN FOR THE GROUP (A): -36.8520 6.1720 79.8590
REMARK 3 T TENSOR
REMARK 3 T11: 0.7072 T22: 0.5765
REMARK 3 T33: 0.9857 T12: -0.3721
REMARK 3 T13: -0.2650 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 3.4899 L22: 1.8469
REMARK 3 L33: 0.3169 L12: -0.9067
REMARK 3 L13: 0.0483 L23: 0.4305
REMARK 3 S TENSOR
REMARK 3 S11: 0.3976 S12: -0.0087 S13: -1.1513
REMARK 3 S21: -0.0062 S22: -0.1647 S23: 0.0075
REMARK 3 S31: 0.3363 S32: -0.3272 S33: -0.2328
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 72 B 101
REMARK 3 ORIGIN FOR THE GROUP (A): -41.5070 17.8330 85.1180
REMARK 3 T TENSOR
REMARK 3 T11: 0.4419 T22: 0.6216
REMARK 3 T33: 0.7030 T12: -0.3137
REMARK 3 T13: -0.0806 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.8861 L22: 4.6080
REMARK 3 L33: 6.2671 L12: 1.5009
REMARK 3 L13: -0.8173 L23: -1.6720
REMARK 3 S TENSOR
REMARK 3 S11: 0.2412 S12: -0.1544 S13: -0.3054
REMARK 3 S21: 0.6687 S22: -0.0468 S23: 0.1267
REMARK 3 S31: -0.1528 S32: -0.7953 S33: -0.1944
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 102 B 279
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5360 19.5350 78.0740
REMARK 3 T TENSOR
REMARK 3 T11: 0.2595 T22: 0.2315
REMARK 3 T33: 0.3356 T12: -0.1118
REMARK 3 T13: -0.0752 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 2.0829 L22: 1.5347
REMARK 3 L33: 0.7395 L12: 0.0649
REMARK 3 L13: 0.8068 L23: 0.1054
REMARK 3 S TENSOR
REMARK 3 S11: 0.3384 S12: 0.0655 S13: -0.6132
REMARK 3 S21: 0.0673 S22: -0.0976 S23: 0.0071
REMARK 3 S31: 0.2559 S32: -0.2174 S33: -0.2407
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 280 B 295
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3900 1.5620 87.4490
REMARK 3 T TENSOR
REMARK 3 T11: 0.7838 T22: 0.4866
REMARK 3 T33: 1.4259 T12: -0.0985
REMARK 3 T13: -0.3528 T23: 0.2335
REMARK 3 L TENSOR
REMARK 3 L11: 1.6952 L22: 11.5151
REMARK 3 L33: 8.2410 L12: 2.8065
REMARK 3 L13: -3.4681 L23: -3.6690
REMARK 3 S TENSOR
REMARK 3 S11: 0.2204 S12: -0.4533 S13: -0.6144
REMARK 3 S21: 0.4201 S22: -0.8097 S23: -0.7657
REMARK 3 S31: -0.0705 S32: 0.8157 S33: 0.5893
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 ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4WDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972386
REMARK 200 MONOCHROMATOR : SI (311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22874
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.810
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.87000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.140
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.1.03
REMARK 200 STARTING MODEL: 4WDQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS, 0.1M HEPES; 0.3M MGCL2;
REMARK 280 0.3M CACL2; 20% PEG550MME; 10%PEG20K, PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 62.96850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 36.35488
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 71.27267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 62.96850
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 36.35488
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 71.27267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 62.96850
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 36.35488
