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HEADER IMMUNE SYSTEM 04-MAR-03 1OP3 TITLE CRYSTAL STRUCTURE OF FAB 2G12 BOUND TO MAN1->2MAN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 2G12, LIGHT CHAIN; COMPND 3 CHAIN: L, K; COMPND 4 FRAGMENT: LIGHT CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB 2G12, HEAVY CHAIN; COMPND 8 CHAIN: H, M; COMPND 9 FRAGMENT: HEAVY CHAIN; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 6 EXPRESSION_SYSTEM_ORGAN: OVARY; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 12 EXPRESSION_SYSTEM_ORGAN: OVARY KEYWDS DOMAIN-SWAPPED FAB 2G12; ANTI-CARBOHYDRATE ANTIBODY EXPDTA X-RAY DIFFRACTION AUTHOR D.A.CALARESE,C.N.SCANLAN,M.B.ZWICK,S.DEECHONGKIT,Y.MIMURA, AUTHOR 2 R.KUNERT,R.L.STANFIELD,J.W.KELLY,P.M.RUDD,R.A.DWEK, AUTHOR 3 H.KATINGER,D.R.BURTON,I.A.WILSON REVDAT 1 15-JUL-03 1OP3 0 JRNL AUTH D.A.CALARESE,C.N.SCANLAN,M.B.ZWICK,S.DEECHONGKIT, JRNL AUTH 2 Y.MIMURA,R.KUNERT,P.ZHU,M.R.WORMALD,R.L.STANFIELD, JRNL AUTH 3 K.H.ROUX,J.W.KELLY,P.M.RUDD,R.A.DWEK,H.KATINGER, JRNL AUTH 4 D.R.BURTON,I.A.WILSON JRNL TITL ANTIBODY DOMAIN EXCHANGE IS AN IMMUNOLOGICAL JRNL TITL 2 SOLUTION TO CARBOHYDRATE CLUSTER RECOGNITION. JRNL REF SCIENCE V. 300 2065 2003 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7 REMARK 3 NUMBER OF REFLECTIONS : 119708 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 6410 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW : 1.79 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6684 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.4260 REMARK 3 BIN FREE R VALUE SET COUNT : NULL REMARK 3 BIN FREE R VALUE : 0.4370 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 7114 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.54000 REMARK 3 B22 (A**2) : 2.27000 REMARK 3 B33 (A**2) : -3.81000 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 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.115 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.824 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6683 ; 0.014 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9071 ; 1.300 ; 1.954 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 836 ; 6.464 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1047 ; 0.089 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4927 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2766 ; 0.221 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 542 ; 0.124 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 41 ; 0.175 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.121 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4235 ; 0.528 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6837 ; 1.053 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2448 ; 1.774 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2234 ; 2.685 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 114 REMARK 3 ORIGIN FOR THE GROUP (A): -1.8392 46.4879 41.1493 REMARK 3 T TENSOR REMARK 3 T11: 0.0757 T22: 0.1671 REMARK 3 T33: 0.1469 T12: 0.0187 REMARK 3 T13: -0.0295 T23: -0.0832 REMARK 3 L TENSOR REMARK 3 L11: 2.2113 L22: 2.3854 REMARK 3 L33: 3.2826 L12: -1.7180 REMARK 3 L13: -1.3910 L23: 2.3239 REMARK 3 S TENSOR REMARK 3 S11: -0.0346 S12: 0.0082 S13: -0.0255 REMARK 3 S21: -0.1296 S22: -0.1170 S23: 0.2194 REMARK 3 S31: 0.0016 S32: -0.3462 S33: 0.1516 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 115 L 211 REMARK 3 ORIGIN FOR THE GROUP (A): 24.9975 29.4603 52.7624 REMARK 3 T TENSOR REMARK 3 T11: 0.5871 T22: 0.4441 REMARK 