HEADER IMMUNE SYSTEM 13-AUG-15 5D72
TITLE CRYSTAL STRUCTURE OF MOR04252, A NEUTRALIZING ANTI-HUMAN GM-CSF
TITLE 2 ANTIBODY FAB FRAGMENT IN COMPLEX WITH HUMAN GM-CSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GM-CSF,COLONY-STIMULATING FACTOR,CSF,MOLGRAMOSTIN,
COMPND 5 SARGRAMOSTIM;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: IMMUNGLOBULIN G1 FAB FRAGMENT, HEAVY CHAIN;
COMPND 9 CHAIN: H, M;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: IMMUNGLOBULIN G1 FAB FRAGMENT, LIGHT CHAIN;
COMPND 13 CHAIN: L, N;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CSF2, GMCSF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GM-CSF, AFFINITY MATURATION, PHAGE DISPLAY, CYTOKINE, ANTIBODY,
KEYWDS 2 PROTEROS BIOSTRUCTURES GMBH, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.EYLENSTEIN,D.WEINFURTNER,S.STEIDL,J.BOETTCHER,M.AUGUSTIN
REVDAT 3 13-JAN-16 5D72 1 JRNL
REVDAT 2 28-OCT-15 5D72 1 JRNL
REVDAT 1 14-OCT-15 5D72 0
JRNL AUTH R.EYLENSTEIN,D.WEINFURTNER,S.HARTLE,R.STROHNER,J.BOTTCHER,
JRNL AUTH 2 M.AUGUSTIN,R.OSTENDORP,S.STEIDL
JRNL TITL MOLECULAR BASIS OF IN VITRO AFFINITY MATURATION AND
JRNL TITL 2 FUNCTIONAL EVOLUTION OF A NEUTRALIZING ANTI-HUMAN GM-CSF
JRNL TITL 3 ANTIBODY.
JRNL REF MABS V. 8 176 2016
JRNL REFN ESSN 1942-0870
JRNL PMID 26406987
JRNL DOI 10.1080/19420862.2015.1099774
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 40852
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 897
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2983
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.4210
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.5230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8096
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.43000
REMARK 3 B22 (A**2) : 9.97000
REMARK 3 B33 (A**2) : -4.55000
REMARK 3 B12 (A**2) : 0.00000
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): 0.547
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.307
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.272
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.435
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7964 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6925 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10912 ; 1.146 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16018 ; 0.884 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1058 ; 6.051 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 275 ;32.990 ;24.109
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1079 ;12.504 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.505 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1253 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9029 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1569 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1147 ; 0.151 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6115 ; 0.135 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3794 ; 0.154 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4412 ; 0.072 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 148 ; 0.093 ; 0.200
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): 9 ; 0.134 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.103 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.090 ; 0.200
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): 6737 ; 1.141 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2159 ; 0.195 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8499 ; 1.512 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3202 ; 2.174 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2412 ; 3.048 ; 6.000
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
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 10 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): 23.019 12.032 58.791
REMARK 3 T TENSOR
REMARK 3 T11: -0.2725 T22: -0.3670
REMARK 3 T33: -0.3215 T12: 0.0202
REMARK 3 T13: -0.0464 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 5.0133 L22: 1.3161
