HEADER MEMBRANE PROTEIN 24-OCT-17 6BDZ
TITLE ADAM10 EXTRACELLULAR DOMAIN BOUND BY THE 11G2 FAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 11G2 FAB LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 11G2 FAB HEAVY CHAIN;
COMPND 7 CHAIN: H;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN
COMPND 11 10;
COMPND 12 CHAIN: A;
COMPND 13 SYNONYM: ADAM 10,CDW156,KUZBANIAN PROTEIN HOMOLOG,MAMMALIAN
COMPND 14 DISINTEGRIN-METALLOPROTEASE;
COMPND 15 EC: 3.4.24.81;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_TAXID: 10090;
SOURCE 4 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: ADAM10, KUZ, MADM;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS ADAM10, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.C.M.SEEGAR
REVDAT 3 29-JUL-20 6BDZ 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 01-JAN-20 6BDZ 1 REMARK
REVDAT 1 27-DEC-17 6BDZ 0
JRNL AUTH T.C.M.SEEGAR,L.B.KILLINGSWORTH,N.SAHA,P.A.MEYER,D.PATRA,
JRNL AUTH 2 B.ZIMMERMAN,P.W.JANES,E.RUBINSTEIN,D.B.NIKOLOV,G.SKINIOTIS,
JRNL AUTH 3 A.C.KRUSE,S.C.BLACKLOW
JRNL TITL STRUCTURAL BASIS FOR REGULATED PROTEOLYSIS BY THE
JRNL TITL 2 ALPHA-SECRETASE ADAM10.
JRNL REF CELL V. 171 1638 2017
JRNL REFN ISSN 1097-4172
JRNL PMID 29224781
JRNL DOI 10.1016/J.CELL.2017.11.014
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 35539
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.267
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.317
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3582
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.7960 - 9.1644 1.00 1226 143 0.2385 0.2724
REMARK 3 2 9.1644 - 7.2818 1.00 1258 139 0.2410 0.2867
REMARK 3 3 7.2818 - 6.3636 1.00 1217 137 0.2679 0.3255
REMARK 3 4 6.3636 - 5.7828 1.00 1235 141 0.2490 0.2868
REMARK 3 5 5.7828 - 5.3689 1.00 1234 138 0.2242 0.2947
REMARK 3 6 5.3689 - 5.0527 1.00 1244 135 0.2089 0.3072
REMARK 3 7 5.0527 - 4.7998 1.00 1218 143 0.2278 0.2395
REMARK 3 8 4.7998 - 4.5911 1.00 1247 136 0.2101 0.2735
REMARK 3 9 4.5911 - 4.4145 1.00 1220 139 0.2168 0.2831
REMARK 3 10 4.4145 - 4.2622 1.00 1251 140 0.2255 0.3085
REMARK 3 11 4.2622 - 4.1290 1.00 1242 135 0.2224 0.2866
REMARK 3 12 4.1290 - 4.0110 1.00 1225 142 0.2423 0.3132
REMARK 3 13 4.0110 - 3.9055 1.00 1217 133 0.2435 0.3150
REMARK 3 14 3.9055 - 3.8102 1.00 1278 142 0.2719 0.3009
REMARK 3 15 3.8102 - 3.7237 1.00 1213 131 0.2688 0.3604
REMARK 3 16 3.7237 - 3.6444 1.00 1227 137 0.3069 0.3063
REMARK 3 17 3.6444 - 3.5716 1.00 1238 140 0.2882 0.3263
REMARK 3 18 3.5716 - 3.5042 1.00 1228 135 0.2899 0.3706
REMARK 3 19 3.5042 - 3.4416 1.00 1247 139 0.3034 0.3807
REMARK 3 20 3.4416 - 3.3833 1.00 1250 136 0.3055 0.3845
REMARK 3 21 3.3833 - 3.3287 1.00 1215 138 0.3445 0.3832
REMARK 3 22 3.3287 - 3.2775 1.00 1228 141 0.3443 0.3789
REMARK 3 23 3.2775 - 3.2293 1.00 1260 140 0.3333 0.4473
REMARK 3 24 3.2293 - 3.1839 0.99 1214 138 0.3514 0.3685
REMARK 3 25 3.1839 - 3.1408 0.99 1149 128 0.3500 0.4187
REMARK 3 26 3.1408 - 3.1001 0.91 1176 136 0.3852 0.3983
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.570
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 6844