3 T33: 0.3033 T12: 0.2293 REMARK 3 T13: -0.2035 T23: -0.0848 REMARK 3 L TENSOR REMARK 3 L11: 4.2189 L22: 4.5868 REMARK 3 L33: 10.5891 L12: 0.5371 REMARK 3 L13: 3.0495 L23: 0.4955 REMARK 3 S TENSOR REMARK 3 S11: 0.2276 S12: -0.4748 S13: -0.4274 REMARK 3 S21: 1.1192 S22: 0.1560 S23: -0.8708 REMARK 3 S31: 1.5103 S32: 0.9812 S33: -0.3836 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 113 REMARK 3 ORIGIN FOR THE GROUP (A): 1.0280 55.9122 60.6815 REMARK 3 T TENSOR REMARK 3 T11: 0.0128 T22: 0.0806 REMARK 3 T33: 0.1094 T12: 0.0311 REMARK 3 T13: -0.0166 T23: -0.0540 REMARK 3 L TENSOR REMARK 3 L11: 1.8536 L22: 2.4297 REMARK 3 L33: 2.7580 L12: -0.4768 REMARK 3 L13: 0.2808 L23: 0.8609 REMARK 3 S TENSOR REMARK 3 S11: 0.0721 S12: 0.1788 S13: -0.0606 REMARK 3 S21: -0.0787 S22: -0.1110 S23: 0.0438 REMARK 3 S31: -0.0197 S32: 0.0059 S33: 0.0388 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 114 H 228 REMARK 3 ORIGIN FOR THE GROUP (A): 26.6486 36.5367 91.6306 REMARK 3 T TENSOR REMARK 3 T11: 0.5193 T22: 0.1098 REMARK 3 T33: 0.3808 T12: 0.0002 REMARK 3 T13: -0.2446 T23: 0.0183 REMARK 3 L TENSOR REMARK 3 L11: 4.0725 L22: 1.7792 REMARK 3 L33: 6.6695 L12: -0.0026 REMARK 3 L13: 2.9315 L23: 0.5165 REMARK 3 S TENSOR REMARK 3 S11: 0.8198 S12: -0.1796 S13: -0.8679 REMARK 3 S21: -0.0278 S22: -0.3410 S23: 0.1490 REMARK 3 S31: 1.0005 S32: -0.1095 S33: -0.4788 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : K 1 K 114 REMARK 3 ORIGIN FOR THE GROUP (A): 16.0229 70.1729 99.6137 REMARK 3 T TENSOR REMARK 3 T11: 0.0563 T22: 0.0719 REMARK 3 T33: 0.0964 T12: -0.0187 REMARK 3 T13: -0.0043 T23: -0.0059 REMARK 3 L TENSOR REMARK 3 L11: 2.2710 L22: 1.4221 REMARK 3 L33: 1.4739 L12: -1.3834 REMARK 3 L13: 1.3138 L23: -0.7515 REMARK 3 S TENSOR REMARK 3 S11: -0.0388 S12: -0.1966 S13: 0.0605 REMARK 3 S21: 0.0385 S22: -0.0157 S23: 0.0483 REMARK 3 S31: -0.1139 S32: -0.1070 S33: 0.0545 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : K 115 K 211 REMARK 3 ORIGIN FOR THE GROUP (A): 38.8533 47.2460 88.8508 REMARK 3 T TENSOR REMARK 3 T11: 0.3069 T22: 0.1170 REMARK 3 T33: 0.1677 T12: 0.0937 REMARK 3 T13: -0.0300 T23: -0.0050 REMARK 3 L TENSOR REMARK 3 L11: 2.5614 L22: 3.8903 REMARK 3 L33: 2.6599 L12: -1.7083 REMARK 3 L13: -0.3183 L23: 1.7975 REMARK 3 S TENSOR REMARK 3 S11: 0.4988 S12: 0.4293 S13: -0.2694 REMARK 3 S21: -0.6603 S22: -0.2824 S23: -0.1833 REMARK 3 S31: 0.1541 S32: 0.0096 S33: -0.2164 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : M 1 M 113 REMARK 3 ORIGIN FOR THE GROUP (A): 8.6381 65.8270 79.4512 REMARK 3 T TENSOR REMARK 3 T11: 0.0090 T22: 0.0255 REMARK 3 T33: 0.0802 T12: 0.0065 REMARK 3 T13: -0.0097 T23: -0.0169 REMARK 3 L TENSOR REMARK 3 L11: 2.7084 L22: 1.9417 REMARK 3 L33: 2.3990 L12: -0.5499 REMARK 3 L13: 0.6582 L23: 0.3475 REMARK 3 S TENSOR REMARK 3 S11: -0.0290 S12: 0.0018 S13: -0.0512 REMARK 3 S21: 0.0973 S22: 0.0075 S23: 0.0282 REMARK 3 S31: 0.0419 S32: -0.0287 S33: 0.0215 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : M 114 M 228 REMARK 3 ORIGIN FOR THE GROUP (A): 33.3614 43.7050 49.7625 REMARK 3 T TENSOR REMARK 3 T11: 0.1509 T22: 0.7934 REMARK 3 T33: 0.4496 T12: 0.0544 REMARK 3 T13: -0.0189 T23: -0.3879 REMARK 3 L TENSOR REMARK 3 L11: 3.0517 L22: 4.1969 REMARK 3 L33: 8.8359 L12: -0.4824 REMARK 3 L13: -0.4664 L23: 4.4060 REMARK 3 S TENSOR REMARK 3 S11: -0.1343 S12: 0.2114 S13: 0.0541 REMARK 3 S21: -0.1034 S22: 1.1255 S23: -1.0103 REMARK 3 S31: 0.0788 S32: 1.8121 S33: -0.9912 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OP3 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB018526. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUL-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.984 REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT REMARK 200 MONOCHROMATOR (HORIZONTAL REMARK 200 FOCUSING) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126453 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07400 REMARK 200 FOR THE DATA SET : 41.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78 REMARK 200 COMPLETENESS FOR SHELL (%) : 68.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.40700 REMARK 200 FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA/K PHOSPHATE, PH 7.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 320K 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 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.86250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.59350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.01700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.59350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.86250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.01700 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: L, H, K, M 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 GLU L 213 REMARK 465 SER H 229 REMARK 465 GLU K 213 REMARK 465 SER M 229 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 REMARK 500 CA SER H 128 O HOH 399 1.12 REMARK 500 C SER H 128 O HOH 399 1.14 REMARK 500 O SER H 128 O HOH 399 1.49 REMARK 500 CB SER H 128 O HOH 399 1.52 REMARK 500 CA SER M 130 O HOH 390 1.59 REMARK 500 NZ LYS H 129 O HOH 447 1.83 REMARK 500 N SER M 130 O HOH 390 2.14 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO L 119 C PRO L 119 O 0.246 REMARK 500 PRO L 119 C PRO L 120 N 0.115 REMARK 500 SER L 121 CB SER L 121 OG 0.322 REMARK 500 SER L 131 CB SER L 131 OG 0.157 REMARK 500 SER L 182 CB SER L 182 OG 0.108 REMARK 500 MET H 82C SD MET H 82C CE -0.257 REMARK 500 SER H 128 N SER H 128 CA -0.177 REMARK 500 SER H 127 C SER H 128 N -0.331 REMARK 500 VAL H 154 C SER H 156 N 0.394 REMARK 500 LYS K 183 C LYS K 183 O 0.116 REMARK 500 MET M 82C SD MET M 82C CE -0.229 REMARK 500 PRO M 123 C PRO M 123 O 0.106 REMARK 500 ALA M 125 C PRO M 126 N -0.566 REMARK 500 GLY M 135 C GLY M 136 N -0.134 REMARK 500 THR M 137 C THR M 137 O 0.131 REMARK 500 THR M 137 C ALA M 138 N 0.128 REMARK 500 ALA M 139 C ALA M 139 O 0.126 REMARK 500 ALA M 139 C LEU M 140 N 0.111 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 SER H 128 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 SER H 127 O - C - N ANGL. DEV. =-17.3 DEGREES REMARK 500 LEU K 78 CA - CB - CG ANGL. DEV. = 9.8 DEGREES REMARK 500 PRO M 126 CB - CA - C ANGL. DEV. =-12.5 DEGREES REMARK 500 ALA M 125 CA - C - N ANGL. DEV. = 28.6 DEGREES REMARK 500 ALA M 125 O - C - N ANGL. DEV. =-27.8 DEGREES REMARK 500 PRO M 126 C - N - CA ANGL. DEV. = 16.1 DEGREES REMARK 500 PRO M 126 C - N - CD ANGL. DEV. =-21.0 DEGREES REMARK 500 LYS M 129 CB - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 500 SER M 134 CB - CA - C ANGL. DEV. = 11.0 DEGREES REMARK 500 GLY M 135 O - C - N ANGL. DEV. =-12.7 DEGREES REMARK 500 GLY M 136 C - N - CA ANGL. DEV. = 25.3 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ALA L 51 -44.46 69.32 REMARK 500 SER H 130 -78.06 64.57 REMARK 500 SER H 134 -64.64 123.19 REMARK 500 ALA K 51 -40.82 71.50 REMARK 500 LEU M 100 120.76 92.20 REMARK 500 SER M 130 -74.16 65.96 REMARK 500 SER M 134 -90.84 125.03 