HEADER IMMUNE SYSTEM 03-MAR-08 3CFE
TITLE CRYSTAL STRUCTURE OF PURPLE-FLUORESCENT ANTIBODY EP2-25C10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURPLE-FLUORESCENT ANTIBODY EP2-25C10-KAPPA LIGHT CHAIN;
COMPND 3 CHAIN: L, A;
COMPND 4 FRAGMENT: FAB;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PURPLE-FLUORESCENT ANTIBODY EP2-25C10-IGG2B HEAVY CHAIN;
COMPND 7 CHAIN: H, B;
COMPND 8 FRAGMENT: FAB
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL: HYBRIDOMA CELLS FROM 129GIX+ SPLEEN CELLS FUSED WITH BALB/C
SOURCE 6 MYELOMA CELLS;
SOURCE 7 OTHER_DETAILS: PURIFIED FROM ASCITIC FLUID;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 CELL: HYBRIDOMA CELLS FROM 129GIX+ SPLEEN CELLS FUSED WITH BALB/C
SOURCE 13 MYELOMA CELLS;
SOURCE 14 OTHER_DETAILS: PURIFIED FROM ASCITIC FLUID
KEYWDS IMMUNOGLOBULIN, PURPLE-FLUORESCENT ANTIBODY, HAPTEN COMPLEX, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR E.W.DEBLER,A.HEINE,I.A.WILSON
REVDAT 5 30-AUG-23 3CFE 1 REMARK DBREF
REVDAT 4 13-JUL-11 3CFE 1 VERSN
REVDAT 3 24-FEB-09 3CFE 1 VERSN
REVDAT 2 19-AUG-08 3CFE 1 REMARK
REVDAT 1 18-MAR-08 3CFE 0
JRNL AUTH E.W.DEBLER,G.F.KAUFMANN,M.M.MEIJLER,A.HEINE,J.M.MEE,
JRNL AUTH 2 G.PLJEVALJCIC,A.J.DI BILIO,P.G.SCHULTZ,D.P.MILLAR,K.D.JANDA,
JRNL AUTH 3 I.A.WILSON,H.B.GRAY,R.A.LERNER
JRNL TITL DEEPLY INVERTED ELECTRON-HOLE RECOMBINATION IN A LUMINESCENT
JRNL TITL 2 ANTIBODY-STILBENE COMPLEX.
JRNL REF SCIENCE V. 319 1232 2008
JRNL REFN ISSN 0036-8075
JRNL PMID 18309081
JRNL DOI 10.1126/SCIENCE.1153445
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0017
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 18943
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 960
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) : 2.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1201
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.4230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 58.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.65000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 1.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.97000
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): 0.462
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.340
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.913
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6835 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4524 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9323 ; 1.481 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11046 ; 0.911 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 860 ; 7.131 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;34.735 ;24.161
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1078 ;17.637 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;21.498 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1050 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7580 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1346 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1282 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4553 ; 0.214 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3288 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4026 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 206 ; 0.142 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.089 ; 0.200
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): 21 ; 0.278 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 55 ; 0.280 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.313 ; 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): 5405 ; 0.359 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1742 ; 0.085 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7004 ; 0.500 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3031 ; 0.881 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2319 ; 1.322 ; 4.500