REMARK 3 ANGLE : 0.693 9285
REMARK 3 CHIRALITY : 0.048 1028
REMARK 3 PLANARITY : 0.004 1184
REMARK 3 DIHEDRAL : 17.940 2555
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6BDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230742.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35539
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 10.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.23M AMMONIUM SULFATE 100MM TRIS PH
REMARK 280 8.5 2% PEG400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 131.36000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 131.36000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 39.61500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.79000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.61500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.79000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 131.36000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.61500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.79000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 131.36000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.61500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.79000
REMARK 290 SMTRY3 8 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 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY H 239
REMARK 465 CYS H 240
REMARK 465 LYS H 241
REMARK 465 PRO H 242
REMARK 465 CYS H 243
REMARK 465 ILE H 244
REMARK 465 CYS H 245
REMARK 465 SER A 584
REMARK 465 SER A 585
REMARK 465 ASP A 586
REMARK 465 GLY A 587
REMARK 465 LYS A 588
REMARK 465 ASP A 589
REMARK 465 ASP A 590
REMARK 465 VAL A 648
REMARK 465 ASP A 649
REMARK 465 ALA A 650
REMARK 465 ASP A 651
REMARK 465 GLY A 652
REMARK 465 PRO A 653
REMARK 465 LEU A 654
REMARK 465 GLY A 655
REMARK 465 GLY A 656
REMARK 465 HIS A 657
REMARK 465 HIS A 658
REMARK 465 HIS A 659
REMARK 465 HIS A 660
REMARK 465 HIS A 661
REMARK 465 HIS A 662
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 SG CYS A 344 SG CYS A 451 1.35
REMARK 500 NE2 GLN A 551 CD1 ILE A 563 1.61
REMARK 500 OD2 ASP L 193 OG1 THR L 195 1.99
REMARK 500 OE1 GLN A 551 ND2 ASN A 564 2.01
REMARK 500 CE2 PHE A 290 O7 NAG C 1 2.10
REMARK 500 OD1 ASP H 73 OG1 THR H 75 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER H 34 OD2 ASP H 196 4565 2.19
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 GLY A 237 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP L 70 -71.66 -104.00
REMARK 500 THR L 74 -58.13 70.47
REMARK 500 ASN L 161 80.41 56.12
REMARK 500 ASN L 213 -70.45 -118.98
REMARK 500 LEU H 67 -65.19 -108.49
REMARK 500 SER H 151 32.05 -82.91
REMARK 500 ASN H 156 -157.04 -160.44
REMARK 500 SER H 195 87.51 -157.24
REMARK 500 PRO H 212 30.46 -92.69
REMARK 500 SER A 269 -166.13 -128.34
REMARK 500 GLU A 306 1.65 -68.97
REMARK 500 CYS A 344 40.49 74.93
REMARK 500 TYR A 350 -132.16 53.94
REMARK 500 ASN A 359 51.94 -93.41
REMARK 500 LYS A 405 32.89 -90.65
REMARK 500 TYR A 415 -169.57 -107.41
REMARK 500 MET A 417 28.43 -77.65
REMARK 500 ARG A 420 -156.18 -124.04
REMARK 500 SER A 423 105.91 -170.84
REMARK 500 LEU A 427 -67.65 -106.42
