REMARK 2 REMARK 2 RESOLUTION. 2.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) 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) : 2.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 47511 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.192 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 2409 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 49.3888 - 5.7838 0.99 2894 157 0.2013 0.2112 REMARK 3 2 5.7838 - 4.5918 1.00 2782 143 0.1626 0.1794 REMARK 3 3 4.5918 - 4.0117 1.00 2742 137 0.1483 0.1755 REMARK 3 4 4.0117 - 3.6450 1.00 2706 135 0.1628 0.2064 REMARK 3 5 3.6450 - 3.3838 1.00 2681 149 0.1923 0.1994 REMARK 3 6 3.3838 - 3.1844 1.00 2703 151 0.1988 0.2453 REMARK 3 7 3.1844 - 3.0249 1.00 2676 147 0.2011 0.2690 REMARK 3 8 3.0249 - 2.8933 1.00 2667 142 0.2004 0.2532 REMARK 3 9 2.8933 - 2.7819 1.00 2692 116 0.2108 0.2385 REMARK 3 10 2.7819 - 2.6859 1.00 2679 148 0.2107 0.2665 REMARK 3 11 2.6859 - 2.6019 1.00 2644 142 0.2232 0.2947 REMARK 3 12 2.6019 - 2.5275 1.00 2663 147 0.2261 0.2981 REMARK 3 13 2.5275 - 2.4610 0.99 2626 155 0.2291 0.2863 REMARK 3 14 2.4610 - 2.4010 0.98 2613 129 0.2519 0.3160 REMARK 3 15 2.4010 - 2.3464 0.98 2580 161 0.2413 0.3094 REMARK 3 16 2.3464 - 2.2965 0.94 2472 139 0.2474 0.2855 REMARK 3 17 2.2965 - 2.2505 0.86 2282 111 0.2605 0.3110 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.00 REMARK 3 SHRINKAGE RADIUS : 0.89 REMARK 3 K_SOL : 0.35 REMARK 3 B_SOL : 34.72 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.630 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.710 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 39.25 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.43 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 9.71070 REMARK 3 B22 (A**2) : -5.55230 REMARK 3 B33 (A**2) : -4.15840 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : -0.00000 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 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 : 0.008 6307 REMARK 3 ANGLE : 0.863 8557 REMARK 3 CHIRALITY : 0.052 973 REMARK 3 PLANARITY : 0.003 1083 REMARK 3 DIHEDRAL : 13.269 2299 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN G AND (RESID 44:252 OR RESID 474:492 ) ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6309 -1.2791 48.0990 REMARK 3 T TENSOR REMARK 3 T11: 0.1297 T22: 0.2289 REMARK 3 T33: 0.3244 T12: 0.0093 REMARK 3 T13: -0.0484 T23: 0.0262 REMARK 3 L TENSOR REMARK 3 L11: 1.3732 L22: 1.6835 REMARK 3 L33: 1.9767 L12: 0.1771 REMARK 3 L13: -0.6856 L23: -0.0091 REMARK 3 S TENSOR REMARK 3 S11: -0.0252 S12: 0.0727 S13: -0.1330 REMARK 3 S21: -0.1064 S22: -0.0845 S23: -0.1505 REMARK 3 S31: 0.0873 S32: 0.0774 S33: 0.0772 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN G AND RESID 253:473 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.9026 21.4474 50.4728 REMARK 3 T TENSOR REMARK 3 T11: 0.1593 T22: 0.2118 REMARK 3 T33: 0.3561 T12: -0.0341 REMARK 3 T13: -0.0354 T23: 0.0263 REMARK 3 L TENSOR REMARK 3 L11: 1.8104 L22: 1.5139 REMARK 3 L33: 2.4410 L12: -0.4155 REMARK 3 L13: -0.5801 L23: -0.2108 REMARK 3 S TENSOR REMARK 3 S11: 0.0629 S12: -0.0033 S13: 0.2078 REMARK 3 S21: 0.0187 S22: -0.0964 S23: -0.4247 REMARK 3 S31: -0.3390 S32: 0.3227 S33: -0.0476 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN H AND RESID 1:118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.2549 27.2343 28.3522 REMARK 3 T TENSOR REMARK 3 T11: 0.4019 T22: 0.2291 REMARK 3 T33: 0.1975 T12: 0.0516 REMARK 3 T13: -0.0448 T23: -0.0307 REMARK 3 L TENSOR REMARK 3 L11: 2.0381 L22: 2.3341 REMARK 3 L33: 1.9778 L12: -1.4307 REMARK 3 L13: 0.8013 L23: -0.8069 REMARK 3 S TENSOR REMARK 3 S11: 0.1083 S12: 0.1613 S13: 0.0076 REMARK 3 S21: -0.7149 S22: -0.2125 S23: 0.0655 REMARK 3 S31: -0.0235 S32: -0.1772 S33: 0.0694 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN H AND RESID 119:215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.5706 42.0849 0.7513 REMARK 3 T TENSOR REMARK 3 T11: 0.7835 T22: 0.3444 REMARK 