HEADER IMMUNE SYSTEM 21-JUL-24 9CR9 TITLE CRYSTAL STRUCTURE OF MA6 FAB IN COMPLEX WITH PFCSP REPEAT REGION TITLE 2 PEPTIDE NPNA3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MA6 FAB HEAVY CHAIN; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MA6 FAB LIGHT CHAIN; COMPND 7 CHAIN: B, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CIRCUMSPOROZOITE PROTEIN (NPNA)3 REPEAT REGION PEPTIDE; COMPND 11 CHAIN: C, P; COMPND 12 FRAGMENT: RESIDUES 134-145; COMPND 13 SYNONYM: CS; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 14 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM; SOURCE 15 ORGANISM_TAXID: 5833 KEYWDS CIRCUMSPOROZOITE PROTEIN, PFCSP, CSP, PROTECTIVE, NEUTRALIZING, KEYWDS 2 ANTIBODY, FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.A.RUSH,J.S.MCLELLAN REVDAT 1 09-JUL-25 9CR9 0 JRNL AUTH J.R.MCDANIEL,W.N.VOSS,G.BOWYER,S.A.RUSH,A.J.SPENCER, JRNL AUTH 2 D.BELLAMY,J.GOIKE,S.GREGORY,C.R.KING,J.S.MCLELLAN, JRNL AUTH 3 A.V.S.HILL,G.GEORGIOU,K.J.EWER,G.C.IPPOLITO JRNL TITL REPERTOIRE, FUNCTION, AND STRUCTURE OF SEROLOGICAL JRNL TITL 2 ANTIBODIES INDUCED BY THE R21/MATRIX-M MALARIA VACCINE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 3 NUMBER OF REFLECTIONS : 74521 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970 REMARK 3 FREE R VALUE TEST SET COUNT : 3706 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 47.7200 - 5.3300 0.95 2907 151 0.1666 0.1654 REMARK 3 2 5.3300 - 4.2300 0.94 2804 134 0.1274 0.1670 REMARK 3 3 4.2300 - 3.7000 0.94 2799 136 0.1447 0.1691 REMARK 3 4 3.7000 - 3.3600 0.98 2817 194 0.1546 0.1617 REMARK 3 5 3.3600 - 3.1200 0.99 2924 156 0.1678 0.2017 REMARK 3 6 3.1200 - 2.9300 0.91 2629 130 0.1751 0.1955 REMARK 3 7 2.9300 - 2.7900 0.94 2778 148 0.1823 0.2148 REMARK 3 8 2.7900 - 2.6700 0.94 2718 140 0.1928 0.2570 REMARK 3 9 2.6700 - 2.5600 0.95 2789 140 0.1943 0.2360 REMARK 3 10 2.5600 - 2.4800 0.95 2776 156 0.2027 0.2249 REMARK 3 11 2.4800 - 2.4000 0.95 2770 145 0.2018 0.2532 REMARK 3 12 2.4000 - 2.3300 0.91 2595 142 0.1973 0.2221 REMARK 3 13 2.3300 - 2.2700 0.85 2567 106 0.2084 0.2631 REMARK 3 14 2.2700 - 2.2100 0.91 2634 132 0.2060 0.2631 REMARK 3 15 2.2100 - 2.1600 0.92 2670 164 0.2010 0.2361 REMARK 3 16 2.1600 - 2.1200 0.94 2710 133 0.1961 0.2573 REMARK 3 17 2.1200 - 2.0700 0.94 2767 127 0.2110 0.2512 REMARK 3 18 2.0700 - 2.0300 0.95 2692 158 0.2267 0.2379 REMARK 3 19 2.0300 - 2.0000 0.96 2854 142 0.2201 0.2577 REMARK 3 20 2.0000 - 1.9600 0.95 2698 177 0.2133 0.2339 REMARK 3 21 1.9600 - 1.9300 0.91 2639 124 0.2278 0.3208 REMARK 3 22 1.9300 - 1.9000 0.86 2493 152 0.2442 0.2749 REMARK 3 23 1.9000 - 1.8800 0.93 2710 110 0.2505 0.2398 REMARK 3 24 1.8800 - 1.8500 0.93 2726 129 0.2567 0.3141 REMARK 3 25 1.8500 - 1.8200 0.92 2666 135 0.2711 0.2939 REMARK 3 26 1.8200 - 1.8000 0.94 2683 145 0.2945 0.3180 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) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.560 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.05 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 : 0.008 6812 REMARK 3 ANGLE : 0.964 9273 REMARK 3 CHIRALITY : 0.064 1035 REMARK 3 PLANARITY : 0.006 1186 REMARK 3 DIHEDRAL : 17.784 2409 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 9CR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000285992. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JUN-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74608 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 47.720 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 200 DATA REDUNDANCY : 1.800 REMARK 200 R MERGE (I) : 0.07700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.9300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.43350 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.140 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 (%): 43.