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 71.27267
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 62.96850
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 36.35488
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 71.27267
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 62.96850
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 36.35488
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 71.27267
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 62.96850
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 36.35488
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 71.27267
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 72.70976
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 142.54533
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 72.70976
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 142.54533
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 72.70976
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 142.54533
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 72.70976
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 142.54533
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 72.70976
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 142.54533
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 72.70976
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 142.54533
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 CA CA A 302 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 402 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 B 296
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 412 O HOH B 405 17555 2.04
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 292 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 225 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 225 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 39 56.48 -117.57
REMARK 500 THR A 40 -157.82 -108.66
REMARK 500 SER A 41 -168.03 -161.07
REMARK 500 ASP A 108 -132.01 56.07
REMARK 500 GLN A 172 -51.94 -123.66
REMARK 500 ALA A 247 -63.21 -149.72
REMARK 500 ALA A 271 -100.30 -100.70
REMARK 500 PRO B 39 56.17 -115.65
REMARK 500 THR B 40 -160.22 -109.10
REMARK 500 ASP B 108 -133.21 56.70
REMARK 500 GLN B 172 -51.59 -123.96
REMARK 500 ALA B 247 -65.87 -151.46
REMARK 500 ALA B 271 -101.89 -103.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 73 OD1
REMARK 620 2 ASP A 73 OD1 0.0
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 CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302
DBREF 4WDR A 4 296 UNP D4Z2G1 D4Z2G1_SPHJU 4 296
DBREF 4WDR B 4 296 UNP D4Z2G1 D4Z2G1_SPHJU 4 296
SEQADV 4WDR ALA A 140 UNP D4Z2G1 TRP 140 ENGINEERED MUTATION
SEQADV 4WDR LEU A 143 UNP D4Z2G1 PHE 143 ENGINEERED MUTATION
SEQADV 4WDR TRP A 177 UNP D4Z2G1 LEU 177 ENGINEERED MUTATION
SEQADV 4WDR LEU A 211 UNP D4Z2G1 ILE 211 ENGINEERED MUTATION
SEQADV 4WDR ALA B 140 UNP D4Z2G1 TRP 140 ENGINEERED MUTATION
SEQADV 4WDR LEU B 143 UNP D4Z2G1 PHE 143 ENGINEERED MUTATION
SEQADV 4WDR TRP B 177 UNP D4Z2G1 LEU 177 ENGINEERED MUTATION
SEQADV 4WDR LEU B 211 UNP D4Z2G1 ILE 211 ENGINEERED MUTATION
SEQRES 1 A 293 GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE ILE GLU ILE