REMARK 500 ASP A 472 96.44 -164.70
REMARK 500 CYS A 510 46.56 -92.69
REMARK 500 CYS A 567 63.63 -104.78
REMARK 500 MET A 602 -0.40 73.01
REMARK 500 HIS A 618 -65.21 -92.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG B 1
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 ZN A 705 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 383 NE2
REMARK 620 2 HIS A 393 NE2 107.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 704 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 459 O
REMARK 620 2 ASN A 462 OD1 108.5
REMARK 620 3 GLU A 466 OE1 120.9 96.0
REMARK 620 4 GLU A 469 OE1 77.4 173.0 83.7
REMARK 620 5 GLU A 469 OE2 121.9 128.8 66.6 44.8
REMARK 620 6 ASP A 472 OD2 125.0 76.5 112.5 97.2 68.3
REMARK 620 N 1 2 3 4 5
DBREF 6BDZ L 23 237 PDB 6BDZ 6BDZ 23 237
DBREF 6BDZ H 20 245 PDB 6BDZ 6BDZ 20 245
DBREF 6BDZ A 220 654 UNP O14672 ADA10_HUMAN 220 654
SEQADV 6BDZ GLN A 267 UNP O14672 ASN 267 CONFLICT
SEQADV 6BDZ GLN A 439 UNP O14672 ASN 439 CONFLICT
SEQADV 6BDZ GLN A 551 UNP O14672 ASN 551 CONFLICT
SEQADV 6BDZ GLY A 655 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ GLY A 656 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ HIS A 657 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ HIS A 658 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ HIS A 659 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ HIS A 660 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ HIS A 661 UNP O14672 EXPRESSION TAG
SEQADV 6BDZ HIS A 662 UNP O14672 EXPRESSION TAG
SEQRES 1 L 215 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 L 215 SER LEU GLY GLU ARG VAL THR MET THR CYS THR VAL SER
SEQRES 3 L 215 SER SER VAL SER SER GLY TYR LEU HIS TRP TYR GLN GLN
SEQRES 4 L 215 LYS SER GLY SER SER PRO LYS LEU TRP ILE TYR SER THR
SEQRES 5 L 215 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY
SEQRES 6 L 215 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER
SEQRES 7 L 215 MET GLY ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN
SEQRES 8 L 215 TYR ARG ARG SER PRO LEU THR PHE GLY ALA GLY THR LYS
SEQRES 9 L 215 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER
SEQRES 10 L 215 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY
SEQRES 11 L 215 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS
SEQRES 12 L 215 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG
SEQRES 13 L 215 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER
SEQRES 14 L 215 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU
SEQRES 15 L 215 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS
SEQRES 16 L 215 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS
SEQRES 17 L 215 SER PHE ASN ARG ASN GLU CYS
SEQRES 1 H 226 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 H 226 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 H 226 PHE SER LEU THR GLY TYR GLY VAL ASN TRP VAL ARG GLN
SEQRES 4 H 226 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 H 226 GLY ASP GLY THR THR ASP TYR ASN SER THR LEU LYS SER
SEQRES 6 H 226 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 H 226 PHE LEU LYS MET ASN SER LEU GLN THR VAL ASP THR ALA