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG3350, 3% MPD, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 30.52500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4510 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 SER A 127 REMARK 465 SER A 128 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 THR A 131 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 LYS A 214 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 LYS A 218 REMARK 465 GLY A 219 REMARK 465 LEU A 220 REMARK 465 GLU A 221 REMARK 465 VAL A 222 REMARK 465 LEU A 223 REMARK 465 PHE A 224 REMARK 465 GLN A 225 REMARK 465 GLY B 212 REMARK 465 GLU B 213 REMARK 465 CYS B 214 REMARK 465 PRO C 10 REMARK 465 ASN C 11 REMARK 465 ALA C 12 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 LEU H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 GLY L 211 REMARK 465 GLU L 212 REMARK 465 CYS L 213 REMARK 465 PRO P 10 REMARK 465 ASN P 11 REMARK 465 ALA P 12 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 O HOH B 305 O HOH B 327 1.81 REMARK 500 O HOH L 458 O HOH L 468 1.85 REMARK 500 O HOH A 573 O HOH A 591 1.86 REMARK 500 O HOH B 520 O HOH B 550 1.87 REMARK 500 O HOH L 463 O HOH L 504 1.88 REMARK 500 O HOH A 301 O HOH A 454 1.91 REMARK 500 N GLN A 1 O HOH A 301 1.92 REMARK 500 O HOH B 425 O HOH B 538 1.93 REMARK 500 O HOH L 355 O HOH L 451 1.93 REMARK 500 O HOH B 321 O HOH B 548 1.95 REMARK 500 OG SER H 187 O HOH H 301 1.95 REMARK 500 O HOH H 358 O HOH H 383 1.95 REMARK 500 OE1 GLN A 13 O HOH A 302 1.95 REMARK 500 OD1 ASP B 185 O HOH B 301 1.96 REMARK 500 O HOH A 320 O HOH A 548 1.96 REMARK 500 O HOH H 409 O HOH H 540 1.96 REMARK 500 O HOH A 572 O HOH A 585 1.96 REMARK 500 O LEU H 189 O HOH H 302 1.98 REMARK 500 O HOH B 591 O HOH B 592 1.99 REMARK 500 O HOH B 533 O HOH B 537 1.99 REMARK 500 O HOH H 447 O HOH H 449 2.01 REMARK 500 O HOH A 501 O HOH A 529 2.01 REMARK 500 O HOH B 367 O HOH B 535 2.02 REMARK 500 O HOH H 530 O HOH H 537 2.02 REMARK 500 O HOH B 307 O HOH B 494 2.02 REMARK 500 OG1 THR L 10 O HOH L 301 2.05 REMARK 500 O HOH A 430 O HOH A 521 2.07 REMARK 500 O PRO H 213 O HOH H 303 2.08 REMARK 500 NE2 GLN B 199 O HOH B 302 2.09 REMARK 500 O HOH L 466 O HOH L 532 2.09 REMARK 500 O HOH B 505 O HOH H 567 2.09 REMARK 500 OE1 GLU L 186 O HOH L 302 2.11 REMARK 500 O HOH H 330 O HOH H 514 2.12 REMARK 500 NE2 GLN B 199 O HOH B 303 2.12 REMARK 500 O HOH A 458 O HOH A 535 2.12 REMARK 500 O HOH L 371 O HOH L 529 2.12 REMARK 500 O HOH B 487 O HOH B 585 2.12 REMARK 500 O HOH H 412 O HOH H 507 2.13 REMARK 500 O HOH L 449 O HOH L 526 2.13 REMARK 500 O HOH C 103 O HOH C 107 2.13 REMARK 500 NE2 GLN A 105 O HOH A 303 2.14 REMARK 500 O HOH A 518 O HOH A 522 2.14 REMARK 500 O HOH A 303 O HOH A 418 2.14 REMARK 500 O HOH H 536 O HOH P 103 2.14 REMARK 500 O HOH H 432 O HOH H 491 2.16 REMARK 500 O HOH A 597 O HOH A 599 2.16 REMARK 500 O HOH B 503 O HOH B 588 2.17 REMARK 500 O HOH L 342 O HOH L 394 2.18 REMARK 500 O HOH A 348 O HOH A 491 2.18 REMARK 500 OG SER H 188 O HOH H 304 2.18 REMARK 500 REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS 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 O HOH H 576 O HOH L 481 1455 1.80 REMARK 500 O HOH A 481 O HOH L 517 1455 1.84 REMARK 500 O HOH A 428 O HOH B 305 1455 1.89 REMARK 500 O HOH H 563 O HOH P 109 2646 1.91 REMARK 500 O HOH B 547 O HOH H 468 1465 2.02 REMARK 500 O HOH A 458 O HOH L 483 1455 2.17 REMARK 500 O HOH A 414 O HOH B 489 1565 2.19 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 GLY A 118 C PRO A 119 N 0.158 REMARK 500 GLU A 