HEADER TRANSPORT PROTEIN/IMMUNE SYSTEM 18-NOV-13 4NNP TITLE CRYSTAL STRUCTURE OF APO MANGANESE ABC TRANSPORTER MNTC FROM TITLE 2 STAPHYLOCOCCUS AUREUS BOUND TO AN ANTAGONISTIC FAB FRAGMENT CAVEAT 4NNP RESIDUE (A ASN 111 ) AND RESIDUE (A GLU 113 ) ARE LINKED CAVEAT 2 4NNP TOGETHER. COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIPOPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN OF ANTAGONISTIC FAB FRAGMENT; COMPND 7 CHAIN: H, X; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LIGHT CHAIN OF ANTAGONISTIC FAB FRAGMENT; COMPND 11 CHAIN: L, Y; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS; SOURCE 3 ORGANISM_TAXID: 158878; SOURCE 4 STRAIN: MU50 / ATCC 700699; SOURCE 5 GENE: SAV0631; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ABC SUPERFAMILY ATP BINDING CASSETTE TRANSPORTER, MNTC, FAB, APO, KEYWDS 2 MRSA, TRANSPORT PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR L.ROUGE,J.SUDHAMSU REVDAT 1 10-DEC-14 4NNP 0 JRNL AUTH S.AHUJA,L.ROUGE,D.L.SWEM,J.SUDHAMSU,P.WU,S.RUSSELL, JRNL AUTH 2 M.K.ALEXANDER,C.TAM,M.NISHIYAMA,M.A.STAROVASNIK,C.M.KOTH JRNL TITL STRUCTURAL INSIGHTS INTO ANTIBODY INHIBITION OF THE JRNL TITL 2 STAPHYLOCOCCUS AUREUS MNTABC MN2+ IMPORT PATHWAY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.69 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 2.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.27 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9 REMARK 3 NUMBER OF REFLECTIONS : 58231 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.270 REMARK 3 FREE R VALUE TEST SET COUNT : 2485 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 47.2739 - 7.0246 0.87 3139 147 0.2328 0.2671 REMARK 3 2 7.0246 - 5.5785 0.90 3179 132 0.2200 0.2862 REMARK 3 3 5.5785 - 4.8741 0.91 3211 141 0.1895 0.2391 REMARK 3 4 4.8741 - 4.4288 0.89 3097 145 0.1681 0.1915 REMARK 3 5 4.4288 - 4.1116 0.88 3077 148 0.1797 0.2431 REMARK 3 6 4.1116 - 3.8693 0.86 2974 115 0.1891 0.2758 REMARK 3 7 3.8693 - 3.6756 0.91 3178 143 0.2024 0.2894 REMARK 3 8 3.6756 - 3.5157 0.92 3223 137 0.2162 0.3120 REMARK 3 9 3.5157 - 3.3804 0.91 3172 151 0.2306 0.2820 REMARK 3 10 3.3804 - 3.2637 0.92 3212 128 0.2410 0.3002 REMARK 3 11 3.2637 - 3.1617 0.91 3118 151 0.2505 0.3684 REMARK 3 12 3.1617 - 3.0714 0.85 2974 130 0.2647 0.3669 REMARK 3 13 3.0714 - 2.9905 0.88 3046 146 0.2719 0.3268 REMARK 3 14 2.9905 - 2.9176 0.90 3089 147 0.2821 0.3185 REMARK 3 15 2.9176 - 2.8512 0.90 3138 141 0.2953 0.3475 REMARK 3 16 2.8512 - 2.7906 0.90 3106 130 0.3035 0.2928 REMARK 3 17 2.7906 - 2.7348 0.91 3172 133 0.3158 0.4019 REMARK 3 18 2.7348 - 2.6832 0.76 2641 120 0.3331 0.3836 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) : 0.460 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.320 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 : 0.010 11295 REMARK 3 ANGLE : 1.391 15272 REMARK 3 CHIRALITY : 0.055 1682 REMARK 3 PLANARITY : 0.007 1947 REMARK 3 DIHEDRAL : 14.542 4136 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: all REMARK 3 ORIGIN FOR THE GROUP (A): -7.7017 23.2612 -10.3553 REMARK 3 T TENSOR REMARK 3 T11: 0.0342 T22: -0.0268 REMARK 3 T33: 0.0246 T12: 0.0273 REMARK 3 T13: -0.0128 T23: -0.0203 REMARK 3 L TENSOR REMARK 3 L11: 0.0377 L22: 0.0866 REMARK 3 L33: 0.1450 L12: 0.0309 REMARK 3 L13: -0.0455 L23: 0.0023 REMARK 3 S TENSOR REMARK 3 S11: 0.0207 S12: 0.0720 S13: -0.0141 REMARK 3 S21: 0.0130 S22: -0.0043 S23: -0.0094 REMARK 3 S31: -0.0149 S32: -0.0675 S33: 0.0595 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 4NNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-14. REMARK 100 THE RCSB ID CODE IS RCSB083430. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-APR-13 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 : 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) : 0.98 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58231 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 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 (%) : 89.7 REMARK 200 DATA REDUNDANCY : 2.500 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) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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 (%): 65.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL PH 8.5, 20% PEG 10000 REMARK 280 AND 0.7% 1-BUTANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298K 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 46.25500 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 300 REMARK: ONE MOLECULE OF MNTC BOUND TO HEAVY CHAIN AND LIGHT CHAIN REMARK 300 OF A FAB FRAGMENT. 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: 5670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 5670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, X, Y 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 A 19 REMARK 465 THR A 20 REMARK 465 GLY A 21 REMARK 465 GLY A 22 REMARK 465 LYS A 23 REMARK 465 GLN A 24 REMARK 465 SER A 25 REMARK 465 SER A 26 REMARK 465 ASP A 27 REMARK 465 LYS A 28 REMARK 465 SER A 29 REMARK 465 ASN A 30 REMARK 465 GLY A 31 REMARK 465 GLY A 129 REMARK 465 THR A 270 REMARK 465 LYS A 271 REMARK 465 LYS A 272 REMARK 465 ASP A 273 REMARK 465 GLY B 19 REMARK 465 THR B 20 REMARK 465 GLY B 21 REMARK 465 GLY B 22 REMARK 465 LYS B 23 REMARK 465 GLN B 24 REMARK 465 SER B 25 REMARK 465 SER B 26 REMARK 465 ASP B 27 REMARK 465 LYS B 28 REMARK 465 SER B 29 REMARK 465 ASN B 30 REMARK 465 GLY B 31 REMARK 465 LYS B 271 REMARK 465 LYS B 272 REMARK 465 ASP B 273 REMARK 465 ILE B 274 REMARK 465 GLU H -2 REMARK 465 ILE H -1 REMARK 465 SER H 0 REMARK 465 GLU H 1 REMARK 465 VAL H 2 REMARK 465 SER H 230 REMARK 465 CYS H 231 REMARK 465 ASP H 232 REMARK 465 LYS H 233 REMARK 465 THR H 234 REMARK 465 HIS H 235 REMARK 465 GLU X -2 REMARK 465 ILE X -1 REMARK 465 SER X 0 REMARK 465 GLU X 1 REMARK 465 VAL X 2 REMARK 465 SER X 230 REMARK 465 CYS X 231 REMARK 465 ASP X 232 REMARK 465 LYS X 233 REMARK 465 THR X 234 REMARK 465 HIS X 235 REMARK 465 SER L 0 