REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.LAUWEREYS,M.ARBABI GHAHROUDI,A DESMYTER,J.KINNE, REMARK 1 AUTH 2 W.HOLZER,E.DE GENST,L.WYNS,S.MUYLDERMANS REMARK 1 TITL POTENT ENZYME INHIBITORS DERIVED FROM DROMEDARY REMARK 1 TITL 2 HEAVY-CHAIN ANTIBODIES. REMARK 1 REF EMBO J. V. 17 3512 1998 REMARK 1 REFN ISSN 0261-4189 REMARK 1 DOI 10.1093/EMBOJ/17.13.3512 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.QIAN,R.HASER,F.PAYAN REMARK 1 TITL STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG REMARK 1 TITL 2 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 231 785 1993 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1993.1326 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.9 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.79 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1735909.730 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 317086 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 SET) : 0.197 REMARK 3 FREE R VALUE : 0.219 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000 REMARK 3 FREE R VALUE TEST SET COUNT : 9426 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 29934 REMARK 3 BIN R VALUE (WORKING SET) : 0.2580 REMARK 3 BIN FREE R VALUE : 0.2780 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 913 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 19304 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 2807 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.49000 REMARK 3 B22 (A**2) : -1.66000 REMARK 3 B33 (A**2) : -1.83000 REMARK 3 B12 (A**2) : -2.22000 REMARK 3 B13 (A**2) : -2.35000 REMARK 3 B23 (A**2) : 0.85000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19 REMARK 3 ESD FROM SIGMAA (A) : 0.16 REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.21 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.50 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.92 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.38 REMARK 3 BSOL : 48.68 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : ION.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KXQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-02. REMARK 100 THE RCSB ID CODE IS RCSB015445. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-00 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID09 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 : MIRRORS REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 383526 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.06400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 70.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.32200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 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: PDB ENTRY 1JFH, PDB ENTRY 1QD0 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE BUFFER 0.8 M, PH 7.0, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER E 120 OG REMARK 470 SER F 120 OG REMARK 470 SER G 120 OG REMARK 470 SER H 120 OG 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 OE2 GLU A 352 OD1 ASN H 97 1.75 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 CYS A 70 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES REMARK 500 LEU A 293 CA - CB - CG ANGL. DEV. = -16.2 DEGREES REMARK 500 CYS B 70 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 ARG C 72 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES REMARK 500 CYS D 70 CA - CB - SG ANGL. DEV. = 7.4 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 TYR A 31 -57.52 -146.04 REMARK 500 MET A 102 -153.47 -108.19 REMARK 500 VAL A 163 51.50 36.61 REMARK 500 ASP A 317 58.98 -118.55 REMARK 500 SER A 414 -105.59 -132.25 REMARK 500 ASP A 433 32.51 -87.52 REMARK 500 ASN A 460 49.88 -97.21 REMARK 500 PRO A 486 47.01 -76.66 REMARK 500 TYR B 31 -57.24 -149.75 REMARK 500 SER B 66 -179.57 -172.60 REMARK 500 MET B 102 -156.98 -109.77 REMARK 500 VAL B 163 47.48 37.66 REMARK 500 SER B 414 -109.71 -132.91 REMARK 500 ASP B 433 35.49 -90.50 REMARK 500 ASN B 460 40.35 -105.43 REMARK 500 PRO B 486 38.83 -74.71 REMARK 500 TYR C 31 -56.42 -142.82 REMARK 500 MET C 102 -155.88 -109.34 REMARK 500 VAL C 163 49.12 37.50 REMARK 500 ASP C 317 59.65 -115.43 REMARK 500 THR C 376 4.74 82.03 REMARK 500 SER C 414 -110.38 -133.91 REMARK 500 ASP C 433 32.79 -88.13 REMARK 500 PRO C 486 45.43 -79.12 REMARK 500 TYR D 31 -57.48 -141.20 REMARK 500 MET D 102 -145.14 -107.70 REMARK 500 VAL D 163 47.82 37.12 REMARK 500 SER D 414 -109.61 -129.54 REMARK 500 ASP D 433 37.26 -93.16 REMARK 500 PRO D 486 41.14 -77.99 REMARK 500 ASN E 97 16.76 -146.64 REMARK 500 ARG E 100 72.84 -104.91 REMARK 500 VAL F 2 99.90 -179.95 REMARK 500 PRO F 38 107.21 -35.30 REMARK 500 ASN F 97 21.73 -145.81 REMARK 500 ARG F 100 72.43 -119.49 REMARK 500 VAL G 2 103.05 -168.87 REMARK 500 ASN G 97 20.90 -144.42 REMARK 500 ARG G 100 74.15 -105.28 REMARK 500 ASN H 97 19.37 -146.62 REMARK 500 ARG H 100 72.62 -111.15 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 E 208 DISTANCE = 5.14 ANGSTROMS REMARK 525 HOH G 219 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH E 258 DISTANCE = 5.15 ANGSTROMS REMARK 525 HOH C4271 DISTANCE = 5.43 ANGSTROMS REMARK 525 HOH C4273 DISTANCE = 5.33 ANGSTROMS REMARK 525 HOH C4394 DISTANCE = 7.93 ANGSTROMS REMARK 525 HOH C4403 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH C4427 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH C4432 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH C4447 DISTANCE = 8.36 ANGSTROMS REMARK 525 HOH B4498 DISTANCE = 6.91 ANGSTROMS REMARK 525 HOH B4529 DISTANCE = 5.12 ANGSTROMS REMARK 525 HOH D4642 DISTANCE = 9.26 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A4001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 167 OD1 REMARK 620 2 HOH A4094 O 73.5 REMARK 620 3 ARG A 158 O 120.5 76.3 REMARK 620 4 ASP A 167 OD2 52.6 86.5 75.8 REMARK 620 5 HOH A4014 O 76.2 149.6 120.9 75.4 REMARK 620 6 HOH A4125 O 137.2 143.5 70.3 98.9 64.8 REMARK 620 7 ASN A 100 OD1 79.4 102.1 157.4 126.7 71.5 103.1 REMARK 620 8 HIS A 201 O 138.4 80.6 82.7 157.0 123.8 81.0 74.9 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B4003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B4307 O REMARK 620 2 ASN B 100 OD1 72.2 REMARK 620 3 ASP B 167 OD1 74.6 82.4 REMARK 620 4 HIS B 201 O 125.1 73.7 139.9 REMARK 620 5 HOH B4012 O 62.0 98.6 133.5 82.5 REMARK 620 6 HOH B4030 O 145.9 100.2 71.4 81.5 150.7 REMARK 620 7 ASP B 167 OD2 71.9 128.4 53.0 157.6 95.9 89.7 REMARK 620 8 ARG B 158 O 121.8 154.6 120.5 81.1 74.2 79.2 77.0 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C4005 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 100 OD1 REMARK 620 2 ASP C 167 OD1 80.9 REMARK 620 3 ASP C 167 OD2 127.6 52.6 REMARK 620 4 HOH C4047 O 103.1 73.3 86.7 REMARK 620 5 HOH C4060 O 99.8 136.0 99.1 145.6 REMARK 620 6 HIS C 201 O 73.8 139.2 157.8 81.9 80.4 REMARK 620 7 ARG C 158 O 155.9 121.5 76.4 77.7 71.0 82.5 REMARK 620 8 HOH C4022 O 70.6 74.5 74.5 147.8 64.8 123.6 121.1 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D4007 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS D 201 O REMARK 620 2 HOH D4041 O 82.3 REMARK 620 3 ASP D 167 OD2 156.9 88.4 REMARK 620 4 ASN D 100 OD1 75.9 99.8 126.7 REMARK 620 5 ASP D 167 OD1 140.4 70.5 52.5 80.8 REMARK 620 6 HOH D4038 O 79.7 147.6 97.9 101.6 136.9 REMARK 620 7 HOH D4016 O 124.1 147.2 73.1 72.4 76.7 63.6 REMARK 620 8 ARG D 158 O 80.7 78.4 76.8 156.5 119.6 72.3 121.2 REMARK 620 N 1 2 3 4 5 6 7 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4001 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4002 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4003 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4004 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 4005 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4006 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 4007 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4008 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KXT RELATED DB: PDB REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC REMARK 900 ALPHA-AMYLASE REMARK 900 RELATED ID: 1KXV RELATED DB: PDB REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC REMARK 900 ALPHA-AMYLASE REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE DISCREPANCY BETWEEN THE SEQUENCE OF THIS REMARK 999 ENTRY AND THE DATABASE REFERENCE IS EXPLAINED REMARK 999 IN REFERENCE 2 GIVEN ABOVE. REMARK 999 REMARK 999 REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE REMARK 999 FOR THE ANTIBODY VHH FRAGMENT CABAMD9, CHAINS REMARK 999 E, F, G, AND H, WAS NOT AVAILABLE AT THE TIME REMARK 999 OF PROCESSING.