REMARK 3 L33: 5.8922 L12: -0.3672
REMARK 3 L13: -2.2426 L23: 1.7523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: -0.4332 S13: -0.0866
REMARK 3 S21: 0.2844 S22: 0.0189 S23: 0.0626
REMARK 3 S31: 0.2038 S32: 0.1391 S33: 0.0253
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 : L 1 L 105
REMARK 3 ORIGIN FOR THE GROUP (A): 13.550 8.908 34.097
REMARK 3 T TENSOR
REMARK 3 T11: -0.3900 T22: -0.4101
REMARK 3 T33: -0.3814 T12: -0.0731
REMARK 3 T13: 0.0259 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 7.8039 L22: 2.2983
REMARK 3 L33: 4.5152 L12: -1.2582
REMARK 3 L13: 2.0647 L23: -0.7016
REMARK 3 S TENSOR
REMARK 3 S11: 0.2116 S12: -0.2310 S13: -0.2352
REMARK 3 S21: 0.0436 S22: 0.0058 S23: 0.2111
REMARK 3 S31: 0.1753 S32: -0.0964 S33: -0.2175
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 : L 108 L 208
REMARK 3 ORIGIN FOR THE GROUP (A): 12.418 17.255 -2.844
REMARK 3 T TENSOR
REMARK 3 T11: -0.2917 T22: -0.0025
REMARK 3 T33: -0.4141 T12: 0.0783
REMARK 3 T13: -0.0488 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 7.2089 L22: 1.5863
REMARK 3 L33: 4.1491 L12: -0.1228
REMARK 3 L13: 2.3523 L23: -1.8120
REMARK 3 S TENSOR
REMARK 3 S11: 0.1687 S12: 1.2874 S13: -0.1752
REMARK 3 S21: -0.1444 S22: -0.1618 S23: 0.2665
REMARK 3 S31: 0.3815 S32: 0.7619 S33: -0.0070
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 : H 1 H 105
REMARK 3 ORIGIN FOR THE GROUP (A): 35.962 11.771 29.980
REMARK 3 T TENSOR
REMARK 3 T11: -0.3995 T22: -0.4489
REMARK 3 T33: -0.3512 T12: 0.0373
REMARK 3 T13: 0.0108 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 2.6927 L22: 0.3614
REMARK 3 L33: 4.4343 L12: 0.2797
REMARK 3 L13: 0.7497 L23: -0.0181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: 0.1837 S13: 0.0057
REMARK 3 S21: -0.0849 S22: -0.0505 S23: -0.1590
REMARK 3 S31: 0.2026 S32: 0.4008 S33: 0.0589
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 : H 108 H 214
REMARK 3 ORIGIN FOR THE GROUP (A): 25.880 24.314 4.657
REMARK 3 T TENSOR
REMARK 3 T11: -0.4002 T22: -0.0229
REMARK 3 T33: -0.2889 T12: 0.0201
REMARK 3 T13: 0.0985 T23: 0.0953
REMARK 3 L TENSOR
REMARK 3 L11: 3.5253 L22: 4.1980
REMARK 3 L33: 3.3438 L12: 0.2025
REMARK 3 L13: 1.6582 L23: -1.1606
REMARK 3 S TENSOR
REMARK 3 S11: 0.1376 S12: 0.5531 S13: 0.6310
REMARK 3 S21: -0.2333 S22: -0.1814 S23: 0.0217
REMARK 3 S31: -0.1953 S32: 0.2022 S33: 0.0437
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 8 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 11.246 -18.418 60.579
REMARK 3 T TENSOR
REMARK 3 T11: -0.2368 T22: -0.3774
REMARK 3 T33: -0.2825 T12: 0.0291
REMARK 3 T13: -0.0498 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 3.5634 L22: 2.8539
REMARK 3 L33: 3.8169 L12: 0.5916
REMARK 3 L13: -0.1486 L23: 0.2602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: -0.3494 S13: 0.3512
REMARK 3 S21: 0.5005 S22: -0.0658 S23: 0.0273
REMARK 3 S31: -0.3138 S32: 0.0252 S33: 0.0379
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 : M 1 M 105
REMARK 3 ORIGIN FOR THE GROUP (A): 22.199 -27.792 32.193
REMARK 3 T TENSOR
REMARK 3 T11: -0.4196 T22: -0.3987
REMARK 3 T33: -0.3688 T12: 0.0381
REMARK 3 T13: 0.0185 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 3.0669 L22: 1.5972
REMARK 3 L33: 3.9497 L12: 0.1171
REMARK 3 L13: -0.1895 L23: 0.6536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0163 S12: 0.2696 S13: 0.1343
REMARK 3 S21: -0.0737 S22: 0.0109 S23: -0.1498
REMARK 3 S31: 0.0311 S32: 0.4809 S33: 0.0055
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 : M 108 M 213
REMARK 3 ORIGIN FOR THE GROUP (A): 11.362 -23.448 3.779
REMARK 3 T TENSOR
REMARK 3 T11: -0.3704 T22: 0.0152
REMARK 3 T33: -0.3492 T12: -0.0095
REMARK 3 T13: 0.0683 T23: -0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 5.0622 L22: 3.7886
REMARK 3 L33: 4.6570 L12: -1.1623
REMARK 3 L13: 1.6186 L23: -1.3720
REMARK 3 S TENSOR
REMARK 3 S11: 0.1880 S12: 0.1331 S13: 0.3077
REMARK 3 S21: -0.2278 S22: -0.1162 S23: 0.3528
REMARK 3 S31: -0.1143 S32: 0.2202 S33: -0.0719
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 105