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 SER Y 0 REMARK 465 GLU Y 214 REMARK 465 CYS Y 215 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 NH2 ARG H 87 O HOH H 302 2.09 REMARK 500 OG SER L 122 OE1 GLU L 124 2.12 REMARK 500 O HOH A 440 O HOH A 460 2.14 REMARK 500 O VAL A 71 O HOH A 428 2.15 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 OE1 GLU B 198 O HOH H 302 2545 1.21 REMARK 500 CD GLU B 198 O HOH H 302 2545 2.03 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 A 249 CA - CB - CG ANGL. DEV. = 16.6 DEGREES REMARK 500 PRO B 124 C - N - CA ANGL. DEV. = -10.9 DEGREES REMARK 500 LEU B 249 CA - CB - CG ANGL. DEV. = 14.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLU A 93 46.12 -91.18 REMARK 500 GLU A 131 13.15 -56.84 REMARK 500 HIS A 140 48.17 -86.13 REMARK 500 ASP A 163 52.53 -151.73 REMARK 500 ASN A 227 79.41 52.94 REMARK 500 GLU A 229 -57.77 74.21 REMARK 500 GLU A 235 -38.77 146.12 REMARK 500 LYS A 248 127.96 66.72 REMARK 500 LEU A 249 -145.44 -152.90 REMARK 500 THR A 280 -87.87 -139.08 REMARK 500 GLU B 93 46.05 -86.92 REMARK 500 GLU B 130 97.81 -63.00 REMARK 500 HIS B 140 47.49 -85.38 REMARK 500 ASP B 163 55.98 -149.52 REMARK 500 ARG B 200 76.15 -100.42 REMARK 500 SER B 205 -49.00 82.07 REMARK 500 LYS B 248 129.73 70.65 REMARK 500 LEU B 249 -144.81 -152.78 REMARK 500 THR B 280 -87.73 -138.86 REMARK 500 GLU H 89 1.32 -67.64 REMARK 500 SER H 127 143.05 -170.98 REMARK 500 SER H 142 -152.64 -159.45 REMARK 500 ASP H 159 79.39 56.56 REMARK 500 SER H 203 65.33 -101.13 REMARK 500 VAL H 226 76.23 -105.53 REMARK 500 GLU X 89 8.15 -69.12 REMARK 500 SER X 106 112.54 -161.14 REMARK 500 SER X 142 -150.70 -160.70 REMARK 500 ASP X 159 81.57 57.09 REMARK 500 SER X 203 63.45 -103.30 REMARK 500 VAL X 226 72.99 -106.78 REMARK 500 SER L 30 -125.85 47.80 REMARK 500 SER L 50 29.17 48.51 REMARK 500 ALA L 51 -37.48 83.73 REMARK 500 ARG L 66 140.91 79.83 REMARK 500 THR L 69 -38.19 61.74 REMARK 500 LEU L 78 151.67 -49.99 REMARK 500 ASN L 139 70.35 56.19 REMARK 500 PRO L 142 -176.23 -66.97 REMARK 500 ASN L 153 -19.96 75.05 REMARK 500 ARG L 212 66.74 -65.45 REMARK 500 SER Y 30 -123.33 48.20 REMARK 500 SER Y 50 29.64 46.78 REMARK 500 ALA Y 51 -40.08 82.68 REMARK 500 ARG Y 66 139.23 76.99 REMARK 500 THR Y 69 -34.72 63.13 REMARK 500 LEU Y 78 152.55 -47.59 REMARK 500 ASP Y 152 49.99 38.71 REMARK 500 ASN Y 153 -20.46 79.00 REMARK 500 LYS Y 170 -71.42 -87.61 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. 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 B 418 DISTANCE = 5.38 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4K3V RELATED DB: PDB REMARK 900 MNTC REMARK 900 RELATED ID: 1FVE RELATED DB: PDB REMARK 900 HERCEPTIN FAB USED FOR MOLECULAR REPLACEMENT REMARK 900 RELATED ID: 4NNO RELATED DB: PDB DBREF 4NNP A 19 309 UNP Q99VY4 Q99VY4_STAAM 19 309 DBREF 4NNP B 19 309 UNP Q99VY4 Q99VY4_STAAM 19 309 DBREF 4NNP H -2 235 PDB 4NNP 4NNP -2 235 DBREF 4NNP X -2 235 PDB 4NNP 4NNP -2 235 DBREF 4NNP L 0 215 