REMARK 2 REMARK 2 RESOLUTION. 2.42 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.81 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 97.05 REMARK 3 NUMBER OF REFLECTIONS : 70750 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) : 0.18565 REMARK 3 R VALUE (WORKING SET) : 0.18301 REMARK 3 FREE R VALUE : 0.23567 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 3729 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) : 2.424 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.487 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4602 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.56 REMARK 3 BIN R VALUE (WORKING SET) : 0.294 REMARK 3 BIN FREE R VALUE SET COUNT : 227 REMARK 3 BIN FREE R VALUE : 0.325 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 11852 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 475 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.829 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.08 REMARK 3 B22 (A**2) : 0.24 REMARK 3 B33 (A**2) : -0.24 REMARK 3 B12 (A**2) : 0.02 REMARK 3 B13 (A**2) : -0.05 REMARK 3 B23 (A**2) : -0.07 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.340 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.244 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.587 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11881 ; 0.012 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): 7487 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16196 ; 1.491 ; 1.949 REMARK 3 BOND ANGLES OTHERS (DEGREES): 18530 ; 0.902 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1590 ; 6.862 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 465 ;37.423 ;26.753 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1909 ;15.991 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.088 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1996 ; 0.083 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13445 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2127 ; 0.001 ; 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 295 A 920 4 REMARK 3 1 C 295 C 920 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 7501 ; 0.44 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 C (A): 7501 ; 0.44 ; 0.50 REMARK 3 MEDIUM THERMAL 1 A (A**2): 7501 ; 2.84 ; 2.00 REMARK 3 MEDIUM THERMAL 1 C (A**2): 7501 ; 2.84 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 124 4 REMARK 3 1 D 1 D 124 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 B (A): 1512 ; 0.34 ; 0.50 REMARK 3 MEDIUM POSITIONAL 1 D (A): 1512 ; 0.34 ; 0.50 REMARK 3 MEDIUM THERMAL 1 B (A**2): 1512 ; 5.94 ; 2.00 REMARK 3 MEDIUM THERMAL 1 D (A**2): 1512 ; 5.94 ; 2.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 27 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 : B 1 B 15 REMARK 3 ORIGIN FOR THE GROUP (A): 1.3150 -48.5930 26.5150 REMARK 3 T TENSOR REMARK 3 T11: 0.6830 T22: 0.4463 REMARK 3 T33: 0.2765 T12: 0.2540 REMARK 3 T13: 0.1164 T23: -0.0827 REMARK 3 L TENSOR REMARK 3 L11: 1.8680 L22: 10.2201 REMARK 3 L33: 4.6578 L12: 4.2852 REMARK 3 L13: 1.0613 L23: 3.0609 REMARK 3 S TENSOR REMARK 3 S11: -0.1692 S12: 0.0231 S13: 0.5955 REMARK 3 S21: 0.8835 S22: -0.1757 S23: 1.4752 REMARK 3 S31: -0.3723 S32: -0.2187 S33: 0.3449 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 : B 16 B 39 REMARK 3 ORIGIN FOR THE GROUP (A): 1.2070 -54.5760 17.3900 REMARK 3 T TENSOR REMARK 3 T11: 0.0922 T22: 0.2123 REMARK 3 T33: 0.1983 T12: 0.0257 REMARK 3 T13: 0.0308 T23: 0.1567 REMARK 3 L TENSOR REMARK 3 L11: 2.6840 L22: 6.3546 REMARK 3 L33: 2.7954 L12: -2.1856 REMARK 3 L13: 2.1847 L23: 0.3758 REMARK 3 S TENSOR REMARK 3 S11: -0.1846 S12: -0.5213 S13: -0.4535 REMARK 3 S21: 0.2156 S22: 0.4289 S23: 0.6452 REMARK 3 S31: -0.1282 S32: -0.4401 S33: -0.2442 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 : B 40 B 51 REMARK 3 ORIGIN FOR THE GROUP (A): 7.3480 -44.2200 14.6180 REMARK 3 T TENSOR REMARK 3 T11: 0.1436 T22: 0.0487 REMARK 3 T33: 0.1174 T12: 0.0491 REMARK 3 T13: 0.0114 T23: 0.0113 REMARK 3 L TENSOR REMARK 3 L11: 0.7826 L22: 39.5555 REMARK 3 L33: 1.0675 L12: -1.7783 REMARK 3 L13: 0.9096 L23: -1.4783 REMARK 3 S TENSOR REMARK 3 S11: -0.1963 S12: -0.1281 S13: 0.1100 REMARK 3 S21: 0.1096 S22: 0.0546 S23: 0.0209 REMARK 3 S31: -0.2316 S32: -0.1507 S33: 0.1417 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 : B 52 B 67 REMARK 3 ORIGIN