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : L A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 1 L 107 2
REMARK 3 1 A 1 A 107 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 L (A): 1372 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 L (A**2): 1372 ; 0.07 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : L A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 108 L 213 2
REMARK 3 1 A 108 A 213 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 L (A): 1401 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 2 L (A**2): 1401 ; 0.06 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : H B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 2 H 113 2
REMARK 3 1 B 2 B 113 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 H (A): 1611 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 3 H (A**2): 1611 ; 0.08 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : H B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 114 H 227 2
REMARK 3 1 B 114 B 227 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 H (A): 1173 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 4 H (A**2): 1173 ; 0.08 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 1 A 24
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2286 50.3078 139.8862
REMARK 3 T TENSOR
REMARK 3 T11: 0.2462 T22: 0.1059
REMARK 3 T33: 0.1499 T12: -0.0543
REMARK 3 T13: 0.0227 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 2.4974 L22: 8.0568
REMARK 3 L33: 4.9039 L12: -2.9490
REMARK 3 L13: 3.0758 L23: -4.5855
REMARK 3 S TENSOR
REMARK 3 S11: -0.1184 S12: 0.0160 S13: -0.0373
REMARK 3 S21: 0.5341 S22: 0.0565 S23: -0.0278
REMARK 3 S31: -0.9475 S32: -0.0626 S33: 0.0619
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 25 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1630 44.9838 135.5471
REMARK 3 T TENSOR
REMARK 3 T11: 0.1702 T22: 0.1441
REMARK 3 T33: 0.0724 T12: -0.0690
REMARK 3 T13: 0.0171 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.8351 L22: 1.8798
REMARK 3 L33: 0.3940 L12: -0.9522
REMARK 3 L13: 0.3889 L23: -0.0322
REMARK 3 S TENSOR
REMARK 3 S11: -0.0745 S12: 0.1928 S13: 0.2298
REMARK 3 S21: -0.2098 S22: -0.0634 S23: -0.0506
REMARK 3 S31: -0.2059 S32: 0.0445 S33: 0.1379
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 106 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2904 44.9332 126.3564
REMARK 3 T TENSOR
REMARK 3 T11: 0.2821 T22: 0.1945
REMARK 3 T33: 0.0568 T12: 0.0770
REMARK 3 T13: 0.0193 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 7.0610 L22: 2.8273
REMARK 3 L33: 0.4005 L12: 3.4014
REMARK 3 L13: 0.4383 L23: 0.1157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: -0.0837 S13: -0.1585
REMARK 3 S21: 0.1528 S22: 0.0485 S23: -0.0305
REMARK 3 S31: -0.0484 S32: 0.0128 S33: -0.0013
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 183 A 193
REMARK 3 ORIGIN FOR THE GROUP (A): -50.7319 37.7878 126.6932
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.3492
REMARK 3 T33: -0.0393 T12: 0.0026
REMARK 3 T13: 0.0506 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 26.8106 L22: 23.4357
REMARK 3 L33: 1.0132 L12: 5.0192
REMARK 3 L13: 3.8146 L23: -2.5392
REMARK 3 S TENSOR
REMARK 3 S11: 0.2202 S12: -0.7424 S13: -1.3242
REMARK 3 S21: -0.0211 S22: -0.5063 S23: 0.4567
REMARK 3 S31: -0.0678 S32: -0.7894 S33: 0.2861
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 : A 194 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3247 52.1347 124.8146
REMARK 3 T TENSOR
REMARK 3 T11: 0.2570 T22: 0.2875
REMARK 3 T33: 0.3621 T12: 0.1509
REMARK 3 T13: -0.0378 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 11.4299 L22: 8.1439
REMARK 3 L33: 2.7280 L12: 9.2089
REMARK 3 L13: 1.1701 L23: 2.3172
REMARK 3 S TENSOR
REMARK 3 S11: 0.1284 S12: -0.3316 S13: 0.3649
REMARK 3 S21: 0.0302 S22: -0.3362 S23: 0.3605
REMARK 3 S31: -0.4012 S32: -0.4102 S33: 0.2078
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 1 B 9