PDB 4NNP 4NNP 0 215 DBREF 4NNP Y 0 215 PDB 4NNP 4NNP 0 215 SEQRES 1 A 291 GLY THR GLY GLY LYS GLN SER SER ASP LYS SER ASN GLY SEQRES 2 A 291 LYS LEU LYS VAL VAL THR THR ASN SER ILE LEU TYR ASP SEQRES 3 A 291 MET ALA LYS ASN VAL GLY GLY ASP ASN VAL ASP ILE HIS SEQRES 4 A 291 SER ILE VAL PRO VAL GLY GLN ASP PRO HIS GLU TYR GLU SEQRES 5 A 291 VAL LYS PRO LYS ASP ILE LYS LYS LEU THR ASP ALA ASP SEQRES 6 A 291 VAL ILE LEU TYR ASN GLY LEU ASN LEU GLU THR GLY ASN SEQRES 7 A 291 GLY TRP PHE GLU LYS ALA LEU GLU GLN ALA GLY LYS SER SEQRES 8 A 291 LEU LYS ASP LYS LYS VAL ILE ALA VAL SER LYS ASP VAL SEQRES 9 A 291 LYS PRO ILE TYR LEU ASN GLY GLU GLU GLY ASN LYS ASP SEQRES 10 A 291 LYS GLN ASP PRO HIS ALA TRP LEU SER LEU ASP ASN GLY SEQRES 11 A 291 ILE LYS TYR VAL LYS THR ILE GLN GLN THR PHE ILE ASP SEQRES 12 A 291 ASN ASP LYS LYS HIS LYS ALA ASP TYR GLU LYS GLN GLY SEQRES 13 A 291 ASN LYS TYR ILE ALA GLN LEU GLU LYS LEU ASN ASN ASP SEQRES 14 A 291 SER LYS ASP LYS PHE ASN ASP ILE PRO LYS GLU GLN ARG SEQRES 15 A 291 ALA MET ILE THR SER GLU GLY ALA PHE LYS TYR PHE SER SEQRES 16 A 291 LYS GLN TYR GLY ILE THR PRO GLY TYR ILE TRP GLU ILE SEQRES 17 A 291 ASN THR GLU LYS GLN GLY THR PRO GLU GLN MET ARG GLN SEQRES 18 A 291 ALA ILE GLU PHE VAL LYS LYS HIS LYS LEU LYS HIS LEU SEQRES 19 A 291 LEU VAL GLU THR SER VAL ASP LYS LYS ALA MET GLU SER SEQRES 20 A 291 LEU SER GLU GLU THR LYS LYS ASP ILE PHE GLY GLU VAL SEQRES 21 A 291 TYR THR ASP SER ILE GLY LYS GLU GLY THR LYS GLY ASP SEQRES 22 A 291 SER TYR TYR LYS MET MET LYS SER ASN ILE GLU THR VAL SEQRES 23 A 291 HIS GLY SER MET LYS SEQRES 1 B 291 GLY THR GLY GLY LYS GLN SER SER ASP LYS SER ASN GLY SEQRES 2 B 291 LYS LEU LYS VAL VAL THR THR ASN SER ILE LEU TYR ASP SEQRES 3 B 291 MET ALA LYS ASN VAL GLY GLY ASP ASN VAL ASP ILE HIS SEQRES 4 B 291 SER ILE VAL PRO VAL GLY GLN ASP PRO HIS GLU TYR GLU SEQRES 5 B 291 VAL LYS PRO LYS ASP ILE LYS LYS LEU THR ASP ALA ASP SEQRES 6 B 291 VAL ILE LEU TYR ASN GLY LEU ASN LEU GLU THR GLY ASN SEQRES 7 B 291 GLY TRP PHE GLU LYS ALA LEU GLU GLN ALA GLY LYS SER SEQRES 8 B 291 LEU LYS ASP LYS LYS VAL ILE ALA VAL SER LYS ASP VAL SEQRES 9 B 291 LYS PRO ILE TYR LEU ASN GLY GLU GLU GLY ASN LYS ASP SEQRES 10 B 291 LYS GLN ASP PRO HIS ALA TRP LEU SER LEU ASP ASN GLY SEQRES 11 B 291 ILE LYS TYR VAL LYS THR ILE GLN GLN THR PHE ILE ASP SEQRES 12 B 291 ASN ASP LYS LYS HIS LYS ALA ASP TYR GLU LYS GLN GLY SEQRES 13 B 291 ASN LYS TYR ILE ALA GLN LEU GLU LYS LEU ASN ASN ASP SEQRES 14 B 291 SER LYS ASP LYS PHE ASN ASP ILE PRO LYS GLU GLN ARG SEQRES 15 B 291 ALA MET ILE THR SER GLU GLY ALA PHE LYS TYR PHE SER SEQRES 16 B 291 LYS GLN TYR GLY ILE THR PRO GLY TYR ILE TRP GLU ILE SEQRES 17 B 291 ASN THR GLU LYS GLN GLY THR PRO GLU GLN MET ARG GLN SEQRES 18 B 291 ALA ILE GLU PHE VAL LYS LYS HIS LYS LEU LYS HIS LEU SEQRES 19 B 291 LEU VAL GLU THR SER VAL ASP LYS LYS ALA MET GLU SER SEQRES 20 B 291 LEU SER GLU GLU THR LYS LYS ASP ILE PHE GLY GLU VAL SEQRES 21 B 291 TYR THR ASP SER ILE GLY