FOR THE GROUP (A): 12.4460 -56.6290 16.6640 REMARK 3 T TENSOR REMARK 3 T11: 0.0565 T22: 0.0427 REMARK 3 T33: 0.0917 T12: 0.0051 REMARK 3 T13: -0.0459 T23: -0.0167 REMARK 3 L TENSOR REMARK 3 L11: 2.8353 L22: 7.6242 REMARK 3 L33: 3.3223 L12: 1.5862 REMARK 3 L13: 0.3645 L23: 0.6139 REMARK 3 S TENSOR REMARK 3 S11: 0.0145 S12: -0.2205 S13: 0.0482 REMARK 3 S21: 0.2752 S22: 0.1031 S23: -0.4745 REMARK 3 S31: 0.0925 S32: 0.2106 S33: -0.1176 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 68 B 125 REMARK 3 ORIGIN FOR THE GROUP (A): 5.3810 -51.4570 19.7780 REMARK 3 T TENSOR REMARK 3 T11: 0.1202 T22: 0.0703 REMARK 3 T33: 0.0575 T12: -0.0037 REMARK 3 T13: 0.0210 T23: 0.0343 REMARK 3 L TENSOR REMARK 3 L11: 1.7520 L22: 3.5913 REMARK 3 L33: 4.1534 L12: -0.5947 REMARK 3 L13: 1.0459 L23: 1.0408 REMARK 3 S TENSOR REMARK 3 S11: -0.0337 S12: -0.2169 S13: -0.0169 REMARK 3 S21: 0.3569 S22: 0.0623 S23: 0.0526 REMARK 3 S31: -0.1861 S32: -0.2962 S33: -0.0286 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 : A 200 A 394 REMARK 3 ORIGIN FOR THE GROUP (A): -22.1660 -20.1500 2.6740 REMARK 3 T TENSOR REMARK 3 T11: 0.1139 T22: 0.1481 REMARK 3 T33: 0.1640 T12: -0.0002 REMARK 3 T13: 0.0724 T23: -0.0474 REMARK 3 L TENSOR REMARK 3 L11: 0.2203 L22: 2.1977 REMARK 3 L33: 0.5206 L12: 0.4108 REMARK 3 L13: 0.2589 L23: 0.7409 REMARK 3 S TENSOR REMARK 3 S11: 0.0030 S12: 0.0273 S13: 0.0098 REMARK 3 S21: 0.0755 S22: -0.1128 S23: 0.4242 REMARK 3 S31: 0.0254 S32: -0.1394 S33: 0.1097 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 : A 395 A 498 REMARK 3 ORIGIN FOR THE GROUP (A): 24.0620 20.3190 6.2490 REMARK 3 T TENSOR REMARK 3 T11: 0.0192 T22: 0.0162 REMARK 3 T33: 0.1147 T12: 0.0032 REMARK 3 T13: -0.0096 T23: -0.0053 REMARK 3 L TENSOR REMARK 3 L11: 2.0883 L22: 1.5989 REMARK 3 L33: 1.8724 L12: -0.7343 REMARK 3 L13: 1.5569 L23: -1.0874 REMARK 3 S TENSOR REMARK 3 S11: 0.0967 S12: 0.1625 S13: -0.1205 REMARK 3 S21: -0.0707 S22: -0.0677 S23: -0.1690 REMARK 3 S31: 0.0616 S32: 0.1058 S33: -0.0290 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 : A 499 A 734 REMARK 3 ORIGIN FOR THE GROUP (A): -0.3540 -16.5790 3.2040 REMARK 3 T TENSOR REMARK 3 T11: 0.1052 T22: 0.0253 REMARK 3 T33: 0.0990 T12: 0.0020 REMARK 3 T13: 0.0307 T23: -0.0213 REMARK 3 L TENSOR REMARK 3 L11: 0.7960 L22: 1.1528 REMARK 3 L33: 0.4155 L12: -0.0214 REMARK 3 L13: 0.3017 L23: -0.4003 REMARK 3 S TENSOR REMARK 3 S11: 0.0144 S12: 0.0076 S13: -0.0858 REMARK 3 S21: 0.0070 S22: -0.0087 S23: -0.1894 REMARK 3 S31: 0.0683 S32: 0.0055 S33: -0.0057 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 : A 735 A 922 REMARK 3 ORIGIN FOR THE GROUP (A): -7.4870 30.5220 -16.4130 REMARK 3 T TENSOR REMARK 3 T11: 0.0338 T22: 0.0357 REMARK 3 T33: 0.0334 T12: -0.0152 REMARK 3 T13: 0.0024 T23: 0.0130 REMARK 3 L TENSOR REMARK 3 L11: 1.3080 L22: 1.3143 REMARK 3 L33: 0.5751 L12: -0.4491 REMARK 3 L13: 0.3765 L23: -0.2878 REMARK 3 S TENSOR REMARK 3 S11: -0.0465 S12: 0.1450 S13: 0.1228 REMARK 3 S21: -0.0847 S22: 0.0146 S23: -0.0086 REMARK 3 S31: -0.0208 S32: 0.0064 S33: 0.0319 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 : D 1 D 16 REMARK 3 ORIGIN FOR THE GROUP (A): 6.5130 -29.9130 -13.4020 REMARK 3 T TENSOR REMARK 3 T11: 0.4534 T22: 0.2258 REMARK 3 T33: 0.3363 T12: 0.0502 REMARK 3 T13: 0.3461 T23: -0.0355 REMARK 3 L TENSOR REMARK 3 L11: 6.3242 L22: 2.3753 REMARK 3 L33: 3.8856 L12: 2.7850 REMARK 3 L13: -1.0732 L23: 1.4792 REMARK 3 S TENSOR REMARK 3 S11: 0.2211 S12: 0.2075 S13: 0.4777 REMARK 3 S21: 0.2815 S22: 0.0649 S23: 0.3246 REMARK 3 S31: -0.2117 S32: 0.0388 S33: -0.2860 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 : D 17 D 32 REMARK 3 ORIGIN FOR THE GROUP (A): 3.6100 -39.7380 -16.9740 REMARK 3 T TENSOR REMARK 3 T11: 0.1474 T22: 0.1708 REMARK 3 T33: 0.0752 T12: -0.0667 REMARK 3 T13: 0.0086 T23: 0.0805 REMARK 3 L TENSOR REMARK 3 L11: 2.4784 L22: 2.4693 REMARK 3 L33: 1.1099 L12: 1.8761 REMARK 3 L13: 0.1522 L23: 1.1868 REMARK 3 S TENSOR REMARK 3 S11: 0.1823 S12: -0.2490 S13: 0.0182 REMARK 3 S21: 0.4480 S22: -0.2931 S23: 0.1232 REMARK 3 S31: 0.3010 S32: -0.0914 S33: 0.1107 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 : D 33 D 39 REMARK 3 ORIGIN FOR THE GROUP (A): 10.5910 -30.8260 -22.0310 REMARK 3 T TENSOR REMARK 3 T11: 0.1075 T22: 0.0312 REMARK 3 T33: 0.0726 T12: 0.0328 REMARK 3 T13: 0.0145 T23: -0.0127 REMARK 3 L TENSOR REMARK 3 L11: 3.0927 L22: 