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4634 26.3388 123.3979
REMARK 3 T TENSOR
REMARK 3 T11: 0.3386 T22: 0.1274
REMARK 3 T33: 0.0673 T12: 0.1098
REMARK 3 T13: -0.0249 T23: -0.1031
REMARK 3 L TENSOR
REMARK 3 L11: 31.7498 L22: 27.4427
REMARK 3 L33: 10.3264 L12: 22.6696
REMARK 3 L13: -11.1262 L23: -16.4500
REMARK 3 S TENSOR
REMARK 3 S11: -0.0636 S12: 1.5947 S13: 1.0078
REMARK 3 S21: -1.7232 S22: 0.6674 S23: 0.9949
REMARK 3 S31: 0.8254 S32: 0.0616 S33: -0.6038
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 10 B 102
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3388 24.1474 135.3710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1641 T22: 0.0612
REMARK 3 T33: 0.0194 T12: -0.0059
REMARK 3 T13: -0.0395 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 4.5187 L22: 2.7064
REMARK 3 L33: 1.8966 L12: -0.7922
REMARK 3 L13: -0.2263 L23: -0.0266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0697 S12: -0.0233 S13: -0.0945
REMARK 3 S21: 0.1238 S22: 0.0044 S23: 0.0201
REMARK 3 S31: -0.0280 S32: -0.0741 S33: -0.0741
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 103 B 125
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3352 26.3897 126.5147
REMARK 3 T TENSOR
REMARK 3 T11: 0.2235 T22: 0.1697
REMARK 3 T33: 0.3100 T12: -0.0180
REMARK 3 T13: -0.0527 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 4.1049 L22: 0.2183
REMARK 3 L33: 1.8464 L12: 0.9465
REMARK 3 L13: 2.7530 L23: 0.6348
REMARK 3 S TENSOR
REMARK 3 S11: -0.3134 S12: 0.4282 S13: -0.3650
REMARK 3 S21: 0.2155 S22: 0.2050 S23: 0.1627
REMARK 3 S31: -0.2656 S32: -0.0718 S33: 0.1085
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 : B 126 B 152
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2440 37.3865 118.4665
REMARK 3 T TENSOR
REMARK 3 T11: 0.3165 T22: 0.3845
REMARK 3 T33: -0.0125 T12: 0.0422
REMARK 3 T13: 0.0619 T23: -0.1223
REMARK 3 L TENSOR
REMARK 3 L11: 5.1073 L22: 12.6326
REMARK 3 L33: 5.2856 L12: -0.6352
REMARK 3 L13: 2.4914 L23: -6.2735
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.0821 S13: 0.3699
REMARK 3 S21: -0.4060 S22: 0.1121 S23: 0.0959
REMARK 3 S31: -0.1603 S32: -0.3515 S33: -0.0695
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 : B 153 B 227
REMARK 3 ORIGIN FOR THE GROUP (A): -28.8466 35.1697 114.9749
REMARK 3 T TENSOR
REMARK 3 T11: 0.1926 T22: 0.2535
REMARK 3 T33: 0.1699 T12: 0.0224
REMARK 3 T13: 0.0869 T23: -0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 4.5609 L22: 5.1290
REMARK 3 L33: 2.5730 L12: -0.6562
REMARK 3 L13: 2.2024 L23: -1.7480
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: 0.4550 S13: -0.1570
REMARK 3 S21: -0.6517 S22: -0.1456 S23: -0.2962
REMARK 3 S31: 0.2752 S32: 0.2996 S33: 0.1854
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 9
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7695 -12.5014 50.2485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2499 T22: 0.1318
REMARK 3 T33: 0.2175 T12: 0.0961
REMARK 3 T13: -0.0711 T23: 0.1284
REMARK 3 L TENSOR
REMARK 3 L11: 54.5945 L22: 28.2916
REMARK 3 L33: 5.5785 L12: 34.3564
REMARK 3 L13: -15.7988 L23: -7.3509
REMARK 3 S TENSOR
REMARK 3 S11: 0.5843 S12: 0.6901 S13: 0.8834
REMARK 3 S21: -0.9598 S22: 0.0122 S23: 0.4227
REMARK 3 S31: -0.5520 S32: 0.1402 S33: -0.5964
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 10 H 103
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0403 -14.0834 62.0708
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.0805
REMARK 3 T33: -0.0008 T12: 0.0061
REMARK 3 T13: 0.0058 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 4.5145 L22: 3.1916
REMARK 3 L33: 1.6716 L12: -0.6393
REMARK 3 L13: -0.0097 L23: 0.3422
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: 0.0770 S13: -0.1275
REMARK 3 S21: 0.0683 S22: -0.0185 S23: 0.1331
REMARK 3 S31: 0.0329 S32: -0.0192 S33: -0.0302
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 104 H 125