SEQRES 2 A 293 LYS GLY ARG ARG MET ALA TYR ILE ASP GLU GLY THR GLY
SEQRES 3 A 293 ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO THR SER SER
SEQRES 4 A 293 TYR LEU TRP ARG ASN ILE MET PRO HIS CYS ALA GLY LEU
SEQRES 5 A 293 GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET GLY ASP
SEQRES 6 A 293 SER ASP LYS LEU ASP PRO SER GLY PRO GLU ARG TYR ALA
SEQRES 7 A 293 TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA LEU TRP GLU
SEQRES 8 A 293 ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU VAL VAL HIS
SEQRES 9 A 293 ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA ARG ARG
SEQRES 10 A 293 HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR MET GLU ALA
SEQRES 11 A 293 ILE ALA MET PRO ILE GLU ALA ALA ASP LEU PRO GLU GLN
SEQRES 12 A 293 ASP ARG ASP LEU PHE GLN ALA PHE ARG SER GLN ALA GLY
SEQRES 13 A 293 GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE VAL GLU GLN
SEQRES 14 A 293 VAL LEU PRO GLY TRP ILE LEU ARG PRO LEU SER GLU ALA
SEQRES 15 A 293 GLU MET ALA ALA TYR ARG GLU PRO PHE LEU ALA ALA GLY
SEQRES 16 A 293 GLU ALA ARG ARG PRO THR LEU SER TRP PRO ARG GLN LEU
SEQRES 17 A 293 PRO ILE ALA GLY THR PRO ALA ASP VAL VAL ALA ILE ALA
SEQRES 18 A 293 ARG ASP TYR ALA GLY TRP LEU SER GLU SER PRO ILE PRO
SEQRES 19 A 293 LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA LEU THR THR
SEQRES 20 A 293 GLY ARG MET ARG ASP PHE CYS ARG THR TRP PRO ASN GLN
SEQRES 21 A 293 THR GLU ILE THR VAL ALA GLY ALA HIS PHE ILE GLN GLU
SEQRES 22 A 293 ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA ALA PHE
SEQRES 23 A 293 VAL ARG ARG LEU ARG PRO ALA
SEQRES 1 B 293 GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE ILE GLU ILE
SEQRES 2 B 293 LYS GLY ARG ARG MET ALA TYR ILE ASP GLU GLY THR GLY
SEQRES 3 B 293 ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO THR SER SER
SEQRES 4 B 293 TYR LEU TRP ARG ASN ILE MET PRO HIS CYS ALA GLY LEU
SEQRES 5 B 293 GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET GLY ASP
SEQRES 6 B 293 SER ASP LYS LEU ASP PRO SER GLY PRO GLU ARG TYR ALA
SEQRES 7 B 293 TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA LEU TRP GLU
SEQRES 8 B 293 ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU VAL VAL HIS
SEQRES 9 B 293 ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA ARG ARG
SEQRES 10 B 293 HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR MET GLU ALA
SEQRES 11 B 293 ILE ALA MET PRO ILE GLU ALA ALA ASP LEU PRO GLU GLN
SEQRES 12 B 293 ASP ARG ASP LEU PHE GLN ALA PHE ARG SER GLN ALA GLY
SEQRES 13 B 293 GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE VAL GLU GLN
SEQRES 14 B 293 VAL LEU PRO GLY TRP ILE LEU ARG PRO LEU SER GLU ALA
SEQRES 15 B 293 GLU MET ALA ALA TYR ARG GLU PRO PHE LEU ALA ALA GLY
SEQRES 16 B 293 GLU ALA ARG ARG PRO THR LEU SER TRP PRO ARG GLN LEU
SEQRES 17 B 293 PRO ILE ALA GLY THR PRO ALA ASP VAL VAL ALA ILE ALA
SEQRES 18 B 293 ARG ASP TYR ALA GLY TRP LEU SER GLU SER PRO ILE PRO
SEQRES 19 B 293 LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA LEU THR THR
SEQRES 20 B 293 GLY ARG MET ARG ASP PHE CYS ARG THR TRP PRO ASN GLN
SEQRES 21 B 293 THR GLU ILE THR VAL ALA GLY ALA HIS PHE ILE GLN GLU