SEQRES 8 H 226 ARG TYR TYR CYS ALA ARG ASP GLY ASP TYR GLY ARG LEU
SEQRES 9 H 226 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER
SEQRES 10 H 226 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO
SEQRES 11 H 226 GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY
SEQRES 12 H 226 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 226 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR
SEQRES 14 H 226 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER
SEQRES 15 H 226 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU
SEQRES 16 H 226 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR
SEQRES 17 H 226 LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY CYS
SEQRES 18 H 226 LYS PRO CYS ILE CYS
SEQRES 1 A 443 ASN THR CYS GLN LEU TYR ILE GLN THR ASP HIS LEU PHE
SEQRES 2 A 443 PHE LYS TYR TYR GLY THR ARG GLU ALA VAL ILE ALA GLN
SEQRES 3 A 443 ILE SER SER HIS VAL LYS ALA ILE ASP THR ILE TYR GLN
SEQRES 4 A 443 THR THR ASP PHE SER GLY ILE ARG GLN ILE SER PHE MET
SEQRES 5 A 443 VAL LYS ARG ILE ARG ILE ASN THR THR ALA ASP GLU LYS
SEQRES 6 A 443 ASP PRO THR ASN PRO PHE ARG PHE PRO ASN ILE GLY VAL
SEQRES 7 A 443 GLU LYS PHE LEU GLU LEU ASN SER GLU GLN ASN HIS ASP
SEQRES 8 A 443 ASP TYR CYS LEU ALA TYR VAL PHE THR ASP ARG ASP PHE
SEQRES 9 A 443 ASP ASP GLY VAL LEU GLY LEU ALA TRP VAL GLY ALA PRO
SEQRES 10 A 443 SER GLY SER SER GLY GLY ILE CYS GLU LYS SER LYS LEU
SEQRES 11 A 443 TYR SER ASP GLY LYS LYS LYS SER LEU ASN THR GLY ILE
SEQRES 12 A 443 ILE THR VAL GLN ASN TYR GLY SER HIS VAL PRO PRO LYS
SEQRES 13 A 443 VAL SER HIS ILE THR PHE ALA HIS GLU VAL GLY HIS ASN
SEQRES 14 A 443 PHE GLY SER PRO HIS ASP SER GLY THR GLU CYS THR PRO
SEQRES 15 A 443 GLY GLU SER LYS ASN LEU GLY GLN LYS GLU ASN GLY ASN
SEQRES 16 A 443 TYR ILE MET TYR ALA ARG ALA THR SER GLY ASP LYS LEU
SEQRES 17 A 443 ASN ASN ASN LYS PHE SER LEU CYS SER ILE ARG GLN ILE
SEQRES 18 A 443 SER GLN VAL LEU GLU LYS LYS ARG ASN ASN CYS PHE VAL
SEQRES 19 A 443 GLU SER GLY GLN PRO ILE CYS GLY ASN GLY MET VAL GLU
SEQRES 20 A 443 GLN GLY GLU GLU CYS ASP CYS GLY TYR SER ASP GLN CYS
SEQRES 21 A 443 LYS ASP GLU CYS CYS PHE ASP ALA ASN GLN PRO GLU GLY
SEQRES 22 A 443 ARG LYS CYS LYS LEU LYS PRO GLY LYS GLN CYS SER PRO
SEQRES 23 A 443 SER GLN GLY PRO CYS CYS THR ALA GLN CYS ALA PHE LYS
SEQRES 24 A 443 SER LYS SER GLU LYS CYS ARG ASP ASP SER ASP CYS ALA
SEQRES 25 A 443 ARG GLU GLY ILE CYS ASN GLY PHE THR ALA LEU CYS PRO
SEQRES 26 A 443 ALA SER ASP PRO LYS PRO GLN PHE THR ASP CYS ASN ARG
SEQRES 27 A 443 HIS THR GLN VAL CYS ILE ASN GLY GLN CYS ALA GLY SER
SEQRES 28 A 443 ILE CYS GLU LYS TYR GLY LEU GLU GLU CYS THR CYS ALA
SEQRES 29 A 443 SER SER ASP GLY LYS ASP ASP LYS GLU LEU CYS HIS VAL
SEQRES 30 A 443 CYS CYS MET LYS LYS MET ASP PRO SER THR CYS ALA SER
SEQRES 31 A 443 THR GLY SER VAL GLN TRP SER ARG HIS PHE SER GLY ARG
SEQRES 32 A 443 THR ILE THR LEU GLN PRO GLY SER PRO CYS ASN ASP PHE
SEQRES 33 A 443 ARG GLY TYR CYS ASP VAL PHE MET ARG CYS ARG LEU VAL
SEQRES 34 A 443 ASP ALA ASP GLY PRO LEU GLY GLY HIS HIS HIS HIS HIS
SEQRES 35 A 443 HIS
HET NAG B 1 13