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1994 -12.9756 53.2885
REMARK 3 T TENSOR
REMARK 3 T11: 0.1266 T22: 0.2023
REMARK 3 T33: 0.4899 T12: 0.0910
REMARK 3 T13: -0.0541 T23: -0.1837
REMARK 3 L TENSOR
REMARK 3 L11: 4.7902 L22: 1.7300
REMARK 3 L33: 0.2185 L12: -1.9107
REMARK 3 L13: 0.8586 L23: -0.5925
REMARK 3 S TENSOR
REMARK 3 S11: 0.5070 S12: 0.5210 S13: -1.6441
REMARK 3 S21: -0.1692 S22: -0.3561 S23: 0.7653
REMARK 3 S31: 0.0041 S32: -0.0777 S33: -0.1509
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 126 H 152
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2316 -1.5482 45.3752
REMARK 3 T TENSOR
REMARK 3 T11: 0.3287 T22: 0.2411
REMARK 3 T33: 0.3225 T12: 0.1012
REMARK 3 T13: -0.0078 T23: -0.2490
REMARK 3 L TENSOR
REMARK 3 L11: 7.1979 L22: 9.0492
REMARK 3 L33: 5.7699 L12: 0.1759
REMARK 3 L13: 1.1877 L23: -5.7022
REMARK 3 S TENSOR
REMARK 3 S11: 0.2184 S12: 0.3857 S13: -0.8328
REMARK 3 S21: -0.8735 S22: 0.3068 S23: 0.2511
REMARK 3 S31: 0.0184 S32: -0.2944 S33: -0.5252
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 153 H 227
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9705 -3.9018 41.8195
REMARK 3 T TENSOR
REMARK 3 T11: 0.2073 T22: 0.4473
REMARK 3 T33: 0.3788 T12: 0.1919
REMARK 3 T13: 0.0524 T23: -0.2068
REMARK 3 L TENSOR
REMARK 3 L11: 3.3696 L22: 8.1267
REMARK 3 L33: 3.2316 L12: 0.5764
REMARK 3 L13: 1.8044 L23: -1.7883
REMARK 3 S TENSOR
REMARK 3 S11: 0.0654 S12: 0.6898 S13: -0.3353
REMARK 3 S21: -1.0354 S22: -0.1893 S23: -0.5120
REMARK 3 S31: 0.2117 S32: -0.2621 S33: 0.1239
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 24
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1476 11.9659 66.1025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0888 T22: 0.1081
REMARK 3 T33: 0.2104 T12: 0.0211
REMARK 3 T13: 0.0236 T23: -0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 3.9539 L22: 6.7489
REMARK 3 L33: 4.5480 L12: -0.9062
REMARK 3 L13: 1.1649 L23: -3.3383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: -0.4370 S13: 0.4263
REMARK 3 S21: 0.5815 S22: -0.1538 S23: 0.0319
REMARK 3 S31: -0.9504 S32: -0.1327 S33: 0.1427
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 25 L 105
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5395 6.5834 61.8287
REMARK 3 T TENSOR
REMARK 3 T11: 0.0457 T22: 0.0973
REMARK 3 T33: 0.0941 T12: -0.0163
REMARK 3 T13: 0.0305 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 2.2200 L22: 2.2774
REMARK 3 L33: 1.5069 L12: -0.5050
REMARK 3 L13: 0.3029 L23: -0.0148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: 0.2484 S13: 0.3209
REMARK 3 S21: -0.2488 S22: -0.0228 S23: -0.1240
REMARK 3 S31: -0.1275 S32: 0.0596 S33: 0.0259
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 106 L 182
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0248 6.2636 53.0197
REMARK 3 T TENSOR
REMARK 3 T11: 0.1973 T22: 0.1864
REMARK 3 T33: 0.1731 T12: 0.1233
REMARK 3 T13: -0.0435 T23: -0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 7.8611 L22: 3.2078
REMARK 3 L33: 0.1107 L12: 1.8684
REMARK 3 L13: 0.8060 L23: -0.0867
REMARK 3 S TENSOR
REMARK 3 S11: 0.1450 S12: 0.1070 S13: -0.4613
REMARK 3 S21: 0.1827 S22: -0.1109 S23: -0.1131
REMARK 3 S31: 0.0178 S32: 0.0710 S33: -0.0341
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 183 L 193
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5026 -0.7916 53.8424
REMARK 3 T TENSOR
REMARK 3 T11: 0.1637 T22: 0.3226
REMARK 3 T33: 0.5034 T12: 0.1082
REMARK 3 T13: -0.0941 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 1.1905 L22: 5.8506
REMARK 3 L33: 7.3125 L12: 0.7998
REMARK 3 L13: -1.4940 L23: 4.3712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: -0.3072 S13: -1.4380
REMARK 3 S21: 0.1992 S22: -0.1793 S23: -0.3063
REMARK 3 S31: 0.5945 S32: -0.8391 S33: 0.1636
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 194 L 213
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0456 13.4411 51.3766