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER H 127 SER H 128 -133.52 REMARK 500 LYS H 129 SER H 130 137.52 REMARK 500 SER H 130 THR H 133 -124.73 REMARK 500 LYS M 129 SER M 130 145.62 REMARK 500 SER M 130 THR M 133 -135.62 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OM3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FAB 2G12 UNLIGANDED REMARK 900 RELATED ID: 1OP5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FAB 2G12 BOUND TO MAN9GLCNAC2 LIGAND SEQRES 1 L 212 VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 L 212 VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER GLN SEQRES 3 L 212 SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 L 212 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 L 212 LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 L 212 SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU GLN SEQRES 7 L 212 PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR ALA SEQRES 8 L 212 GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL GLU SEQRES 9 L 212 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 212 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 212 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 212 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 212 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 212 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 212 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 212 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 212 ASN ARG GLY GLU SEQRES 1 H 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 225 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN SEQRES 3 H 225 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG SEQRES 4 H 225 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 H 225 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS SEQRES 6 H 225 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE SEQRES 7 H 225 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR SEQRES 8 H 225 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU SEQRES 9 H 225 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR SEQRES 10 H 225 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 H 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 225 GLU PRO LYS SER SEQRES 1 K 212 VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 K 212 VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER GLN SEQRES 3 K 212 SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 K 212 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 K 212 LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 K 212 SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU GLN SEQRES 7 K 212 PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR ALA SEQRES 8 K 212 GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL GLU SEQRES 9 K 212 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 K 212 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 K 212 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 K 212 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 K 212 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 K 212 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 K 212 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 K 212 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 K 212 ASN ARG GLY GLU SEQRES 1 M 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 M 225 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN SEQRES 3 M 225 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG SEQRES 4 M 225 