REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 41695 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 2099 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3331 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 409 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.0 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.9 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 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.024 ; 0.02 REMARK 3 ANGLE DISTANCE (A) : 0.045 ; 0.04 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.066 ; 0.05 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.0284; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.288 ; 0.15 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.188 ; 0.3 REMARK 3 MULTIPLE TORSION (A) : 0.259 ; 0.3 REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : 0.0 ; 15.0 REMARK 3 PLANAR (DEGREES) : 8.2 ; 7.0 REMARK 3 STAGGERED (DEGREES) : 18.4 ; 15.0 REMARK 3 TRANSVERSE (DEGREES) : 21.6 ; 20.0 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.508 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.317 ; 3.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.148 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.378 ; 3.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1E4W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-00. REMARK 100 THE PDBE ID CODE IS EBI-5074. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-JUN-99 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.50 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG REMARK 200 BEAMLINE : BW6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.3 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : XRAY RESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39968 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 74.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 200 DATA REDUNDANCY : 9.900 REMARK 200 R MERGE (I) : 0.08100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 54.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.30 REMARK 200 R MERGE FOR SHELL (I) : 0.28800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.700 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: 1FBI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.1 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.0 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN IN TRIS-HCL, 8.5 REMARK 280 11-14 MG/ML REMARK 280 PRECIPITANT: 12% PEG MME 2000, 5 MM NICL2, REMARK 280 0.1 M TRIS-HCL, PH 8.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.61000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.89500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.17500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.89500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.61000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.17500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24000 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, P, 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 400 REMARK 400 COMPOUND REMARK 400 CHAIN P IS A CIRCULAR CLOSED HEPTAMER OF THE SEQUENCE REMARK 400 SER-HIS-PHE-ASN-GLU-TYR-GLU. THE N-ATOM OF SER-1 IS REMARK 400 COVALENTLY CONNECTED WITH CD OF GLU-7. REMARK 400 CHAIN L: THE C-TERMINAL REGION IS THE CONSTANT REGION REMARK 400 OF THE IG KAPPA LIGHT CHAIN, THE N-TERMINAL REGION REMARK 400 IS THE VARIABLE REGION OF THE IG KAPPA LIGHT CHAIN REMARK 400 THE VARIABLE REGION IS AUTOANTIBODY REACTIVE WITH SPECTRIN, REMARK 400 (4-HYRDOXY-3-NITROPHENYL) ACETYL, AND FLUORESCEIN, REMARK 400 WHICH PROMOTES CENTRAL NERVOUS SYSTEM REMYELINATION 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 GLU P 7 OE2 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 N SER P 1 - CD GLU P 7 1.32 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 PRO H 209 N PRO H 209 CD 0.095 REMARK 500 SER L 168 CA SER L 168 CB 0.094 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 VAL H 2 N - CA - CB ANGL. DEV. = 16.1 DEGREES REMARK 500 VAL H 37 CA - CB - CG1 ANGL. DEV. = 10.4 DEGREES REMARK 500 VAL H 37 CA - CB - CG2 ANGL. DEV. = 10.6 DEGREES REMARK 500 ARG H 56 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 SER H 95 CA - C - O ANGL. DEV. = -12.9 DEGREES REMARK 500 PRO H 96 C - N - CA ANGL. DEV. = 13.3 DEGREES REMARK 500 VAL H 147 N - CA - CB ANGL. DEV. = -14.9 DEGREES REMARK 500 SER H 157 CA - C - O ANGL. DEV. = -13.6 DEGREES REMARK 500 SER H 157 CA - C - N ANGL. DEV. = 20.6 DEGREES REMARK 500 VAL H 166 CG1 - CB - CG2 ANGL. DEV. = 9.9 DEGREES REMARK 500 ASP H 170 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES REMARK 500 LEU H 174 CA - CB - CG ANGL. DEV. = 19.1 DEGREES REMARK 500 VAL H 178 CB - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 ASP H 204 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 ASP L 1 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES REMARK 500 ASP L 1 OD1 - CG - OD2 ANGL. DEV. = -12.5 DEGREES REMARK 500 ASP L 1 O - C - N ANGL. DEV. = -13.0 DEGREES REMARK 500 LEU L 11 CA - CB - CG ANGL. DEV. = 16.1 DEGREES REMARK 500 ARG L 18 CD - NE - CZ ANGL. DEV. = 37.2 DEGREES REMARK 500 ARG L 18 NE - CZ - NH1 ANGL. DEV. = -8.9 DEGREES REMARK 500 ARG L 18 NE - CZ - NH2 ANGL. DEV. = 6.1 DEGREES REMARK 500 ASP L 28 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP L 41 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES REMARK 500 ASP L 41 CB - CG - OD2 ANGL. DEV. = -9.1 DEGREES REMARK 500 ARG L 61 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES REMARK 500 THR L 69 N - CA - CB ANGL. DEV. = -11.7 DEGREES REMARK 500 ARG L 108 CD - NE - CZ ANGL. DEV. = 45.0 DEGREES REMARK 500 ARG L 108 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG L 108 NE - CZ - NH2 ANGL. DEV. = 11.6 DEGREES REMARK 500 ARG L 108 NH1 - CZ - NH2 ANGL. DEV. = -14.7 DEGREES REMARK 500 ASP L 110 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES REMARK 500 ASP L 143 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES REMARK 500 ASP L 165 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 ARG L 188 NE - CZ - NH2 ANGL. DEV. = -8.3 DEGREES REMARK 500 HIS L 189 CE1 - NE2 - CD2 ANGL. DEV. = 8.2 DEGREES REMARK 500 ARG L 211 NE - CZ - NH2 ANGL. DEV. = -3.4 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 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 VAL H 2 80.62 82.36 REMARK 500 ALA H 88 172.58 178.35 REMARK 500 ASP H 127 126.54 163.60 REMARK 500 SER H 169 -129.36 83.55 REMARK 500 HIS L 31 -2.99 72.41 REMARK 500 THR L 51 -52.15 72.45 REMARK 500 ALA L 84 -171.51 -171.10 REMARK 500 GLU L 213 106.86 -43.51 REMARK 500 REMARK 500 REMARK: NULL 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 95 PRO H 96 40.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER H 95 18.95 REMARK 500 ARG L 188 11.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 VAL H 147 47.5 L L OUTSIDE RANGE 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 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 NI L 901 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP L 1 O REMARK 620 2 HOH L2009 O 84.3 REMARK 620 3 ASP L 1 N 76.5 160.0 REMARK 620 4 ASP L 1 OD1 86.5 97.2 87.4 REMARK 620 5 HOH L2003 O 82.8 73.8 97.8 166.6 REMARK 620 6 HIS L 189 NE2 173.5 93.7 105.9 87.7 102.6 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI L 901 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL P 901 REMARK 900 REMARK 900 RELATED ID: 1E4X RELATED DB: PDB REMARK 900 CROSSREACTIVE BINDING OF A CIRCULARIZED PEPTIDE TO AN REMARK 900 ANTI-TGFALPHA ANTIBODY FAB-FRAGMENT REMARK 900 RELATED ID: 1FBI RELATED DB: PDB REMARK 900 FAB FRAGMENT OF THE MONOCLONAL ANTIBODY F9.13.7 (IGG1) REMARK 900 COMPLEXED WITH LYSOZYME