REMARK 3 ORIGIN FOR THE GROUP (A): 0.227 -27.084 37.503
REMARK 3 T TENSOR
REMARK 3 T11: -0.3414 T22: -0.4286
REMARK 3 T33: -0.3620 T12: 0.0017
REMARK 3 T13: 0.0497 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 4.3251 L22: 1.2622
REMARK 3 L33: 2.6152 L12: 0.2047
REMARK 3 L13: 1.1309 L23: 0.3190
REMARK 3 S TENSOR
REMARK 3 S11: 0.0871 S12: -0.1371 S13: 0.0932
REMARK 3 S21: 0.1654 S22: -0.0897 S23: 0.1447
REMARK 3 S31: -0.0203 S32: -0.1965 S33: 0.0027
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 108 N 208
REMARK 3 ORIGIN FOR THE GROUP (A): -2.194 -31.893 0.099
REMARK 3 T TENSOR
REMARK 3 T11: -0.2699 T22: -0.1318
REMARK 3 T33: -0.2972 T12: -0.0236
REMARK 3 T13: -0.0534 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 6.8551 L22: 1.8789
REMARK 3 L33: 4.5117 L12: 0.8298
REMARK 3 L13: 0.2672 L23: -0.6994
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.3350 S13: -0.6944
REMARK 3 S21: -0.2143 S22: 0.0710 S23: 0.1122
REMARK 3 S31: 0.1625 S32: 0.4525 S33: -0.0586
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 4
REMARK 4 5D72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212659.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42619
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 96.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.71500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, PH 4.0-4.3, 39
REMARK 280 -42 % (W/V) PEG 400, 30 MG/ML PROTEIN, PH 4.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 35.91100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.33350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.92650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.33350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.91100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.92650
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, M, N
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -16
REMARK 465 TRP A -15
REMARK 465 LEU A -14
REMARK 465 GLN A -13
REMARK 465 SER A -12
REMARK 465 LEU A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 LEU A -8
REMARK 465 GLY A -7
REMARK 465 THR A -6
REMARK 465 VAL A -5
REMARK 465 ALA A -4
REMARK 465 CYS A -3
REMARK 465 SER A -2
REMARK 465 ILE A -1
REMARK 465 SER A 0
REMARK 465 ALA A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 SER A 7
REMARK 465 PRO A 8
REMARK 465 SER A 9
REMARK 465 MET B -16
REMARK 465 TRP B -15
REMARK 465 LEU B -14
REMARK 465 GLN B -13
REMARK 465 SER B -12
REMARK 465 LEU B -11
REMARK 465 LEU B -10
REMARK 465 LEU B -9
REMARK 465 LEU B -8
REMARK 465 GLY B -7
REMARK 465 THR B -6
REMARK 465 VAL B -5
REMARK 465 ALA B -4
REMARK 465 CYS B -3
REMARK 465 SER B -2
REMARK 465 ILE B -1
REMARK 465 SER B 0
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 3
REMARK 465 ARG B 4
REMARK 465 SER B 5
REMARK 465 PRO B 6
REMARK 465 SER B 7
REMARK 465 SER H 128
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 SER H 215
REMARK 465 GLU H 216
REMARK 465 PHE H 217
REMARK 465 ASP H 218
REMARK 465 TYR H 219
REMARK 465 LYS H 220
REMARK 465 ASP H 221
REMARK 465 ASP H 222
REMARK 465 ASP H 223
REMARK 465 ASP H 224
REMARK 465 LYS H 225
REMARK 465 GLY H 226
REMARK 465 ALA H 227
REMARK 465 PRO H 228
REMARK 465 HIS H 229
REMARK 465 HIS H 230
REMARK 465 HIS H 231
REMARK 465 HIS H 232
REMARK 465 HIS H 233
REMARK 465 HIS H 234
REMARK 465 THR L 209
REMARK 465 GLU L 210
REMARK 465 ALA L 211
REMARK 465 LYS M 129
REMARK 465 SER M 130
REMARK 465 THR M 131
REMARK 465 SER M 132
REMARK 465 LYS M 214
REMARK 465 SER M 215
REMARK 465 GLU M 216
REMARK 465 PHE M 217
REMARK 465 ASP M 218
REMARK 465 TYR M 219
REMARK 465 LYS M 220
REMARK 465 ASP M 221
REMARK 465 ASP M 222
REMARK 465 ASP M 223
REMARK 465 ASP M 224
REMARK 465 LYS M 225
REMARK 465 GLY M 226
REMARK 465 ALA M 227
REMARK 465 PRO M 228
REMARK 465 HIS M 229
REMARK 465 HIS M 230
REMARK 465 HIS M 231
REMARK 465 HIS M 232
REMARK 465 HIS M 233
REMARK 465 HIS M 234
REMARK 465 PRO N 55
REMARK 465 SER N 56
REMARK 465 GLY N 57
REMARK 465 ILE N 58
REMARK 465 PRO N 59