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.3582
REMARK 3 T33: 0.1012 T12: 0.1351
REMARK 3 T13: 0.0829 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 6.7112 L22: 7.8820
REMARK 3 L33: 2.4194 L12: 4.3570
REMARK 3 L13: 1.2882 L23: 0.5268
REMARK 3 S TENSOR
REMARK 3 S11: 0.5292 S12: 0.0917 S13: 0.3788
REMARK 3 S21: 0.3916 S22: -0.5981 S23: 0.0524
REMARK 3 S31: 0.1218 S32: -0.2023 S33: 0.0689
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 3CFE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
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 : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20613
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.990
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASER
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3HFM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, LITHIUM SULFATE,
REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K,
REMARK 280 PH 4.50
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 66.06500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.73000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.06500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.73000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H
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 CYS L 214
REMARK 465 SER H 228
REMARK 465 CYS A 214
REMARK 465 SER B 228
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 ND1 HIS L 55 O4 SO4 L 303 2.17
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 NE2 GLN H 5 O SER B 196 2546 2.19
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 H 58 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN L 31 -8.48 77.23
REMARK 500 THR L 51 -60.81 61.88
REMARK 500 SER L 56 122.25 -38.96
REMARK 500 ASN L 77 65.61 36.92
REMARK 500 ILE L 83 102.41 -56.52
REMARK 500 ALA L 130 115.20 -160.10
REMARK 500 THR L 200 -18.02 -47.06
REMARK 500 ASN L 212 11.53 -62.59
REMARK 500 SER H 15 -14.79 86.46
REMARK 500 TYR H 27 129.61 -170.17
REMARK 500 TYR H 33 172.02 83.10
REMARK 500 PRO H 41 143.27 -35.73
REMARK 500 ASN H 99 -110.36 22.91
REMARK 500 ASP H 130 74.26 -69.56
REMARK 500 THR H 134 -169.94 -119.39
REMARK 500 SER H 163 -59.57 -153.67
REMARK 500 SER H 167 49.92 -87.96
REMARK 500 SER H 180 76.51 44.15
REMARK 500 SER H 202 -74.46 -46.80
REMARK 500 SER H 216 71.84 35.45
REMARK 500 ASN A 31 -8.59 79.78
REMARK 500 THR A 51 -61.02 59.80
REMARK 500 SER A 56 123.15 -38.08
REMARK 500 ASN A 77 66.47 38.24
REMARK 500 ILE A 83 106.05 -58.16
REMARK 500 THR A 200 -18.24 -49.97
REMARK 500 ASN A 212 12.82 -64.18
REMARK 500 SER B 15 -17.81 88.84
REMARK 500 TYR B 33 171.76 80.55
REMARK 500 PRO B 41 143.54 -37.29
REMARK 500 ASN B 99 -112.66 21.69
REMARK 500 SER B 163 -58.05 -152.43
REMARK 500 SER B 180 78.93 42.38
REMARK 500 SER B 202 -74.01 -48.94
REMARK 500 SER B 216 73.46 35.88
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FL3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BLUE FLUORESCENT ANTIBODY (19G2) IN COMPLEX
REMARK 900 WITH STILBENE HAPTEN AT 277K
REMARK 900 RELATED ID: 1UB5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANTIBODY 19G2 WITH HAPTEN AT 100K
REMARK 900 RELATED ID: 1UB6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANTIBODY 19G2 WITH SERA LIGAND
REMARK 900 RELATED ID: 3CFB RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION STRUCTURE OF BLUE FLUORESCENT ANTIBODY EP2-19G2 IN
REMARK 900 COMPLEX WITH STILBENE HAPTEN AT 100K
REMARK 900 RELATED ID: 3CFC RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION STRUCTURE OF BLUE FLUORESCENT ANTIBODY EP2-19G2
REMARK 900 RELATED ID: 3CFD RELATED DB: PDB
REMARK 900 PURPLE-FLUORESCENT ANTIBODY EP2-25C10 IN COMPLEX WITH ITS STILBENE
REMARK 900 HAPTEN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCES OF THE FAB COMPLEXES ARE NOT
REMARK 999 AVAILABLE IN ANY SEQUENCE DATABASES.