SEQRES 22 B 293 ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA ALA PHE
SEQRES 23 B 293 VAL ARG ARG LEU ARG PRO ALA
HET CL A 301 1
HET CA A 302 1
HET CL B 301 1
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
FORMUL 3 CL 2(CL 1-)
FORMUL 4 CA CA 2+
FORMUL 6 HOH *61(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 5 6
HELIX 3 AA3 ALA A 81 LEU A 96 1 16
HELIX 4 AA4 ASP A 108 HIS A 121 1 14
HELIX 5 AA5 GLU A 139 LEU A 143 5 5
HELIX 6 AA6 ASP A 147 ARG A 155 1 9
HELIX 7 AA7 ALA A 158 GLN A 165 1 8
HELIX 8 AA8 ASN A 167 GLN A 172 1 6
HELIX 9 AA9 GLN A 172 TRP A 177 1 6
HELIX 10 AB1 SER A 183 GLU A 192 1 10
HELIX 11 AB2 PRO A 193 LEU A 195 5 3
HELIX 12 AB3 GLY A 198 ALA A 200 5 3
HELIX 13 AB4 ARG A 201 TRP A 207 1 7
HELIX 14 AB5 PRO A 208 LEU A 211 5 4
HELIX 15 AB6 PRO A 217 SER A 232 1 16
HELIX 16 AB7 THR A 250 ARG A 258 1 9
HELIX 17 AB8 PHE A 273 ASP A 277 5 5
HELIX 18 AB9 SER A 278 ARG A 294 1 17
HELIX 19 AC1 SER B 41 ARG B 46 5 6
HELIX 20 AC2 ILE B 48 ALA B 53 5 6
HELIX 21 AC3 ALA B 81 LEU B 96 1 16
HELIX 22 AC4 ASP B 108 HIS B 121 1 14
HELIX 23 AC5 GLU B 139 LEU B 143 5 5
HELIX 24 AC6 ASP B 147 SER B 156 1 10
HELIX 25 AC7 ALA B 158 GLN B 165 1 8
HELIX 26 AC8 ASN B 167 GLN B 172 1 6
HELIX 27 AC9 GLN B 172 TRP B 177 1 6
HELIX 28 AD1 SER B 183 GLU B 192 1 10
HELIX 29 AD2 PRO B 193 LEU B 195 5 3
HELIX 30 AD3 GLY B 198 ALA B 200 5 3
HELIX 31 AD4 ARG B 201 TRP B 207 1 7
HELIX 32 AD5 PRO B 217 SER B 232 1 16
HELIX 33 AD6 THR B 250 ARG B 258 1 9
HELIX 34 AD7 PHE B 273 ASP B 277 5 5
HELIX 35 AD8 SER B 278 ARG B 294 1 17
SHEET 1 AA1 8 LYS A 11 ILE A 16 0
SHEET 2 AA1 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 AA1 8 ARG A 57 CYS A 61 -1 O LEU A 58 N GLU A 26
SHEET 4 AA1 8 PRO A 31 GLN A 35 1 N PHE A 34 O ILE A 59
SHEET 5 AA1 8 VAL A 102 HIS A 107 1 O VAL A 105 N LEU A 33
SHEET 6 AA1 8 VAL A 125 MET A 131 1 O ALA A 129 N LEU A 104
SHEET 7 AA1 8 LYS A 238 PRO A 245 1 O LEU A 239 N TYR A 130
SHEET 8 AA1 8 GLN A 263 GLY A 270 1 O ILE A 266 N ASN A 242
SHEET 1 AA2 8 LYS B 11 ILE B 16 0
SHEET 2 AA2 8 ARG B 19 GLU B 26 -1 O ARG B 19 N ILE B 16
SHEET 3 AA2 8 ARG B 57 CYS B 61 -1 O LEU B 58 N GLU B 26
SHEET 4 AA2 8 PRO B 31 GLN B 35 1 N PHE B 34 O ILE B 59
SHEET 5 AA2 8 VAL B 102 HIS B 107 1 O VAL B 105 N LEU B 33
SHEET 6 AA2 8 VAL B 125 MET B 131 1 O ALA B 129 N LEU B 104
SHEET 7 AA2 8 LYS B 238 PRO B 245 1 O LEU B 239 N TYR B 130
SHEET 8 AA2 8 GLN B 263 GLY B 270 1 O ILE B 266 N ASN B 242
LINK OD1 ASP A 73 CA CA A 302 1555 1555 2.49
LINK OD1 ASP A 73 CA CA A 302 1555 2555 2.49
CISPEP 1 ASN A 38 PRO A 39 0 2.79
CISPEP 2 ASP A 73 PRO A 74 0 -10.97
CISPEP 3 THR A 216 PRO A 217 0 -5.30
CISPEP 4 GLU A 244 PRO A 245 0 -2.59
CISPEP 5 ASN B 38 PRO B 39 0 1.01
CISPEP 6 ASP B 73 PRO B 74 0 -13.52
CISPEP 7 THR B 216 PRO B 217 0 -7.44
CISPEP 8 GLU B 244 PRO B 245 0 -2.89
SITE 1 AC1 3 ASN A 38 TRP A 109 PRO A 208
SITE 1 AC2 1 ASP A 73
CRYST1 125.937 125.937 213.818 90.00 90.00 120.00 H 3 2 36
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 0.007940 0.004584 0.000000 0.00000
SCALE2 0.000000 0.009169 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004677 0.00000
TER 2308 ALA A 296
TER 4611 PRO B 295
MASTER 555 0 3 35 16 0 2 6 4673 2 2 46
END |