REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 85066 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) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4480 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6256 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.38 REMARK 3 BIN R VALUE (WORKING SET) : 0.3290 REMARK 3 BIN FREE R VALUE SET COUNT : 316 REMARK 3 BIN FREE R VALUE : 0.3820 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 22435 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 368 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.25000 REMARK 3 B22 (A**2) : -0.18000 REMARK 3 B33 (A**2) : -4.81000 REMARK 3 B12 (A**2) : -0.99000 REMARK 3 B13 (A**2) : 5.47000 REMARK 3 B23 (A**2) : 1.39000 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): 0.409 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.335 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.896 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23435 ; 0.007 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 31789 ; 1.262 ; 1.978 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2911 ; 6.649 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 996 ;36.030 ;24.458 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3703 ;18.426 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;19.543 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3550 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17752 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 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 3VI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-11. REMARK 100 THE RCSB ID CODE IS RCSB095071. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-APR-10 REMARK 200 TEMPERATURE (KELVIN) : 90 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-17A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90446 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 116.390 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 2.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06100 REMARK 200 FOR THE DATA SET : 11.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.46200 REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS (PH6.5), 20%(W/V) REMARK 280 PEG8000, 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 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, L, 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 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 LEU A 602 REMARK 465 ASP A 603 REMARK 465 CYS A 604 REMARK 465 GLY A 605 REMARK 465 GLU A 606 REMARK 465 ASP A 607 REMARK 465 ASN A 608 REMARK 465 ILE A 609 REMARK 465 CYS A 610 REMARK 465 VAL A 611 REMARK 465 PRO A 612 REMARK 465 ASP A 613 REMARK 465 LEU A 614 REMARK 465 GLN A 615 REMARK 465 LEU A 616 REMARK 465 GLU A 617 REMARK 465 VAL A 618 REMARK 465 PHE A 619 REMARK 465 GLY A 620 REMARK 465 GLU A 621 REMARK 465 GLN A 622 REMARK 465 ASN A 623 REMARK 465 GLY A 624 REMARK 465 GLY A 625 REMARK 465 LEU A 626 REMARK 465 GLU A 627 REMARK 465 ASN A 628 REMARK 465 LEU A 629 REMARK 465 TYR A 630 REMARK 465 PHE A 631 REMARK 465 GLN A 632 REMARK 465 GLN B 1 REMARK 465 THR B 2 REMARK 465 ASP B 3 REMARK 465 GLU B 4 REMARK 465 ASN B 5 REMARK 465 ASN B 30 REMARK 465 SER B 31 REMARK 465 THR B 32 REMARK 465 PHE B 33 REMARK 465 LEU B 34 REMARK 465 GLN B 35 REMARK 465 GLU B 36 REMARK 465 GLY B 37 REMARK 465 MET B 38 REMARK 465 PRO B 39 REMARK 465 THR B 40 REMARK 465 SER B 41 REMARK 465 ALA B 42 REMARK 465 GLY B 446 REMARK 465 GLY B 447 REMARK 465 LEU B 448 REMARK 465 GLU B 449 REMARK 465 ASN B 450 REMARK 465 LEU B 451 REMARK 465 TYR B 452 REMARK 465 PHE B 453 REMARK 465 GLN B 454 REMARK 465 LYS C 513 REMARK 465 GLY C 514 REMARK 465 GLY C 515 REMARK 465 VAL C 516 REMARK 465 ARG C 517 REMARK 465 SER C 554 REMARK 465 GLU C 555 REMARK 465 PHE C 556 REMARK 465 ARG C 557 REMARK 465 ASP C 558 REMARK 465 LYS C 559 REMARK 465 LEU C 601 REMARK 465 LEU C 602 REMARK 465 ASP C 603 REMARK 465 CYS C 604 REMARK 465 GLY C 605 REMARK 465 GLU C 606 REMARK 465 ASP C 607 REMARK 465 ASN C 608 REMARK 465 ILE C 609 REMARK 465 CYS C 610 REMARK 465 VAL C 611 REMARK 465 PRO C 612 REMARK 465 ASP C 613 REMARK 465 LEU C 614 REMARK 465 GLN