7.1033 REMARK 3 L33: 4.4026 L12: -0.7106 REMARK 3 L13: 3.1294 L23: 2.1238 REMARK 3 S TENSOR REMARK 3 S11: 0.0758 S12: -0.0669 S13: -0.0088 REMARK 3 S21: 0.0861 S22: -0.0227 S23: -0.2149 REMARK 3 S31: -0.0021 S32: -0.1368 S33: -0.0531 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 : D 40 D 51 REMARK 3 ORIGIN FOR THE GROUP (A): 13.7060 -25.8760 -24.3960 REMARK 3 T TENSOR REMARK 3 T11: 0.2962 T22: 0.0596 REMARK 3 T33: 0.0451 T12: -0.0117 REMARK 3 T13: -0.0100 T23: 0.0341 REMARK 3 L TENSOR REMARK 3 L11: 4.7534 L22: 43.1659 REMARK 3 L33: 0.3663 L12: 2.6799 REMARK 3 L13: -1.0251 L23: -1.5768 REMARK 3 S TENSOR REMARK 3 S11: 0.0100 S12: 0.2545 S13: 0.3240 REMARK 3 S21: -0.5108 S22: 0.0715 S23: 0.3284 REMARK 3 S31: -0.1798 S32: -0.0413 S33: -0.0816 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 : D 52 D 60 REMARK 3 ORIGIN FOR THE GROUP (A): 14.4990 -43.4610 -22.9080 REMARK 3 T TENSOR REMARK 3 T11: 0.1009 T22: 0.0664 REMARK 3 T33: 0.0835 T12: 0.0414 REMARK 3 T13: -0.0349 T23: 0.0110 REMARK 3 L TENSOR REMARK 3 L11: 5.7701 L22: 9.2732 REMARK 3 L33: 4.0771 L12: -3.4259 REMARK 3 L13: 0.2958 L23: 2.4894 REMARK 3 S TENSOR REMARK 3 S11: -0.3366 S12: -0.4199 S13: -0.1043 REMARK 3 S21: 0.4065 S22: 0.6268 S23: -0.3460 REMARK 3 S31: 0.5369 S32: 0.1869 S33: -0.2901 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 : D 61 D 67 REMARK 3 ORIGIN FOR THE GROUP (A): 22.5900 -31.4850 -19.4330 REMARK 3 T TENSOR REMARK 3 T11: 0.0600 T22: 0.1937 REMARK 3 T33: 0.2259 T12: -0.0838 REMARK 3 T13: 0.0089 T23: -0.0532 REMARK 3 L TENSOR REMARK 3 L11: 1.9029 L22: 8.8692 REMARK 3 L33: 17.8514 L12: -3.9268 REMARK 3 L13: -3.1361 L23: 3.3552 REMARK 3 S TENSOR REMARK 3 S11: 0.0016 S12: -0.2675 S13: 0.0634 REMARK 3 S21: 0.1170 S22: 0.5058 S23: -0.0395 REMARK 3 S31: -0.5020 S32: 0.6510 S33: -0.5075 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 : D 68 D 77 REMARK 3 ORIGIN FOR THE GROUP (A): 10.4430 -41.7420 -15.6270 REMARK 3 T TENSOR REMARK 3 T11: 0.0682 T22: 0.1163 REMARK 3 T33: 0.1410 T12: -0.0436 REMARK 3 T13: 0.0232 T23: -0.0222 REMARK 3 L TENSOR REMARK 3 L11: 14.1725 L22: 9.8727 REMARK 3 L33: 3.2035 L12: 7.8134 REMARK 3 L13: -4.9011 L23: -5.2812 REMARK 3 S TENSOR REMARK 3 S11: 0.0895 S12: -0.8919 S13: -0.4441 REMARK 3 S21: -0.1026 S22: -0.3405 S23: -0.0275 REMARK 3 S31: 0.0912 S32: 0.1369 S33: 0.2509 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 : D 78 D 84 REMARK 3 ORIGIN FOR THE GROUP (A): 13.0720 -35.6660 -12.7130 REMARK 3 T TENSOR REMARK 3 T11: 0.0720 T22: 0.0565 REMARK 3 T33: 0.0810 T12: 0.0074 REMARK 3 T13: 0.0125 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 14.3813 L22: 15.2740 REMARK 3 L33: 9.6062 L12: 14.2291 REMARK 3 L13: 2.6766 L23: 2.4885 REMARK 3 S TENSOR REMARK 3 S11: 0.2699 S12: -0.1503 S13: -0.2373 REMARK 3 S21: 0.0749 S22: -0.0382 S23: -0.1305 REMARK 3 S31: 0.0169 S32: 0.1161 S33: -0.2317 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 : D 85 D 99 REMARK 3 ORIGIN FOR THE GROUP (A): 13.0890 -26.0520 -17.5680 REMARK 3 T TENSOR REMARK 3 T11: 0.2763 T22: 0.0428 REMARK 3 T33: 0.0882 T12: 0.0647 REMARK 3 T13: 0.0889 T23: 0.0395 REMARK 3 L TENSOR REMARK 3 L11: 1.5568 L22: 7.3839 REMARK 3 L33: 8.6422 L12: 0.0256 REMARK 3 L13: 3.0250 L23: 4.4276 REMARK 3 S TENSOR REMARK 3 S11: -0.1638 S12: -0.0040 S13: 0.1634 REMARK 3 S21: 0.3558 S22: 0.0409 S23: -0.2159 REMARK 3 S31: -0.3727 S32: -0.0758 S33: 0.1229 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 : D 100 D 110 REMARK 3 ORIGIN FOR THE GROUP (A): 11.2150 -37.9770 -31.4150 REMARK 3 T TENSOR REMARK 3 T11: 0.0529 T22: 0.1788 REMARK 3 T33: 0.2958 T12: 0.0044 REMARK 3 T13: -0.0251 T23: 0.1439 REMARK 3 L TENSOR REMARK 3 L11: 0.0926 L22: 5.5893 REMARK 3 L33: 7.7824 L12: -0.5739 REMARK 3 L13: 0.0316 L23: -3.1320 REMARK 3 S TENSOR REMARK 3 S11: 0.0538 S12: 0.0674 S13: -0.0353 REMARK 3 S21: -0.2917 S22: 0.0356 S23: 0.7557 REMARK 3 S31: -0.0372 S32: -0.3100 S33: -0.0894 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 : D 111 D 125 REMARK 3 ORIGIN FOR THE GROUP (A): 6.7960 -27.3880 -19.2810 REMARK 3 T TENSOR REMARK 3 T11: 0.1220 T22: 0.0944 REMARK 3 T33: 0.1458 T12: 0.0311 REMARK 3 T13: 0.0476 T23: 0.0375 REMARK 3 L TENSOR REMARK 3 L11: 4.7875 L22: 5.3649 REMARK 3 L33: 8.2896 L12: 1.0442 REMARK 3 L13: 3.4404 L23: 3.9152 REMARK 3 S TENSOR REMARK 3 S11: -0.1145 S12: -0.2362 S13: 0.4509 REMARK 3 S21: -0.0113 S22: -0.1278 S23: 0.5309 REMARK 3 S31: -0.6188 S32: -0.3931 S33: 0.2423 REMARK 3 REMARK 3 TLS GROUP : 21 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 293 C 358 REMARK 3 ORIGIN FOR THE GROUP (A): -6.7070 10.6050 -34.1240 REMARK 3 T TENSOR REMARK 3 T11: 0.1508 T22: 0.1006 REMARK 3 T33: 0.0809 T12: -0.0206 REMARK 3 T13: 0.0698 T23: -0.0141 REMARK 3 L TENSOR REMARK 3 L11: 2.9289 L22: 2.4203 REMARK 3 L33: 3.7162 L12: -0.0559 REMARK 3 L13: 1.6466 L23: 0.4153 REMARK 3 S TENSOR REMARK 3 S11: -0.0102 S12: -0.0302 S13: 0.2712 REMARK 3 S21: -0.0178 S22: -0.0518 S23: 0.1782 REMARK 3 S31: -0.0508 S32: -0.4033 S33: 0.0620 REMARK 3 REMARK 3 TLS GROUP : 22 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 359 C 394 REMARK 3 ORIGIN FOR THE GROUP (A): 0.8940 11.6730 -34.7180 REMARK 3 T TENSOR REMARK 3 T11: 0.2387 T22: 0.1376 REMARK 3 T33: 0.2854 T12: -0.0509 REMARK 3 T13: 0.0933 T23: -0.0976 REMARK 3 L TENSOR REMARK 3 L11: 0.7053 L22: 2.8365 REMARK 3 L33: 0.8296 L12: 1.1790 REMARK 3 L13: 0.7294 L23: 1.0401 REMARK 3 S TENSOR REMARK 3 S11: 0.0890 S12: -0.2132 S13: 0.2832 REMARK 3 S21: -0.0397 S22: -0.3836 S23: 0.4289 REMARK 3 S31: 0.1985 S32: -0.1856 S33: 0.2945 REMARK 3 REMARK 3 TLS GROUP : 23 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 395 C 471 REMARK 3 ORIGIN FOR THE GROUP (A): 30.9000 38.2450 -33.5900 REMARK 3 T TENSOR REMARK 3 T11: 0.0287 T22: 0.0698 REMARK 3 T33: 0.0755 T12: -0.0174 REMARK 3 T13: 0.0187 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 2.1798 L22: 1.8737 REMARK 3 L33: 2.5877 L12: -1.1009 REMARK 3 L13: 1.6714 L23: -1.2168 REMARK 3 S TENSOR REMARK 3 S11: 0.0480 S12: 0.2502 S13: -0.1334 REMARK 3 S21: -0.1865 S22: 0.0173 S23: -0.1258 REMARK 3 S31: 0.1003 S32: 0.1884 S33: -0.0653 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 472 C 529 REMARK 3 ORIGIN FOR THE GROUP (A): 22.4240 18.6630 -27.3030 REMARK 3 T TENSOR REMARK 3 T11: 0.1216 T22: 0.0314 REMARK 3 T33: 0.1410 T12: 0.0085 REMARK 3 T13: 0.0049 T23: 0.0018 REMARK 3 L TENSOR REMARK 3 L11: 0.9099 L22: 1.6744 REMARK 3 L33: 0.2007 L12: 1.0571 REMARK 3 L13: 0.1690 L23: 0.0777 REMARK 3 S TENSOR REMARK 3 S11: 0.0619 S12: 0.0498 S13: -0.2000 REMARK 3 S21: 0.0958 S22: -0.0398 S23: -0.3302 REMARK 3 S31: 0.1006 S32: 0.0633 S33: -0.0221 REMARK 3 REMARK 3 TLS GROUP : 25 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 530 C 623 REMARK 3 ORIGIN FOR THE GROUP (A): 18.1950 -3.1780 -24.8800 REMARK 3 T TENSOR REMARK 3 T11: 0.2025 T22: 0.0370 REMARK 3 T33: 0.1129 T12: 0.0005 REMARK 3 T13: 0.0161 T23: -0.0021 REMARK 3 L TENSOR REMARK 3 L11: 3.1527 L22: 3.7933 REMARK 3 L33: 1.0426 L12: 1.8372 REMARK 3 L13: 1.6172 L23: 0.4203 REMARK 3 S TENSOR REMARK 3 S11: 0.0900 S12: -0.0826 S13: -0.1816 REMARK 3 S21: 0.1732 S22: -0.0716 S23: -0.4143 REMARK 3 S31: 0.0803 S32: 0.0187 S33: -0.0184 REMARK 3 REMARK 3 TLS GROUP : 26 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 624 C 734 REMARK 3 ORIGIN FOR THE GROUP (A): -0.9320 6.3030 -50.1090 REMARK 3 T TENSOR REMARK 3 T11: 0.2045 T22: 0.0829 REMARK 3 T33: 0.0329 T12: -0.0145 REMARK 3 T13: 0.0232 T23: -0.0219 REMARK 3 L TENSOR REMARK 3 L11: 0.9726 L22: 4.5836 REMARK 3 L33: 1.2174 L12: 1.0888 REMARK 3 L13: -0.2520 L23: -2.2427 REMARK 3 S TENSOR REMARK 3 S11: 0.0109 S12: 0.0529 S13: -0.1282 REMARK 3 S21: -0.2790 S22: 0.0384 S23: 0.0012 REMARK 3 S31: 0.1966 S32: -0.0292 S33: -0.0494 REMARK 3 REMARK 3 TLS GROUP : 27 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 735 C 921 REMARK 3 ORIGIN FOR THE GROUP (A): 4.9560 47.5190 -60.2440 REMARK 3 T TENSOR REMARK 3 T11: 0.0498 T22: 0.0733 REMARK 3 T33: 0.0523 T12: -0.0003 REMARK 3 T13: 0.0001 T23: 0.0155 REMARK 3 L TENSOR REMARK 3 L11: 1.5081 L22: 1.4955 REMARK 3 L33: 0.8645 L12: -0.1998 REMARK 3 L13: 0.6567 L23: -0.3658 REMARK 3 S TENSOR REMARK 3 S11: -0.0785 S12: 0.1630 S13: 0.2282 REMARK 3 S21: -0.0354 S22: -0.0330 S23: -0.0536 REMARK 3 S31: -0.0694 S32: 0.0892 S33: 0.1114 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 REMARK 3 RIDING POSITIONS. U VALUES WITH TLS ADDED REMARK 4 REMARK 4 4AQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-12. REMARK 100 THE PDBE ID CODE IS EBI-52016. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JUN-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : BM30A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R) REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74487 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40 REMARK 200 RESOLUTION RANGE LOW (A) : 58.50 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 4.0 REMARK 200 R MERGE (I) : 0.11 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.00 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.0 REMARK 200 R MERGE FOR SHELL (I) : 0.65 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.50 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.3 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M KSCN, 0.1 M BIS-TRIS REMARK 280 PROPANE PH 6.5 AND 20% PEG 3350 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: 1940 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 39150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL 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 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 8.17480 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 88.12164 REMARK 350 BIOMT3 2 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: 1940 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 39150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL 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 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -8.17480 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -88.12164 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 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: 1890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 34490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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 APPLY THE FOLLOWING TO CHAINS: D REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 8.17480 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 88.12164 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 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: 1890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 34490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D 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 APPLY THE FOLLOWING TO CHAINS: C REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -8.17480 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -88.12164 REMARK 350 BIOMT3 2 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 31 REMARK 465 ALA A 32 REMARK 465 SER A 33 REMARK 465 PHE A 34 REMARK 465 THR A 35 REMARK 465 ASP A 36 REMARK 465 VAL A 37 REMARK 465 ALA A 38 REMARK 465 PRO A 39 REMARK 465 GLN A 40 REMARK 465 TYR A 41 REMARK 465 LYS A 42 REMARK 465 ASP A 43 REMARK 465 ALA A 44 REMARK 465 ILE A 45 REMARK 465 ASP A 46 REMARK 465 PHE A 47 REMARK 465 LEU A 48 REMARK 465 VAL A 49 REMARK 465 SER A 50 REMARK 465 THR A 51 REMARK 465 GLY A 52 REMARK 465 ALA A 53 REMARK 465 THR A 54 REMARK 465 LYS A 55 REMARK 465 GLY A 56 REMARK 465 LYS A 57 REMARK 465 THR A 58 REMARK 465 GLU A 59 REMARK 465 THR A 60 REMARK 465 LYS A 61 REMARK 465 PHE A 62 REMARK 465 GLY A 63 REMARK 465 VAL A 64 REMARK 465 TYR A 65 REMARK 465 ASP A 66 REMARK 465 GLU A 67 REMARK 465 ILE A 68 REMARK 465 THR A 69 REMARK 465 ARG A 70 REMARK 465 LEU A 71 REMARK 465 ASP A 72 REMARK 465 ALA A 73 REMARK 465 ALA A 74 REMARK 465 VAL A 75 REMARK 465 ILE A 76 REMARK 465 LEU A 77 REMARK 465 ALA A 78 REMARK 465 ARG A 79 REMARK 465 VAL A 80 REMARK 465 LEU A 81 REMARK 465 LYS A 82 REMARK 465 LEU A 83 REMARK 465 ASP A 84 REMARK 465 VAL A 85 REMARK 465 GLY A 86 REMARK 465 ASN A 87 REMARK 465 ALA A 88 REMARK 465 LYS A 89 REMARK 465 ASP A 90 REMARK 465 ALA A 91 REMARK 465 GLY A 92 REMARK 465 PHE A 93 REMARK 465 THR A 94 REMARK 465 ASP A 95 REMARK 465 VAL A 96 REMARK 465 PRO A 97 REMARK 465 LYS A 98 REMARK 465 ASP A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 LYS A 102 REMARK 465 TYR A 103 REMARK 465 VAL A 104 REMARK 465 ASN A 105 REMARK 465 ALA A 106 REMARK 465 LEU A 107 REMARK 465 VAL A 108 REMARK 465 GLU A 109 REMARK 465 ALA A 110 REMARK 465 GLY A 111 REMARK 465 VAL A 112 REMARK 465 LEU A 113 REMARK 465 ASN A 114 REMARK 465 GLY A 115 REMARK 465 LYS A 116 REMARK 465 ALA A 117 REMARK 465 PRO A 118 REMARK 465 GLY A 119 REMARK 465 LYS A 120 REMARK 465 PHE A 121 REMARK 465 GLY A 122 REMARK 465 ALA A 123 REMARK 465 TYR A 124 REMARK 465 ASP A 125 REMARK 465 PRO A 126 REMARK 465 LEU A 127 REMARK 465 THR A 128 REMARK 465 ARG A 129 REMARK 465 VAL A 130 REMARK 465 GLU A 131 REMARK 465 MET A 132 REMARK 465 ALA A 133 REMARK 465 LYS A 134 REMARK 465 