3 T33: 0.4170 T12: -0.0660 REMARK 3 T13: -0.1424 T23: 0.0707 REMARK 3 L TENSOR REMARK 3 L11: 3.3102 L22: 2.5217 REMARK 3 L33: 2.8409 L12: 0.1810 REMARK 3 L13: 0.9495 L23: 0.9905 REMARK 3 S TENSOR REMARK 3 S11: -0.2075 S12: 0.3355 S13: -0.1519 REMARK 3 S21: -0.2356 S22: 0.1739 S23: 0.3820 REMARK 3 S31: 0.2805 S32: -0.1758 S33: 0.0009 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN L AND RESID 1:108 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8531 17.1187 9.8956 REMARK 3 T TENSOR REMARK 3 T11: 1.1273 T22: 0.5471 REMARK 3 T33: 0.2252 T12: 0.4455 REMARK 3 T13: 0.0719 T23: -0.0233 REMARK 3 L TENSOR REMARK 3 L11: 0.0700 L22: 0.6488 REMARK 3 L33: 0.6742 L12: -0.1384 REMARK 3 L13: -0.1958 L23: 0.1693 REMARK 3 S TENSOR REMARK 3 S11: 0.2115 S12: 0.2933 S13: -0.0346 REMARK 3 S21: -0.7277 S22: -0.2606 S23: 0.0459 REMARK 3 S31: 0.2498 S32: 0.1816 S33: -0.2641 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN L AND RESID 109:212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.9273 45.6784 -7.1408 REMARK 3 T TENSOR REMARK 3 T11: 0.8051 T22: 0.4650 REMARK 3 T33: 0.3650 T12: 0.0448 REMARK 3 T13: -0.0912 T23: 0.0990 REMARK 3 L TENSOR REMARK 3 L11: 2.0992 L22: 4.3267 REMARK 3 L33: 2.0355 L12: -0.5228 REMARK 3 L13: 0.2349 L23: 0.0066 REMARK 3 S TENSOR REMARK 3 S11: 0.0959 S12: 0.5486 S13: 0.2419 REMARK 3 S21: -0.1237 S22: 0.0013 S23: -0.3894 REMARK 3 S31: 0.3190 S32: 0.1953 S33: -0.0985 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 4LSQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-13. REMARK 100 THE RCSB ID CODE IS RCSB081038. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-NOV-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : APS 22ID REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47596 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 5.500 REMARK 200 R MERGE (I) : 0.11600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 0.52200 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 (%): 56.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 8.25% PEG 8000, REMARK 280 0.02 M CDCL2, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 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 33.25700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.54400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.81050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.54400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.25700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.81050 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: 10230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 34930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 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 403 REMARK 465 ASN G 404 REMARK 465 ASP H 28A REMARK 465 TYR H 28B REMARK 465 SER H 28C REMARK 465 PRO H 28D REMARK 465 TYR H 28E REMARK 465 TRP H 28F REMARK 465 VAL H 28G REMARK 465 ASN H 28H REMARK 465 PRO H 28I REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 CYS L 214 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 HE ARG G 480 O HOH G 741 1.32 REMARK 500 HH12 ARG L 61 O HOH L 418 1.43 REMARK 500 H THR G 394 O HOH G 822 1.53 REMARK 500 O GLU G 460 HE1 TRP H 61 1.53 REMARK 500 H ALA L 25 O HOH L 411 1.57 REMARK 500 O GLN L 69 O HOH L 411 1.90 REMARK 500 O HOH G 607 O HOH G 786 1.99 REMARK 500 O PHE G 391 O HOH G 815 1.99 REMARK 500 O HOH G 805 O HOH G 806 2.02 REMARK 500 NE2 GLN L 155 O HOH L 420 2.05 REMARK 500 O HOH H 1060 O HOH H 1061 2.06 REMARK 500 O ILE L 75 O HOH L 424 2.07 REMARK 500 O HOH H 1043 O HOH H 1051 2.10 REMARK 500 O HOH H 1067 O HOH H 1074 2.11 REMARK 500 O HOH G 703 O HOH G 762 2.13 REMARK 500 N ALA L 25 O HOH L 411 2.13 REMARK 500 O SER L 76 O HOH L 407 2.13 REMARK 500 NE2 GLN H 1 O HOH H 1068 2.14 REMARK 500 O CYS G 239 O HOH G 735 2.14 REMARK 500 O ALA L 51 O HOH L 412 2.14 REMARK 500 NZ LYS G 357 OD1 ASP L 1 2.16 REMARK 500 NE ARG G 480 O HOH G 741 2.16 REMARK 500 OH TYR H 62 O HOH H 1037 2.17 REMARK 500 