LYS GLU GLY THR LYS GLY ASP SEQRES 22 B 291 SER TYR TYR LYS MET MET LYS SER ASN ILE GLU THR VAL SEQRES 23 B 291 HIS GLY SER MET LYS SEQRES 1 H 238 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 238 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 238 ALA SER GLY PHE ASN PHE SER SER SER SER ILE HIS TRP SEQRES 4 H 238 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 238 SER ILE TYR SER TYR SER GLY TYR THR TYR TYR ALA ASP SEQRES 6 H 238 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 238 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 238 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN SER SER SEQRES 9 H 238 ALA GLU ILE GLU SER TRP TYR TYR TYR SER GLY GLU ALA SEQRES 10 H 238 MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 H 238 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 H 238 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 H 238 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 H 238 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 H 238 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 H 238 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 H 238 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 H 238 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 19 H 238 ASP LYS THR HIS SEQRES 1 L 216 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 216 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 216 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 216 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 216 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 216 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 216 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 216 SER TYR TYR SER SER PRO PHE THR PHE GLY GLN GLY THR SEQRES 9 L 216 LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 L 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 X 238 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 X 238 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 X 238 ALA SER GLY PHE ASN PHE SER SER SER SER ILE HIS TRP SEQRES 4 X 238 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 X 238 SER ILE TYR SER TYR SER GLY TYR THR TYR TYR ALA ASP SEQRES 6 X 238 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 X 238 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 X 238 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLN SER SER SEQRES 9 X 238 ALA GLU ILE GLU SER TRP TYR TYR TYR SER GLY GLU ALA SEQRES 10 X 238 MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 X 238 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 X 238 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 X 238 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 X 238 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 X 238 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 X 238 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 X 238 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 X 238 