ILE A 135 REMARK 465 ILE A 136 REMARK 465 ALA A 137 REMARK 465 ASN A 138 REMARK 465 ALA A 139 REMARK 465 HIS A 140 REMARK 465 LYS A 141 REMARK 465 LEU A 142 REMARK 465 LYS A 143 REMARK 465 ALA A 144 REMARK 465 ASP A 145 REMARK 465 ASP A 146 REMARK 465 VAL A 147 REMARK 465 LYS A 148 REMARK 465 LEU A 149 REMARK 465 PRO A 150 REMARK 465 PHE A 151 REMARK 465 THR A 152 REMARK 465 ASP A 153 REMARK 465 VAL A 154 REMARK 465 ASN A 155 REMARK 465 ASP A 156 REMARK 465 THR A 157 REMARK 465 TRP A 158 REMARK 465 ALA A 159 REMARK 465 PRO A 160 REMARK 465 TYR A 161 REMARK 465 VAL A 162 REMARK 465 LYS A 163 REMARK 465 ALA A 164 REMARK 465 LEU A 165 REMARK 465 TYR A 166 REMARK 465 LYS A 167 REMARK 465 TYR A 168 REMARK 465 GLU A 169 REMARK 465 VAL A 170 REMARK 465 THR A 171 REMARK 465 LYS A 172 REMARK 465 GLY A 173 REMARK 465 LYS A 174 REMARK 465 THR A 175 REMARK 465 PRO A 176 REMARK 465 THR A 177 REMARK 465 SER A 178 REMARK 465 PHE A 179 REMARK 465 GLY A 180 REMARK 465 ALA A 181 REMARK 465 TYR A 182 REMARK 465 GLN A 183 REMARK 465 ASN A 184 REMARK 465 ILE A 185 REMARK 465 THR A 186 REMARK 465 ARG A 187 REMARK 465 GLY A 188 REMARK 465 ASP A 189 REMARK 465 PHE A 190 REMARK 465 ALA A 191 REMARK 465 GLN A 192 REMARK 465 PHE A 193 REMARK 465 VAL A 194 REMARK 465 TYR A 195 REMARK 465 ARG A 196 REMARK 465 ALA A 197 REMARK 465 VAL A 198 REMARK 465 ASN A 199 REMARK 465 ILE A 200 REMARK 465 ASN A 201 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 MET C 31 REMARK 465 ALA C 32 REMARK 465 SER C 33 REMARK 465 PHE C 34 REMARK 465 THR C 35 REMARK 465 ASP C 36 REMARK 465 VAL C 37 REMARK 465 ALA C 38 REMARK 465 PRO C 39 REMARK 465 GLN C 40 REMARK 465 TYR C 41 REMARK 465 LYS C 42 REMARK 465 ASP C 43 REMARK 465 ALA C 44 REMARK 465 ILE C 45 REMARK 465 ASP C 46 REMARK 465 PHE C 47 REMARK 465 LEU C 48 REMARK 465 VAL C 49 REMARK 465 SER C 50 REMARK 465 THR C 51 REMARK 465 GLY C 52 REMARK 465 ALA C 53 REMARK 465 THR C 54 REMARK 465 LYS C 55 REMARK 465 GLY C 56 REMARK 465 LYS C 57 REMARK 465 THR C 58 REMARK 465 GLU C 59 REMARK 465 THR C 60 REMARK 465 LYS C 61 REMARK 465 PHE C 62 REMARK 465 GLY C 63 REMARK 465 VAL C 64 REMARK 465 TYR C 65 REMARK 465 ASP C 66 REMARK 465 GLU C 67 REMARK 465 ILE C 68 REMARK 465 THR C 69 REMARK 465 ARG C 70 REMARK 465 LEU C 71 REMARK 465 ASP C 72 REMARK 465 ALA C 73 REMARK 465 ALA C 74 REMARK 465 VAL C 75 REMARK 465 ILE C 76 REMARK 465 LEU C 77 REMARK 465 ALA C 78 REMARK 465 ARG C 79 REMARK 465 VAL C 80 REMARK 465 LEU C 81 REMARK 465 LYS C 82 REMARK 465 LEU C 83 REMARK 465 ASP C 84 REMARK 465 VAL C 85 REMARK 465 GLY C 86 REMARK 465 ASN C 87 REMARK 465 ALA C 88 REMARK 465 LYS C 89 REMARK 465 ASP C 90 REMARK 465 ALA C 91 REMARK 465 GLY C 92 REMARK 465 PHE C 93 REMARK 465 THR C 94 REMARK 465 ASP C 95 REMARK 465 VAL C 96 REMARK 465 PRO C 97 REMARK 465 LYS C 98 REMARK 465 ASP C 99 REMARK 465 ARG C 100 REMARK 465 ALA C 101 REMARK 465 LYS C 102 REMARK 465 TYR C 103 REMARK 465 VAL C 104 REMARK 465 ASN C 105 REMARK 465 ALA C 106 REMARK 465 LEU C 107 REMARK 465 VAL C 108 REMARK 465 GLU C 109 REMARK 465 ALA C 110 REMARK 465 GLY C 111 REMARK 465 VAL C 112 REMARK 465 LEU C 113 REMARK 465 ASN C 114 REMARK 465 GLY C 115 REMARK 465 LYS C 116 REMARK 465 ALA C 117 REMARK 465 PRO C 118 REMARK 465 GLY C 119 REMARK 465 LYS C 120 REMARK 465 PHE C 121 REMARK 465 GLY C 122 REMARK 465 ALA C 123 REMARK 465 TYR C 124 REMARK 465 ASP C 125 REMARK 465 PRO C 126 REMARK 465 LEU C 127 REMARK 465 THR C 128 REMARK 465 ARG C 129 REMARK 465 VAL C 130 REMARK 465 GLU C 131 REMARK 465 MET C 132 REMARK 465 ALA C 133 REMARK 465 LYS C 134 REMARK 465 ILE C 135 REMARK 465 ILE C 136 REMARK 465 ALA C 137 REMARK 465 ASN C 138 REMARK 465 ALA C 139 REMARK 465 HIS C 140 REMARK 465 LYS C 141 REMARK 465 LEU C 142 REMARK 465 LYS C 143 REMARK 465 ALA C 144 REMARK 465 ASP C 145 REMARK 465 ASP C 146 REMARK 465 VAL C 147 REMARK 465 LYS C 148 REMARK 465 LEU C 149 REMARK 465 PRO C 150 REMARK 465 PHE C 151 REMARK 465 THR C 152 REMARK 465 ASP C 153 REMARK 465 VAL C 154 REMARK 465 ASN C 155 REMARK 465 ASP C 156 REMARK 465 THR C 157 REMARK 465 TRP C 158 REMARK 465 ALA C 159 REMARK 465 PRO C 160 REMARK 465 TYR C 161 REMARK 465 VAL C 162 REMARK 465 LYS C 163 REMARK 465 ALA C 164 REMARK 465 LEU C 165 REMARK 465 TYR C 166 REMARK 465 LYS C 167 REMARK 465 TYR C 168 REMARK 465 GLU C 169 REMARK 465 VAL C 170 REMARK 465 THR C 171 REMARK 465 LYS C 172 REMARK 