148 C PRO A 149 N 0.156 REMARK 500 LYS A 201 C PRO A 202 N 0.164 REMARK 500 PRO C 6 N PRO C 6 CA 0.230 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 PRO A 119 C - N - CA ANGL. DEV. = 13.6 DEGREES REMARK 500 PRO A 119 C - N - CD ANGL. DEV. = -13.2 DEGREES REMARK 500 PRO A 202 C - N - CA ANGL. DEV. = 14.1 DEGREES REMARK 500 PRO A 202 C - N - CD ANGL. DEV. = -12.8 DEGREES REMARK 500 PRO C 6 C - N - CA ANGL. DEV. = 18.0 DEGREES REMARK 500 PRO C 6 CA - N - CD ANGL. DEV. = -9.6 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 SER A 55 -75.56 -86.29 REMARK 500 SER B 30 -123.96 52.00 REMARK 500 ALA B 51 -54.23 72.55 REMARK 500 TYR B 94 -154.89 63.34 REMARK 500 SER H 55 -75.31 -96.37 REMARK 500 ASP H 144 62.67 65.79 REMARK 500 SER L 30 -121.21 54.38 REMARK 500 ALA L 51 -51.37 72.33 REMARK 500 TYR L 94 -151.75 61.68 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 A 595 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH A 596 DISTANCE = 6.35 ANGSTROMS REMARK 525 HOH A 597 DISTANCE = 6.63 ANGSTROMS REMARK 525 HOH A 598 DISTANCE = 6.78 ANGSTROMS REMARK 525 HOH A 599 DISTANCE = 6.92 ANGSTROMS REMARK 525 HOH A 600 DISTANCE = 7.71 ANGSTROMS REMARK 525 HOH A 601 DISTANCE = 7.77 ANGSTROMS REMARK 525 HOH A 602 DISTANCE = 8.47 ANGSTROMS REMARK 525 HOH A 603 DISTANCE = 9.11 ANGSTROMS REMARK 525 HOH B 591 DISTANCE = 7.62 ANGSTROMS REMARK 525 HOH B 592 DISTANCE = 7.93 ANGSTROMS REMARK 525 HOH H 584 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH H 585 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH H 586 DISTANCE = 6.43 ANGSTROMS REMARK 525 HOH L 561 DISTANCE = 7.63 ANGSTROMS DBREF 9CR9 A 1 225 PDB 9CR9 9CR9 1 225 DBREF 9CR9 B 1 214 PDB 9CR9 9CR9 1 214 DBREF 9CR9 C 1 12 UNP P05691 CSP_PLAFL 134 145 DBREF 9CR9 H 1 225 PDB 9CR9 9CR9 1 225 DBREF 9CR9 L 1 213 PDB 9CR9 9CR9 1 213 DBREF 9CR9 P 1 12 UNP P05691 CSP_PLAFL 134 145 SEQRES 1 A 235 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 235 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 235 PHE THR PHE SER SER TYR GLY ILE HIS TRP VAL ARG GLN SEQRES 4 A 235 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE TRP SEQRES 5 A 235 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 235 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 235 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 235 ALA VAL TYR TYR CYS ALA ARG ASP GLY GLY HIS SER THR SEQRES 9 A 235 SER TRP SER ASN ALA PHE ASP ILE TRP GLY GLN GLY THR SEQRES 10 A 235 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 235 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 235 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 235 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 235 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 235 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 235 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 235 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 A 235 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL LEU PHE SEQRES 19 A 235 GLN SEQRES 1 B 213 ASP ILE GLN VAL THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 B 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 213 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 B 213 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 213 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 213 ASN SER TYR TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 B 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 B 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 B 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 B 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 B 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 B 