REMARK 2 REMARK 2 RESOLUTION. 2.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1334) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 27838 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1390 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 34.8486 - 6.0659 0.97 2781 151 0.2047 0.2214 REMARK 3 2 6.0659 - 4.8187 0.98 2686 139 0.1664 0.1900 REMARK 3 3 4.8187 - 4.2108 0.98 2639 141 0.1394 0.1530 REMARK 3 4 4.2108 - 3.8263 0.99 2621 140 0.1710 0.2353 REMARK 3 5 3.8263 - 3.5524 0.99 2641 134 0.1870 0.2288 REMARK 3 6 3.5524 - 3.3431 0.99 2647 135 0.2127 0.2514 REMARK 3 7 3.3431 - 3.1758 0.99 2601 136 0.2279 0.3037 REMARK 3 8 3.1758 - 3.0376 0.99 2626 143 0.2565 0.3333 REMARK 3 9 3.0376 - 2.9207 0.99 2591 134 0.2851 0.3668 REMARK 3 10 2.9207 - 2.8200 0.99 2615 137 0.2997 0.3331 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.860 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 6397 REMARK 3 ANGLE : 1.027 8674 REMARK 3 CHIRALITY : 0.064 995 REMARK 3 PLANARITY : 0.014 1091 REMARK 3 DIHEDRAL : 12.992 2366 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'G' and (resid 44 through 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.4051 34.3372 4.3199 REMARK 3 T TENSOR REMARK 3 T11: 0.5468 T22: 0.4964 REMARK 3 T33: 0.6319 T12: 0.1808 REMARK 3 T13: -0.0586 T23: -0.0110 REMARK 3 L TENSOR REMARK 3 L11: 1.2378 L22: 1.8841 REMARK 3 L33: 1.9362 L12: 1.0613 REMARK 3 L13: -0.2704 L23: 0.9510 REMARK 3 S TENSOR REMARK 3 S11: -0.0617 S12: -0.1458 S13: 0.2724 REMARK 3 S21: 0.1393 S22: 0.1959 S23: 0.0426 REMARK 3 S31: -0.1314 S32: 0.1784 S33: -0.1068 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'G' and (resid 99 through 258 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.7356 27.7803 4.4416 REMARK 3 T TENSOR REMARK 3 T11: 0.3339 T22: 0.3812 REMARK 3 T33: 0.4423 T12: -0.0332 REMARK 3 T13: 0.0358 T23: 0.0211 REMARK 3 L TENSOR REMARK 3 L11: 4.2583 L22: 1.1428 REMARK 3 L33: 3.3837 L12: -0.9094 REMARK 3 L13: 0.1804 L23: 0.4721 REMARK 3 S TENSOR REMARK 3 S11: -0.2059 S12: -0.1870 S13: -0.1876 REMARK 3 S21: 0.3280 S22: 0.0353 S23: 0.0968 REMARK 3 S31: 0.0971 S32: -0.3150 S33: 0.1157 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'G' and (resid 259 through 442 ) REMARK 3 ORIGIN FOR THE GROUP (A): 73.7656 32.5316 2.4748 REMARK 3 T TENSOR REMARK 3 T11: 0.3461 T22: 0.3479 REMARK 3 T33: 0.4673 T12: -0.0989 REMARK 3 T13: -0.0218 T23: 0.0499 REMARK 3 L TENSOR REMARK 3 L11: 3.4538 L22: 2.2153 REMARK 3 L33: 4.1661 L12: -0.9878 REMARK 3 L13: 0.1346 L23: 0.8473 REMARK 3 S TENSOR REMARK 3 S11: -0.1313 S12: -0.0297 S13: 0.3181 REMARK 3 S21: -0.0077 S22: 0.0679 S23: 0.0085 REMARK 3 S31: -0.1843 S32: 0.3194 S33: 0.0527 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain 'G' and (resid 443 through 492 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.6914 34.7718 11.0814 REMARK 3 T TENSOR REMARK 3 T11: 0.4335 T22: 0.2889 REMARK 3 T33: 0.4175 T12: 0.0095 REMARK 3 T13: -0.0266 T23: -0.1109 REMARK 3 L TENSOR REMARK 3 L11: 3.1224 L22: 1.9418 REMARK 3 L33: 1.9243 L12: 0.6671 REMARK 3 L13: -0.5403 L23: -1.0192 REMARK 3 S TENSOR REMARK 3 S11: -0.1089 S12: -0.4612 S13: 0.3730 REMARK 3 S21: -0.0167 S22: -0.0257 S23: 0.2236 REMARK 3 S31: -0.2071 S32: -0.0617 S33: 0.1801 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain 'L' and (resid 3 through 24 ) REMARK 3 ORIGIN FOR THE GROUP (A): 74.3005 33.0765 50.8732 REMARK 3 T TENSOR REMARK 3 T11: 0.9643 T22: 1.0654 REMARK 3 T33: 0.5684 T12: 0.4639 REMARK 3 T13: -0.0302 T23: -0.3227 REMARK 3 L TENSOR REMARK 3 L11: 4.4998 L22: 2.3700 REMARK 3 L33: 0.0961 L12: 2.0763 REMARK 3 L13: -0.6453 L23: -0.3061 REMARK 3 S TENSOR REMARK 3 S11: 0.0356 S12: -1.7448 S13: 0.1714 REMARK 3 S21: 1.5316 S22: -0.2716 S23: 0.6143 REMARK 3 S31: -1.3991 S32: -0.1696 