REMARK 465 THR N 209
REMARK 465 GLU N 210
REMARK 465 ALA N 211
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 30 CG CD NE CZ NH1 NH2
REMARK 480 ASP A 31 CG OD1 OD2
REMARK 480 THR A 32 OG1 CG2
REMARK 480 GLU A 35 CG CD OE1 OE2
REMARK 480 ASN A 37 CG OD1 ND2
REMARK 480 GLU A 38 OE1 OE2
REMARK 480 GLU A 45 CG CD OE1 OE2
REMARK 480 LEU A 49 CD1 CD2
REMARK 480 GLN A 50 CG CD OE1 NE2
REMARK 480 GLU A 51 CG CD OE1 OE2
REMARK 480 LYS A 63 CE NZ
REMARK 480 LEU A 70 CD1 CD2
REMARK 480 LYS A 72 CD CE NZ
REMARK 480 LYS A 74 CG CD CE NZ
REMARK 480 GLN A 99 CG CD OE1 NE2
REMARK 480 ILE A 100 CD1
REMARK 480 LYS A 111 CE NZ
REMARK 480 ILE A 117 CD1
REMARK 480 GLU A 123 CD OE1 OE2
REMARK 480 ARG B 30 CD NE CZ NH1 NH2
REMARK 480 ASP B 31 CG OD1 OD2
REMARK 480 GLU B 35 CG CD OE1 OE2
REMARK 480 ASN B 37 CG OD1 ND2
REMARK 480 GLU B 38 CG CD OE1 OE2
REMARK 480 GLU B 41 CG CD OE1 OE2
REMARK 480 SER B 44 OG
REMARK 480 GLU B 45 CG CD OE1 OE2
REMARK 480 GLN B 50 OE1 NE2
REMARK 480 GLU B 51 OE1 OE2
REMARK 480 LEU B 61 CD1 CD2
REMARK 480 ARG B 67 CG CD NE CZ NH1 NH2
REMARK 480 LEU B 70 CD1 CD2
REMARK 480 LYS B 72 CD CE NZ
REMARK 480 LYS B 74 CD CE NZ
REMARK 480 LYS B 85 NZ
REMARK 480 SER B 95 OG
REMARK 480 GLN B 99 CG CD OE1 NE2
REMARK 480 ILE B 100 CD1
REMARK 480 ILE B 101 CD1
REMARK 480 GLU B 104 CG CD OE1 OE2
REMARK 480 GLU B 108 CD OE1 OE2
REMARK 480 LYS B 111 CE NZ
REMARK 480 ILE B 117 CD1
REMARK 480 GLU B 123 CG CD OE1 OE2
REMARK 480 GLN H 1 CD OE1 NE2
REMARK 480 GLN H 13 CG CD OE1 NE2
REMARK 480 LYS H 43 CD CE NZ
REMARK 480 LYS H 52B CG CD CE NZ
REMARK 480 LYS H 64 CE NZ
REMARK 480 LYS H 117 CG CD CE NZ
REMARK 480 SER H 127 OG
REMARK 480 LEU H 138 CD1 CD2
REMARK 480 LYS H 143 CE NZ
REMARK 480 SER H 161 OG
REMARK 480 VAL H 184 CG1 CG2
REMARK 480 SER H 188 OG
REMARK 480 LEU H 189 CG CD1 CD2
REMARK 480 THR H 191 OG1 CG2
REMARK 480 ILE H 195 CD1
REMARK 480 LYS H 201 CG CD CE NZ
REMARK 480 LYS H 206 CD CE NZ
REMARK 480 LYS H 210 CE NZ
REMARK 480 VAL H 211 CG1 CG2
REMARK 480 GLU H 212 CG CD OE1 OE2
REMARK 480 LYS H 214 CG CD CE NZ
REMARK 480 ASP L 26 CG OD1 OD2
REMARK 480 SER L 27 OG
REMARK 480 LYS L 30 CE NZ
REMARK 480 LYS L 31 NZ
REMARK 480 LYS L 51 CG CD CE NZ
REMARK 480 ILE L 58 CD1
REMARK 480 LYS L 103 CE NZ
REMARK 480 LYS L 110 CD CE NZ
REMARK 480 LEU L 117 CD1 CD2
REMARK 480 GLU L 123 CG CD OE1 OE2
REMARK 480 LEU L 125 CD1 CD2
REMARK 480 GLN L 126 CG CD OE1 NE2
REMARK 480 ASN L 128 CG OD1 ND2
REMARK 480 LYS L 129 CG CD CE NZ
REMARK 480 ILE L 136 CD1
REMARK 480 LYS L 149 CE NZ
REMARK 480 SER L 152 OG
REMARK 480 LYS L 156 CG CD CE NZ
REMARK 480 LYS L 171 CE NZ
REMARK 480 LEU L 178 CD1 CD2
REMARK 480 SER L 179 OG
REMARK 480 GLU L 183 CG CD OE1 OE2
REMARK 480 LYS L 186 CG CD CE NZ
REMARK 480 ARG L 189 CG CD NE CZ NH1 NH2
REMARK 480 GLN M 1 CD OE1 NE2
REMARK 480 GLN M 13 CD OE1 NE2
REMARK 480 LYS M 43 CD CE NZ
REMARK 480 LYS M 52B CG CD CE NZ
REMARK 480 LYS M 64 CD CE NZ
REMARK 480 SER M 74 OG
REMARK 480 LYS M 75 CE NZ
REMARK 480 LYS M 117 NZ
REMARK 480 SER M 127 OG
REMARK 480 LEU M 159 CD1 CD2
REMARK 480 SER M 161 OG
REMARK 480 SER M 188 OG
REMARK 480 LEU M 189 CD1 CD2
REMARK 480 THR M 191 OG1 CG2
REMARK 480 GLN M 192 CG CD OE1 NE2
REMARK 480 ILE M 195 CD1
REMARK 480 LYS M 201 CG CD CE NZ
REMARK 480 ASN M 204 OD1 ND2
REMARK 480 LYS M 206 NZ
REMARK 480 LYS M 209 CG CD CE NZ
REMARK 480 LYS M 210 NZ
REMARK 480 LYS N 30 NZ
REMARK 480 LYS N 39 NZ
REMARK 480 LYS N 51 CG CD CE NZ
REMARK 480 ARG N 52 CG CD NE CZ NH1 NH2
REMARK 480 GLU N 60 CG CD OE1 OE2
REMARK 480 GLU N 81 CG CD OE1 OE2
REMARK 480 LYS N 103 CD CE NZ
REMARK 480 GLN N 108 CD OE1 NE2
REMARK 480 LYS N 110 CG CD CE NZ
REMARK 480 GLN N 126 CG CD OE1 NE2
REMARK 480 ASN N 128 OD1 ND2
REMARK 480 LYS N 129 CD CE NZ
REMARK 480 LYS N 149 CE NZ
REMARK 480 SER N 153 OG
REMARK 480 LYS N 156 CG CD CE NZ
REMARK 480 LYS N 166 CG CD CE NZ
REMARK 480 LYS N 171 NZ
REMARK 480 LEU N 180 CD1 CD2
REMARK 480 GLU N 183 CG CD OE1 OE2
REMARK 480 LYS N 186 CG CD CE NZ
REMARK 480 SER N 187 OG
REMARK 480 ARG N 189 CD NE CZ NH1 NH2