HET NAG B 2 14
HET MAN B 3 11
HET MAN B 4 11
HET NAG C 1 14
HET NAG C 2 14
HET MAN C 3 11
HET SO4 L 301 5
HET SO4 L 302 5
HET CA A 704 1
HET ZN A 705 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 4 NAG 4(C8 H15 N O6)
FORMUL 4 MAN 3(C6 H12 O6)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 8 CA CA 2+
FORMUL 9 ZN ZN 2+
FORMUL 10 HOH *(H2 O)
HELIX 1 AA1 SER L 52 GLY L 54 5 3
HELIX 2 AA2 SER L 144 GLY L 151 1 8
HELIX 3 AA3 LYS L 206 GLU L 210 1 5
HELIX 4 AA4 GLN H 105 THR H 109 5 5
HELIX 5 AA5 GLY H 118 ARG H 122 5 5
HELIX 6 AA6 SER H 179 SER H 181 5 3
HELIX 7 AA7 PRO H 223 SER H 226 5 4
HELIX 8 AA8 ASP A 229 GLY A 237 1 9
HELIX 9 AA9 THR A 238 THR A 259 1 22
HELIX 10 AB1 THR A 279 GLU A 283 5 5
HELIX 11 AB2 GLY A 296 GLU A 306 1 11
HELIX 12 AB3 PHE A 323 VAL A 327 5 5
HELIX 13 AB4 PRO A 373 PHE A 389 1 17
HELIX 14 AB5 THR A 400 SER A 404 5 5
HELIX 15 AB6 ASN A 406 GLY A 413 1 8
HELIX 16 AB7 SER A 433 PHE A 452 1 20
HELIX 17 AB8 SER A 570 GLY A 576 5 7
HELIX 18 AB9 ASP A 603 CYS A 607 5 5
HELIX 19 AC1 TRP A 615 SER A 620 1 6
SHEET 1 AA1 3 LEU L 26 SER L 29 0
SHEET 2 AA1 3 VAL L 41 VAL L 51 -1 O THR L 46 N THR L 27
SHEET 3 AA1 3 PHE L 85 ILE L 98 -1 O LEU L 96 N MET L 43
SHEET 1 AA2 6 ILE L 32 ALA L 35 0
SHEET 2 AA2 6 THR L 125 ILE L 129 1 O GLU L 128 N MET L 33
SHEET 3 AA2 6 THR L 108 GLN L 113 -1 N TYR L 109 O THR L 125
SHEET 4 AA2 6 LEU L 56 GLN L 61 -1 N HIS L 57 O HIS L 112
SHEET 5 AA2 6 LYS L 68 TYR L 72 -1 O ILE L 71 N TRP L 58
SHEET 6 AA2 6 ASN L 76 LEU L 77 -1 O ASN L 76 N TYR L 72
SHEET 1 AA3 4 ILE L 32 ALA L 35 0
SHEET 2 AA3 4 THR L 125 ILE L 129 1 O GLU L 128 N MET L 33
SHEET 3 AA3 4 THR L 108 GLN L 113 -1 N TYR L 109 O THR L 125
SHEET 4 AA3 4 THR L 120 PHE L 121 -1 O THR L 120 N GLN L 113
SHEET 1 AA4 4 THR L 137 PHE L 141 0
SHEET 2 AA4 4 GLY L 152 PHE L 162 -1 O PHE L 158 N SER L 139
SHEET 3 AA4 4 TYR L 196 THR L 205 -1 O LEU L 202 N VAL L 155
SHEET 4 AA4 4 VAL L 182 TRP L 186 -1 N LEU L 183 O THR L 201
SHEET 1 AA5 4 SER L 176 ARG L 178 0
SHEET 2 AA5 4 ILE L 167 ILE L 173 -1 N TRP L 171 O ARG L 178
SHEET 3 AA5 4 SER L 214 HIS L 221 -1 O THR L 216 N LYS L 172
SHEET 4 AA5 4 ILE L 228 ASN L 233 -1 O LYS L 230 N CYS L 217
SHEET 1 AA6 4 GLN H 22 SER H 26 0
SHEET 2 AA6 4 LEU H 37 SER H 44 -1 O THR H 40 N SER H 26
SHEET 3 AA6 4 GLN H 96 MET H 101 -1 O VAL H 97 N CYS H 41
SHEET 4 AA6 4 SER H 87 ASP H 91 -1 N SER H 89 O PHE H 98
SHEET 1 AA7 6 LEU H 30 VAL H 31 0
SHEET 2 AA7 6 THR H 130 VAL H 134 1 O THR H 133 N VAL H 31
SHEET 3 AA7 6 ALA H 110 ASP H 117 -1 N ALA H 110 O LEU H 132
SHEET 4 AA7 6 GLY H 52 GLN H 58 -1 N GLY H 52 O ASP H 117
SHEET 5 AA7 6 GLU H 65 ILE H 70 -1 O LEU H 67 N TRP H 55
SHEET 6 AA7 6 THR H 76 TYR H 78 -1 O ASP H 77 N VAL H 69
SHEET 1 AA8 4 SER H 143 LEU H 147 0
SHEET 2 AA8 4 MET H 158 TYR H 168 -1 O GLY H 162 N LEU H 147
SHEET 3 AA8 4 TYR H 198 PRO H 207 -1 O VAL H 204 N LEU H 161
SHEET 4 AA8 4 VAL H 186 THR H 188 -1 N HIS H 187 O SER H 203
SHEET 1 AA9 4 SER H 143 LEU H 147 0
SHEET 2 AA9 4 MET H 158 TYR H 168 -1 O GLY H 162 N LEU H 147
SHEET 3 AA9 4 TYR H 198 PRO H 207 -1 O VAL H 204 N LEU H 161