465 GLY C 173 REMARK 465 LYS C 174 REMARK 465 THR C 175 REMARK 465 PRO C 176 REMARK 465 THR C 177 REMARK 465 SER C 178 REMARK 465 PHE C 179 REMARK 465 GLY C 180 REMARK 465 ALA C 181 REMARK 465 TYR C 182 REMARK 465 GLN C 183 REMARK 465 ASN C 184 REMARK 465 ILE C 185 REMARK 465 THR C 186 REMARK 465 ARG C 187 REMARK 465 GLY C 188 REMARK 465 ASP C 189 REMARK 465 PHE C 190 REMARK 465 ALA C 191 REMARK 465 GLN C 192 REMARK 465 PHE C 193 REMARK 465 VAL C 194 REMARK 465 TYR C 195 REMARK 465 ARG C 196 REMARK 465 ALA C 197 REMARK 465 VAL C 198 REMARK 465 ASN C 199 REMARK 465 ILE C 200 REMARK 465 ASN C 201 REMARK 465 ALA C 202 REMARK 465 VAL C 203 REMARK 465 PRO C 204 REMARK 465 GLU C 205 REMARK 465 ILE C 206 REMARK 465 VAL C 207 REMARK 465 GLU C 208 REMARK 465 VAL C 209 REMARK 465 THR C 210 REMARK 465 ALA C 211 REMARK 465 VAL C 212 REMARK 465 ASN C 213 REMARK 465 SER C 214 REMARK 465 THR C 215 REMARK 465 THR C 216 REMARK 465 VAL C 217 REMARK 465 LYS C 218 REMARK 465 VAL C 219 REMARK 465 THR C 220 REMARK 465 PHE C 221 REMARK 465 ASN C 222 REMARK 465 THR C 223 REMARK 465 GLN C 224 REMARK 465 ILE C 225 REMARK 465 ALA C 226 REMARK 465 ASP C 227 REMARK 465 VAL C 228 REMARK 465 ASP C 229 REMARK 465 PHE C 230 REMARK 465 THR C 231 REMARK 465 ASN C 232 REMARK 465 PHE C 233 REMARK 465 ALA C 234 REMARK 465 ILE C 235 REMARK 465 ASP C 236 REMARK 465 ASN C 237 REMARK 465 GLY C 238 REMARK 465 LEU C 239 REMARK 465 THR C 240 REMARK 465 VAL C 241 REMARK 465 THR C 242 REMARK 465 LYS C 243 REMARK 465 ALA C 244 REMARK 465 THR C 245 REMARK 465 LEU C 246 REMARK 465 SER C 247 REMARK 465 ARG C 248 REMARK 465 ASP C 249 REMARK 465 LYS C 250 REMARK 465 LYS C 251 REMARK 465 SER C 252 REMARK 465 VAL C 253 REMARK 465 GLU C 254 REMARK 465 VAL C 255 REMARK 465 VAL C 256 REMARK 465 VAL C 257 REMARK 465 ASN C 258 REMARK 465 LYS C 259 REMARK 465 PRO C 260 REMARK 465 PHE C 261 REMARK 465 THR C 262 REMARK 465 ARG C 263 REMARK 465 ASN C 264 REMARK 465 GLN C 265 REMARK 465 GLU C 266 REMARK 465 TYR C 267 REMARK 465 THR C 268 REMARK 465 ILE C 269 REMARK 465 THR C 270 REMARK 465 ALA C 271 REMARK 465 THR C 272 REMARK 465 GLY C 273 REMARK 465 ILE C 274 REMARK 465 LYS C 275 REMARK 465 ASN C 276 REMARK 465 LEU C 277 REMARK 465 LYS C 278 REMARK 465 GLY C 279 REMARK 465 GLU C 280 REMARK 465 THR C 281 REMARK 465 ALA C 282 REMARK 465 LYS C 283 REMARK 465 GLU C 284 REMARK 465 LEU C 285 REMARK 465 THR C 286 REMARK 465 GLY C 287 REMARK 465 LYS C 288 REMARK 465 PHE C 289 REMARK 465 VAL C 290 REMARK 465 TRP C 291 REMARK 465 SER C 292 REMARK 465 VAL C 293 REMARK 465 GLN C 294 REMARK 465 SER C 922 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 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 GLU A 205 CG CD OE1 OE2 REMARK 480 GLU A 208 CG CD OE1 OE2 REMARK 480 ASN A 222 CG OD1 ND2 REMARK 480 LEU A 246 CG CD1 CD2 REMARK 480 ARG A 248 CG CD NE CZ NH1 NH2 REMARK 480 LYS A 250 CE NZ REMARK 480 LYS A 251 CB CG CD CE NZ REMARK 480 LYS A 259 CD CE NZ REMARK 480 ILE A 269 CD1 REMARK 480 LYS A 275 CD CE NZ REMARK 480 LEU A 277 CG CD1 CD2 REMARK 480 LYS A 278 CE NZ REMARK 480 GLU A 280 CB CG CD OE1 OE2 REMARK 480 LYS A 283 CB CG CD CE NZ REMARK 480 GLN A 294 CB CG CD OE1 NE2 REMARK 480 LYS A 322 CD CE NZ REMARK 480 VAL A 386 CG1 CG2 REMARK 480 GLN A 389 CG CD OE1 NE2 REMARK 480 GLU A 415 CD OE1 OE2 REMARK 480 LYS A 446 CE NZ REMARK 480 LYS A 486 CD CE NZ REMARK 480 LYS A 499 CD CE NZ REMARK 480 LYS A 546 CD CE NZ REMARK 480 LYS A 593 NZ REMARK 480 ASN A 621 OD1 ND2 REMARK 480 LYS A 626 CE NZ REMARK 480 LYS B 101 CE NZ REMARK 480 LYS C 322 CG CD CE NZ REMARK 480 VAL C 386 CB CG1 CG2 REMARK 480 VAL C 388 CB CG1 CG2 REMARK 480 GLN C 389 CG CD OE1 NE2 REMARK 480 LYS C 446 CD CE NZ REMARK 480 LYS C 486 CD CE NZ REMARK 480 LYS C 546 CE NZ REMARK 480 LYS C 626 CG CD CE NZ REMARK 480 LYS D 76 CD CE NZ REMARK 480 LYS D 101 CD CE NZ REMARK 480 SER D 124 OG 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 OE1 GLN B 3 OG SER C 756 2546 2.