C 615 REMARK 465 LEU C 616 REMARK 465 GLU C 617 REMARK 465 VAL C 618 REMARK 465 PHE C 619 REMARK 465 GLY C 620 REMARK 465 GLU C 621 REMARK 465 GLN C 622 REMARK 465 ASN C 623 REMARK 465 GLY C 624 REMARK 465 GLY C 625 REMARK 465 LEU C 626 REMARK 465 GLU C 627 REMARK 465 ASN C 628 REMARK 465 LEU C 629 REMARK 465 TYR C 630 REMARK 465 PHE C 631 REMARK 465 GLN C 632 REMARK 465 GLN D 1 REMARK 465 THR D 2 REMARK 465 ASP D 3 REMARK 465 GLU D 4 REMARK 465 LEU D 34 REMARK 465 GLN D 35 REMARK 465 GLU D 36 REMARK 465 GLY D 37 REMARK 465 MET D 38 REMARK 465 PRO D 39 REMARK 465 THR D 40 REMARK 465 SER D 41 REMARK 465 ALA D 42 REMARK 465 GLY D 446 REMARK 465 GLY D 447 REMARK 465 LEU D 448 REMARK 465 GLU D 449 REMARK 465 ASN D 450 REMARK 465 LEU D 451 REMARK 465 TYR D 452 REMARK 465 PHE D 453 REMARK 465 GLN D 454 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 ND2 ASN C 256 C2 NAG C 2008 1.82 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 L 94 CA - CB - CG ANGL. DEV. = 13.9 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 GLN A 51 64.95 37.50 REMARK 500 PRO A 64 -71.64 -64.72 REMARK 500 GLN A 66 -71.38 -74.28 REMARK 500 ARG A 78 138.94 -37.75 REMARK 500 SER A 85 -46.88 -143.20 REMARK 500 SER A 86 -78.33 36.80 REMARK 500 GLU A 90 -1.74 -144.54 REMARK 500 LYS A 125 -128.74 -106.23 REMARK 500 ASP A 140 68.78 39.51 REMARK 500 SER A 153 -162.09 -127.00 REMARK 500 LEU A 212 107.33 -56.53 REMARK 500 ASP A 243 -153.16 -74.21 REMARK 500 THR A 258 -5.48 66.44 REMARK 500 ILE A 270 108.56 -39.86 REMARK 500 ALA A 282 4.80 56.08 REMARK 500 TYR A 284 45.90 -93.01 REMARK 500 ARG A 350 93.28 -53.09 REMARK 500 PRO A 374 -1.48 -53.85 REMARK 500 ASP A 432 -169.24 -125.64 REMARK 500 LEU A 474 -89.06 -144.00 REMARK 500 GLN A 512 22.03 -72.35 REMARK 500 GLU A 541 103.78 -59.16 REMARK 500 ASN A 552 68.33 -67.55 REMARK 500 SER A 554 35.86 -94.12 REMARK 500 LEU A 560 -73.20 -73.53 REMARK 500 PRO A 573 35.26 -77.89 REMARK 500 ALA A 575 50.53 36.28 REMARK 500 ASP A 578 -109.35 -104.98 REMARK 500 LYS B 9 -152.02 -82.57 REMARK 500 ALA B 10 89.51 -66.98 REMARK 500 LYS B 13 -149.99 -143.72 REMARK 500 SER B 14 -102.80 -86.95 REMARK 500 CYS B 15 -72.85 -115.83 REMARK 500 CYS B 25 118.67 -37.61 REMARK 500 ASP B 45 -62.71 -123.46 REMARK 500 GLU B 48 20.35 -78.96 REMARK 500 PRO B 57 46.74 -69.68 REMARK 500 ASN B 62 89.18 -155.40 REMARK 500 ASN B 72 57.87 -158.84 REMARK 500 ARG B 78 35.94 -95.63 REMARK 500 VAL B 168 -73.27 -129.05 REMARK 500 THR B 171 54.26 -92.82 REMARK 500 CYS B 187 -160.37 -112.77 REMARK 500 SER B 222 -155.49 -117.57 REMARK 500 VAL B 250 -169.37 -119.47 REMARK 500 ALA B 265 133.74 -39.31 REMARK 500 VAL B 274 -13.43 -141.55 REMARK 500 ASN B 277 134.78 -38.18 REMARK 500 HIS B 282 51.12 -141.88 REMARK 500 PRO B 416 -102.34 -96.06 REMARK 500 REMARK 500 THIS ENTRY HAS 150 RAMACHANDRAN OUTLIERS. 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 PHE C 155 SER C 156 -146.52 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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE 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 THR A 258 24.4 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL 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 MG B2003 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 229 OE1 REMARK 620 2 SER B 132 OG 94.7 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG D2003 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU D 229 OE1 REMARK 620 2 SER D 132 OG 90.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 430 O REMARK 620 2 ASP A 426 OD1 167.1 REMARK 620 3 ASP A 424 OD1 79.9 87.9 REMARK 620 4 ASP A 432 OD2 79.5 109.7 112.6 REMARK 620 5 ASN A 428 OD1 102.0 73.7 92.0 155.1 REMARK 620 6 ASP A 432 OD1 93.8 86.3 70.5 48.0 154.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 366 O REMARK 620 2 ASP A 364 OD2 99.8 REMARK 620 3 ASP A 362 OD1 159.1 83.8 REMARK 620 4 ASP A 368 OD2 75.3 154.4 109.9 REMARK 620 5 ASP A 360 OD2 73.2 71.8 88.6 128.2 REMARK 620 6 ASP A 368 OD1 104.7 152.3 68.7 48.3 103.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR C 430 O REMARK 620 2 ASP C 426 OD1 165.6 REMARK 620 3 ASN C 428 OD1 85.0 106.1 REMARK 620 4 ASP C 432 OD2 77.3 89.0 121.0 REMARK 620 5 ASP C 424 OD1 78.0 106.6 106.8 123.0 REMARK 620 6 ASP C 432 OD1 93.8 73.3 167.6 46.9 85.