DBREF 3CFE L 1 214 PDB 3CFE 3CFE 1 214
DBREF 3CFE H 1 228 PDB 3CFE 3CFE 1 228
DBREF 3CFE A 1 214 PDB 3CFE 3CFE 1 214
DBREF 3CFE B 1 228 PDB 3CFE 3CFE 1 228
SEQRES 1 L 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA
SEQRES 2 L 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER
SEQRES 3 L 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER
SEQRES 5 L 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU
SEQRES 7 L 214 ASP GLN ASP ASP ILE ALA THR TYR PHE CYS GLN GLN GLY
SEQRES 8 L 214 THR THR LEU PRO PRO THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 220 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS
SEQRES 2 H 220 PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY
SEQRES 3 H 220 TYR SER ILE THR SER ASP TYR ALA TRP ASN TRP LEU ARG
SEQRES 4 H 220 GLN LEU PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE
SEQRES 5 H 220 SER TYR SER GLY ARG ILE ARG TYR ASN PRO SER LEU LYS
SEQRES 6 H 220 ARG ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN
SEQRES 7 H 220 PHE PHE LEU GLN LEU ASN SER VAL THR THR GLU ASP THR
SEQRES 8 H 220 ALA THR TYR TYR CYS ALA ARG SER ASP TYR GLY ASN TYR
SEQRES 9 H 220 GLY ARG GLY ASP TYR TRP GLY GLN GLY THR SER VAL THR
SEQRES 10 H 220 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 H 220 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL
SEQRES 12 H 220 THR SER GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER
SEQRES 13 H 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER
SEQRES 14 H 220 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR
SEQRES 15 H 220 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 H 220 PRO SER GLU THR VAL THR CYS SER VAL ALA HIS PRO ALA
SEQRES 17 H 220 SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER
SEQRES 1 A 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA
SEQRES 2 A 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER
SEQRES 3 A 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS
SEQRES 4 A 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER
SEQRES 5 A 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 A 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU
SEQRES 7 A 214 ASP GLN ASP ASP ILE ALA THR TYR PHE CYS GLN GLN GLY
SEQRES 8 A 214 THR THR LEU PRO PRO THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 A 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 A 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 A 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 A 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 A 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 A 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 A 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 A 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 A 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 B 220 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS
SEQRES 2 B 220 PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY
SEQRES 3 B 220 TYR SER ILE THR SER ASP TYR ALA TRP ASN TRP LEU ARG
SEQRES 4 B 220 GLN LEU PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE
SEQRES 5 B 220 SER TYR SER GLY ARG ILE ARG TYR ASN PRO SER LEU LYS
SEQRES 6 B 220 ARG ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN
SEQRES 7 B 220 PHE PHE LEU GLN LEU ASN SER VAL THR THR GLU ASP THR
SEQRES 8 B 220 ALA THR TYR TYR CYS ALA ARG SER ASP TYR GLY ASN TYR
SEQRES 9 B 220 GLY ARG GLY ASP TYR TRP GLY GLN GLY THR SER VAL THR
SEQRES 10 B 220 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 B 220 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL
SEQRES 12 B 220 THR SER GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER
SEQRES 13 B 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER
SEQRES 14 B 220 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR
SEQRES 15 B 220 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 B 220 PRO SER GLU THR VAL THR CYS SER VAL ALA HIS PRO ALA
SEQRES 17 B 220 SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER
HET SO4 L 302 5
HET SO4 L 303 5
HET GOL L 402 6
HET GOL H 401 6
HET SO4 A 301 5
HET SO4 A 304 5
HET GOL A 403 6
HET SO4 B 305 5
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 7 GOL 3(C3 H8 O3)
HELIX 1 1 ASP L 79 ILE L 83 5 5
HELIX 2 2 SER L 121 SER L 127 1 7
HELIX 3 3 LYS L 183 ARG L 188 1 6
HELIX 4 4 PRO H 41 ASN H 43 5 3
HELIX 5 5 PRO H 61 LYS H 64 5 4
HELIX 6 6 THR H 83 THR H 87 5 5
HELIX 7 7 ASP A 79 ILE A 83 5 5
HELIX 8 8 SER A 121 SER A 127 1 7
HELIX 9 9 LYS A 183 ARG A 188 1 6
HELIX 10 10 PRO B 41 ASN B 43 5 3
HELIX 11 11 PRO B 61 LYS B 64 5 4
HELIX 12 12 THR B 83 THR B 87 5 5
HELIX 13 13 SER B 196 TRP B 199 5 3
HELIX 14 14 PRO B 213 SER B 216 5 4
SHEET 1 A 4 MET L 4 THR L 5 0
SHEET 2 A 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 A 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 B 6 SER L 10 ALA L 13 0
SHEET 2 B 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11
SHEET 3 B 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 B 6 LEU L 33 GLN L 38 -1 N TYR L 36 O PHE L 87
SHEET 5 B 6 VAL L 44 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 B 6 ARG L 53 LEU L 54 -1 O ARG L 53 N TYR L 49
SHEET 1 C 4 SER L 10 ALA L 13 0
SHEET 2 C 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11
SHEET 3 C 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 C 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 D 4 THR L 114 PHE L 118 0
SHEET 2 D 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114
SHEET 3 D 4 TYR L 173 THR L 182 -1 O SER L 177 N CYS L 134
SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178
SHEET 1 E 4 SER L 153 ARG L 155 0
SHEET 2 E 4 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 E 4 SER L 191 HIS L 198 -1 O THR L 193 N LYS L 149
SHEET 4 E 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196
SHEET 1 F 4 GLN H 3 SER H 7 0
SHEET 2 F 4 LEU H 18 THR H 25 -1 O THR H 21 N SER H 7
SHEET 3 F 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22
SHEET 4 F 4 ILE H 67 ASP H 72 -1 N ASP H 72 O GLN H 77
SHEET 1 G 6 LEU H 11 VAL H 12 0
SHEET 2 G 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 G 6 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107
SHEET 4 G 6 ALA H 34 LEU H 40 -1 N LEU H 37 O TYR H 91
SHEET 5 G 6 LYS H 44 SER H 52 -1 O MET H 48 N TRP H 36
SHEET 6 G 6 ILE H 57 TYR H 59 -1 O ARG H 58 N TYR H 50
SHEET 1 H 4 LEU H 11 VAL H 12 0
SHEET 2 H 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 H 4 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107
SHEET 4 H 4 GLY H 100C TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 I 4 SER H 120 LEU H 124 0
SHEET 2 I 4 SER H 137 TYR H 147 -1 O LEU H 143 N TYR H 122
SHEET 3 I 4 LEU H 184 PRO H 194 -1 O VAL H 193 N VAL H 138
SHEET 4 I 4 SER H 169 GLN H 179 -1 N GLN H 179 O LEU H 184
SHEET 1 J 3 THR H 153 ASN H 162 0
SHEET 2 J 3 THR H 206 HIS H 212 -1 O ALA H 211 N THR H 153
SHEET 3 J 3 THR H 217 LYS H 222 -1 O THR H 217 N HIS H 212
SHEET 1 K 4 MET A 4 THR A 5 0
SHEET 2 K 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5