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 LYS A 275 CG LYS A 275 CD -0.232 REMARK 500 GLU A 280 CA GLU A 280 CB -0.236 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 204 115.50 -21.55 REMARK 500 ALA A 211 95.64 -62.24 REMARK 500 LYS A 243 148.86 -171.37 REMARK 500 LYS A 250 16.67 24.88 REMARK 500 LEU A 277 -74.44 -5.69 REMARK 500 LYS A 278 28.34 -153.10 REMARK 500 ASP A 371 0.21 -66.84 REMARK 500 ASP A 447 -11.95 66.58 REMARK 500 LYS A 499 153.07 -48.64 REMARK 500 VAL A 528 -76.47 -106.74 REMARK 500 ASP A 592 12.30 58.42 REMARK 500 ASN A 794 43.17 -148.27 REMARK 500 ASP A 795 17.72 55.89 REMARK 500 TYR A 799 -125.41 -109.21 REMARK 500 VAL A 867 149.09 -171.11 REMARK 500 VAL B 48 -62.02 -102.11 REMARK 500 ASN B 103 40.33 -147.43 REMARK 500 SER B 123 -169.48 -69.40 REMARK 500 VAL C 528 -76.57 -109.59 REMARK 500 ASN C 566 34.95 73.87 REMARK 500 ASP C 592 14.40 59.59 REMARK 500 ASN C 704 54.76 -93.47 REMARK 500 TYR C 799 -120.13 -110.66 REMARK 500 VAL C 867 140.18 175.84 REMARK 500 THR C 880 -60.65 -92.33 REMARK 500 ALA C 885 149.09 -172.99 REMARK 500 ALA C 900 -153.80 -96.50 REMARK 500 VAL D 48 -60.60 -101.39 REMARK 500 SER D 63 -4.92 69.94 REMARK 500 ASN D 103 33.43 -145.74 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 A1923 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLN A 406 O REMARK 620 2 GLN A 406 OE1 87.9 REMARK 620 3 ASP A 779 OD2 78.0 86.8 REMARK 620 4 THR A 440 O 79.7 167.4 92.8 REMARK 620 5 ASP A 779 OD1 126.5 100.2 50.2 89.2 REMARK 620 6 ASP A 781 OD2 152.1 99.0 129.0 91.0 79.1 REMARK 620 7 HOH A2063 O 75.9 75.8 149.0 98.7 157.4 79.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1924 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 654 OD1 REMARK 620 2 HOH A2153 O 135.5 REMARK 620 3 HOH A2154 O 62.9 74.4 REMARK 620 4 SER A 651 O 78.0 94.4 94.8 REMARK 620 5 ALA A 646 O 97.2 87.3 80.5 174.4 REMARK 620 6 THR A 649 O 140.6 78.1 151.5 79.8 105.8 REMARK 620 7 THR A 649 OG1 75.8 148.4 132.9 97.8 83.4 75.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1925 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 835 OD1 REMARK 620 2 GLU A 836 OE1 94.7 REMARK 620 3 ASN A 824 OD1 173.4 78.8 REMARK 620 4 GLU A 784 OE2 93.3 167.1 92.8 REMARK 620 5 GLY A 822 O 85.1 94.7 94.0 76.0 REMARK 620 6 GLU A 837 OE1 80.2 101.7 102.4 89.5 158.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1926 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 517 OD1 REMARK 620 2 ASP A 517 OD2 45.9 REMARK 620 3 GLU A 518 OE2 98.3 78.6 REMARK 620 4 ASP A 592 OD1 121.9 79.5 86.1 REMARK 620 5 ASN A 624 OD1 76.8 95.9 174.3 94.1 REMARK 620 6 VAL A 625 O 71.1 113.1 93.0 167.0 88.0 REMARK 620 7 HOH A2125 O 155.4 157.5 97.0 78.2 88.6 89.0 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C1922 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 835 OD1 REMARK 620 2 GLU C 836 OE1 89.4 REMARK 620 3 GLU C 837 OE1 84.2 103.4 REMARK 620 4 GLU C 784 OE2 97.6 172.8 79.2 REMARK 620 5 GLY C 822 O 92.6 89.4 166.8 88.6 REMARK 620 6 ASN C 824 OD1 172.1 87.1 89.8 86.2 94.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C1923 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLN C 406 OE1 REMARK 620 2 ASP C 779 OD2 87.7 REMARK 620 3 ASP C 781 OD2 100.0 126.3 REMARK 620 4 GLN C 406 O 82.8 81.2 152.2 REMARK 620 5 HOH C2028 O 79.4 151.7 81.0 72.3 REMARK 620 6 ASP C 779 OD1 105.4 50.6 76.5 129.8 157.5 REMARK 620 7 THR C 440 O 168.6 95.3 87.2 86.8 93.1 84.8 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C1924 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA C 646 O REMARK 620 2 ASP C 654 OD1 101.1 REMARK 620 3 HOH C2092 O 83.9 63.7 REMARK 620 4 THR C 649 OG1 85.6 75.5 134.8 REMARK 620 5 SER C 651 O 172.1 73.9 88.3 98.8 REMARK 620 6 HOH C2093 O 87.5 132.2 70.9 152.2 91.5 REMARK 620 7 THR C 649 O 103.7 140.0 149.6 75.6 83.8 80.0 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C1925 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 517 OD1 REMARK 620 2 ASP C 517 OD2 44.9 REMARK 620 3 GLU C 518 OE2 100.8 95.2 REMARK 620 4 ASP C 592 OD1 121.4 79.2 100.1 REMARK 620 5 ASN C 624 OD1 74.8 81.7 175.6 82.5 REMARK 620 6 VAL C 625 O 73.0 117.6 89.0 160.4 89.7 REMARK 620 7 HOH C2072 O 151.4 160.3 90.7 81.4 93.2 81.2 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1923 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1924 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1925 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1926 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C1922 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C1923 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C1924 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C1925 REMARK 999 REMARK 999 SEQUENCE REMARK 999 CHAINS B, D RESIDUES 125-130 IS HEXA-HIS EXPRESSION TAG.