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 GLN B 50 CD GLN B 50 OE1 -0.195
REMARK 500 SER M 188 CB SER M 188 OG -0.089
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 29 109.13 -59.52
REMARK 500 GLU A 51 69.98 -158.68
REMARK 500 ASP H 144 77.21 56.89
REMARK 500 THR H 160 -34.18 -132.94
REMARK 500 ILE L 58 88.11 33.41
REMARK 500 ASP L 151 -83.72 57.82
REMARK 500 SER L 152 41.24 -151.15
REMARK 500 ASP M 144 78.69 57.21
REMARK 500 LEU N 106A 30.65 -98.09
REMARK 500 ASP N 151 -110.36 56.90
REMARK 500 ASN N 170 -10.21 65.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG N 301
DBREF 5D72 A -16 110 UNP P04141 CSF2_HUMAN 1 127
DBREF 5D72 B -16 110 UNP P04141 CSF2_HUMAN 1 127
DBREF 5D72 H 1 234 PDB 5D72 5D72 1 234
DBREF 5D72 L 1 211 PDB 5D72 5D72 1 211
DBREF 5D72 M 1 234 PDB 5D72 5D72 1 234
DBREF 5D72 N 1 211 PDB 5D72 5D72 1 211
SEQADV 5D72 LYS A 111 UNP P04141 EXPRESSION TAG
SEQADV 5D72 ASP A 112 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PHE A 113 UNP P04141 EXPRESSION TAG
SEQADV 5D72 LEU A 114 UNP P04141 EXPRESSION TAG
SEQADV 5D72 LEU A 115 UNP P04141 EXPRESSION TAG
SEQADV 5D72 VAL A 116 UNP P04141 EXPRESSION TAG
SEQADV 5D72 ILE A 117 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PRO A 118 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PHE A 119 UNP P04141 EXPRESSION TAG
SEQADV 5D72 ASP A 120 UNP P04141 EXPRESSION TAG
SEQADV 5D72 CYS A 121 UNP P04141 EXPRESSION TAG
SEQADV 5D72 TRP A 122 UNP P04141 EXPRESSION TAG
SEQADV 5D72 GLU A 123 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PRO A 124 UNP P04141 EXPRESSION TAG
SEQADV 5D72 LYS B 111 UNP P04141 EXPRESSION TAG
SEQADV 5D72 ASP B 112 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PHE B 113 UNP P04141 EXPRESSION TAG
SEQADV 5D72 LEU B 114 UNP P04141 EXPRESSION TAG
SEQADV 5D72 LEU B 115 UNP P04141 EXPRESSION TAG
SEQADV 5D72 VAL B 116 UNP P04141 EXPRESSION TAG
SEQADV 5D72 ILE B 117 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PRO B 118 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PHE B 119 UNP P04141 EXPRESSION TAG
SEQADV 5D72 ASP B 120 UNP P04141 EXPRESSION TAG
SEQADV 5D72 CYS B 121 UNP P04141 EXPRESSION TAG
SEQADV 5D72 TRP B 122 UNP P04141 EXPRESSION TAG
SEQADV 5D72 GLU B 123 UNP P04141 EXPRESSION TAG
SEQADV 5D72 PRO B 124 UNP P04141 EXPRESSION TAG
SEQRES 1 A 141 MET TRP LEU GLN SER LEU LEU LEU LEU GLY THR VAL ALA
SEQRES 2 A 141 CYS SER ILE SER ALA PRO ALA ARG SER PRO SER PRO SER
SEQRES 3 A 141 THR GLN PRO TRP GLU HIS VAL ASN ALA ILE GLN GLU ALA
SEQRES 4 A 141 ARG ARG LEU LEU ASN LEU SER ARG ASP THR ALA ALA GLU
SEQRES 5 A 141 MET ASN GLU THR VAL GLU VAL ILE SER GLU MET PHE ASP
SEQRES 6 A 141 LEU GLN GLU PRO THR CYS LEU GLN THR ARG LEU GLU LEU
SEQRES 7 A 141 TYR LYS GLN GLY LEU ARG GLY SER LEU THR LYS LEU LYS
SEQRES 8 A 141 GLY PRO LEU THR MET MET ALA SER HIS TYR LYS GLN HIS
SEQRES 9 A 141 CYS PRO PRO THR PRO GLU THR SER CYS ALA THR GLN ILE
SEQRES 10 A 141 ILE THR PHE GLU SER PHE LYS GLU ASN LEU LYS ASP PHE
SEQRES 11 A 141 LEU LEU VAL ILE PRO PHE ASP CYS TRP GLU PRO
SEQRES 1 B 141 MET TRP LEU GLN SER LEU LEU LEU LEU GLY THR VAL ALA
SEQRES 2 B 141 CYS SER ILE SER ALA PRO ALA ARG SER PRO SER PRO SER
SEQRES 3 B 141 THR GLN PRO TRP GLU HIS VAL ASN ALA ILE GLN GLU ALA
SEQRES 4 B 141 ARG ARG LEU LEU ASN LEU SER ARG ASP THR ALA ALA GLU
SEQRES 5 B 141 MET ASN GLU THR VAL GLU VAL ILE SER GLU MET PHE ASP
SEQRES 6 B 141 LEU GLN GLU PRO THR CYS LEU GLN THR ARG LEU GLU LEU
SEQRES 7 B 141 TYR LYS GLN GLY LEU ARG GLY SER LEU THR LYS LEU LYS
SEQRES 8 B 141 GLY PRO LEU THR MET MET ALA SER HIS TYR LYS GLN HIS
SEQRES 9 B 141 CYS PRO PRO THR PRO GLU THR SER CYS ALA THR GLN ILE
SEQRES 10 B 141 ILE THR PHE GLU SER PHE LYS GLU ASN LEU LYS ASP PHE
SEQRES 11 B 141 LEU LEU VAL ILE PRO PHE ASP CYS TRP GLU PRO
SEQRES 1 H 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 238 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 238 PHE THR PHE SER SER TYR TRP MET ASN TRP VAL ARG GLN
SEQRES 4 H 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE GLU