SHEET 3 K 4 ASP A 70 ILE A 75 -1 O TYR A 71 N CYS A 23
SHEET 4 K 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74
SHEET 1 L 6 SER A 10 ALA A 13 0
SHEET 2 L 6 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11
SHEET 3 L 6 ALA A 84 GLN A 90 -1 N TYR A 86 O THR A 102
SHEET 4 L 6 LEU A 33 GLN A 38 -1 N ASN A 34 O GLN A 89
SHEET 5 L 6 VAL A 44 TYR A 49 -1 O LEU A 47 N TRP A 35
SHEET 6 L 6 ARG A 53 LEU A 54 -1 O ARG A 53 N TYR A 49
SHEET 1 M 4 SER A 10 ALA A 13 0
SHEET 2 M 4 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11
SHEET 3 M 4 ALA A 84 GLN A 90 -1 N TYR A 86 O THR A 102
SHEET 4 M 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90
SHEET 1 N 4 THR A 114 PHE A 118 0
SHEET 2 N 4 GLY A 129 PHE A 139 -1 O ASN A 137 N THR A 114
SHEET 3 N 4 TYR A 173 THR A 182 -1 O TYR A 173 N PHE A 139
SHEET 4 N 4 VAL A 159 TRP A 163 -1 N LEU A 160 O THR A 178
SHEET 1 O 4 SER A 153 ARG A 155 0
SHEET 2 O 4 ASN A 145 ILE A 150 -1 N ILE A 150 O SER A 153
SHEET 3 O 4 SER A 191 THR A 197 -1 O THR A 193 N LYS A 149
SHEET 4 O 4 ILE A 205 ASN A 210 -1 O ILE A 205 N ALA A 196
SHEET 1 P 4 GLN B 3 SER B 7 0
SHEET 2 P 4 LEU B 18 THR B 25 -1 O THR B 25 N GLN B 3
SHEET 3 P 4 GLN B 77 LEU B 82 -1 O PHE B 78 N CYS B 22
SHEET 4 P 4 ILE B 67 ASP B 72 -1 N ASP B 72 O GLN B 77
SHEET 1 Q 6 LEU B 11 VAL B 12 0
SHEET 2 Q 6 THR B 107 VAL B 111 1 O THR B 110 N VAL B 12
SHEET 3 Q 6 ALA B 88 SER B 95 -1 N TYR B 90 O THR B 107
SHEET 4 Q 6 ALA B 34 LEU B 40 -1 N LEU B 37 O TYR B 91
SHEET 5 Q 6 LYS B 44 SER B 52 -1 O GLU B 46 N ARG B 38
SHEET 6 Q 6 ILE B 57 TYR B 59 -1 O ARG B 58 N TYR B 50
SHEET 1 R 4 LEU B 11 VAL B 12 0
SHEET 2 R 4 THR B 107 VAL B 111 1 O THR B 110 N VAL B 12
SHEET 3 R 4 ALA B 88 SER B 95 -1 N TYR B 90 O THR B 107
SHEET 4 R 4 GLY B 100C TRP B 103 -1 O TYR B 102 N ARG B 94
SHEET 1 S 4 SER B 120 LEU B 124 0
SHEET 2 S 4 SER B 137 TYR B 147 -1 O LEU B 143 N TYR B 122
SHEET 3 S 4 LEU B 184 PRO B 194 -1 O VAL B 191 N SER B 140
SHEET 4 S 4 SER B 169 GLN B 179 -1 N GLN B 179 O LEU B 184
SHEET 1 T 3 THR B 153 ASN B 162 0
SHEET 2 T 3 THR B 206 HIS B 212 -1 O SER B 209 N THR B 156
SHEET 3 T 3 THR B 217 LYS B 222 -1 O THR B 217 N HIS B 212
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.14
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.09
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.14
SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.06
SSBOND 5 CYS A 23 CYS A 88 1555 1555 2.14
SSBOND 6 CYS A 134 CYS A 194 1555 1555 2.07
SSBOND 7 CYS B 22 CYS B 92 1555 1555 2.12
SSBOND 8 CYS B 142 CYS B 208 1555 1555 2.07
CISPEP 1 LEU L 94 PRO L 95 0 -9.41
CISPEP 2 TYR L 140 PRO L 141 0 -0.41
CISPEP 3 PHE H 148 PRO H 149 0 -5.55
CISPEP 4 GLU H 150 SER H 151 0 15.10
CISPEP 5 TRP H 199 PRO H 200 0 9.69
CISPEP 6 LEU A 94 PRO A 95 0 -8.07
CISPEP 7 TYR A 140 PRO A 141 0 2.66
CISPEP 8 PHE B 148 PRO B 149 0 -3.29
CISPEP 9 GLU B 150 SER B 151 0 17.83
CISPEP 10 TRP B 199 PRO B 200 0 10.73
SITE 1 AC1 4 ARG A 24 GLY A 152 SER A 153 GLU A 154
SITE 1 AC2 5 SER H 54 ARG H 56 ARG L 24 SER L 153
SITE 2 AC2 5 GLU L 154
SITE 1 AC3 4 ARG H 100B TYR L 49 HIS L 55 SER L 56
SITE 1 AC4 4 TYR A 49 HIS A 55 SER A 56 ARG B 100B
SITE 1 AC5 3 ASP A 151 HIS A 189 ARG B 71
SITE 1 AC6 3 ARG H 71 ASP L 151 HIS L 189
SITE 1 AC7 3 LYS H 64 SER L 65 GLY L 66
SITE 1 AC8 3 SER A 65 GLY A 66 LYS B 64
CRYST1 132.130 59.460 149.370 90.00 100.37 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 0.007568 0.000000 0.001385 0.00000
SCALE2 0.000000 0.016818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