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 M 225 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS SEQRES 6 M 225 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE SEQRES 7 M 225 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR SEQRES 8 M 225 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU SEQRES 9 M 225 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR SEQRES 10 M 225 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 M 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 M 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 M 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 M 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 M 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 M 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 M 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 M 225 GLU PRO LYS SER HET MAN 501 12 HET MAN 502 11 HET MAN 503 12 HET BEZ 504 9 HETNAM MAN ALPHA-D-MANNOSE HETNAM BEZ BENZOIC ACID FORMUL 5 MAN 3(C6 H12 O6) FORMUL 7 BEZ C7 H6 O2 FORMUL 8 HOH *484(H2 O) HELIX 1 1 GLN L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 LYS L 126 1 6 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 ARG H 28 HIS H 32 5 5 HELIX 5 5 THR H 52A THR H 55 5 4 HELIX 6 6 ARG H 83 THR H 87 5 5 HELIX 7 7 TRP H 157 TRP H 157 5 1 HELIX 8 8 ASN H 162 ALA H 165 5 4 HELIX 9 9 SER H 196 LEU H 198 5 3 HELIX 10 10 LYS H 213 ASN H 216 5 4 HELIX 11 11 GLN K 79 PHE K 83 5 5 HELIX 12 12 SER K 121 SER K 127 1 7 HELIX 13 13 LYS K 183 GLU K 187 1 5 HELIX 14 14 ARG M 28 HIS M 32 5 5 HELIX 15 15 THR M 52A THR M 55 5 4 HELIX 16 16 ARG M 83 THR M 87 5 5 HELIX 17 17 TRP M 157 TRP M 157 5 1 HELIX 18 18 ASN M 162 ALA M 165 5 4 HELIX 19 19 SER M 196 GLY M 199 5 4 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 THR L 18 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 A 4 GLU L 70 SER L 76 -1 O LEU L 73 N ILE L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 B 5 THR L 53 LEU L 54 0 SHEET 2 B 5 LYS L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 B 5 THR L 85 TYR L 91 -1 O HIS L 87 N TYR L 36 SHEET 5 B 5 ALA L 96 PHE L 98 -1 O THR L 97 N HIS L 90 SHEET 1 C 6 THR L 53 LEU L 54 0 SHEET 2 C 6 LYS L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 C 6 THR L 85 TYR L 91 -1 O HIS L 87 N TYR L 36 SHEET 5 C 6 THR L 102 ILE L 106 -1 O THR L 102 N TYR L 86 SHEET 6 C 6 THR L 10 ALA L 13 1 N LEU L 11 O ARG L 103 SHEET 1 D 4 SER L 114 PHE L 118 0 SHEET 2 D 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 D 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 D 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 E 3 ALA L 144 VAL L 150 0 SHEET 2 E 3 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 3 E 3 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 F 4 GLN H 3 SER H 7 0 SHEET 2 F 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 F 4 PHE H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 F 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 G 6 GLY H 10 LYS H 13 0 SHEET 2 G 6 THR H 107 SER H 112 1 O THR H 110 N GLY H 10 SHEET 3 G 6 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 G 6 MET H 34 ARG H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 G 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 G 6 ARG H 57 TYR H 59 -1 O ASP H 58 N SER H 50 SHEET 1 H 4 GLY H 10 LYS H 13 0 SHEET 2 H 4 THR H 107 SER H 112 1 O THR H 110 N GLY H 10 SHEET 3 H 4 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 I 4 TYR H 185 PRO H 194 -1 O LEU H 187 N VAL H 144 SHEET 