SEQRES 5 H 238 ASN LYS TYR ALA GLY GLY ALA THR TYR TYR ALA ALA SER
SEQRES 6 H 238 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS
SEQRES 7 H 238 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU
SEQRES 8 H 238 ASP THR ALA VAL TYR TYR CYS ALA ARG GLY PHE GLY THR
SEQRES 9 H 238 ASP PHE TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 10 H 238 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 H 238 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 12 H 238 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 238 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 H 238 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 H 238 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 H 238 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 17 H 238 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER GLU PHE
SEQRES 18 H 238 ASP TYR LYS ASP ASP ASP ASP LYS GLY ALA PRO HIS HIS
SEQRES 19 H 238 HIS HIS HIS HIS
SEQRES 1 L 209 ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA
SEQRES 2 L 209 PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER
SEQRES 3 L 209 ILE GLY LYS LYS TYR ALA TYR TRP TYR GLN GLN LYS PRO
SEQRES 4 L 209 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS LYS ARG PRO
SEQRES 5 L 209 SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SER GLY
SEQRES 6 L 209 ASN THR ALA THR LEU THR ILE SER GLY THR GLN ALA GLU
SEQRES 7 L 209 ASP GLU ALA ASP TYR TYR CYS SER SER TRP ASP SER THR
SEQRES 8 L 209 GLY LEU VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU
SEQRES 9 L 209 GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO
SEQRES 10 L 209 PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU
SEQRES 11 L 209 VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR
SEQRES 12 L 209 VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY
SEQRES 13 L 209 VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS
SEQRES 14 L 209 TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN
SEQRES 15 L 209 TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS
SEQRES 16 L 209 GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU
SEQRES 17 L 209 ALA
SEQRES 1 M 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 M 238 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 M 238 PHE THR PHE SER SER TYR TRP MET ASN TRP VAL ARG GLN
SEQRES 4 M 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE GLU
SEQRES 5 M 238 ASN LYS TYR ALA GLY GLY ALA THR TYR TYR ALA ALA SER
SEQRES 6 M 238 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS
SEQRES 7 M 238 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU
SEQRES 8 M 238 ASP THR ALA VAL TYR TYR CYS ALA ARG GLY PHE GLY THR
SEQRES 9 M 238 ASP PHE TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 10 M 238 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 M 238 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 12 M 238 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 M 238 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 M 238 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 M 238 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 M 238 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 17 M 238 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER GLU PHE
SEQRES 18 M 238 ASP TYR LYS ASP ASP ASP ASP LYS GLY ALA PRO HIS HIS
SEQRES 19 M 238 HIS HIS HIS HIS
SEQRES 1 N 209 ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA
SEQRES 2 N 209 PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER
SEQRES 3 N 209 ILE GLY LYS LYS TYR ALA TYR TRP TYR GLN GLN LYS PRO
SEQRES 4 N 209 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS LYS ARG PRO
SEQRES 5 N 209 SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SER GLY
SEQRES 6 N 209 ASN THR ALA THR LEU THR ILE SER GLY THR GLN ALA GLU
SEQRES 7 N 209 ASP GLU ALA ASP TYR TYR CYS SER SER TRP ASP SER THR
SEQRES 8 N 209 GLY LEU VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU
SEQRES 9 N 209 GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO
SEQRES 10 N 209 PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU
SEQRES 11 N 209 VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR
SEQRES 12 N 209 VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY
SEQRES 13 N 209 VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS
SEQRES 14 N 209 TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN
SEQRES 15 N 209 TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS
SEQRES 16 N 209 GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU
SEQRES 17 N 209 ALA
HET PEG H 301 7
HET PEG N 301 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 7 PEG 2(C4 H10 O3)
FORMUL 9 HOH *32(H2 O)
HELIX 1 AA1 GLU A 14 SER A 29 1 16
HELIX 2 AA2 THR A 32 ASN A 37 1 6
HELIX 3 AA3 CYS A 54 LEU A 66 1 13
HELIX 4 AA4 ARG A 67 LYS A 72 5 6
HELIX 5 AA5 LEU A 73 CYS A 88 1 16
HELIX 6 AA6 PHE A 103 ILE A 117 1 15
HELIX 7 AA7 TRP B 13 SER B 29 1 17
HELIX 8 AA8 ALA B 33 GLU B 38 1 6
HELIX 9 AA9 CYS B 54 GLY B 65 1 12
HELIX 10 AB1 ARG B 67 LYS B 72 5 6
HELIX 11 AB2 LEU B 73 CYS B 88 1 16
HELIX 12 AB3 PHE B 103 ILE B 117 1 15
HELIX 13 AB4 THR H 28 TYR H 32 5 5
HELIX 14 AB5 ARG H 83 THR H 87 5 5
HELIX 15 AB6 SER H 187 GLN H 192 1 6
HELIX 16 AB7 LYS H 201 ASN H 204 5 4
HELIX 17 AB8 GLN L 79 GLU L 83 5 5
HELIX 18 AB9 SER L 121 GLN L 126 1 6
HELIX 19 AC1 THR L 181 HIS L 188 1 8
HELIX 20 AC2 THR M 28 TYR M 32 5 5
HELIX 21 AC3 ARG M 83 THR M 87 5 5
HELIX 22 AC4 SER M 187 LEU M 189 5 3
HELIX 23 AC5 LYS M 201 ASN M 204 5 4
HELIX 24 AC6 SER N 27 LYS N 31 5 5
HELIX 25 AC7 GLN N 79 GLU N 83 5 5
HELIX 26 AC8 SER N 121 ALA N 127 1 7
HELIX 27 AC9 THR N 181 HIS N 188 1 8
SHEET 1 AA1 2 THR A 39 ILE A 43 0
SHEET 2 AA1 2 THR A 98 THR A 102 -1 O ILE A 101 N VAL A 40
SHEET 1 AA2 2 THR B 39 ILE B 43 0
SHEET 2 AA2 2 THR B 98 THR B 102 -1 O ILE B 101 N VAL B 40
SHEET 1 AA3 4 GLN H 3 SER H 7 0
SHEET 2 AA3 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3
SHEET 3 AA3 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18
SHEET 4 AA3 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 AA4 6 LEU H 11 VAL H 12 0
SHEET 2 AA4 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 AA4 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107
SHEET 4 AA4 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 AA4 6 GLU H 46 ILE H 51 -1 O VAL H 48 N TRP H 36
SHEET 6 AA4 6 THR H 57 TYR H 59 -1 O TYR H 58 N GLY H 50
SHEET 1 AA5 4 SER H 120 LEU H 124 0
SHEET 2 AA5 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AA5 4 TYR H 176 VAL H 184 -1 O TYR H 176 N TYR H 145
SHEET 4 AA5 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AA6 4 SER H 120 LEU H 124 0
SHEET 2 AA6 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AA6 4 TYR H 176 VAL H 184 -1 O TYR H 176 N TYR H 145
SHEET 4 AA6 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AA7 3 THR H 151 TRP H 154 0
SHEET 2 AA7 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 AA7 3 THR H 205 VAL H 211 -1 O THR H 205 N HIS H 200
SHEET 1 AA8 5 SER L 9 VAL L 13 0
SHEET 2 AA8 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AA8 5 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104
SHEET 4 AA8 5 TYR L 34 GLN L 38 -1 N GLN L 38 O ASP L 85
SHEET 5 AA8 5 VAL L 45 LEU L 46 -1 O VAL L 45 N GLN L 37
SHEET 1 AA9 4 SER L 9 VAL L 13 0
SHEET 2 AA9 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AA9 4 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104
SHEET 4 AA9 4 GLY L 95 PHE L 98 -1 O VAL L 97 N SER L 90
SHEET 1 AB1 3 ALA L 19 SER L 24 0
SHEET 2 AB1 3 THR L 70 ILE L 75 -1 O ILE L 75 N ALA L 19
SHEET 3 AB1 3 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72
SHEET 1 AB2 4 SER L 114 PHE L 118 0
SHEET 2 AB2 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AB2 4 TYR L 172 LEU L 180 -1 O ALA L 174 N ILE L 136
SHEET 4 AB2 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177
SHEET 1 AB3 4 SER L 114 PHE L 118 0
SHEET 2 AB3 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AB3 4 TYR L 172 LEU L 180 -1 O ALA L 174 N ILE L 136
SHEET 4 AB3 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173