O HOH G 770 O HOH G 816 2.18 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 OG SER H 156 O HOH L 444 4465 2.04 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 ASP G 211 107.49 -167.17 REMARK 500 GLN G 258 -57.19 72.85 REMARK 500 GLU G 268 -90.31 -105.52 REMARK 500 ASN G 354 -105.99 50.51 REMARK 500 ASN G 355 24.57 -148.97 REMARK 500 PHE G 391 72.91 -105.61 REMARK 500 THR G 406 72.70 -62.24 REMARK 500 ASN G 411 178.61 -59.47 REMARK 500 SER H 128 49.18 -79.59 REMARK 500 SER L 7 147.47 -170.33 REMARK 500 ALA L 51 -48.37 75.88 REMARK 500 HIS L 68 -85.36 66.29 REMARK 500 ALA L 84 -172.67 -176.70 REMARK 500 TYR L 91 -116.99 53.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH G 749 DISTANCE = 5.39 ANGSTROMS REMARK 525 HOH G 752 DISTANCE = 5.60 ANGSTROMS REMARK 525 HOH H1042 DISTANCE = 5.33 ANGSTROMS 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 CD L 301 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS L 189 NE2 REMARK 620 2 HOH L 444 O 158.3 REMARK 620 3 HOH L 448 O 97.7 87.4 REMARK 620 4 HOH L 442 O 83.9 79.5 142.6 REMARK 620 5 HOH L 401 O 79.6 79.3 91.0 52.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD H 901 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 33 ND1 REMARK 620 2 GLU H 100B OE1 94.9 REMARK 620 3 HOH H1032 O 96.7 108.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD G 510 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS G 216 NE2 REMARK 620 2 HOH G 636 O 99.6 REMARK 620 3 HOH G 601 O 107.0 91.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD H 902 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 164 NE2 REMARK 620 2 ASN L 138 OD1 83.9 REMARK 620 3 HOH L 441 O 104.9 138.3 REMARK 620 4 HOH L 440 O 74.6 54.8 87.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD G 511 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP G 107 OD1 REMARK 620 2 HOH G 780 O 151.6 REMARK 620 3 HOH G 779 O 79.4 107.7 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA G 514 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR H 59 O REMARK 620 2 ASP G 457 OD2 115.2 REMARK 620 3 HOH H1038 O 119.1 116.5 REMARK 620 4 HOH G 649 O 97.3 95.4 107.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA G 515 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR H 53 O REMARK 620 2 HOH G 809 O 112.4 REMARK 620 3 HOH H1020 O 69.2 61.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA G 516 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR G 388 OG1 REMARK 620 2 HOH G 784 O 101.0 REMARK 620 3 HOH G 665 O 107.7 134.0 REMARK 620 4 HOH G 605 O 123.4 107.9 85.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA G 517 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG G 379 O REMARK 620 2 HOH G 639 O 91.8 REMARK 620 3 HOH G 631 O 122.6 105.4 REMARK 620 N 1 2 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 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD G 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD G 511 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU3 G 512 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 513 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 514 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 515 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 516 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 517 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD H 901 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD H 902 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 903 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 904 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD L 301 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3NGB RELATED DB: PDB REMARK 900 RELATED ID: 3SE8 RELATED DB: PDB REMARK 900 RELATED ID: 3SE9 RELATED DB: PDB REMARK 900 RELATED ID: 4JPV RELATED DB: PDB REMARK 900 RELATED ID: 4JPW RELATED DB: PDB REMARK 900 RELATED ID: 4U7Y RELATED DB: PDB REMARK 900 RELATED ID: 4JB9 RELATED DB: PDB REMARK 900 RELATED ID: 4J6R RELATED DB: PDB