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 19 X 238 ASP LYS THR HIS SEQRES 1 Y 216 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 Y 216 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 Y 216 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 Y 216 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 Y 216 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 Y 216 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 Y 216 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 Y 216 SER TYR TYR SER SER PRO PHE THR PHE GLY GLN GLY THR SEQRES 9 Y 216 LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 Y 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 Y 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 Y 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 Y 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 Y 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 Y 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 Y 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 Y 216 LYS SER PHE ASN ARG GLY GLU CYS FORMUL 7 HOH *248(H2 O) HELIX 1 1 ASN A 39 GLY A 51 1 13 HELIX 2 2 LYS A 72 ASP A 81 1 10 HELIX 3 3 THR A 94 ASN A 96 5 3 HELIX 4 4 GLY A 97 ALA A 106 1 10 HELIX 5 5 SER A 119 VAL A 122 5 4 HELIX 6 6 ASN A 133 GLN A 137 5 5 HELIX 7 7 HIS A 140 LEU A 143 5 4 HELIX 8 8 SER A 144 ASP A 163 1 20 HELIX 9 9 HIS A 166 ASP A 194 1 29 HELIX 10 10 PRO A 196 GLN A 199 5 4 HELIX 11 11 PHE A 209 GLY A 217 1 9 HELIX 12 12 GLU A 235 LYS A 248 1 14 HELIX 13 13 LYS A 261 GLU A 268 1 8 HELIX 14 14 SER A 292 SER A 307 1 16 HELIX 15 15 ASN B 39 GLY B 51 1 13 HELIX 16 16 LYS B 72 ASP B 81 1 10 HELIX 17 17 ASN B 91 ASN B 96 5 6 HELIX 18 18 GLY B 97 ALA B 106 1 10 HELIX 19 19 TYR B 126 GLU B 130 5 5 HELIX 20 20 ASN B 133 GLN B 137 5 5 HELIX 21 21 HIS B 140 LEU B 143 5 4 HELIX 22 22 SER B 144 ASP B 163 1 20 HELIX 23 23 HIS B 166 ASP B 194 1 29 HELIX 24 24 PRO B 196 GLN B 199 5 4 HELIX 25 25 PHE B 209 GLY B 217 1 9 HELIX 26 26 THR B 233 LYS B 248 1 16 HELIX 27 27 ALA B 262 GLU B 268 1 7 HELIX 28 28 SER B 292 SER B 307 1 16 HELIX 29 29 ARG H 87 THR H 91 5 5 HELIX 30 30 SER H 171 ALA H 173 5 3 HELIX 31 31 ARG X 87 THR X 91 5 5 HELIX 32 32 SER X 171 ALA X 173 5 3 HELIX 33 33 GLN L 79 PHE L 83 5 5 HELIX 34 34 SER L 122 SER L 128 1 7 HELIX 35 35 LYS L 184 GLU L 188 1 5 HELIX 36 36 GLN Y 79 PHE Y 83 5 5 HELIX 37 37 SER Y 122 SER Y 128 1 7 HELIX 38 38 LYS Y 184 GLU Y 188 1 5 SHEET 1 A 4 VAL A 54 SER A 58 0 SHEET 2 A 4 LEU A 33 THR A 37 1 N LEU A 33 O ASP A 55 SHEET 3 A 4 VAL A 84 TYR A 87 1 O LEU A 86 N VAL A 36 SHEET 4 A 4 VAL A 115 ALA A 117 1 O ILE A 116 N ILE A 85 SHEET 1 B 2 ALA A 201 GLU A 206 0 SHEET 2 B 2 THR A 219 TRP A 224 1 O GLY A 221 N THR A 204 SHEET 1 C 2 LEU A 252 VAL A 254 0 SHEET 2 C 2 GLY A 276 VAL A 278 1 O GLY A 276 N LEU A 253 SHEET 1 D 4 VAL B 54 SER B 58 0 SHEET 2 D 4 LEU B 33 THR B 37 1 N LEU B 33 O ASP B 55 SHEET 3 D 4 VAL B 84 TYR B 87 1 O LEU B 86 N VAL B 36 SHEET 4 D 4 VAL B 115 ALA B 117 1 O ILE B 