S33: -0.0551 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain 'L' and (resid 25 through 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.9056 28.5612 44.1876 REMARK 3 T TENSOR REMARK 3 T11: 0.8089 T22: 1.3898 REMARK 3 T33: 0.5882 T12: 0.4332 REMARK 3 T13: 0.0330 T23: -0.0710 REMARK 3 L TENSOR REMARK 3 L11: 2.2033 L22: 0.6006 REMARK 3 L33: 2.3427 L12: -0.1909 REMARK 3 L13: 0.2554 L23: 1.1798 REMARK 3 S TENSOR REMARK 3 S11: -0.5305 S12: -1.5871 S13: 0.3932 REMARK 3 S21: 0.7123 S22: 0.5029 S23: 0.5134 REMARK 3 S31: -0.3048 S32: -1.0408 S33: 0.1007 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain 'L' and (resid 89 through 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 78.2619 25.9579 53.4416 REMARK 3 T TENSOR REMARK 3 T11: 0.6808 T22: 1.6002 REMARK 3 T33: 0.2572 T12: 0.3359 REMARK 3 T13: 0.0619 T23: -0.0904 REMARK 3 L TENSOR REMARK 3 L11: 0.3194 L22: 0.5802 REMARK 3 L33: 1.5515 L12: 0.6081 REMARK 3 L13: 0.8305 L23: 0.8888 REMARK 3 S TENSOR REMARK 3 S11: -0.3962 S12: -1.2548 S13: 0.3492 REMARK 3 S21: 0.3363 S22: 0.2329 S23: 0.3683 REMARK 3 S31: -0.6438 S32: -0.3716 S33: -0.5878 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain 'L' and (resid 110 through 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): 100.4158 16.9574 64.5702 REMARK 3 T TENSOR REMARK 3 T11: 0.7301 T22: 0.6790 REMARK 3 T33: 0.5275 T12: 0.0750 REMARK 3 T13: -0.1446 T23: 0.0664 REMARK 3 L TENSOR REMARK 3 L11: 3.5877 L22: 2.8262 REMARK 3 L33: 4.2336 L12: 0.3209 REMARK 3 L13: 0.1956 L23: 0.6103 REMARK 3 S TENSOR REMARK 3 S11: 0.0486 S12: -0.1707 S13: -0.0277 REMARK 3 S21: 0.4375 S22: -0.0477 S23: -0.3020 REMARK 3 S31: -0.3229 S32: -0.4176 S33: 0.0459 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain 'H' and (resid 2 through 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 77.6094 18.8465 26.6614 REMARK 3 T TENSOR REMARK 3 T11: 0.3159 T22: 0.5648 REMARK 3 T33: 0.3507 T12: 0.0125 REMARK 3 T13: 0.0139 T23: 0.0247 REMARK 3 L TENSOR REMARK 3 L11: 2.5524 L22: 4.0473 REMARK 3 L33: 4.5726 L12: -1.9474 REMARK 3 L13: 0.5021 L23: -0.0001 REMARK 3 S TENSOR REMARK 3 S11: -0.1177 S12: -0.4291 S13: -0.0668 REMARK 3 S21: 0.1963 S22: 0.0336 S23: 0.1492 REMARK 3 S31: 0.1203 S32: -0.2486 S33: 0.0904 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain 'H' and (resid 116 through 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.7924 5.9433 55.8214 REMARK 3 T TENSOR REMARK 3 T11: 0.6853 T22: 0.5428 REMARK 3 T33: 0.5680 T12: 0.0275 REMARK 3 T13: -0.1600 T23: -0.0436 REMARK 3 L TENSOR REMARK 3 L11: 1.8155 L22: 2.4777 REMARK 3 L33: 8.1559 L12: 0.5233 REMARK 3 L13: 0.9429 L23: -1.5796 REMARK 3 S TENSOR REMARK 3 S11: -0.2121 S12: -0.0478 S13: -0.3144 REMARK 3 S21: 0.3740 S22: -0.6210 S23: -0.0790 REMARK 3 S31: 0.4197 S32: 0.4376 S33: 0.7592 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain 'H' and (resid 150 through 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 94.3759 2.3307 56.9820 REMARK 3 T TENSOR REMARK 3 T11: 0.6655 T22: 0.5820 REMARK 3 T33: 0.6407 T12: -0.0159 REMARK 3 T13: -0.1211 T23: 0.0337 REMARK 3 L TENSOR REMARK 3 L11: 2.7284 L22: 1.7942 REMARK 3 L33: 2.6439 L12: -0.9187 REMARK 3 L13: -0.2870 L23: 0.1821 REMARK 3 S TENSOR REMARK 3 S11: 0.1474 S12: 0.0414 S13: -0.3770 REMARK 3 S21: -0.1691 S22: -0.2148 S23: -0.0202 REMARK 3 S31: 0.6843 S32: -0.2667 S33: 0.0993 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4JKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-13. REMARK 100 THE RCSB ID CODE IS RCSB078167. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-MAR-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE REMARK 200 CRYSTAL 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 : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27846 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.820 REMARK 200 RESOLUTION RANGE LOW (A) : 34.850 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 999999.