4 I 4 HIS H 172 THR H 173 -1 N HIS H 172 O VAL H 190 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 J 4 TYR H 185 PRO H 194 -1 O LEU H 187 N VAL H 144 SHEET 4 J 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186 SHEET 1 K 3 THR H 153 SER H 156 0 SHEET 2 K 3 CYS H 208 HIS H 212 -1 O ASN H 211 N THR H 153 SHEET 3 K 3 THR H 217 LYS H 221 -1 O THR H 217 N HIS H 212 SHEET 1 L 4 MET K 4 SER K 7 0 SHEET 2 L 4 THR K 18 ALA K 25 -1 O THR K 22 N SER K 7 SHEET 3 L 4 GLU K 70 SER K 76 -1 O LEU K 73 N ILE K 21 SHEET 4 L 4 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 M 5 THR K 53 LEU K 54 0 SHEET 2 M 5 LYS K 45 TYR K 49 -1 N TYR K 49 O THR K 53 SHEET 3 M 5 LEU K 33 GLN K 38 -1 N TRP K 35 O LEU K 47 SHEET 4 M 5 THR K 85 TYR K 91 -1 O THR K 85 N GLN K 38 SHEET 5 M 5 ALA K 96 PHE K 98 -1 O THR K 97 N HIS K 90 SHEET 1 N 6 THR K 53 LEU K 54 0 SHEET 2 N 6 LYS K 45 TYR K 49 -1 N TYR K 49 O THR K 53 SHEET 3 N 6 LEU K 33 GLN K 38 -1 N TRP K 35 O LEU K 47 SHEET 4 N 6 THR K 85 TYR K 91 -1 O THR K 85 N GLN K 38 SHEET 5 N 6 THR K 102 ILE K 106 -1 O THR K 102 N TYR K 86 SHEET 6 N 6 THR K 10 ALA K 13 1 N LEU K 11 O ARG K 103 SHEET 1 O 4 SER K 114 PHE K 118 0 SHEET 2 O 4 THR K 129 PHE K 139 -1 O LEU K 135 N PHE K 116 SHEET 3 O 4 TYR K 173 SER K 182 -1 O LEU K 179 N VAL K 132 SHEET 4 O 4 SER K 159 VAL K 163 -1 N GLN K 160 O THR K 178 SHEET 1 P 4 ALA K 153 LEU K 154 0 SHEET 2 P 4 LYS K 145 VAL K 150 -1 N VAL K 150 O ALA K 153 SHEET 3 P 4 VAL K 191 THR K 197 -1 O GLU K 195 N GLN K 147 SHEET 4 P 4 VAL K 205 ASN K 210 -1 O VAL K 205 N VAL K 196 SHEET 1 Q 4 GLN M 3 SER M 7 0 SHEET 2 Q 4 LEU M 18 SER M 25 -1 O SER M 21 N SER M 7 SHEET 3 Q 4 PHE M 77 MET M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 Q 4 PHE M 67 ASP M 72 -1 N ASP M 72 O PHE M 77 SHEET 1 R 6 GLY M 10 LYS M 13 0 SHEET 2 R 6 THR M 107 SER M 112 1 O THR M 110 N VAL M 12 SHEET 3 R 6 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107 SHEET 4 R 6 MET M 34 ARG M 39 -1 N VAL M 37 O TYR M 91 SHEET 5 R 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 R 6 ARG M 57 TYR M 59 -1 O ASP M 58 N SER M 50 SHEET 1 S 4 GLY M 10 LYS M 13 0 SHEET 2 S 4 THR M 107 SER M 112 1 O THR M 110 N VAL M 12 SHEET 3 S 4 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107 SHEET 1 T 4 SER M 120 LEU M 124 0 SHEET 2 T 4 THR M 137 TYR M 147 -1 O LYS M 145 N SER M 120 SHEET 3 T 4 TYR M 185 PRO M 194 -1 O LEU M 187 N VAL M 144 SHEET 4 T 4 VAL M 171 THR M 173 -1 N HIS M 172 O VAL M 190 SHEET 1 U 4 SER M 120 LEU M 124 0 SHEET 2 U 4 THR M 137 TYR M 147 -1 O LYS M 145 N SER M 120 SHEET 3 U 4 TYR M 185 PRO M 194 -1 O LEU M 187 N VAL M 144 SHEET 4 U 4 VAL M 177 LEU M 178 -1 N VAL M 177 O SER M 186 SHEET 1 V 2 CYS M 208 HIS M 212 0 SHEET 2 V 2 THR M 217 LYS M 221 -1 O VAL M 219 N VAL M 210 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 142 CYS H 208 SSBOND 5 CYS K 23 CYS K 88 SSBOND 6 CYS K 134 CYS K 194 SSBOND 7 CYS M 22 CYS M 92 SSBOND 8 CYS M 142 CYS M 208 LINK O2 MAN 501 C1 MAN 502 CISPEP 1 SER L 7 PRO L 8 0 -4.40 CISPEP 2 TYR L 140 PRO L 141 0 1.73 CISPEP 3 PHE H 148 PRO H 149 0 -6.63 CISPEP 4 GLU H 150 PRO H 151 0 -2.52 CISPEP 5 SER K 7 PRO K 8 0 -3.92 CISPEP 6 TYR K 140 PRO K 141 0 0.21 CISPEP 7 PHE M 148 PRO M 149 0 -8.13 CISPEP 8 GLU M 150 PRO M 151 0 -5.22 CRYST1 81.725 94.034 169.187 90.00 90.00 90.00 P 21 21 21 8 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 0.012236 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010634 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005911 0.00000