116 N ILE B 85 SHEET 1 E 2 ALA B 201 ILE B 203 0 SHEET 2 E 2 THR B 219 GLY B 221 1 O GLY B 221 N MET B 202 SHEET 1 F 2 LEU B 252 LEU B 253 0 SHEET 2 F 2 GLY B 276 GLU B 277 1 O GLY B 276 N LEU B 253 SHEET 1 G 4 LEU H 4 SER H 7 0 SHEET 2 G 4 LEU H 18 ALA H 24 -1 O ALA H 23 N VAL H 5 SHEET 3 G 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 G 4 PHE H 68 ALA H 72 -1 N THR H 69 O GLN H 82 SHEET 1 H 6 GLY H 10 VAL H 12 0 SHEET 2 H 6 THR H 122 VAL H 126 1 O THR H 125 N GLY H 10 SHEET 3 H 6 ALA H 92 SER H 100 -1 N ALA H 92 O VAL H 124 SHEET 4 H 6 SER H 31 GLN H 39 -1 N SER H 32 O GLN H 99 SHEET 5 H 6 LEU H 45 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 H 6 THR H 58 TYR H 60 -1 O TYR H 59 N SER H 50 SHEET 1 I 4 GLY H 10 VAL H 12 0 SHEET 2 I 4 THR H 122 VAL H 126 1 O THR H 125 N GLY H 10 SHEET 3 I 4 ALA H 92 SER H 100 -1 N ALA H 92 O VAL H 124 SHEET 4 I 4 TYR H 117 TRP H 118 -1 O TYR H 117 N ARG H 98 SHEET 1 J 4 SER H 135 LEU H 139 0 SHEET 2 J 4 THR H 150 TYR H 160 -1 O LEU H 156 N PHE H 137 SHEET 3 J 4 TYR H 191 PRO H 200 -1 O TYR H 191 N TYR H 160 SHEET 4 J 4 VAL H 178 THR H 180 -1 N HIS H 179 O VAL H 196 SHEET 1 K 4 SER H 135 LEU H 139 0 SHEET 2 K 4 THR H 150 TYR H 160 -1 O LEU H 156 N PHE H 137 SHEET 3 K 4 TYR H 191 PRO H 200 -1 O TYR H 191 N TYR H 160 SHEET 4 K 4 VAL H 184 LEU H 185 -1 N VAL H 184 O SER H 192 SHEET 1 L 3 THR H 166 TRP H 169 0 SHEET 2 L 3 ILE H 210 HIS H 215 -1 O ASN H 214 N THR H 166 SHEET 3 L 3 THR H 220 LYS H 225 -1 O THR H 220 N HIS H 215 SHEET 1 M 4 LEU X 4 SER X 7 0 SHEET 2 M 4 LEU X 18 ALA X 24 -1 O ALA X 23 N VAL X 5 SHEET 3 M 4 THR X 78 MET X 83 -1 O MET X 83 N LEU X 18 SHEET 4 M 4 PHE X 68 ALA X 72 -1 N THR X 69 O GLN X 82 SHEET 1 N 6 GLY X 10 VAL X 12 0 SHEET 2 N 6 THR X 122 VAL X 126 1 O THR X 125 N GLY X 10 SHEET 3 N 6 ALA X 92 SER X 100 -1 N ALA X 92 O VAL X 124 SHEET 4 N 6 SER X 31 GLN X 39 -1 N VAL X 37 O TYR X 95 SHEET 5 N 6 LEU X 45 TYR X 52 -1 O GLU X 46 N ARG X 38 SHEET 6 N 6 THR X 58 TYR X 60 -1 O TYR X 59 N SER X 50 SHEET 1 O 4 GLY X 10 VAL X 12 0 SHEET 2 O 4 THR X 122 VAL X 126 1 O THR X 125 N GLY X 10 SHEET 3 O 4 ALA X 92 SER X 100 -1 N ALA X 92 O VAL X 124 SHEET 4 O 4 TYR X 117 TRP X 118 -1 O TYR X 117 N ARG X 98 SHEET 1 P 4 SER X 135 LEU X 139 0 SHEET 2 P 4 THR X 150 TYR X 160 -1 O LEU X 156 N PHE X 137 SHEET 3 P 4 TYR X 191 PRO X 200 -1 O TYR X 191 N TYR X 160 SHEET 4 P 4 VAL X 178 THR X 180 -1 N HIS X 179 O VAL X 196 SHEET 1 Q 4 SER X 135 LEU X 139 0 SHEET 2 Q 4 THR X 150 TYR X 160 -1 O LEU X 156 N PHE X 137 SHEET 3 Q 4 TYR X 191 PRO X 200 -1 O TYR X 191 N TYR X 160 SHEET 4 Q 4 VAL X 184 LEU X 185 -1 N VAL X 184 O SER X 192 SHEET 1 R 3 THR X 166 TRP X 169 0 SHEET 2 R 3 ILE X 210 HIS X 215 -1 O ASN X 212 N SER X 168 SHEET 3 R 3 THR X 220 LYS X 225 -1 O VAL X 222 N VAL X 213 SHEET 1 S 4 MET L 4 SER L 7 0 SHEET 2 S 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 S 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 S 4 PHE L 62 SER L 65 -1 N SER L 63 O THR