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (V/V) ISOPROPANOL, 10% (W/V) REMARK 280 POLYETHYLENE GLYCOL 10,000 KD, 0.1 M CITRATE , PH 5.0, VAPOR REMARK 280 DIFFUSION, SITTING 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 34.66500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.11000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.24500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.11000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.66500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.24500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: 11390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 35100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 52.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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 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 GLY G 318 REMARK 465 GLY G 319 REMARK 465 SER G 320 REMARK 465 GLY G 321 REMARK 465 SER G 322 REMARK 465 GLY G 323 REMARK 465 GLY G 324 REMARK 465 GLY G 403 REMARK 465 ASN G 404 REMARK 465 GLU G 405 REMARK 465 THR G 406 REMARK 465 MET G 407 REMARK 465 LYS G 408 REMARK 465 GLY G 493 REMARK 465 SER G 494 REMARK 465 HIS G 495 REMARK 465 HIS G 496 REMARK 465 HIS G 497 REMARK 465 HIS G 498 REMARK 465 HIS G 499 REMARK 465 HIS G 500 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 SER H 219 REMARK 465 CYS H 220 REMARK 465 ASP H 221 REMARK 465 GLU L 1 REMARK 465 ILE L 2 REMARK 465 CYS L 210 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 ND2 ASN L 70 C2 NAG L 501 2.03 REMARK 500 OD2 ASP H 103 O HOH H 312 2.03 REMARK 500 SG CYS G 395 CB CYS G 410 2.05 REMARK 500 NZ LYS G 207 O4 MAN G 610 2.09 REMARK 500 NZ LYS G 97 OD2 ASP H 99C 2.15 REMARK 500 SG CYS H 144 CB CYS H 200 2.18 REMARK 500 ND2 ASN G 276 C2 NAG G 601 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 LEU G 122 CA - CB - CG ANGL. DEV. = 16.8 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 G 94 88.86 -158.86 REMARK 500 ASN G 241 66.00 -118.47 REMARK 500 GLN G 258 -55.02 60.59 REMARK 500 GLU G 268 -90.96 -117.23 REMARK 500 PHE G 391 52.38 -118.44 REMARK 500 ASN G 411 8.54 -153.43 REMARK 500 ASN G 462 -138.74 55.84 REMARK 500 THR G 463 168.61 59.84 REMARK 500 SER H 75 18.58 -143.27 REMARK 500 PHE H 104 92.18 -57.95 REMARK 500 SER H 131 -152.95 -133.18 REMARK 500 ASP H 148 65.06 60.33 REMARK 500 SER H 191 45.33 -89.05 REMARK 500 SER H 192 -6.66 -154.64 REMARK 500 THR H 195 -73.53 -110.11 REMARK 500 SER L 26 -8.14 -140.47 REMARK 500 SER L 30 110.50 -11.50 REMARK 500 PRO L 38 107.91 -44.08 REMARK 500 TYR L 89 -120.38 57.22 REMARK 500 ASN L 134 76.53 46.35 REMARK 500 PRO L 137 -168.84 -74.81 REMARK 500 LYS L 186 -55.06 -121.06 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 NAG G 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA G 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN G 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN G 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN G 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 608 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA G 609 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN G 610 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN G 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 612 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 613 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA G 614 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 615 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 616 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 617 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 501