SHEET 4 AA9 4 VAL H 192 LEU H 193 -1 N VAL H 192 O THR H 199
SHEET 1 AB1 3 THR H 174 TRP H 177 0
SHEET 2 AB1 3 THR H 217 HIS H 222 -1 O ASN H 219 N THR H 176
SHEET 3 AB1 3 THR H 227 LYS H 232 -1 O THR H 227 N HIS H 222
SHEET 1 AB2 5 MET A 271 ILE A 277 0
SHEET 2 AB2 5 GLN A 223 THR A 228 1 N LEU A 224 O MET A 271
SHEET 3 AB2 5 LEU A 314 THR A 319 1 O PHE A 318 N GLN A 227
SHEET 4 AB2 5 THR A 360 THR A 364 1 O ILE A 363 N THR A 319
SHEET 5 AB2 5 GLY A 329 ALA A 331 -1 N LEU A 330 O ILE A 362
SHEET 1 AB3 2 GLN A 366 ASN A 367 0
SHEET 2 AB3 2 SER A 370 HIS A 371 -1 O SER A 370 N ASN A 367
SHEET 1 AB4 2 GLU A 522 LYS A 523 0
SHEET 2 AB4 2 ILE A 535 CYS A 536 -1 O CYS A 536 N GLU A 522
SHEET 1 AB5 2 THR A 553 CYS A 555 0
SHEET 2 AB5 2 GLN A 560 CYS A 562 -1 O GLN A 560 N CYS A 555
SHEET 1 AB6 2 CYS A 597 CYS A 598 0
SHEET 2 AB6 2 ALA A 608 SER A 609 -1 O ALA A 608 N CYS A 598
SHEET 1 AB7 3 SER A 630 CYS A 632 0
SHEET 2 AB7 3 GLY A 637 CYS A 639 -1 O GLY A 637 N CYS A 632
SHEET 3 AB7 3 CYS A 645 ARG A 646 -1 O ARG A 646 N TYR A 638
SSBOND 1 CYS L 45 CYS L 111 1555 1555 2.03
SSBOND 2 CYS L 157 CYS L 217 1555 1555 2.03
SSBOND 3 CYS L 237 CYS H 238 1555 1555 2.03
SSBOND 4 CYS H 41 CYS H 114 1555 1555 2.03
SSBOND 5 CYS H 163 CYS H 218 1555 1555 2.03
SSBOND 6 CYS A 222 CYS A 313 1555 1555 2.02
SSBOND 7 CYS A 399 CYS A 435 1555 1555 2.03
SSBOND 8 CYS A 460 CYS A 495 1555 1555 2.03
SSBOND 9 CYS A 471 CYS A 484 1555 1555 2.03
SSBOND 10 CYS A 473 CYS A 479 1555 1555 2.03
SSBOND 11 CYS A 483 CYS A 515 1555 1555 2.03
SSBOND 12 CYS A 503 CYS A 511 1555 1555 2.03
SSBOND 13 CYS A 510 CYS A 536 1555 1555 2.03
SSBOND 14 CYS A 524 CYS A 543 1555 1555 2.02
SSBOND 15 CYS A 530 CYS A 562 1555 1555 2.03
SSBOND 16 CYS A 555 CYS A 567 1555 1555 2.03
SSBOND 17 CYS A 572 CYS A 598 1555 1555 2.03
SSBOND 18 CYS A 580 CYS A 607 1555 1555 2.03
SSBOND 19 CYS A 582 CYS A 597 1555 1555 2.03
SSBOND 20 CYS A 594 CYS A 639 1555 1555 2.03
SSBOND 21 CYS A 632 CYS A 645 1555 1555 2.03
LINK ND2 ASN H 79 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 278 C1 NAG C 1 1555 1555 1.44
LINK CD2 PHE A 290 O7 NAG C 1 1555 1555 1.38
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.46
LINK O6 MAN B 3 C1 MAN B 4 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 MAN C 3 1555 1555 1.45
LINK NE2 HIS A 383 ZN ZN A 705 1555 1555 2.20
LINK NE2 HIS A 393 ZN ZN A 705 1555 1555 2.19
LINK O ILE A 459 CA CA A 704 1555 1555 2.25
LINK OD1 ASN A 462 CA CA A 704 1555 1555 2.32
LINK OE1 GLU A 466 CA CA A 704 1555 1555 2.25
LINK OE1 GLU A 469 CA CA A 704 1555 1555 3.12
LINK OE2 GLU A 469 CA CA A 704 1555 1555 2.40
LINK OD2 ASP A 472 CA CA A 704 1555 1555 2.17
CISPEP 1 SER L 29 PRO L 30 0 -10.87
CISPEP 2 SER L 117 PRO L 118 0 -3.00
CISPEP 3 TYR L 163 PRO L 164 0 0.20
CISPEP 4 PHE H 169 PRO H 170 0 -5.06
CISPEP 5 GLU H 171 PRO H 172 0 0.79
CISPEP 6 TRP H 211 PRO H 212 0 1.90
CRYST1 79.230 97.580 262.720 90.00 90.00 90.00 C 2 2 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 0.012621 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010248 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END