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 B 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 B 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 B 213 ASN ARG GLY GLU CYS SEQRES 1 C 12 ASN PRO ASN ALA ASN PRO ASN ALA ASN PRO ASN ALA SEQRES 1 H 235 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 235 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 235 PHE THR PHE SER SER TYR GLY ILE HIS TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE TRP SEQRES 5 H 235 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 235 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 235 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA ARG ASP GLY GLY HIS SER THR SEQRES 9 H 235 SER TRP SER ASN ALA PHE ASP ILE TRP GLY GLN GLY THR SEQRES 10 H 235 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 235 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 235 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 235 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 235 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 235 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 235 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 235 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 235 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL LEU PHE SEQRES 19 H 235 GLN SEQRES 1 L 213 ASP ILE GLN VAL THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 213 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 L 213 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 213 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 213 ASN SER TYR TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 L 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1 P 12 ASN PRO ASN ALA ASN PRO ASN ALA ASN PRO ASN ALA FORMUL 7 HOH *1162(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 73 LYS A 75 5 3 HELIX 3 AA3 ARG A 83 THR A 87 5 5 HELIX 4 AA4 SER A 156 ALA A 158 5 3 HELIX 5 AA5 SER A 187 LEU A 189 5 3 HELIX 6 AA6 LYS A 201 ASN A 204 5 4 HELIX 7 AA7 GLN B 79 PHE B 83 5 5 HELIX 8 AA8 SER B 121 SER B 127 1 7 HELIX 9 AA9 LYS B 183 LYS B 188 1 6 HELIX 10 AB1 THR H 28 TYR H 32 5 5 HELIX 11 AB2 ASN H 73 LYS H 75 5 3 HELIX 12 AB3 ARG H 83 THR H 87 5 5 HELIX 13 AB4 SER H 156 ALA H 158 5 3 HELIX 14 AB5 SER H 187 LEU H 189 5 3 HELIX 15 AB6 LYS H 201 ASN H 204 5 4 HELIX 16 AB7 GLN L 79 PHE L 83 5 5 HELIX 17 AB8 SER L 120 LYS L 125 1 6 HELIX 18 AB9 LYS L 182 GLU L 186 1 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N SER A 70 O TYR A 79 SHEET 1 AA2 6 VAL A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 ASP A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AA2 6 ILE A 34 GLN A 39 -1 N VAL A 37 O TYR A 91 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 LYS A 57 TYR A 59 -1 O TYR A 58 N LEU A 50 SHEET 1 AA3 4 VAL A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA3 4 ALA A 88 ASP A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AA3 4 PHE A 100F TRP A 103 -1 O ILE A 102 N ARG A 94 SHEET 1 AA4 4 SER A 120 LEU A 124 0 SHEET 2 AA4 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA4 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AA5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 ILE A 195 HIS A 200 -1 O ASN A 199 N THR A 151 SHEET 3 AA6 3 THR A 205 LYS A 210 -1 O VAL A 207 N VAL A 198 SHEET 1 AA7 4 VAL B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 GLU B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 THR B 10 ALA B 13 0 SHEET 2 AA8 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 6 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 SER B 53 LEU B 54 -1 O SER B 53 N TYR B 49 SHEET 1 AA9 4 THR B 10 ALA B 13 0 SHEET 2 AA9 