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR C 366 O REMARK 620 2 ASP C 362 OD1 171.2 REMARK 620 3 ASP C 364 OD2 80.8 92.1 REMARK 620 4 ASP C 368 OD2 71.5 117.3 127.7 REMARK 620 5 ASP C 360 OD2 73.6 99.8 77.8 131.1 REMARK 620 6 ASP C 368 OD1 107.3 80.3 169.4 51.9 110.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO D 228 O REMARK 620 2 ASN D 224 OD1 170.4 REMARK 620 3 GLU D 169 OE1 74.8 99.6 REMARK 620 4 ASP D 226 O 98.0 83.0 150.1 REMARK 620 5 ASP D 226 OD1 88.5 82.9 81.3 69.3 REMARK 620 6 GLU D 229 OE2 88.9 100.4 108.6 100.1 168.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN B 224 OD1 REMARK 620 2 GLU B 169 OE1 84.0 REMARK 620 3 PRO B 228 O 163.3 79.4 REMARK 620 4 ASP B 226 O 91.6 153.2 104.0 REMARK 620 5 GLU B 229 OE2 85.7 103.3 96.2 102.8 REMARK 620 6 ASP B 226 OD1 93.1 81.3 86.3 72.5 175.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 241 OG REMARK 620 2 THR A 245 O 175.1 REMARK 620 3 ASP A 243 OD1 98.9 84.1 REMARK 620 4 ASP A 247 OD2 85.4 93.0 160.8 REMARK 620 5 GLU A 239 OE2 81.3 102.5 92.1 69.9 REMARK 620 6 ASP A 247 OD1 75.7 99.8 150.0 49.2 115.6 REMARK 620 7 GLU A 239 OE1 125.8 58.1 84.5 77.9 44.6 122.9 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER C 241 OG REMARK 620 2 THR C 245 O 164.7 REMARK 620 3 ASP C 243 OD1 62.4 102.6 REMARK 620 4 GLU C 239 OE2 70.1 117.6 97.3 REMARK 620 5 ASP C 247 OD2 83.7 110.3 144.6 79.2 REMARK 620 6 GLU C 239 OE1 120.5 69.2 122.5 50.5 82.4 REMARK 620 7 ASP C 247 OD1 80.7 103.8 112.0 121.9 47.9 125.3 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 295 OD1 REMARK 620 2 LEU C 299 O 146.0 REMARK 620 3 ASP C 293 OD2 72.4 74.0 REMARK 620 4 ASP C 301 OD1 118.9 84.8 125.2 REMARK 620 5 ASP C 297 OD1 80.2 90.7 82.0 149.3 REMARK 620 6 ASP C 301 OD2 87.6 90.5 78.9 50.9 159.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 297 OD1 REMARK 620 2 ASN A 295 OD1 66.1 REMARK 620 3 ASP A 293 OD2 83.4 91.2 REMARK 620 4 LEU A 299 O 116.4 145.4 56.6 REMARK 620 5 ASP A 301 OD1 156.5 100.9 117.5 85.6 REMARK 620 6 ASP A 301 OD2 133.3 69.6 83.5 92.3 47.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 138 OD1 REMARK 620 2 ASP B 137 OD2 68.4 REMARK 620 3 SER B 134 O 89.2 72.7 REMARK 620 4 ALA B 342 O 74.7 100.0 163.9 REMARK 620 5 ASP B 137 OD1 103.2 55.9 115.8 68.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 137 OD1 REMARK 620 2 ASP D 138 OD1 84.9 REMARK 620 3 ALA D 342 O 68.7 71.3 REMARK 620 4 SER D 134 O 125.4 96.8 161.7 REMARK 620 5 ASP D 137 OD2 55.7 69.5 113.0 73.8 REMARK 620 N 1 2 3 4 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 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2008 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2009 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2010 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2011 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2012 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2013 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2014 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2015 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2008 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2009 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2010 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2011 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C 2012 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 2013 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 2014 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 2015 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2016 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2004 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3VI4 RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 1. THE SEQUENCE CONFLICTS OF ENTITY 2 (INTEGRIN BETA-1) ARE BASED REMARK 999 ON REFERENCE 1 OF DATABASE UNIPROTKB/SWISS-PROT P05556 (ITB1_HUMAN) REMARK 999 . 2. THE SEQUENCE OF SG/19 LIGHT CHAIN HAS BEEN DEPOSITED TO EMBL REMARK 999 WITH ACCESSION NUMBER HE578878, AND SG/19 HEAVY CHAIN SG/19 HAS REMARK 999 BEEN DEPOSITED TO EMBL WITH ACCESSION NUMBER HE578877.