L 74 SHEET 1 T 6 SER L 10 SER L 14 0 SHEET 2 T 6 THR L 103 LYS L 108 1 O GLU L 106 N LEU L 11 SHEET 3 T 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 T 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 T 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 T 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 U 4 SER L 10 SER L 14 0 SHEET 2 U 4 THR L 103 LYS L 108 1 O GLU L 106 N LEU L 11 SHEET 3 U 4 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 U 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 90 SHEET 1 V 4 SER L 115 PHE L 119 0 SHEET 2 V 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 V 4 TYR L 174 SER L 183 -1 O TYR L 174 N PHE L 140 SHEET 4 V 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 W 4 ALA L 154 LEU L 155 0 SHEET 2 W 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 W 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 W 4 VAL L 206 ASN L 211 -1 O LYS L 208 N CYS L 195 SHEET 1 X 4 MET Y 4 SER Y 7 0 SHEET 2 X 4 VAL Y 19 ALA Y 25 -1 O THR Y 22 N SER Y 7 SHEET 3 X 4 ASP Y 70 ILE Y 75 -1 O PHE Y 71 N CYS Y 23 SHEET 4 X 4 PHE Y 62 SER Y 65 -1 N SER Y 63 O THR Y 74 SHEET 1 Y 6 SER Y 10 SER Y 14 0 SHEET 2 Y 6 THR Y 103 LYS Y 108 1 O LYS Y 108 N ALA Y 13 SHEET 3 Y 6 ALA Y 84 GLN Y 90 -1 N ALA Y 84 O VAL Y 105 SHEET 4 Y 6 VAL Y 33 GLN Y 38 -1 N TYR Y 36 O TYR Y 87 SHEET 5 Y 6 LYS Y 45 TYR Y 49 -1 O LEU Y 47 N TRP Y 35 SHEET 6 Y 6 SER Y 53 LEU Y 54 -1 O SER Y 53 N TYR Y 49 SHEET 1 Z 4 SER Y 10 SER Y 14 0 SHEET 2 Z 4 THR Y 103 LYS Y 108 1 O LYS Y 108 N ALA Y 13 SHEET 3 Z 4 ALA Y 84 GLN Y 90 -1 N ALA Y 84 O VAL Y 105 SHEET 4 Z 4 THR Y 98 PHE Y 99 -1 O THR Y 98 N GLN Y 90 SHEET 1 AA 4 SER Y 115 PHE Y 119 0 SHEET 2 AA 4 THR Y 130 PHE Y 140 -1 O LEU Y 136 N PHE Y 117 SHEET 3 AA 4 TYR Y 174 SER Y 183 -1 O TYR Y 174 N PHE Y 140 SHEET 4 AA 4 SER Y 160 VAL Y 164 -1 N GLN Y 161 O THR Y 179 SHEET 1 AB 4 ALA Y 154 LEU Y 155 0 SHEET 2 AB 4 LYS Y 146 VAL Y 151 -1 N VAL Y 151 O ALA Y 154 SHEET 3 AB 4 TYR Y 193 THR Y 198 -1 O ALA Y 194 N LYS Y 150 SHEET 4 AB 4 VAL Y 206 PHE Y 210 -1 O VAL Y 206 N VAL Y 197 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.07 SSBOND 2 CYS H 155 CYS H 211 1555 1555 2.04 SSBOND 3 CYS X 22 CYS X 96 1555 1555 2.09 SSBOND 4 CYS X 155 CYS X 211 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 6 CYS L 135 CYS L 195 1555 1555 2.02 SSBOND 7 CYS Y 23 CYS Y 88 1555 1555 2.05 SSBOND 8 CYS Y 135 CYS Y 195 1555 1555 2.04 CISPEP 1 ILE B 226 ASN B 227 0 -15.19 CISPEP 2 PHE H 161 PRO H 162 0 -8.26 CISPEP 3 GLU H 163 PRO H 164 0 -3.91 CISPEP 4 PHE X 161 PRO X 162 0 -8.85 CISPEP 5 GLU X 163 PRO X 164 0 -2.84 CISPEP 6 SER L 7 PRO L 8 0 1.45 CISPEP 7 TYR L 141 PRO L 142 0 1.21 CISPEP 8 SER Y 7 PRO Y 8 0 0.15 CISPEP 9 TYR Y 141 PRO Y 142 0 4.69 CRYST1 100.110 92.510 127.861 90.00 92.48 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 0.009989 0.000000 0.000433 0.00000 SCALE2 0.000000 0.010810 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007828 0.00000