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA9 4 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA9 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AB1 4 TYR B 173 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AB1 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB2 4 ALA B 153 LEU B 154 0 SHEET 2 AB2 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB2 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 4 AB2 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB3 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AB3 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AB4 6 VAL H 11 VAL H 12 0 SHEET 2 AB4 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB4 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB4 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AB4 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB4 6 LYS H 57 TYR H 59 -1 O TYR H 58 N LEU H 50 SHEET 1 AB5 4 VAL H 11 VAL H 12 0 SHEET 2 AB5 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB5 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB5 4 PHE H 100F TRP H 103 -1 O ILE H 102 N ARG H 94 SHEET 1 AB6 4 SER H 120 LEU H 124 0 SHEET 2 AB6 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB6 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB6 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB7 4 SER H 120 LEU H 124 0 SHEET 2 AB7 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB7 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB7 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB8 3 THR H 151 TRP H 154 0 SHEET 2 AB8 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB8 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AB9 4 VAL L 4 SER L 7 0 SHEET 2 AB9 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB9 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB9 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AC1 6 THR L 10 ALA L 13 0 SHEET 2 AC1 6 THR L 101 ILE L 105 1 O LYS L 102 N LEU L 11 SHEET 3 AC1 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AC1 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AC1 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC1 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AC2 4 THR L 10 ALA L 13 0 SHEET 2 AC2 4 THR L 101 ILE L 105 1 O LYS L 102 N LEU L 11 SHEET 3 AC2 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AC2 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 90 SHEET 1 AC3 4 SER L 113 PHE L 117 0 SHEET 2 AC3 4 THR L 128 PHE L 138 -1 O LEU L 134 N PHE L 115 SHEET 3 AC3 4 TYR L 172 SER L 181 -1 O LEU L 180 N ALA L 129 SHEET 4 AC3 4 SER L 158 VAL L 162 -1 N SER L 161 O SER L 175 SHEET 1 AC4 4 ALA L 152 LEU L 153 0 SHEET 2 AC4 4 LYS L 144 VAL L 149 -1 N VAL L 149 O ALA L 152 SHEET 3 AC4 4 VAL L 190 THR L 196 -1 O GLU L 194 N GLN L 146 SHEET 4 AC4 4 VAL L 204 ASN L 209 -1 O VAL L 204 N VAL L 195 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.01 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.02 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 6 CYS H 140 CYS H 196 1555 1555 2.02 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.02 SSBOND 8 CYS L 133 CYS L 193 1555 1555 2.03 CISPEP 1 PHE A 146 PRO A 147 0 -0.25 CISPEP 2 GLU A 148 PRO A 149 0 -8.55 CISPEP 3 SER B 7 PRO B 8 0 -8.43 CISPEP 4 TYR B 140 PRO B 141 0 1.20 CISPEP 5 PHE H 146 PRO H 147 0 -5.35 CISPEP 6 GLU H 148 PRO H 149 0 -0.02 CISPEP 7 SER L 7 PRO L 8 0 -6.35 CISPEP 8 TYR L 139 PRO L 140 0 4.12 CRYST1 46.600 61.050 152.999 90.00 90.00 90.00 P 1 21 1 4 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 0.021459 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016380 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006536 0.00000