SHEET 1 AB4 4 SER L 153 PRO L 154 0
SHEET 2 AB4 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153
SHEET 3 AB4 4 TYR L 191 HIS L 197 -1 O THR L 196 N THR L 145
SHEET 4 AB4 4 SER L 200 VAL L 206 -1 O SER L 200 N HIS L 197
SHEET 1 AB5 4 GLN M 3 SER M 7 0
SHEET 2 AB5 4 LEU M 18 SER M 25 -1 O ALA M 23 N VAL M 5
SHEET 3 AB5 4 THR M 77 MET M 82 -1 O MET M 82 N LEU M 18
SHEET 4 AB5 4 PHE M 67 ASP M 72 -1 N THR M 68 O GLN M 81
SHEET 1 AB6 6 LEU M 11 VAL M 12 0
SHEET 2 AB6 6 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12
SHEET 3 AB6 6 ALA M 88 ARG M 94 -1 N ALA M 88 O VAL M 109
SHEET 4 AB6 6 MET M 34 GLN M 39 -1 N VAL M 37 O TYR M 91
SHEET 5 AB6 6 GLU M 46 ILE M 51 -1 O GLU M 46 N ARG M 38
SHEET 6 AB6 6 THR M 57 TYR M 59 -1 O TYR M 58 N GLY M 50
SHEET 1 AB7 4 LEU M 11 VAL M 12 0
SHEET 2 AB7 4 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12
SHEET 3 AB7 4 ALA M 88 ARG M 94 -1 N ALA M 88 O VAL M 109
SHEET 4 AB7 4 PHE M 102 TRP M 103 -1 O PHE M 102 N ARG M 94
SHEET 1 AB8 4 SER M 120 LEU M 124 0
SHEET 2 AB8 4 THR M 135 TYR M 145 -1 O LEU M 141 N PHE M 122
SHEET 3 AB8 4 TYR M 176 PRO M 185 -1 O TYR M 176 N TYR M 145
SHEET 4 AB8 4 VAL M 163 THR M 165 -1 N HIS M 164 O VAL M 181
SHEET 1 AB9 4 SER M 120 LEU M 124 0
SHEET 2 AB9 4 THR M 135 TYR M 145 -1 O LEU M 141 N PHE M 122
SHEET 3 AB9 4 TYR M 176 PRO M 185 -1 O TYR M 176 N TYR M 145
SHEET 4 AB9 4 VAL M 169 LEU M 170 -1 N VAL M 169 O SER M 177
SHEET 1 AC1 3 THR M 151 TRP M 154 0
SHEET 2 AC1 3 TYR M 194 HIS M 200 -1 O ASN M 197 N SER M 153
SHEET 3 AC1 3 THR M 205 VAL M 211 -1 O THR M 205 N HIS M 200
SHEET 1 AC2 5 SER N 9 VAL N 13 0
SHEET 2 AC2 5 THR N 102 VAL N 106 1 O THR N 105 N VAL N 11
SHEET 3 AC2 5 ASP N 85 ASP N 92 -1 N TYR N 86 O THR N 102
SHEET 4 AC2 5 TYR N 34 GLN N 38 -1 N TYR N 36 O TYR N 87
SHEET 5 AC2 5 VAL N 45 LEU N 46 -1 O VAL N 45 N GLN N 37
SHEET 1 AC3 4 SER N 9 VAL N 13 0
SHEET 2 AC3 4 THR N 102 VAL N 106 1 O THR N 105 N VAL N 11
SHEET 3 AC3 4 ASP N 85 ASP N 92 -1 N TYR N 86 O THR N 102
SHEET 4 AC3 4 GLY N 95 PHE N 98 -1 O VAL N 97 N SER N 90
SHEET 1 AC4 3 ALA N 19 SER N 24 0
SHEET 2 AC4 3 THR N 70 ILE N 75 -1 O ILE N 75 N ALA N 19
SHEET 3 AC4 3 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74
SHEET 1 AC5 4 SER N 114 PHE N 118 0
SHEET 2 AC5 4 ALA N 130 PHE N 139 -1 O SER N 137 N SER N 114
SHEET 3 AC5 4 TYR N 172 LEU N 180 -1 O ALA N 174 N ILE N 136
SHEET 4 AC5 4 VAL N 159 THR N 161 -1 N GLU N 160 O TYR N 177
SHEET 1 AC6 4 SER N 114 PHE N 118 0
SHEET 2 AC6 4 ALA N 130 PHE N 139 -1 O SER N 137 N SER N 114
SHEET 3 AC6 4 TYR N 172 LEU N 180 -1 O ALA N 174 N ILE N 136
SHEET 4 AC6 4 SER N 165 LYS N 166 -1 N SER N 165 O ALA N 173
SHEET 1 AC7 4 SER N 153 VAL N 155 0
SHEET 2 AC7 4 THR N 145 ALA N 150 -1 N ALA N 150 O SER N 153
SHEET 3 AC7 4 TYR N 191 HIS N 197 -1 O GLN N 194 N ALA N 147
SHEET 4 AC7 4 SER N 200 VAL N 206 -1 O VAL N 206 N TYR N 191
SSBOND 1 CYS A 54 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 88 CYS A 121 1555 1555 2.05
SSBOND 3 CYS B 54 CYS B 96 1555 1555 2.04
SSBOND 4 CYS B 88 CYS B 121 1555 1555 2.05
SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.05
SSBOND 6 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 8 CYS L 134 CYS L 193 1555 1555 2.04
SSBOND 9 CYS M 22 CYS M 92 1555 1555 2.04
SSBOND 10 CYS M 140 CYS M 196 1555 1555 2.02
SSBOND 11 CYS N 23 CYS N 88 1555 1555 2.03
SSBOND 12 CYS N 134 CYS N 193 1555 1555 2.03
CISPEP 1 PHE H 146 PRO H 147 0 -6.57
CISPEP 2 GLU H 148 PRO H 149 0 -8.51
CISPEP 3 TYR L 140 PRO L 141 0 -3.24
CISPEP 4 PHE M 146 PRO M 147 0 -4.06
CISPEP 5 GLU M 148 PRO M 149 0 -7.55
CISPEP 6 TYR N 140 PRO N 141 0 -0.16
SITE 1 AC1 3 LYS H 43 GLY H 44 GLY L 100
SITE 1 AC2 2 TYR M 91 GLY N 41
CRYST1 71.822 97.853 192.667 90.00 90.00 90.00 P 21 21 21 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 0.013923 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010219 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005190 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
